|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-242 |
1.42e-95 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 279.26 E-value: 1.42e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDATNYRKQIGYIPE 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 82 TPSLYEELTLREHIETVAMAYGIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFL 161
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 162 GLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQQLRevfdmpEASLNDIYLALTKEE 241
Cdd:COG1131 161 GLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELK------ARLLEDVFLELTGEE 234
|
.
gi 577038301 242 E 242
Cdd:COG1131 235 A 235
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-242 |
3.47e-75 |
|
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: 227.82 E-value: 3.47e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDATNYRKQIGYIP 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 81 ETPSLYEELTLREHIETVAMAYGIEQKVAFNRVEPLLKMFRLDQKLDwFPVH-FSKGMKQKVMIICAFVVDPSLFIVDEP 159
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLD-RRVGeLSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 160 FLGLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQQLREVFDmpEASLNDIYLALTK 239
Cdd:COG4555 160 TNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIG--EENLEDAFVALIG 237
|
...
gi 577038301 240 EEE 242
Cdd:COG4555 238 SEE 240
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-210 |
1.75e-70 |
|
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: 213.41 E-value: 1.75e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDATNYRKQIGYIPE 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 82 TPSLYEELTLREHIEtvamaygieqkvafnrvepllkmfrldqkldwfpvhFSKGMKQKVMIICAFVVDPSLFIVDEPFL 161
Cdd:cd03230 81 EPSLYENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 577038301 162 GLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEV 210
Cdd:cd03230 125 GLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-223 |
1.31e-65 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 205.34 E-value: 1.31e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDAtnyRKQIGYIP 80
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED---RRRIGYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 81 ETPSLYEELTLREHIETVAMAYGIEQKVAFNRVEPLLKMFRLDQKLDwFPVH-FSKGMKQKVMIICAFVVDPSLFIVDEP 159
Cdd:COG4152 78 EERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRAN-KKVEeLSKGNQQKVQLIAALLHDPELLILDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 577038301 160 FLGLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQQLREVF 223
Cdd:COG4152 157 FSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQF 220
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-220 |
1.99e-58 |
|
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: 184.25 E-value: 1.99e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKL--TGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDATNYRKQIGYI 79
Cdd:cd03263 1 LQIRNLtkTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 80 PETPSLYEELTLREHIETVAMAYGIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEP 159
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 577038301 160 FLGLDPLA---IADLIQllevEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQQLR 220
Cdd:cd03263 161 TSGLDPASrraIWDLIL----EVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-214 |
1.51e-53 |
|
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: 171.69 E-value: 1.51e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDAtnyRKQIGYIPE 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA---RNRIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 82 TPSLYEELTLREHIETVAMAYGIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFL 161
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 577038301 162 GLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQG 214
Cdd:cd03269 158 GLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-214 |
3.01e-53 |
|
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: 170.86 E-value: 3.01e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDAtNYRKQIGYIPE 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI-EALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 82 TPSLYEELTLREHIETVAMAYGIEQKvafnRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFL 161
Cdd:cd03268 80 APGFYPNLTARENLRLLARLLGIRKK----RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 577038301 162 GLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQG 214
Cdd:cd03268 156 GLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-214 |
2.29e-52 |
|
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: 169.09 E-value: 2.29e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGY----VHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDATNYRKQI 76
Cdd:cd03266 1 MITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 77 GYIPETPSLYEELTLREHIETVAMAYGIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIV 156
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 577038301 157 DEPFLGLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQG 214
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-220 |
1.95e-50 |
|
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: 164.08 E-value: 1.95e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDATNYRKQIGYIPE 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 82 TPSLYEELTLREHIETVAMAYGIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFL 161
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 162 GLDPLAIADLIQLLE-VEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQQLR 220
Cdd:cd03265 161 GLDPQTRAHVWEYIEkLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
11-221 |
1.09e-49 |
|
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: 164.87 E-value: 1.09e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 11 YVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDATNYRKQIGYIPETPSLYEELT 90
Cdd:TIGR01188 3 YGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDEDLT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 91 LREHIETVAMAYGIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDPLAIAD 170
Cdd:TIGR01188 83 GRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 577038301 171 LIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQQLRE 221
Cdd:TIGR01188 163 IWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKR 213
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-190 |
1.12e-48 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 159.18 E-value: 1.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDATNYRKQIGYIP 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 81 ETPSLYEELTLREHIETVAMAYGIEQKVAfnRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPF 160
Cdd:COG4133 82 HADGLKPELTVRENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
170 180 190
....*....|....*....|....*....|
gi 577038301 161 LGLDPLAIADLIQLLEVEKQKGKSILMSTH 190
Cdd:COG4133 160 TALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-228 |
9.78e-48 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 157.49 E-value: 9.78e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYV-HVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLRE-DATNYRKQIGYI 79
Cdd:COG1122 1 IELENLSFSYPgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKkNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 80 ---PET----PSLYEEltlrehietVA---MAYGIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVV 149
Cdd:COG1122 81 fqnPDDqlfaPTVEED---------VAfgpENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 577038301 150 DPSLFIVDEPFLGLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNlqqLREVFDMPEA 228
Cdd:COG1122 152 EPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGT---PREVFSDYEL 227
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-214 |
1.31e-46 |
|
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: 153.89 E-value: 1.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYVHVPVLKDVSFTVESGqLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDATNYRKQIGYIPE 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 82 TPSLYEELTLREHIETVAMAYGIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFL 161
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 577038301 162 GLDPlaiADLIQL--LEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQG 214
Cdd:cd03264 160 GLDP---EERIRFrnLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-221 |
3.86e-46 |
|
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: 152.97 E-value: 3.86e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGltlrEDATNY------RKQ 75
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDG----RDITGLppheraRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 76 IGYIPETPSLYEELTLREHIETVAMAYGIEQKVAfnRVEPLLKMF-RLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLF 154
Cdd:cd03224 77 IGYVPEGRRIFPELTVEENLLLGAYARRRAKRKA--RLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 577038301 155 IVDEPFLGLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQQLRE 221
Cdd:cd03224 155 LLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-209 |
1.43e-45 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 151.08 E-value: 1.43e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 3 EIKKLTGGYVH--VPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDATN-YRKQIGYI 79
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKeLRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 80 ---PE----TPSLYEEltlrehIETVAMAYGIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPS 152
Cdd:cd03225 81 fqnPDdqffGPTVEEE------VAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 577038301 153 LFIVDEPFLGLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGE 209
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-214 |
1.98e-44 |
|
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: 148.81 E-value: 1.98e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLT----GGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKING---LTL-REDATNY 72
Cdd:cd03257 1 LLEVKNLSvsfpTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdlLKLsRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 73 RKQIGYIPETP--SLYEELTLREHIETVAMAYGIEQKVAFNRVEPLLKMFRL---DQKLDWFPVHFSKGMKQKVMIICAF 147
Cdd:cd03257 81 RKEIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 577038301 148 VVDPSLFIVDEPFLGLDPLAIADLIQLL-EVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQG 214
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLkKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-214 |
7.38e-44 |
|
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: 146.91 E-value: 7.38e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 3 EIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDatnyRKQIGYIPET 82
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE----RKRIGYVPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 83 PSLYEE--LTLRehiETVAMA-------YGIEQKVAFNRVEPLLKMFRL----DQKLDwfpvHFSKGMKQKVMIICAFVV 149
Cdd:cd03235 77 RSIDRDfpISVR---DVVLMGlyghkglFRRLSKADKAKVDEALERVGLselaDRQIG----ELSGGQQQRVLLARALVQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 577038301 150 DPSLFIVDEPFLGLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAfVILHKGEVRAQG 214
Cdd:cd03235 150 DPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDR-VLLLNRTVVASG 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-228 |
1.83e-43 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 153.14 E-value: 1.83e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYVH--VPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTP---YSGEIKINGLTLREDATNYR-K 74
Cdd:COG1123 4 LLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRgR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 75 QIGYIPETP--SLyEELTLREHIETVAMAYGIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPS 152
Cdd:COG1123 84 RIGMVFQDPmtQL-NPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 577038301 153 LFIVDEPFLGLDPLAIADLIQLL-EVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNlqqLREVFDMPEA 228
Cdd:COG1123 163 LLIADEPTTALDVTTQAEILDLLrELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGP---PEEILAAPQA 236
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-226 |
2.57e-43 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 152.75 E-value: 2.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYV-----HVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTL----REDATN 71
Cdd:COG1123 260 LLEVRNLSKRYPvrgkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLtklsRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 72 YRKQIGYI---PETpSLYEELTLREHIETVAMAYGI-EQKVAFNRVEPLLKMFRLDQK-LDWFPVHFSKGMKQKVMIICA 146
Cdd:COG1123 340 LRRRVQMVfqdPYS-SLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPPDlADRYPHELSGGQRQRVAIARA 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 147 FVVDPSLFIVDEPFLGLDPLAIADLIQLL-EVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNlqqLREVFDM 225
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQAQILNLLrDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGP---TEEVFAN 495
|
.
gi 577038301 226 P 226
Cdd:COG1123 496 P 496
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-220 |
3.25e-43 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 146.39 E-value: 3.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDatnyRKQIGYIP 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA----RRRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 81 ETPSLYEE--LTLRehiETVAM-------AYGIEQKVAFNRVEPLLKMFRLDQKLDWfPV-HFSKGMKQKVMIICAFVVD 150
Cdd:COG1121 82 QRAEVDWDfpITVR---DVVLMgrygrrgLFRRPSRADREAVDEALERVGLEDLADR-PIgELSGGQQQRVLLARALAQD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 577038301 151 PSLFIVDEPFLGLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKG--------EVRAQGNLQQLR 220
Cdd:COG1121 158 PDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGlvahgppeEVLTPENLSRAY 235
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
2-223 |
1.01e-42 |
|
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: 144.46 E-value: 1.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGltlREDATNYRKQIGYIPE 81
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDG---HPWTRKDLHKIGSLIE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 82 TPSLYEELTLREHIETVAMAYGieqkVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFL 161
Cdd:TIGR03740 78 SPPLYENLTARENLKVHTTLLG----LPDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 577038301 162 GLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNL---QQLREVF 223
Cdd:TIGR03740 154 GLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLGYQGKInksENLEKLF 218
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-221 |
3.81e-41 |
|
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: 140.50 E-value: 3.81e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGltlrEDATNY------RK 74
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDG----EDITGLpphriaRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 75 QIGYIPETPSLYEELTLREHIETVAMAYGIEQKVAFnRVEPLLKMF-----RLDQK---LdwfpvhfSKGMKQKVMIICA 146
Cdd:COG0410 79 GIGYVPEGRRIFPSLTVEENLLLGAYARRDRAEVRA-DLERVYELFprlkeRRRQRagtL-------SGGEQQMLAIGRA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 577038301 147 FVVDPSLFIVDEPFLGLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQQLRE 221
Cdd:COG0410 151 LMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-219 |
9.66e-41 |
|
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: 139.60 E-value: 9.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGltlrEDATNY------RKQ 75
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDG----QDITKLpmhkraRLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 76 IGYIPETPSLYEELTLREHIETVAMAYGIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFI 155
Cdd:cd03218 77 IGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 577038301 156 VDEPFLGLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQQL 219
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEI 220
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-219 |
4.30e-40 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 140.74 E-value: 4.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDATNYRKQIGYIPE 81
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 82 TPSLYEELTLREHIETVAMAYGIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFL 161
Cdd:PRK13536 122 FDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTT 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 577038301 162 GLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQQL 219
Cdd:PRK13536 202 GLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-226 |
4.97e-40 |
|
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: 138.25 E-value: 4.97e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKING-----LTLREDAtnyrKQ 75
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrdlasLSRRELA----RR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 76 IGYIPETPSLYEELTLRehiETVAM-------AYGIEQKVAFNRVEPLLKMFRLDQKLDWfPVH-FSKGMKQKVMIICAF 147
Cdd:COG1120 77 IAYVPQEPPAPFGLTVR---ELVALgryphlgLFGRPSAEDREAVEEALERTGLEHLADR-PVDeLSGGERQRVLIARAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 148 VVDPSLFIVDEPFLGLDP---LAIADLIQllEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQQ------ 218
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLahqLEVLELLR--RLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEvltpel 230
|
....*...
gi 577038301 219 LREVFDMP 226
Cdd:COG1120 231 LEEVYGVE 238
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-160 |
7.78e-40 |
|
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: 134.70 E-value: 7.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 17 LKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTL-REDATNYRKQIGYIPETPSLYEELTLREHI 95
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLtDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 577038301 96 ETVAMAYGIEQKVAFNRVEPLLKMFRL----DQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPF 160
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLgdlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
11-214 |
2.01e-39 |
|
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: 136.31 E-value: 2.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 11 YVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDATNYRKQIGYI-PETPSLYEEL 89
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVfGQKTQLWWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 90 TLREHIETVAMAYGIEQKVAFNRVEPLLKMFRLDQKLDwFPV-HFSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDPLAI 168
Cdd:cd03267 111 PVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLD-TPVrQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQ 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 577038301 169 ADLIQ-LLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQG 214
Cdd:cd03267 190 ENIRNfLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-209 |
3.79e-39 |
|
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: 133.14 E-value: 3.79e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 3 EIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTL-REDATNYRKQIGYIPE 81
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIaKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 82 tpslyeeltlrehietvamaygieqkvafnrvepllkmfrldqkldwfpvhFSKGMKQKVMIICAFVVDPSLFIVDEPFL 161
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 577038301 162 GLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGE 209
Cdd:cd00267 110 GLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-215 |
6.65e-39 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 134.77 E-value: 6.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGltlrEDATNY------RK 74
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDG----EDITHLpmhkraRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 75 QIGYIPETPSLYEELTLREHIETVAMAYGIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLF 154
Cdd:COG1137 79 GIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 577038301 155 IVDEPFLGLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGN 215
Cdd:COG1137 159 LLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGT 219
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-215 |
2.83e-38 |
|
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: 133.58 E-value: 2.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYVHV-PVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLRE-DATNYRKQIGYI 79
Cdd:cd03295 1 IEFENVTKRYGGGkKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREqDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 80 PETPSLYEELTLREHIETVAMAYGIEQKVAFNRVEPLLKMFRLDQK--LDWFPVHFSKGMKQKVMIICAFVVDPSLFIVD 157
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 577038301 158 EPFLGLDPLAIADLIQ-LLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGN 215
Cdd:cd03295 161 EPFGALDPITRDQLQEeFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGT 219
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-210 |
3.16e-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: 132.61 E-value: 3.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLT----GGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKING-----LTLREDATNY 72
Cdd:cd03255 1 IELKNLSktygGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGtdiskLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 73 RKQIGYIPETPSLYEELTLREHIETVAMAYGIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPS 152
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 577038301 153 LFIVDEPFLGLDPLAIADLIQLL-EVEKQKGKSILMSTHVLDSAEkMCDAFVILHKGEV 210
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLrELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-209 |
3.19e-38 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 131.16 E-value: 3.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDATNY---RKQIGY 78
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpplRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 79 IPETPSLYEELTLREhietvamaygieqkvafNRVEPLlkmfrldqkldwfpvhfSKGMKQKVMIICAFVVDPSLFIVDE 158
Cdd:cd03229 81 VFQDFALFPHLTVLE-----------------NIALGL-----------------SGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 577038301 159 PFLGLDPLAIADLIQLL-EVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGE 209
Cdd:cd03229 127 PTSALDPITRREVRALLkSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-221 |
3.73e-38 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 134.93 E-value: 3.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDATNYRKQIGYIPE 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 82 TPSLYEELTLREHIETVAMAYGIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFL 161
Cdd:PRK13537 88 FDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 162 GLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQQLRE 221
Cdd:PRK13537 168 GLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-220 |
1.03e-37 |
|
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: 131.86 E-value: 1.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTL----REDATNYRKQIG 77
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglsEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 78 YIPETPSLYEELTLREHIetvamAYGIEQKVAFN------RVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDP 151
Cdd:cd03261 81 MLFQSGALFDSLTVFENV-----AFPLREHTRLSeeeireIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 577038301 152 SLFIVDEPFLGLDPLA---IADLIQLLevEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQQLR 220
Cdd:cd03261 156 ELLLYDEPTAGLDPIAsgvIDDLIRSL--KKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELR 225
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-221 |
1.27e-37 |
|
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: 131.64 E-value: 1.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKING---LTLREDA-TNYRKQI 76
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqdiTGLSEKElYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 77 GYIPETPSLYEELT--------LREHietvamaYGIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFV 148
Cdd:COG1127 85 GMLFQGGALFDSLTvfenvafpLREH-------TDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 577038301 149 VDPSLFIVDEPFLGLDPL---AIADLIqlLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQQLRE 221
Cdd:COG1127 158 LDPEILLYDEPTAGLDPItsaVIDELI--RELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-227 |
1.98e-36 |
|
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: 128.47 E-value: 1.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLT----GGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKING---LTLREDA-TNY 72
Cdd:cd03258 1 MIELKNVSkvfgDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGtdlTLLSGKElRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 73 RKQIGYIPETPSLYEELTLREHIETVAMAYGIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPS 152
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 577038301 153 LFIVDEPFLGLDPLAIADLIQLL-EVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNlqqLREVFDMPE 227
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLrDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGT---VEEVFANPQ 233
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-214 |
4.62e-36 |
|
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: 126.87 E-value: 4.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGltlrEDATN---YRKQIGY 78
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDG----RDVTGvppERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 79 IPETPSLYEELTLREHIetvamAYGIE-----QKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSL 153
Cdd:cd03259 77 VFQDYALFPHLTVAENI-----AFGLKlrgvpKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 577038301 154 FIVDEPFLGLDPLAIADLIQLL-EVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQG 214
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELkELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-213 |
4.84e-36 |
|
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: 126.82 E-value: 4.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLT----GGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGltlrEDATNYRKQIG 77
Cdd:cd03293 1 LEVRNVSktygGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG----EPVTGPGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 78 YIPETPSLYEELTLREHIETVAMAYGIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVD 157
Cdd:cd03293 77 YVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 577038301 158 EPFLGLDPLAIADLIQ-LLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHK--GEVRAQ 213
Cdd:cd03293 157 EPFSALDALTREQLQEeLLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAE 215
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
11-223 |
8.08e-36 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 129.05 E-value: 8.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 11 YVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDATNYRKQIG-----------YI 79
Cdd:COG4586 32 YREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRIGvvfgqrsqlwwDL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 80 PetpsLYEELTLREHIetvamaYGIEQKVAFNRVEPLLKMFRLDQKLDwFPV-HFSKGMKQKVMIICAFVVDPSLFIVDE 158
Cdd:COG4586 112 P----AIDSFRLLKAI------YRIPDAEYKKRLDELVELLDLGELLD-TPVrQLSLGQRMRCELAAALLHRPKILFLDE 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 577038301 159 PFLGLDPLAIADLIQLL-EVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQQLREVF 223
Cdd:COG4586 181 PTIGLDVVSKEAIREFLkEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKERF 246
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-234 |
2.31e-34 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 123.24 E-value: 2.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYV-HVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTL----REDATNYRKQ 75
Cdd:COG3638 2 MLELRNLSKRYPgGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVtalrGRALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 76 IGYIPETPSLYEELTL-----------------------REHIETvAMAY----GIEQKvAFNRVEPLlkmfrldqkldw 128
Cdd:COG3638 82 IGMIFQQFNLVPRLSVltnvlagrlgrtstwrsllglfpPEDRER-ALEAlervGLADK-AYQRADQL------------ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 129 fpvhfSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDPLAIADLIQLL-EVEKQKGKSILMSTHVLDSAEKMCDAFVILHK 207
Cdd:COG3638 148 -----SGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLrRIAREDGITVVVNLHQVDLARRYADRIIGLRD 222
|
250 260 270
....*....|....*....|....*....|..
gi 577038301 208 GEVraqgnlqqlreVFDMP-----EASLNDIY 234
Cdd:COG3638 223 GRV-----------VFDGPpaeltDAVLREIY 243
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-212 |
3.28e-34 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 123.28 E-value: 3.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYVH----VPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGltlrEDATNYRKQI 76
Cdd:COG1116 7 ALELRGVSKRFPTggggVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG----KPVTGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 77 GYIPETPSLYEELTLREHIETVAMAYGIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIV 156
Cdd:COG1116 83 GVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLM 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 577038301 157 DEPFLGLDPLAIADL-IQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHK--GEVRA 212
Cdd:COG1116 163 DEPFGALDALTRERLqDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVE 221
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-214 |
9.40e-34 |
|
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: 119.85 E-value: 9.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 3 EIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLRE-DATNYRKQIGYIPE 81
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 82 tpslyeeltlrehietvAMAY-GIEQKvafnrvepllkmfrLDQKLDwfpvHFSKGMKQKVMIICAFVVDPSLFIVDEPF 160
Cdd:cd03214 81 -----------------ALELlGLAHL--------------ADRPFN----ELSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 577038301 161 LGLDP---LAIADLIQllEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQG 214
Cdd:cd03214 126 SHLDIahqIELLELLR--RLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-220 |
9.98e-34 |
|
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: 121.39 E-value: 9.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLT---GGyvhVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKING---LTLREDATNyRKQ 75
Cdd:cd03219 1 LEVRGLTkrfGG---LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGediTGLPPHEIA-RLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 76 IGYIPETPSLYEELTLREHIETVAMAYGI----------EQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIIC 145
Cdd:cd03219 77 IGRTFQIPRLFPELTVLENVMVAAQARTGsglllararrEEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIAR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 577038301 146 AFVVDPSLFIVDEPFLGLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQQLR 220
Cdd:cd03219 157 ALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVR 231
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
17-239 |
1.25e-33 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 122.17 E-value: 1.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 17 LKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTL----REDATNYRKQIGYI---PETpSLYEEl 89
Cdd:TIGR04521 21 LDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDItakkKKKLKDLRKKVGLVfqfPEH-QLFEE- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 90 TLREHIETVAMAYGIEQKVAFNRVEPLLKMFRLDQK-LDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDPLAI 168
Cdd:TIGR04521 99 TVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEEyLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGR 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 577038301 169 ADLIQLL-EVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNlqqLREVFDMPEAsLNDIYLALTK 239
Cdd:TIGR04521 179 KEILDLFkRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGT---PREVFSDVDE-LEKIGLDVPE 246
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-210 |
1.28e-33 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 120.93 E-value: 1.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYVH-VPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGL---TLREDATNY-RKQ 75
Cdd:COG2884 1 MIRFENVSKRYPGgREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQdlsRLKRREIPYlRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 76 IGYIPETPSLYEELTLREHIETVAMAYGIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFI 155
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 577038301 156 VDEPFLGLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEV 210
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-232 |
2.27e-33 |
|
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: 120.75 E-value: 2.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYVH-VPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDAT----NYRKQI 76
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGkalrQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 77 GYIPETPSLYEELTLREHIETVAMAYGIEQKVAFNRVEP--LLKMFRLDQKLDWFPVHF------SKGMKQKVMIICAFV 148
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRLGRRSTWRSLFGLFPKeeKQRALAALERVGLLDKAYqradqlSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 149 VDPSLFIVDEPFLGLDPLAIADLIQLL-EVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVraqgnlqqlreVFDMPE 227
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLkRINREEGITVIVSLHQVDLAREYADRIVGLKDGRI-----------VFDGPP 229
|
....*
gi 577038301 228 ASLND 232
Cdd:cd03256 230 AELTD 234
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-209 |
1.39e-32 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 116.33 E-value: 1.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGY--VHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLRE-DATNYRKQIGY 78
Cdd:cd03228 1 IEFKNVSFSYpgRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 79 IPETPSLYEElTLREHIetvamaygieqkvafnrvepllkmfrldqkldwfpvhFSKGMKQKVMIICAFVVDPSLFIVDE 158
Cdd:cd03228 81 VPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 577038301 159 PFLGLDPLAIADLIQLLEvEKQKGKSILMSTHVLdSAEKMCDAFVILHKGE 209
Cdd:cd03228 123 ATSALDPETEALILEALR-ALAKGKTVIVIAHRL-STIRDADRIIVLDDGR 171
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
15-221 |
3.04e-32 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 123.33 E-value: 3.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 15 PVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLRE-DATNYRKQIGYIPETP-----SLYEE 88
Cdd:COG4988 351 PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDlDPASWRRQIAWVPQNPylfagTIREN 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 89 LTL------REHIETVAMAYGIEQKVAfnrvepllkmfRLDQKLDwFPVH-----FSKGMKQKVMIICAFVVDPSLFIVD 157
Cdd:COG4988 431 LRLgrpdasDEELEAALEAAGLDEFVA-----------ALPDGLD-TPLGeggrgLSGGQAQRLALARALLRDAPLLLLD 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 577038301 158 EPFLGLDPLAIADLIQLLEvEKQKGKSILMSTHVLDSAEKMcDAFVILHKGEVRAQGNLQQLRE 221
Cdd:COG4988 499 EPTAHLDAETEAEILQALR-RLAKGRTVILITHRLALLAQA-DRILVLDDGRIVEQGTHEELLA 560
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
15-221 |
8.77e-32 |
|
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: 122.64 E-value: 8.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 15 PVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLRE-DATNYRKQIGYIPETP-----SLYEE 88
Cdd:COG2274 489 PVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQiDPASLRRQIGVVLQDVflfsgTIREN 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 89 LTL------REHIETVAMAYGIEQKVAfnrvepllkmfRLDQKLDwFPVH-----FSKGMKQKVMIICAFVVDPSLFIVD 157
Cdd:COG2274 569 ITLgdpdatDEEIIEAARLAGLHDFIE-----------ALPMGYD-TVVGeggsnLSGGQRQRLAIARALLRNPRILILD 636
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 577038301 158 EPFLGLDPLAIADLIQLLEvEKQKGKSILMSTHVLDSAeKMCDAFVILHKGEVRAQGNLQQLRE 221
Cdd:COG2274 637 EATSALDAETEAIILENLR-RLLKGRTVIIIAHRLSTI-RLADRIIVLDKGRIVEDGTHEELLA 698
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
15-210 |
2.91e-31 |
|
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: 113.80 E-value: 2.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 15 PVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTP--YSGEIKINGLTLREDatNYRKQIGYIPETPSLYEELTLR 92
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDKR--SFRKIIGYVPQDDILHPTLTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 93 EHIETVAMAYGIeqkvafnrvepllkmfrldqkldwfpvhfSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDPLAIADLI 172
Cdd:cd03213 101 ETLMFAAKLRGL-----------------------------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVM 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 577038301 173 QLLEVEKQKGKSILMSTH-VLDSAEKMCDAFVILHKGEV 210
Cdd:cd03213 152 SLLRRLADTGRTIICSIHqPSSEIFELFDKLLLLSQGRV 190
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-214 |
1.42e-30 |
|
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: 113.60 E-value: 1.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLT---GGyvhVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGltlrEDATN------ 71
Cdd:COG0411 4 LLEVRGLTkrfGG---LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDG----RDITGlpphri 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 72 YRKQIGYIPETPSLYEELTLREHIETVAMA---------------YGIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKG 136
Cdd:COG0411 77 ARLGIARTFQNPRLFPELTVLENVLVAAHArlgrgllaallrlprARREEREARERAEELLERVGLADRADEPAGNLSYG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 577038301 137 MKQKVMIICAFVVDPSLFIVDEPFLGLDPLAIADLIQLL-EVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQG 214
Cdd:COG0411 157 QQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIrRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEG 235
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
17-236 |
1.73e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 114.37 E-value: 1.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 17 LKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDATNY---RKQIGYIPETP--SLYEElTL 91
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLsdiRKKVGLVFQYPeyQLFEE-TI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 92 REHIETVAMAYGIEQKVAFNRVEPLLKMFRLDQK--LDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDPLAIA 169
Cdd:PRK13637 102 EKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEdyKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRD 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 577038301 170 DLI-QLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNlqqLREVFDMPEAsLNDIYLA 236
Cdd:PRK13637 182 EILnKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGT---PREVFKEVET-LESIGLA 245
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
10-242 |
3.19e-30 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 112.48 E-value: 3.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 10 GYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGltlredatnyrkqigyipETPSLYE-- 87
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG------------------RVSALLElg 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 88 -----ELTLREHIETVAMAYGieqkvaFNRVEPllkmfrlDQKLD---WF---------PV-HFSKGMKQKVMIICAFVV 149
Cdd:COG1134 97 agfhpELTGRENIYLNGRLLG------LSRKEI-------DEKFDeivEFaelgdfidqPVkTYSSGMRARLAFAVATAV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 150 DPSLFIVDEpflgldPLAIADL------IQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNlqqLREVF 223
Cdd:COG1134 164 DPDILLVDE------VLAVGDAafqkkcLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGD---PEEVI 234
|
250
....*....|....*....
gi 577038301 224 dmpeaslnDIYLALTKEEE 242
Cdd:COG1134 235 --------AAYEALLAGRE 245
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-210 |
9.18e-30 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 110.42 E-value: 9.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 3 EIKKLTGGYVHVP-VLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDATnyRKQIGYIPE 81
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKER--RKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 82 TP-------SLYEELTLRehietvAMAYGIEQkvafNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLF 154
Cdd:cd03226 79 DVdyqlftdSVREELLLG------LKELDAGN----EQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 577038301 155 IVDEPFLGLDPLA---IADLIqlLEVEKQkGKSILMSTHVLDSAEKMCDAFVILHKGEV 210
Cdd:cd03226 149 IFDEPTSGLDYKNmerVGELI--RELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-227 |
4.26e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 110.28 E-value: 4.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYV-HVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTL-REDATNYRKQIGY 78
Cdd:PRK13652 3 LIETRDLCYSYSgSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPItKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 79 IPETP--SLYEElTLREHIETVAMAYGIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIV 156
Cdd:PRK13652 83 VFQNPddQIFSP-TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 577038301 157 DEPFLGLDPLAIADLIQLL-EVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQqlrEVFDMPE 227
Cdd:PRK13652 162 DEPTAGLDPQGVKELIDFLnDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVE---EIFLQPD 230
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-210 |
4.93e-29 |
|
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: 108.65 E-value: 4.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYVH-VPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLT---LREDATNY-RKQI 76
Cdd:cd03292 1 IEFINVTKTYPNgTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDvsdLRGRAIPYlRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 77 GYIPETPSLYEELTLREHIETVAMAYGIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIV 156
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 577038301 157 DEPFLGLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEV 210
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
4-214 |
1.24e-28 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 108.00 E-value: 1.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 4 IKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGltlredatnyrkQIGYIPE-T 82
Cdd:cd03220 25 ILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------------RVSSLLGlG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 83 PSLYEELTLREHIETVAMAYGIEQKVAFNRVEPLLKMFRLDQKLDwFPV-HFSKGMKQKVMIICAFVVDPSLFIVDEpfl 161
Cdd:cd03220 93 GGFNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFID-LPVkTYSSGMKARLAFAIATALEPDILLIDE--- 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 577038301 162 gldPLAIADL------IQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQG 214
Cdd:cd03220 169 ---VLAVGDAafqekcQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
15-226 |
2.29e-28 |
|
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: 107.86 E-value: 2.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 15 PVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTP-YSGEIKINGLTL-REDATNYRKQIGYIpeTPSLYEELTLR 92
Cdd:COG1119 17 TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPtYGNDVRLFGERRgGEDVWELRKRIGLV--SPALQLRFPRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 93 EHIETVAM--AYGI---------EQKvafNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFL 161
Cdd:COG1119 95 ETVLDVVLsgFFDSiglyreptdEQR---ERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 577038301 162 GLDPLAIADLIQLLE-VEKQKGKSILMSTHvldSAEKMCDAF---VILHKGEVRAQGNLQQ------LREVFDMP 226
Cdd:COG1119 172 GLDLGARELLLALLDkLAAEGAPTLVLVTH---HVEEIPPGIthvLLLKDGRVVAAGPKEEvltsenLSEAFGLP 243
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-232 |
2.29e-28 |
|
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: 107.77 E-value: 2.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGY-VHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTL----REDATNYRKQ 75
Cdd:TIGR02315 1 MLEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDItklrGKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 76 IGYIPETPSLYEELTLREHIETVAMAYGIEQKVAFNRVEP--------LLKMFRLDQKLDWFPVHFSKGMKQKVMIICAF 147
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHGRLGYKPTWRSLLGRFSEedkeralsALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 148 VVDPSLFIVDEPFLGLDPLA---IADLiqLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVraqgnlqqlreVFD 224
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTskqVMDY--LKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEI-----------VFD 227
|
....*...
gi 577038301 225 MPEASLND 232
Cdd:TIGR02315 228 GAPSELDD 235
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-232 |
2.63e-28 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 107.67 E-value: 2.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKING-----LTLREDAtnyRKQI 76
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDedislLPLHARA---RRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 77 GYIPETPSLYEELTLREHIETV-AMAYGIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFI 155
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVlQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 577038301 156 VDEPFLGLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNlqqlrevfdmPEASLND 232
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGT----------PTEILQD 227
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
19-214 |
3.04e-28 |
|
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: 106.61 E-value: 3.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 19 DVSFTVeSGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDATN-----YRKQIGYIPETPSLYEELTLRE 93
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKinlppQQRKIGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 94 HIETVAMayGIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGLD-PLAIADLI 172
Cdd:cd03297 95 NLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDrALRLQLLP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 577038301 173 QLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQG 214
Cdd:cd03297 173 ELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-190 |
4.89e-28 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 105.80 E-value: 4.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDATNYRKQIGYIP 80
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 81 ETPSLYEELTLREH----IETVAMAYGIEQkvafnrvepLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIV 156
Cdd:PRK13540 81 HRSGINPYLTLRENclydIHFSPGAVGITE---------LCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLL 151
|
170 180 190
....*....|....*....|....*....|....
gi 577038301 157 DEPFLGLDPLAIADLIQLLEVEKQKGKSILMSTH 190
Cdd:PRK13540 152 DEPLVALDELSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-225 |
5.29e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 107.02 E-value: 5.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLRE-DATNYRKQIGYI 79
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMlSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 80 PETPSLYEELTLREHIetvamAYGIEQKVAF---------NRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVD 150
Cdd:PRK11231 82 PQHHLTPEGITVRELV-----AYGRSPWLSLwgrlsaednARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 151 PSLFIVDEPFLGLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQQ------LREVFD 224
Cdd:PRK11231 157 TPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEvmtpglLRTVFD 236
|
.
gi 577038301 225 M 225
Cdd:PRK11231 237 V 237
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-210 |
1.07e-27 |
|
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: 107.45 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLT------GGYVHVpvLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPY---SGEIKING---LTLRED 68
Cdd:COG0444 1 LLEVRNLKvyfptrRGVVKA--VDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGedlLKLSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 69 A-TNYR-KQIGYIPETP--SLYEELTLREHI-ETVAMAYGIEQKVAFNRVEPLLKMFRLDQK---LDWFPVHFSKGMKQK 140
Cdd:COG0444 79 ElRKIRgREIQMIFQDPmtSLNPVMTVGDQIaEPLRIHGGLSKAEARERAIELLERVGLPDPerrLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 577038301 141 VMIICAFVVDPSLFIVDEPFLGLDPLAIADLIQLL-EVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEV 210
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLkDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRI 229
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-214 |
2.17e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 105.84 E-value: 2.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYV--HVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDATNY-RKQIG 77
Cdd:PRK13632 7 MIKVENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEiRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 78 YIPETP-SLYEELTLREHIetvamAYGIEQKvAFNR------VEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVD 150
Cdd:PRK13632 87 IIFQNPdNQFIGATVEDDI-----AFGLENK-KVPPkkmkdiIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 577038301 151 PSLFIVDEPFLGLDPLAIADLIQLL-EVEKQKGKSILMSTHVLDSAEKmCDAFVILHKGEVRAQG 214
Cdd:PRK13632 161 PEIIIFDESTSMLDPKGKREIKKIMvDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQG 224
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
15-223 |
2.24e-27 |
|
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: 110.10 E-value: 2.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 15 PVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDATNYRKQIGYIPETPSLYEELTLREH 94
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 95 IETVAMAYGIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDPLAIADLIQL 174
Cdd:TIGR01257 1024 ILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDL 1103
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 577038301 175 LeVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQQLREVF 223
Cdd:TIGR01257 1104 L-LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCF 1151
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
15-198 |
2.76e-27 |
|
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: 109.30 E-value: 2.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 15 PVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLRE-DATNYRKQIGYIPETPSLYEElTLRE 93
Cdd:TIGR02857 336 PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADaDADSWRDQIAWVPQHPFLFAG-TIAE 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 94 HIE------TVAMAYGIEQKVAFNRVEPLLKMfRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDPLA 167
Cdd:TIGR02857 415 NIRlarpdaSDAEIREALERAGLDEFVAALPQ-GLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAET 493
|
170 180 190
....*....|....*....|....*....|.
gi 577038301 168 IADLIQLLEvEKQKGKSILMSTHVLDSAEKM 198
Cdd:TIGR02857 494 EAEVLEALR-ALAQGRTVLLVTHRLALAALA 523
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-210 |
3.13e-27 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 102.51 E-value: 3.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGltlredatnyrkqigyipe 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 82 tpslyEELTLREHIEtvAMAYGIEqkvafnrvepllkmfrldqkldwfPVH-FSKGMKQKVMIICAFVVDPSLFIVDEPF 160
Cdd:cd03216 62 -----KEVSFASPRD--ARRAGIA------------------------MVYqLSVGERQMVEIARALARNARLLILDEPT 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 577038301 161 LGLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEV 210
Cdd:cd03216 111 AALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
15-219 |
4.77e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 105.10 E-value: 4.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 15 PVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDAT-NYRKQIGYIPETP-SLYEELTLR 92
Cdd:PRK13635 21 YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVwDVRRQVGMVFQNPdNQFVGATVQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 93 ehiETVAMAY---GIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDPLAIA 169
Cdd:PRK13635 101 ---DDVAFGLeniGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRR 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 577038301 170 DLIQLL-EVEKQKGKSILMSTHVLDSAEKmCDAFVILHKGEVRAQGNLQQL 219
Cdd:PRK13635 178 EVLETVrQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEI 227
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-226 |
8.07e-27 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 103.57 E-value: 8.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGltlrEDATNY---RKQIGY 78
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGG----EDATDVpvqERNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 79 IPETPSLYEELTLREHIetvamAYGIEQKVAFNR---------VEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVV 149
Cdd:cd03296 79 VFQHYALFRHMTVFDNV-----AFGLRVKPRSERppeaeirakVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 577038301 150 DPSLFIVDEPFLGLDPLAIADLIQLL-EVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQqlrEVFDMP 226
Cdd:cd03296 154 EPKVLLLDEPFGALDAKVRKELRRWLrRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPD---EVYDHP 228
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-210 |
1.14e-26 |
|
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: 102.22 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTL---REDATNYRKQIGY 78
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtddKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 79 IPETPSLYEELTLREHIeTVAM--AYGIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIV 156
Cdd:cd03262 81 VFQQFNLFPHLTVLENI-TLAPikVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 577038301 157 DEPFLGLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEV 210
Cdd:cd03262 160 DEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-211 |
3.88e-26 |
|
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: 101.18 E-value: 3.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGltlrEDATN---YRKQIGY 78
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGG----RDVTDlppKDRDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 79 IPETPSLYEELTLREHietvaMAYGIEQ----KVAFN-RVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSL 153
Cdd:cd03301 77 VFQNYALYPHMTVYDN-----IAFGLKLrkvpKDEIDeRVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 577038301 154 FIVDEPFLGLDP-LAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVR 211
Cdd:cd03301 152 FLMDEPLSNLDAkLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-235 |
4.02e-26 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 101.37 E-value: 4.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYVHVPvlKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGltlrEDATNYRkqigyIP 80
Cdd:COG3840 1 MLRLDDLTYRYGDFP--LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNG----QDLTALP-----PA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 81 ETP--SLYEELTLREHIeTVA--MAYGI--------EQKvafNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFV 148
Cdd:COG3840 70 ERPvsMLFQENNLFPHL-TVAqnIGLGLrpglkltaEQR---AQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 149 VDPSLFIVDEPFLGLDPLAIADLIQLL-EVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQQLrevFDMPE 227
Cdd:COG3840 146 RKRPILLLDEPFSALDPALRQEMLDLVdELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAAL---LDGEP 222
|
....*...
gi 577038301 228 ASLNDIYL 235
Cdd:COG3840 223 PPALAAYL 230
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
17-223 |
5.94e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 102.23 E-value: 5.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 17 LKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTL---REDATNYRKQIGYIPETP-------SLY 86
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysRKGLMKLRESVGMVFQDPdnqlfsaSVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 87 EELTLRehietvAMAYGIEQKVAFNRVEPLLKMFRLDQkLDWFPVH-FSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDP 165
Cdd:PRK13636 102 QDVSFG------AVNLKLPEDEVRKRVDNALKRTGIEH-LKDKPTHcLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDP 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 577038301 166 LAIADLIQLL-EVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNlqqLREVF 223
Cdd:PRK13636 175 MGVSEIMKLLvEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGN---PKEVF 230
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
15-219 |
6.80e-26 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 105.25 E-value: 6.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 15 PVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLRE-DATNYRKQIGYIPETPSLYEElTLRE 93
Cdd:COG1132 354 PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDlTLESLRRQIGVVPQDTFLFSG-TIRE 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 94 HIetvamAYGIEQkVAFNRVEPLLKMFRLDQKLDWFP-----------VHFSKGMKQKVMIICAFVVDPSLFIVDEPFLG 162
Cdd:COG1132 433 NI-----RYGRPD-ATDEEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALLKDPPILILDEATSA 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 577038301 163 LDPLAIADLIQLLEvEKQKGKSILMSTHVLDSAeKMCDAFVILHKGEVRAQGNLQQL 219
Cdd:COG1132 507 LDTETEALIQEALE-RLMKGRTTIVIAHRLSTI-RNADRILVLDDGRIVEQGTHEEL 561
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-221 |
8.04e-26 |
|
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: 105.23 E-value: 8.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGY--VHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLRE-DATNYRKQIGY 78
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDlDEDDLRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 79 IPETPSLYEElTLREHI----------ETVAMAygieQKVafnRVEPLLKmfRLDQKLDWFP----VHFSKGMKQKVMII 144
Cdd:COG4987 414 VPQRPHLFDT-TLRENLrlarpdatdeELWAAL----ERV---GLGDWLA--ALPDGLDTWLgeggRRLSGGERRRLALA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 577038301 145 CAFVVDPSLFIVDEPFLGLDPLAIADLIQLLEvEKQKGKSILMSTHVLDSAEKMcDAFVILHKGEVRAQGNLQQLRE 221
Cdd:COG4987 484 RALLRDAPILLLDEPTEGLDAATEQALLADLL-EALAGRTVLLITHRLAGLERM-DRILVLEDGRIVEQGTHEELLA 558
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
3-210 |
1.60e-25 |
|
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: 100.80 E-value: 1.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 3 EIKKLTGGYVHVpvlKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTL----REDATNYR-KQIG 77
Cdd:cd03294 29 EILKKTGQTVGV---NDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIaamsRKELRELRrKKIS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 78 YIPETPSLYEELTLREHIetvamAYGIE-----QKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPS 152
Cdd:cd03294 106 MVFQSFALLPHRTVLENV-----AFGLEvqgvpRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPD 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 577038301 153 LFIVDEPFLGLDPLAIADL-IQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEV 210
Cdd:cd03294 181 ILLMDEAFSALDPLIRREMqDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
19-221 |
2.25e-25 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 104.05 E-value: 2.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 19 DVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLreDATNY--RKQIGYIPETPSLYEELTLREHIE 96
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV--DAGDIatRRRVGYMSQAFSLYGELTVRQNLE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 97 TVAMAYGIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDPLAIADLIQLL- 175
Cdd:NF033858 362 LHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLi 441
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 577038301 176 EVEKQKGKSILMSTHVLDSAEKmCDAFVILHKGEVRAQGNLQQLRE 221
Cdd:NF033858 442 ELSREDGVTIFISTHFMNEAER-CDRISLMHAGRVLASDTPAALVA 486
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-228 |
2.55e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 100.54 E-value: 2.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYVH-VPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDAT---NYRKQI 76
Cdd:PRK13639 1 ILETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKsllEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 77 GYIPETPSlyEEL---TLREHIETVAMAYGIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSL 153
Cdd:PRK13639 81 GIVFQNPD--DQLfapTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 577038301 154 FIVDEPFLGLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNlqqLREVFDMPEA 228
Cdd:PRK13639 159 IVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGT---PKEVFSDIET 230
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-230 |
2.95e-25 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 101.31 E-value: 2.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYVH----VPVLKDVSFTVESGQLVGLIGLNGAGKST---TINeiiGLLTPYSGEIKINGL---TLREDA- 69
Cdd:COG1135 1 MIELENLSKTFPTkggpVTALDDVSLTIEKGEIFGIIGYSGAGKSTlirCIN---LLERPTSGSVLVDGVdltALSEREl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 70 TNYRKQIGYIPETPSLYEELTLREHIetvamAY-----GIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMII 144
Cdd:COG1135 78 RAARRKIGMIFQHFNLLSSRTVAENV-----ALpleiaGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 145 CAFVVDPSLFIVDEPFLGLDP---LAIADLiqLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNlqqLRE 221
Cdd:COG1135 153 RALANNPKVLLCDEATSALDPettRSILDL--LKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGP---VLD 227
|
....*....
gi 577038301 222 VFDMPEASL 230
Cdd:COG1135 228 VFANPQSEL 236
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
15-210 |
3.06e-25 |
|
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: 97.67 E-value: 3.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 15 PVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLRE-DATNYRKQIGYIPETPSLYEElTLRE 93
Cdd:cd03246 16 PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwDPNELGDHVGYLPQDDELFSG-SIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 94 HIetvamaygieqkvafnrvepllkmfrldqkldwfpvhFSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDPL---AIAD 170
Cdd:cd03246 95 NI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEgerALNQ 137
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 577038301 171 LIQLLeveKQKGKSILMSTHVLdSAEKMCDAFVILHKGEV 210
Cdd:cd03246 138 AIAAL---KAAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
17-227 |
3.52e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 100.48 E-value: 3.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 17 LKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDATN-----YRKQIGYIPETP--SLYEEl 89
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNkklkpLRKKVGIVFQFPehQLFEE- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 90 TLREHIETVAMAYGIEQKVAFNRVEPLLKMFRLDQK-LDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDPLAI 168
Cdd:PRK13634 102 TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEElLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGR 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 169 ADLIQLL-EVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNlqqLREVFDMPE 227
Cdd:PRK13634 182 KEMMEMFyKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGT---PREIFADPD 238
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-200 |
4.69e-25 |
|
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: 98.66 E-value: 4.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLT--------GGyVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKING---------- 62
Cdd:COG4778 4 LLEVENLSktftlhlqGG-KRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHdggwvdlaqa 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 63 -----LTLRedatnyRKQIGY-------IPETPSLyeeltlrehiETVA---MAYGIEQKVAFNRVEPLLKMFRLDQKLd 127
Cdd:COG4778 83 spreiLALR------RRTIGYvsqflrvIPRVSAL----------DVVAeplLERGVDREEARARARELLARLNLPERL- 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 577038301 128 W--FPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCD 200
Cdd:COG4778 146 WdlPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVAD 220
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
16-195 |
6.52e-25 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 97.11 E-value: 6.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 16 VLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTL---REDATNYRKQIGYIPETPSlyEEL--- 89
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLdysRKGLLERRQRVGLVFQDPD--DQLfaa 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 90 TLREHIETVAMAYGIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDPLAIA 169
Cdd:TIGR01166 85 DVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGRE 164
|
170 180
....*....|....*....|....*.
gi 577038301 170 DLIQLLEVEKQKGKSILMSTHVLDSA 195
Cdd:TIGR01166 165 QMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-210 |
8.24e-25 |
|
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: 96.73 E-value: 8.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGyvhvPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKING--LTLREDATNYRKQIGY 78
Cdd:cd03215 4 VLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGkpVTRRSPRDAIRAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 79 IPETPSlyeeltlrehietvamAYGI--EQKVAFNRVepllkmfrldqkldwFPVHFSKGMKQKVMIICAFVVDPSLFIV 156
Cdd:cd03215 80 VPEDRK----------------REGLvlDLSVAENIA---------------LSSLLSGGNQQKVVLARWLARDPRVLIL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 577038301 157 DEPFLGLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEV 210
Cdd:cd03215 129 DEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-214 |
1.48e-24 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 100.30 E-value: 1.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLRE-DATNYRKQIGYI 79
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEAlSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 80 PETPSLYEELTLREHIE-------------TVAMAYGIEQkvAFNRVEpllkmfrLDQKLDWFPVHFSKGMKQKVMIICA 146
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVEmgrtphrsrfdtwTETDRAAVER--AMERTG-------VAQFADRPVTSLSGGERQRVLLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 577038301 147 FVVDPSLFIVDEPFLGLDplaIADLIQLLEVEK---QKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQG 214
Cdd:PRK09536 154 LAQATPVLLLDEPTASLD---INHQVRTLELVRrlvDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
14-226 |
1.77e-24 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 99.03 E-value: 1.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 14 VPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTP---YSGEIKING---LTLREDATN--YRKQIGYIPETP-- 83
Cdd:PRK09473 29 VTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGreiLNLPEKELNklRAEQISMIFQDPmt 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 84 SLYEELTLREHIETVAMAY-GIEQKVAFN---RVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEP 159
Cdd:PRK09473 109 SLNPYMRVGEQLMEVLMLHkGMSKAEAFEesvRMLDAVKMPEARKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEP 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 577038301 160 FLGLDPLAIADLIQLL-EVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGnlqQLREVFDMP 226
Cdd:PRK09473 189 TTALDVTVQAQIMTLLnELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG---NARDVFYQP 253
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
17-214 |
3.59e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 97.11 E-value: 3.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 17 LKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDATNY-RKQIGYIPETPSlyEELTLREHI 95
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvRSKVGLVFQDPD--DQVFSSTVW 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 96 ETVAMA---YGIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDPLAIADLI 172
Cdd:PRK13647 99 DDVAFGpvnMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLM 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 577038301 173 QLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQG 214
Cdd:PRK13647 179 EILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
2-214 |
3.87e-24 |
|
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: 95.64 E-value: 3.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYVHVPVlkDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLtlredatnyrkQIGYIP- 80
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGV-----------DVTAAPp 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 81 -ETP--SLYEELTLREHIEtvamaygIEQKVAFNRVePLLKMFRLDQK----------LDWF----PVHFSKGMKQKVMI 143
Cdd:cd03298 68 aDRPvsMLFQENNLFAHLT-------VEQNVGLGLS-PGLKLTAEDRQaievalarvgLAGLekrlPGELSGGERQRVAL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 577038301 144 ICAFVVDPSLFIVDEPFLGLDPLAIADLIQL-LEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQG 214
Cdd:cd03298 140 ARVLVRDKPVLLLDEPFAALDPALRAEMLDLvLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-226 |
4.72e-24 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 98.22 E-value: 4.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGltlrEDATN---YRKQIG 77
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGG----RDVTDlppKDRNIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 78 YIPETPSLYEELTLREHietvaMAYG----------IEQkvafnRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAF 147
Cdd:COG3839 79 MVFQSYALYPHMTVYEN-----IAFPlklrkvpkaeIDR-----RVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 148 VVDPSLFIVDEPFLGLDPL----AIADLIQLLeveKQKGKSILMSTHvlDSAEKM--CDAFVILHKGEVraqgnlQQL-- 219
Cdd:COG3839 149 VREPKVFLLDEPLSNLDAKlrveMRAEIKRLH---RRLGTTTIYVTH--DQVEAMtlADRIAVMNDGRI------QQVgt 217
|
....*...
gi 577038301 220 -REVFDMP 226
Cdd:COG3839 218 pEELYDRP 225
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-223 |
1.09e-23 |
|
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: 99.32 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGY--VHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDATNYRKQIGY 78
Cdd:TIGR01257 1937 ILRLNELTKVYsgTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGY 2016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 79 IPETPSLYEELTLREHIETVAMAYGIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDE 158
Cdd:TIGR01257 2017 CPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDE 2096
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 577038301 159 PFLGLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQQLREVF 223
Cdd:TIGR01257 2097 PTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKF 2161
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
5-198 |
1.72e-23 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 94.50 E-value: 1.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 5 KKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDATNYR-----KQIGYI 79
Cdd:PRK11629 13 KRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKaelrnQKLGFI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 80 PETPSLYEELTLrehIETVAMAY---GIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIV 156
Cdd:PRK11629 93 YQFHHLLPDFTA---LENVAMPLligKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 577038301 157 DEPFLGLDPLAIADLIQLL-EVEKQKGKSILMSTHVLDSAEKM 198
Cdd:PRK11629 170 DEPTGNLDARNADSIFQLLgELNRLQGTAFLVVTHDLQLAKRM 212
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-214 |
3.28e-23 |
|
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: 93.49 E-value: 3.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 16 VLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPY---SGEIKINGLTLREDATnyRKQIGYIPETPSLYEELTLR 92
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKPDQF--QKCVAYVRQDDILLPGLTVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 93 EHIETVAMAYGIEQKVAFNRVE----PLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDPLAI 168
Cdd:cd03234 100 ETLTYTAILRLPRKSSDAIRKKrvedVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 577038301 169 ADLIQLLEVEKQKGKSILMSTHVLDS-AEKMCDAFVILHKGEVRAQG 214
Cdd:cd03234 180 LNLVSTLSQLARRNRIVILTIHQPRSdLFRLFDRILLLSSGEIVYSG 226
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
14-214 |
3.29e-23 |
|
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: 93.42 E-value: 3.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 14 VPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLRE-DATNYRKQIGYIPETPSLYEElTLR 92
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQlDPADLRRNIGYVPQDVTLFYG-TLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 93 EHIeTVAMAYGIEQkvafnRVEPLLKMFRLDQKLDWFPVHF-----------SKGMKQKVMIICAFVVDPSLFIVDEPFL 161
Cdd:cd03245 96 DNI-TLGAPLADDE-----RILRAAELAGVTDFVNKHPNGLdlqigergrglSGGQRQAVALARALLNDPPILLLDEPTS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 577038301 162 GLDPLAIADLIQLLEvEKQKGKSILMSTHVLdSAEKMCDAFVILHKGEVRAQG 214
Cdd:cd03245 170 AMDMNSEERLKERLR-QLLGDKTLIIITHRP-SLLDLVDRIIVMDSGRIVADG 220
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-215 |
5.58e-23 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 93.54 E-value: 5.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTInEIIGLL-TPYSGEIKINGLTL-------REDATNYR 73
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLL-RVLNLLeTPDSGQLNIAGHQFdfsqkpsEKAIRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 74 KQIGYIPETPSLYEELTLREH-IETVAMAYGIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPS 152
Cdd:COG4161 82 QKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 577038301 153 LFIVDEPFLGLDP---LAIADLIQLLeveKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGN 215
Cdd:COG4161 162 VLLFDEPTAALDPeitAQVVEIIREL---SQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-210 |
9.55e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 95.86 E-value: 9.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLT---GGyvhVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKING--LTLRE--DATNYR 73
Cdd:COG3845 5 ALELRGITkrfGG---VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRSprDAIALG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 74 kqIGYIPETPSLYEELTLREHI----ETVAMAYgIEQKVAFNRVEPLLKMFRLDqkLDWF-PVH-FSKGMKQKVMIICAF 147
Cdd:COG3845 82 --IGMVHQHFMLVPNLTVAENIvlglEPTKGGR-LDRKAARARIRELSERYGLD--VDPDaKVEdLSVGEQQRVEILKAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 577038301 148 VVDPSLFIVDEPFLGLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEV 210
Cdd:COG3845 157 YRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
17-228 |
1.18e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 93.64 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 17 LKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTL-----REDATNYRKQIGYIPETP--SLYEEL 89
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVsstskQKEIKPVRKKVGVVFQFPesQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 90 TLREhIETVAMAYGIEQKVAFNRVEPLLKMFRLDQKL-DWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDPLAI 168
Cdd:PRK13643 102 VLKD-VAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKAR 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 169 ADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQQLREVFDMPEA 228
Cdd:PRK13643 181 IEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDFLKA 240
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-227 |
1.21e-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: 92.30 E-value: 1.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGltlrEDATN---YRKQIGY 78
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDG----KDITNlppHKRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 79 IPETPSLYEELTLREHIetvamAYGIE-----QKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSL 153
Cdd:cd03300 77 VFQNYALFPHLTVFENI-----AFGLRlkklpKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 577038301 154 FIVDEPFLGLD-PLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVraqgnlQQL---REVFDMPE 227
Cdd:cd03300 152 LLLDEPLGALDlKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKI------QQIgtpEEIYEEPA 223
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-219 |
1.22e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 93.26 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGY---VHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDAT-NYRKQI 76
Cdd:PRK13650 4 IIEVKNLTFKYkedQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVwDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 77 GYIPETP-SLYEELTLREHIETVAMAYGIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFI 155
Cdd:PRK13650 84 GMVFQNPdNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 577038301 156 VDEPFLGLDPLAIADLIQLL-EVEKQKGKSILMSTHVLDSAeKMCDAFVILHKGEVRAQGNLQQL 219
Cdd:PRK13650 164 LDEATSMLDPEGRLELIKTIkGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPREL 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-219 |
2.21e-22 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 95.14 E-value: 2.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLT----GGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLtPY-----SGEIKING---LTLRED 68
Cdd:COG4172 6 LLSVEDLSvafgQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLL-PDpaahpSGSILFDGqdlLGLSER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 69 ATN-YR-KQIGYI---PETpSLYEELTLREHI-ETVAMAYGIEQKVAFNRVEPLLKMFRLD---QKLDWFPVHFSKGMKQ 139
Cdd:COG4172 85 ELRrIRgNRIAMIfqePMT-SLNPLHTIGKQIaEVLRLHRGLSGAAARARALELLERVGIPdpeRRLDAYPHQLSGGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 140 KVMIICAFVVDPSLFIVDEPFLGLDPLAIADLIQLL-EVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQQ 218
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLkDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAE 243
|
.
gi 577038301 219 L 219
Cdd:COG4172 244 L 244
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
16-214 |
2.57e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 91.61 E-value: 2.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 16 VLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDATNYRKQI-------GYIPETPSLYEE 88
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDKAIrelrrnvGMVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 89 LTLREH-IETVAMAYGIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDPLA 167
Cdd:PRK11124 97 LTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 577038301 168 IADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQG 214
Cdd:PRK11124 177 TAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-219 |
2.97e-22 |
|
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: 91.09 E-value: 2.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKST---TINEIIGLL--TPYSGEIKING---LTLREDATNYR 73
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTllrLLNRLNDLIpgAPDEGEVLLDGkdiYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 74 KQIGYIPETPSLYeELTLREHIETVAMAYGI-EQKVAFNRVEPLLKMFRLDQKLD--WFPVHFSKGMKQKVMIICAFVVD 150
Cdd:cd03260 81 RRVGMVFQKPNPF-PGSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKdrLHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 577038301 151 PSLFIVDEPFLGLDPLAIADlIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQQL 219
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAK-IEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
14-227 |
5.10e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 91.79 E-value: 5.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 14 VPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGE---IKINGLTLREDAT-NYRKQIGYIPETP-SLYEE 88
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVwDIREKVGIVFQNPdNQFVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 89 LTLREHIetvamAYGIEqkvafNRVEPLLKMFRLDQK-------LDWF---PVHFSKGMKQKVMIICAFVVDPSLFIVDE 158
Cdd:PRK13640 100 ATVGDDV-----AFGLE-----NRAVPRPEMIKIVRDvladvgmLDYIdsePANLSGGQKQRVAIAGILAVEPKIIILDE 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 159 PFLGLDPLAIADLIQLL-EVEKQKGKSILMSTHVLDSAEkMCDAFVILHKGEVRAQGNlqqLREVFDMPE 227
Cdd:PRK13640 170 STSMLDPAGKEQILKLIrKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGS---PVEIFSKVE 235
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
14-225 |
5.21e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 94.40 E-value: 5.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 14 VPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLRE-DATNYRKQIGYIPETPSLYEElTLR 92
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQyDHHYLHRQVALVGQEPVLFSG-SVR 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 93 EHIetvamAYGIEQKvAFNRVEPLLKMFRLDQKLDWFP-----------VHFSKGMKQKVMIICAFVVDPSLFIVDEPFL 161
Cdd:TIGR00958 573 ENI-----AYGLTDT-PDEEIMAAAKAANAHDFIMEFPngydtevgekgSQLSGGQKQRIAIARALVRKPRVLILDEATS 646
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 577038301 162 GLDplaiADLIQLL-EVEKQKGKSILMSTHVLDSAEKmCDAFVILHKGEVRAQGNLQQLREVFDM 225
Cdd:TIGR00958 647 ALD----AECEQLLqESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQGC 706
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
17-226 |
5.64e-22 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 90.67 E-value: 5.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 17 LKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLtPYSGEIKINGLTLRE-DATNYRKQIGYIPE--TPSL----YEEL 89
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDwSAAELARHRAYLSQqqSPPFampvFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 90 TLreHIETVAMAYGIEQKVAFnrvepLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFV-VDPS------LFIVDEPFLG 162
Cdd:COG4138 91 AL--HQPAGASSEAVEQLLAQ-----LAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqVWPTinpegqLLLLDEPMNS 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 163 LDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQQ------LREVFDMP 226
Cdd:COG4138 164 LDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEvmtpenLSEVFGVK 233
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
15-221 |
1.41e-21 |
|
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: 89.21 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 15 PVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLRE-DATNYRKQIGYIPETPSLYEElTLRE 93
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLRSMIGVVLQDTFLFSG-TIME 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 94 HIetvamAYGI------EQKVAFNRVEPLLKMFRLDQKLDWFPVH----FSKGMKQKVMIICAFVVDPSLFIVDEPFLGL 163
Cdd:cd03254 96 NI-----RLGRpnatdeEVIEAAKEAGAHDFIMKLPNGYDTVLGEnggnLSQGERQLLAIARAMLRDPKILILDEATSNI 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 577038301 164 DP---LAIADLIQLLevekQKGKSILMSTHVLdSAEKMCDAFVILHKGEVRAQGNLQQLRE 221
Cdd:cd03254 171 DTeteKLIQEALEKL----MKGRTSIIIAHRL-STIKNADKILVLDDGKIIEEGTHDELLA 226
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-230 |
1.43e-21 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 91.40 E-value: 1.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLT----GGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKING---LTLREDA-TNY 72
Cdd:PRK11153 1 MIELKNISkvfpQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGqdlTALSEKElRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 73 RKQIGYIPETPSLyeeLTLREHIETVAMAY---GIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVV 149
Cdd:PRK11153 81 RRQIGMIFQHFNL---LSSRTVFDNVALPLelaGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALAS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 150 DPSLFIVDEPFLGLDPLAIADLIQLL-EVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQqlrEVFDMPEA 228
Cdd:PRK11153 158 NPKVLLCDEATSALDPATTRSILELLkDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVS---EVFSHPKH 234
|
..
gi 577038301 229 SL 230
Cdd:PRK11153 235 PL 236
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-214 |
1.46e-21 |
|
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: 88.14 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYVH--VPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDATNYRKQIGYI 79
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 80 PETPSLYEElTLREHIETvamaygieqkvafnrvepllkmfrldqkldwfpvHFSKGMKQKVMIICAFVVDPSLFIVDEP 159
Cdd:cd03247 81 NQRPYLFDT-TLRNNLGR----------------------------------RFSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 577038301 160 FLGLDPLAIADLIQLLeVEKQKGKSILMSTHVLDSAEKMcDAFVILHKGEVRAQG 214
Cdd:cd03247 126 TVGLDPITERQLLSLI-FEVLKDKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-219 |
1.65e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 92.60 E-value: 1.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGgyvhVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLtPYSGEIKINGLTLRE-DATNYRKQIGYIP 80
Cdd:PRK11174 355 LEILSPDG----KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRElDPESWRKHLSWVG 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 81 ETPSLYEElTLREHI---------ETVAMAygIEQKVAFNRVEpllkmfRLDQKLDwFPVH-----FSKGMKQKVMIICA 146
Cdd:PRK11174 430 QNPQLPHG-TLRDNVllgnpdasdEQLQQA--LENAWVSEFLP------LLPQGLD-TPIGdqaagLSVGQAQRLALARA 499
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 577038301 147 FVVDPSLFIVDEPFLGLDPLAIADLIQLLEVEKQkGKSILMSTHVLDSAEKMcDAFVILHKGEVRAQGNLQQL 219
Cdd:PRK11174 500 LLQPCQLLLLDEPTASLDAHSEQLVMQALNAASR-RQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAEL 570
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
15-214 |
1.70e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 90.19 E-value: 1.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 15 PVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDATN-----YRKQIGYIPETP--SLYE 87
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNkdikqIRKKVGLVFQFPesQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 88 ELTLREhietVAMA---YGIEQKVAFNRVEPLLKMFRLDQKL-DWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGL 163
Cdd:PRK13649 101 ETVLKD----VAFGpqnFGVSQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 577038301 164 DPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQG 214
Cdd:PRK13649 177 DPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSG 227
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
17-215 |
1.72e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 90.45 E-value: 1.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 17 LKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKIN------GLTLREDATNYRKQIGYIPETP--SLYEE 88
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGdyaipaNLKKIKEVKRLRKEIGLVFQFPeyQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 89 lTLREHIETVAMAYGIEQKVAFNRVEPLLKMFRLDQK-LDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDPLA 167
Cdd:PRK13645 107 -TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDyVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKG 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 577038301 168 IADLIQLLE-VEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGN 215
Cdd:PRK13645 186 EEDFINLFErLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-226 |
1.89e-21 |
|
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: 89.06 E-value: 1.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 17 LKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDA-------TNYrkqigyipetpSLYEEL 89
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGpdrmvvfQNY-----------SLLPWL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 90 TLREHIETVA------MAYGIEQKVafnrVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGL 163
Cdd:TIGR01184 70 TVRENIALAVdrvlpdLSKSERRAI----VEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 577038301 164 DPLAIADLI-QLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGevrAQGNLQQLREV-FDMP 226
Cdd:TIGR01184 146 DALTRGNLQeELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG---PAANIGQILEVpFPRP 207
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
13-215 |
2.66e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 90.15 E-value: 2.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 13 HVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEI-------KINGLTLRED----------------- 68
Cdd:PRK13651 19 ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeKNKKKTKEKEkvleklviqktrfkkik 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 69 -ATNYRKQIGYIPETP--SLYEElTLREHIETVAMAYGIEQKVAFNRVEPLLKMFRLDQK-LDWFPVHFSKGMKQKVMII 144
Cdd:PRK13651 99 kIKEIRRRVGVVFQFAeyQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESyLQRSPFELSGGQKRRVALA 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 577038301 145 CAFVVDPSLFIVDEPFLGLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGN 215
Cdd:PRK13651 178 GILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGD 248
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
17-210 |
3.38e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 89.50 E-value: 3.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 17 LKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDATN-----YRKQIGYI---PETpSLYEE 88
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNknlkkLRKKVSLVfqfPEA-QLFEN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 89 lTLREHIETVAMAYGIEQKVAFNRVEPLLKMFRLDQKL-DWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDPLA 167
Cdd:PRK13641 102 -TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLiSKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 577038301 168 IADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEV 210
Cdd:PRK13641 181 RKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-219 |
3.49e-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: 88.44 E-value: 3.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGY--VHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLRE-DATNYRKQIGY 78
Cdd:cd03251 1 VEFKNVTFRYpgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDyTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 79 IPETPSLYEElTLREHIetvamAYGIEQkVAFNRVEPLLKMFRLDQKLDWFP-----------VHFSKGMKQKVMIICAF 147
Cdd:cd03251 81 VSQDVFLFND-TVAENI-----AYGRPG-ATREEVEEAARAANAHEFIMELPegydtvigergVKLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 577038301 148 VVDPSLFIVDEPFLGLDpLAIADLIQLLEVEKQKGKSILMSTHVLdSAEKMCDAFVILHKGEVRAQGNLQQL 219
Cdd:cd03251 154 LKDPPILILDEATSALD-TESERLVQAALERLMKNRTTFVIAHRL-STIENADRIVVLEDGKIVERGTHEEL 223
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-219 |
4.31e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 88.10 E-value: 4.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYVHVPVLKDvsFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGltlrEDATNY---RKQIG 77
Cdd:PRK10771 1 MLKLTDITWLYHHLPMRFD--LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG----QDHTTTppsRRPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 78 YIPETPSLYEELTLREHIetvamAYGI--------EQKvafNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVV 149
Cdd:PRK10771 75 MLFQENNLFSHLTVAQNI-----GLGLnpglklnaAQR---EKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 577038301 150 DPSLFIVDEPFLGLDPLAIADLIQLL-EVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQQL 219
Cdd:PRK10771 147 EQPILLLDEPFSALDPALRQEMLTLVsQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-227 |
7.25e-21 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 89.76 E-value: 7.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKING-----LTLREdatnyrKQI 76
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGtdvsrLHARD------RKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 77 GYIPETPSLYEELTLREHIE---TV------AMAYGIEQKVAfnrvePLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAF 147
Cdd:PRK10851 77 GFVFQHYALFRHMTVFDNIAfglTVlprrerPNAAAIKAKVT-----QLLEMVQLAHLADRYPAQLSGGQKQRVALARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 148 VVDPSLFIVDEPFLGLDPLAIADLIQLLEV--EKQKGKSILMsTHVLDSAEKMCDAFVILhkgevrAQGNLQQL---REV 222
Cdd:PRK10851 152 AVEPQILLLDEPFGALDAQVRKELRRWLRQlhEELKFTSVFV-THDQEEAMEVADRVVVM------SQGNIEQAgtpDQV 224
|
....*
gi 577038301 223 FDMPE 227
Cdd:PRK10851 225 WREPA 229
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-228 |
7.64e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 88.53 E-value: 7.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTL---REDATNYRKQIG 77
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdysKRGLLALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 78 YI---PETPSLYEELTlrEHIETVAMAYGIEQKVAFNRVEPLLKMFRLdQKLDWFPVH-FSKGMKQKVMIICAFVVDPSL 153
Cdd:PRK13638 81 TVfqdPEQQIFYTDID--SDIAFSLRNLGVPEAEITRRVDEALTLVDA-QHFRHQPIQcLSHGQKKRVAIAGALVLQARY 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 577038301 154 FIVDEPFLGLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGnlqQLREVFDMPEA 228
Cdd:PRK13638 158 LLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHG---APGEVFACTEA 229
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-219 |
8.77e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 90.46 E-value: 8.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKING--LTLR--EDATnyRKQI 76
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRspRDAQ--AAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 77 GYIPETPSLYEELTLREHI---ETVAMAYGIEQKVAFNRVEPLLKMFRLDQKLDWfPV-HFSKGMKQKVMIICAFVVDPS 152
Cdd:COG1129 82 AIIHQELNLVPNLSVAENIflgREPRRGGLIDWRAMRRRARELLARLGLDIDPDT-PVgDLSVAQQQLVEIARALSRDAR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 577038301 153 LFIVDEPFLGLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQQL 219
Cdd:COG1129 161 VLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-219 |
1.07e-20 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 87.72 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLR--------------E 67
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadkN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 68 DATNYRKQIGYIPETPSLYEELTLREHI-ETVAMAYGIEQKVAFNRVEPLLKMFRLDQKL-DWFPVHFSKGMKQKVMIIC 145
Cdd:PRK10619 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 577038301 146 AFVVDPSLFIVDEPFLGLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQQL 219
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
17-237 |
1.17e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 87.88 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 17 LKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTL-REDATNYRKQIGYIPETPslyeELTLREHI 95
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAItDDNFEKLRKHIGIVFQNP----DNQFVGSI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 96 ETVAMAYGIE-QKVAFN----RVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDPLAIAD 170
Cdd:PRK13648 101 VKYDVAFGLEnHAVPYDemhrRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQN 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 577038301 171 LIQLL-EVEKQKGKSILMSTHVLDSAEKmCDAFVILHKGEVRAQGNLQqlrEVFDMPEaSLNDIYLAL 237
Cdd:PRK13648 181 LLDLVrKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPT---EIFDHAE-ELTRIGLDL 243
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
7-210 |
1.96e-20 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 87.05 E-value: 1.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 7 LTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTL-----------RED------- 68
Cdd:PRK10419 18 LSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLaklnraqrkafRRDiqmvfqd 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 69 ---ATNYRKQIGYIPETPslyeeltLReHIETVAMAygiEQKVafnRVEPLLKMFRLDQK-LDWFPVHFSKGMKQKVMII 144
Cdd:PRK10419 98 sisAVNPRKTVREIIREP-------LR-HLLSLDKA---ERLA---RASEMLRAVDLDDSvLDKRPPQLSGGQLQRVCLA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 577038301 145 CAFVVDPSLFIVDEPFLGLDPLAIADLIQLLE-VEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEV 210
Cdd:PRK10419 164 RALAVEPKLLILDEAVSNLDLVLQAGVIRLLKkLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-223 |
2.08e-20 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 89.48 E-value: 2.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGL--LTPYSGEI--------------------- 58
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 59 --KINGLTLREDATNY-----------RKQIG-YIPETPSLYEELTLREHIETVAMAYGIEQKVAFNRVEPLLKMFRLDQ 124
Cdd:TIGR03269 81 pcPVCGGTLEPEEVDFwnlsdklrrriRKRIAiMLQRTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 125 KLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDPLAiADLIQ--LLEVEKQKGKSILMSTHVLDSAEKMCDAF 202
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQT-AKLVHnaLEEAVKASGISMVLTSHWPEVIEDLSDKA 239
|
250 260
....*....|....*....|.
gi 577038301 203 VILHKGEVRAQGNLQQLREVF 223
Cdd:TIGR03269 240 IWLENGEIKEEGTPDEVVAVF 260
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
17-219 |
2.26e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 87.14 E-value: 2.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 17 LKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDATN-----YRKQIGYI---PETpSLYEE 88
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDkyirpVRKRIGMVfqfPES-QLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 89 LTLREhIETVAMAYGIEQKVAFNRVEPLLKMFRLDQK-LDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDPLA 167
Cdd:PRK13646 102 TVERE-IIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDvMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQS 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 577038301 168 IADLIQLL-EVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQQL 219
Cdd:PRK13646 181 KRQVMRLLkSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-212 |
2.60e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 88.92 E-value: 2.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGyvhvPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLR----EDATNYRkqI 76
Cdd:COG1129 256 VLEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRirspRDAIRAG--I 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 77 GYIPE---TPSLYEELTLREHI-----ETVAMAYGIEQKVAFNRVEPLLKMFR-----LDQkldwfPV-HFSKGMKQKVM 142
Cdd:COG1129 330 AYVPEdrkGEGLVLDLSIRENItlaslDRLSRGGLLDRRRERALAEEYIKRLRiktpsPEQ-----PVgNLSGGNQQKVV 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 143 IICAFVVDPSLFIVDEPFLGLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRA 212
Cdd:COG1129 405 LAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVG 474
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-219 |
2.72e-20 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 86.30 E-value: 2.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDATN---YRKQIG 77
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDerlIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 78 YIPETPSLYEELTLrehIETVAMA----YGIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSL 153
Cdd:PRK09493 81 MVFQQFYLFPHLTA---LENVMFGplrvRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 577038301 154 FIVDEPFLGLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQQL 219
Cdd:PRK09493 158 MLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVL 223
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
17-214 |
4.27e-20 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 86.48 E-value: 4.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 17 LKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDATnyRKQIGYIPET-------PSLYEEL 89
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQ--KNLVAYVPQSeevdwsfPVLVEDV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 90 TLRE---HIETVAMAYGIEQKV---AFNRVEPLLKMFRLDQKLdwfpvhfSKGMKQKVMIICAFVVDPSLFIVDEPFLGL 163
Cdd:PRK15056 101 VMMGrygHMGWLRRAKKRDRQIvtaALARVDMVEFRHRQIGEL-------SGGQKKRVFLARAIAQQGQVILLDEPFTGV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 577038301 164 DPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDaFVILHKGEVRAQG 214
Cdd:PRK15056 174 DVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASG 223
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
16-214 |
6.57e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 86.44 E-value: 6.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 16 VLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSG-----EIKINGLTLREDATNY------------RKQIGY 78
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGtiqvgDIYIGDKKNNHELITNpyskkiknfkelRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 79 IPETP--SLYEElTLREHIETVAMAYGIEQKVAFNRVEPLLKMFRLDQK-LDWFPVHFSKGMKQKVMIICAFVVDPSLFI 155
Cdd:PRK13631 121 VFQFPeyQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSyLERSPFGLSGGQKRRVAIAGILAIQPEILI 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 577038301 156 VDEPFLGLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQG 214
Cdd:PRK13631 200 FDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTG 258
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
14-233 |
8.24e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 87.86 E-value: 8.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 14 VPVLKDVSFTVESGQLVGLIGLNGAGKSTTINeIIGLL-TPYSGEIKING---LTLREDATNY--RKQIGYIPETPSLYE 87
Cdd:PRK10535 21 VEVLKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLdKPTSGTYRVAGqdvATLDADALAQlrREHFGFIFQRYHLLS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 88 ELTLREHIETVAMAYGIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDPLA 167
Cdd:PRK10535 100 HLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHS 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 577038301 168 IADLIQLLEVEKQKGKSILMSTH---VLDSAEKMCDafviLHKGEVRAQGNLQQLREVFDMPEASLNDI 233
Cdd:PRK10535 180 GEEVMAILHQLRDRGHTVIIVTHdpqVAAQAERVIE----IRDGEIVRNPPAQEKVNVAGGTEPVVNTA 244
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
2-190 |
8.53e-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: 84.08 E-value: 8.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDATNYRKQIGYIPE 81
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 82 TPSLYEELTLREHIETVAMAYGIEQkvafnrVEPLLKMFRLdQKLDWFPVH-FSKGMKQKVMIICAFVVDPSLFIVDEPF 160
Cdd:cd03231 81 APGIKTTLSVLENLRFWHADHSDEQ------VEEALARVGL-NGFEDRPVAqLSAGQQRRVALARLLLSGRPLWILDEPT 153
|
170 180 190
....*....|....*....|....*....|
gi 577038301 161 LGLDPLAIADLIQLLEVEKQKGKSILMSTH 190
Cdd:cd03231 154 TALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
5-210 |
1.09e-19 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 84.41 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 5 KKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKING--LT-LRED--ATNYRKQIGYI 79
Cdd:COG4181 16 KTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGqdLFaLDEDarARLRARHVGFV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 80 PETPSLYEELTLrehIETVAMAygIE---QKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIV 156
Cdd:COG4181 96 FQSFQLLPTLTA---LENVMLP--LElagRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 577038301 157 DEPFLGLDP---LAIADLiqLLEVEKQKGKSILMSTHVLDSAEKmCDAFVILHKGEV 210
Cdd:COG4181 171 DEPTGNLDAatgEQIIDL--LFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRL 224
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-210 |
1.22e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 84.55 E-value: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKING--LTLREDATNYRKQIGY 78
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGkdITDWQTAKIMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 79 IPETPSLYEELTLREHIetvAM-AYGIEQKVAFNRVEPLLKMF-RLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIV 156
Cdd:PRK11614 85 VPEGRRVFSRMTVEENL---AMgGFFAERDQFQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 577038301 157 DEPFLGLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEV 210
Cdd:PRK11614 162 DEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-221 |
1.96e-19 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 86.04 E-value: 1.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLrEDATNYRKQIGYIP 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL-SHVPPYQRPINMMF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 81 ETPSLYEELTLREHIetvamAYGIEQ-KVA----FNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFI 155
Cdd:PRK11607 98 QSYALFPHMTVEQNI-----AFGLKQdKLPkaeiASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 577038301 156 VDEPFLGLDPlAIADLIQL--LEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQQLRE 221
Cdd:PRK11607 173 LDEPMGALDK-KLRDRMQLevVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE 239
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-210 |
2.20e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 84.37 E-value: 2.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGY---VHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLR-EDATNYRKQI 76
Cdd:PRK13642 4 ILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTaENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 77 GYIPETP-SLYEELTLREHIETVAMAYGIEQKVAFNRV-EPLLKMFRLDQKLDWfPVHFSKGMKQKVMIICAFVVDPSLF 154
Cdd:PRK13642 84 GMVFQNPdNQFVGATVEDDVAFGMENQGIPREEMIKRVdEALLAVNMLDFKTRE-PARLSGGQKQRVAVAGIIALRPEII 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 577038301 155 IVDEPFLGLDPLAIADLIQLL-EVEKQKGKSILMSTHVLDSAEKmCDAFVILHKGEV 210
Cdd:PRK13642 163 ILDESTSMLDPTGRQEIMRVIhEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEI 218
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
15-223 |
2.56e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 84.37 E-value: 2.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 15 PVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGL--TLREDATNYRKQIGYIPETPSLYEELTLR 92
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLdtSDEENLWDIRNKAGMVFQNPDNQIVATIV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 93 EhiETVAMA---YGIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDPLAIA 169
Cdd:PRK13633 104 E--EDVAFGpenLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRR 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 577038301 170 DLIQLL-EVEKQKGKSILMSTHVLDSAEKmCDAFVILHKGEVRAQGNlqqLREVF 223
Cdd:PRK13633 182 EVVNTIkELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGT---PKEIF 232
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-219 |
2.57e-19 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 83.65 E-value: 2.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLreDAT---------- 70
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITI--DTArslsqqkgli 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 71 -NYRKQIGYIPETPSLYEELTLREH-IETVAMAYGIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFV 148
Cdd:PRK11264 81 rQLRQHVGFVFQNFNLFPHRTVLENiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 577038301 149 VDPSLFIVDEPFLGLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQQL 219
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
17-241 |
2.89e-19 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 86.33 E-value: 2.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 17 LKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDAtnYRKQ----IGYIPET--PSLYEELT 90
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADAR--HRRAvcprIAYMPQGlgKNLYPTLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 91 LREHIETVAMAYGIEQKVAFNRVEPLLKMFRLD-------QKLdwfpvhfSKGMKQKVMIICAFVVDPSLFIVDEPFLGL 163
Cdd:NF033858 95 VFENLDFFGRLFGQDAAERRRRIDELLRATGLApfadrpaGKL-------SGGMKQKLGLCCALIHDPDLLILDEPTTGV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 164 DPLAIA---DLIQLLEVEkQKGKSILMSTHVLDSAEKmCDAFVILHKGEVRAQGNLQQLREvfDMPEASLNDIYLALTKE 240
Cdd:NF033858 168 DPLSRRqfwELIDRIRAE-RPGMSVLVATAYMEEAER-FDWLVAMDAGRVLATGTPAELLA--RTGADTLEAAFIALLPE 243
|
.
gi 577038301 241 E 241
Cdd:NF033858 244 E 244
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-219 |
3.31e-19 |
|
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: 83.05 E-value: 3.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYV-HVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLRE-DATNYRKQIGYI 79
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 80 PETPSLYEElTLREHIetvamAYGiEQKVAFNRVEPLLKMFRLDQKLDWFP-----------VHFSKGMKQKVMIICAFV 148
Cdd:cd03253 81 PQDTVLFND-TIGYNI-----RYG-RPDATDEEVIEAAKAAQIHDKIMRFPdgydtivgergLKLSGGEKQRVAIARAIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 577038301 149 VDPSLFIVDEPFLGLDPLAIADLIQLLEvEKQKGKSILMSTHVLdSAEKMCDAFVILHKGEVRAQGNLQQL 219
Cdd:cd03253 154 KNPPILLLDEATSALDTHTEREIQAALR-DVSKGRTTIVIAHRL-STIVNADKIIVLKDGRIVERGTHEEL 222
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
13-219 |
5.29e-19 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 82.59 E-value: 5.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 13 HVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDATN-YRKQIGYIPETPSLYeELTL 91
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRwLRSQIGLVSQEPVLF-DGTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 92 REHIetvamAYGIEQKVAfNRVEPLLKMFRLDQKLDWFPVHF-----------SKGMKQKVMIICAFVVDPSLFIVDEPF 160
Cdd:cd03249 94 AENI-----RYGKPDATD-EEVEEAAKKANIHDFIMSLPDGYdtlvgergsqlSGGQKQRIAIARALLRNPKILLLDEAT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 577038301 161 LGLDplaiadliqlLEVEKQ---------KGKSILMSTHVLdSAEKMCDAFVILHKGEVRAQGNLQQL 219
Cdd:cd03249 168 SALD----------AESEKLvqealdramKGRTTIVIAHRL-STIRNADLIAVLQNGQVVEQGTHDEL 224
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-220 |
6.07e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 85.10 E-value: 6.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDATNYRKQIG-Y- 78
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGiYl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 79 IPETPSLYEELTLREHIetvamAYGIEQK-VAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVD 157
Cdd:PRK15439 91 VPQEPLLFPNLSVKENI-----LFGLPKRqASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 577038301 158 EPFLGLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQQLR 220
Cdd:PRK15439 166 EPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLS 228
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-233 |
1.30e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 81.98 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLT----PYSgEIKINGLT------LREDAT 70
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksAGS-HIELLGRTvqregrLARDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 71 NYRKQIGYIPETPSLYEELTLREHIETVAMAYGIEQKVAFNRVEPLLKMFRLDQKLDWFPVHF--------SKGMKQKVM 142
Cdd:PRK09984 83 KSRANTGYIFQQFNLVNRLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQALTRVGMVHFahqrvstlSGGQQQRVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 143 IICAFVVDPSLFIVDEPFLGLDPLAIADLIQLL-EVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQQL-R 220
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLrDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFdN 242
|
250
....*....|...
gi 577038301 221 EVFDMPEASLNDI 233
Cdd:PRK09984 243 ERFDHLYRSINRV 255
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-217 |
1.97e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 81.28 E-value: 1.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLrEDATNYRkqiGYIP 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV-EGPGAER---GVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 81 ETPSLyeeLTLREHIETVAMAY---GIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVD 157
Cdd:PRK11248 77 QNEGL---LPWRNVQDNVAFGLqlaGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 577038301 158 EPFLGLDPLAiADLIQ--LLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQ 217
Cdd:PRK11248 154 EPFGALDAFT-REQMQtlLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPGPGRVVERLP 214
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-215 |
2.92e-18 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 81.37 E-value: 2.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGY---------VHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDATN 71
Cdd:PRK15112 4 LLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 72 YRKQ-IGYIPETPSlyEELTLREHIETV-----AMAYGIEQKVAFNRVEPLLKMFRL-DQKLDWFPVHFSKGMKQKVMII 144
Cdd:PRK15112 84 YRSQrIRMIFQDPS--TSLNPRQRISQIldfplRLNTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 577038301 145 CAFVVDPSLFIVDEPFLGLDPLAIADLIQL-LEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGN 215
Cdd:PRK15112 162 RALILRPKVIIADEALASLDMSMRSQLINLmLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGS 233
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
17-224 |
4.25e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 82.79 E-value: 4.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 17 LKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTP---YSGEIKINGLtlREDATNYRKQIGYIPETPSLYEELTLRE 93
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGM--PIDAKEMRAISAYVQQDDLFIPTLTVRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 94 HIETVA---MAYGIEQKVAFNRVEPLLKMFRL----DQKLDWFPVH--FSKGMKQKVMIICAFVVDPSLFIVDEPFLGLD 164
Cdd:TIGR00955 119 HLMFQAhlrMPRRVTKKEKRERVDEVLQALGLrkcaNTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 577038301 165 PLAIADLIQLLEVEKQKGKSILMSTHvLDSAEKMC--DAFVILHKGEVRAQGNLQQLREVFD 224
Cdd:TIGR00955 199 SFMAYSVVQVLKGLAQKGKTIICTIH-QPSSELFElfDKIILMAEGRVAYLGSPDQAVPFFS 259
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
17-210 |
5.67e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 82.00 E-value: 5.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 17 LKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLRE--DA---TNYRKQIGYIPETPSLYEELTL 91
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKisDAelrEVRRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 92 REHietvaMAYGIEQK--VAFNRVEPLLKMFR---LDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDPL 166
Cdd:PRK10070 124 LDN-----TAFGMELAgiNAEERREKALDALRqvgLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 577038301 167 AIADLI-QLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEV 210
Cdd:PRK10070 199 IRTEMQdELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
4-238 |
7.36e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 82.06 E-value: 7.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 4 IKKLTGGYVHVpvLKDVSFTVESGQLVGLIGLNGAGKSTTineiiGL----LTPYSGEIKINGLTL----REDATNYRKQ 75
Cdd:PRK15134 291 ILKRTVDHNVV--VKNISFTLRPGETLGLVGESGSGKSTT-----GLallrLINSQGEIWFDGQPLhnlnRRQLLPVRHR 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 76 IGYIPETP--SLYEELT--------LREHIETVAMAygiEQKvafNRVEPLLKMFRLDQKLDW-FPVHFSKGMKQKVMII 144
Cdd:PRK15134 364 IQVVFQDPnsSLNPRLNvlqiieegLRVHQPTLSAA---QRE---QQVIAVMEEVGLDPETRHrYPAEFSGGQRQRIAIA 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 145 CAFVVDPSLFIVDEPFLGLDPLAIADLIQLLEVEKQKGK-SILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQQlreVF 223
Cdd:PRK15134 438 RALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQlAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCER---VF 514
|
250
....*....|....*
gi 577038301 224 DMPEASLNDIYLALT 238
Cdd:PRK15134 515 AAPQQEYTRQLLALS 529
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2-210 |
1.02e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 81.64 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTG-GYvhvpvlKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDATNYRKQIG--Y 78
Cdd:PRK15439 269 LTVEDLTGeGF------RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGlvY 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 79 IPE---TPSLYEELTLREHIETVA---MAYGIEQKVAFNRVEPL-----LKMFRLDQkldwfPVH-FSKGMKQKVMIICA 146
Cdd:PRK15439 343 LPEdrqSSGLYLDAPLAWNVCALThnrRGFWIKPARENAVLERYrralnIKFNHAEQ-----AARtLSGGNQQKVLIAKC 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 577038301 147 FVVDPSLFIVDEPFLGLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEV 210
Cdd:PRK15439 418 LEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-219 |
1.46e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 81.29 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYVHV----PVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLL-TP---Y-SGEIKINGLT-LREDAT 70
Cdd:PRK15134 5 LLAIENLSVAFRQQqtvrTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLpSPpvvYpSGDIRFHGESlLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 71 NYRK----QIGYIPETP--SLYEELTLREHI-ETVAMAYGIEQKVAfnRVEPLLKMFRLD-----QKLDWFPVHFSKGMK 138
Cdd:PRK15134 85 TLRGvrgnKIAMIFQEPmvSLNPLHTLEKQLyEVLSLHRGMRREAA--RGEILNCLDRVGirqaaKRLTDYPHQLSGGER 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 139 QKVMIICAFVVDPSLFIVDEPFLGLDPLAIADLIQLL-EVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQ 217
Cdd:PRK15134 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLrELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAA 242
|
..
gi 577038301 218 QL 219
Cdd:PRK15134 243 TL 244
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-219 |
1.49e-17 |
|
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: 78.68 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 16 VLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLRE-DATNYRKQIGYIPETPSLYEElTLREH 94
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALaDPAWLRRQVGVVLQENVLFNR-SIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 95 IETVAMAYGIEQKVAFNRV----EPLLKMFR-LDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDPLAIA 169
Cdd:cd03252 96 IALADPGMSMERVIEAAKLagahDFISELPEgYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEH 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 577038301 170 DLIQLLEvEKQKGKSILMSTHVLdSAEKMCDAFVILHKGEVRAQGNLQQL 219
Cdd:cd03252 176 AIMRNMH-DICAGRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
34-218 |
1.75e-17 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 80.30 E-value: 1.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 34 GLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDATN-----YRKQIGYIPETPSLYEELTLREHIEtvamaYGIEQKV 108
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGiclppEKRRIGYVFQDARLFPHYKVRGNLR-----YGMAKSM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 109 A--FNRVEPLLKMFRLdqkLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDPLAIADLIQLLEVEKQKGK-SI 185
Cdd:PRK11144 106 VaqFDKIVALLGIEPL---LDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINiPI 182
|
170 180 190
....*....|....*....|....*....|...
gi 577038301 186 LMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQQ 218
Cdd:PRK11144 183 LYVSHSLDEILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
17-241 |
1.82e-17 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 81.09 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 17 LKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGltlredatnyrkQIGYIPETPSLYEELTLREHIE 96
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG------------SAALIAISSGLNGQLTGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 97 TVAMAYGIEQKvAFNRVEPLLKMFRLDQKLDWFPVH-FSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDPLAIADLIQLL 175
Cdd:PRK13545 108 LKGLMMGLTKE-KIKEIIPEIIEFADIGKFIYQPVKtYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKM 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 577038301 176 EVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNlqqLREVFDMPEASLNDiYLALTKEE 241
Cdd:PRK13545 187 NEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGD---IKEVVDHYDEFLKK-YNQMSVEE 248
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-190 |
3.31e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 77.22 E-value: 3.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLT---GGyvhVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGltlrEDAT--NYRKQ 75
Cdd:PRK13539 2 MLEGEDLAcvrGG---RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG----GDIDdpDVAEA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 76 IGYIPETPSLYEELTLREHIETVAMAYGIEQKvafnRVEPLLKMFRLDQKLDwfpVHF---SKGMKQKVMIICAFVVDPS 152
Cdd:PRK13539 75 CHYLGHRNAMKPALTVAENLEFWAAFLGGEEL----DIAAALEAVGLAPLAH---LPFgylSAGQKRRVALARLLVSNRP 147
|
170 180 190
....*....|....*....|....*....|....*...
gi 577038301 153 LFIVDEPFLGLDPLAIADLIQLLEVEKQKGKSILMSTH 190
Cdd:PRK13539 148 IWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-226 |
4.18e-17 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 79.22 E-value: 4.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGltlrEDATNY---RKQIGY 78
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDG----QDITHVpaeNRHVNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 79 IPETPSLYEELTLREHIetvamAYGIE-QKVAFN----RVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSL 153
Cdd:PRK09452 91 VFQSYALFPHMTVFENV-----AFGLRmQKTPAAeitpRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 577038301 154 FIVDEPFLGLD-PLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNlqqLREVFDMP 226
Cdd:PRK09452 166 LLLDESLSALDyKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT---PREIYEEP 236
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
15-215 |
4.78e-17 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 77.15 E-value: 4.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 15 PVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLRE-DATNYRKQIGYIPETPSLYEElTLRE 93
Cdd:cd03244 18 PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiGLHDLRSRISIIPQDPVLFSG-TIRS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 94 HIE-----TVAMAYGIEQKVAF-NRVEPLLKMfrLDQKLDWFPVHFSKGMKQkvmIIC---AFVVDPSLFIVDEPFLGLD 164
Cdd:cd03244 97 NLDpfgeySDEELWQALERVGLkEFVESLPGG--LDTVVEEGGENLSVGQRQ---LLClarALLRKSKILVLDEATASVD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 577038301 165 PlAIADLIQLLEVEKQKGKSILMSTH----VLDsaekmCDAFVILHKGEVRAQGN 215
Cdd:cd03244 172 P-ETDALIQKTIREAFKDCTVLTIAHrldtIID-----SDRILVLDKGRVVEFDS 220
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-190 |
5.72e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 76.38 E-value: 5.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLT---GGYVhvpVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDATNYRKQIG 77
Cdd:PRK13538 1 MLEARNLAcerDERI---LFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 78 YIPETPSLYEELTLREHietVAMAYGIEQKVAFNRVEPLLKMFRLDQKLDwFPVH-FSKGMKQKVMIICAFVVDPSLFIV 156
Cdd:PRK13538 78 YLGHQPGIKTELTALEN---LRFYQRLHGPGDDEALWEALAQVGLAGFED-VPVRqLSAGQQRRVALARLWLTRAPLWIL 153
|
170 180 190
....*....|....*....|....*....|....
gi 577038301 157 DEPFLGLDPLAIADLIQLLEVEKQKGKSILMSTH 190
Cdd:PRK13538 154 DEPFTAIDKQGVARLEALLAQHAEQGGMVILTTH 187
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
14-219 |
6.82e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 79.51 E-value: 6.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 14 VPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLR---EDATNYRKQ------------IGY 78
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRrrsRQVIELSEQsaaqmrhvrgadMAM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 79 IPETP--SLYEELTLREHI-ETVAMAYGIEQKVAFNRVEPLLKMFRLDQK---LDWFPVHFSKGMKQKVMIICAFVVDPS 152
Cdd:PRK10261 109 IFQEPmtSLNPVFTVGEQIaESIRLHQGASREEAMVEAKRMLDQVRIPEAqtiLSRYPHQLSGGMRQRVMIAMALSCRPA 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 577038301 153 LFIVDEPFLGLDPLAIADLIQLLEV-EKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQQL 219
Cdd:PRK10261 189 VLIADEPTTALDVTIQAQILQLIKVlQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-235 |
8.45e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 77.01 E-value: 8.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 16 VLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTL-------REDATNYRKQIGYIPETPSLYEE 88
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgkdifQIDAIKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 89 LTLREHIETVAMAYGIEQKVAFNRV--EPLLKM---FRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGL 163
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIKEKREIKKIveECLRKVglwKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 577038301 164 DPLAIADLIQLLeVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQqlrEVFDMPEASLNDIYL 235
Cdd:PRK14246 185 DIVNSQAIEKLI-TELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSN---EIFTSPKNELTEKYV 252
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
15-221 |
9.50e-17 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 77.11 E-value: 9.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 15 PVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTL----REDATNYRKQIGYIPETPSLYEELT 90
Cdd:PRK11831 21 CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsRSRLYTVRKRMSMLFQSGALFTDMN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 91 --------LREHIetvamaygieqkvafNRVEPLLK---MFRLDQ-----KLDWFPVHFSKGMKQKVMIICAFVVDPSLF 154
Cdd:PRK11831 101 vfdnvaypLREHT---------------QLPAPLLHstvMMKLEAvglrgAAKLMPSELSGGMARRAALARAIALEPDLI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 577038301 155 IVDEPFLGLDPLAIADLIQLL-EVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQQLRE 221
Cdd:PRK11831 166 MFDEPFVGQDPITMGVLVKLIsELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQA 233
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-159 |
1.25e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.57 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 4 IKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGltlredatnyRKQIGYIPETP 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK----------GLRIGYLPQEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 84 SLYEELTLrehIETVAMAYG-----------IEQKVAFNRVEpLLKMFRLDQKLD----W--------------FPV--- 131
Cdd:COG0488 71 PLDDDLTV---LDTVLDGDAelraleaeleeLEAKLAEPDED-LERLAELQEEFEalggWeaearaeeilsglgFPEedl 146
|
170 180 190
....*....|....*....|....*....|...
gi 577038301 132 -----HFSKGMKQKVMIICAFVVDPSLFIVDEP 159
Cdd:COG0488 147 drpvsELSGGWRRRVALARALLSEPDLLLLDEP 179
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
20-226 |
1.42e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 77.47 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 20 VSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTpYSGEI-----KINGLTLREDATNYRKQI-----GYIPETP--SLYE 87
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLID-YPGRVmaeklEFNGQDLQRISEKERRNLvgaevAMIFQDPmtSLNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 88 ELTLREHI-ETVAMAYGIEQKVAFNRVEPLLKMFRL---DQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGL 163
Cdd:PRK11022 105 CYTVGFQImEAIKVHQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTAL 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 577038301 164 DPLAIADLIQLL-EVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGnlqQLREVFDMP 226
Cdd:PRK11022 185 DVTIQAQIIELLlELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETG---KAHDIFRAP 245
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-219 |
1.57e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 78.33 E-value: 1.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYV--HVPVLKDVSFTVESGQLVGLIGLNGAGKSTtineIIGLLT----PYSGEIKINGLTLRE-DATNYRK 74
Cdd:PRK11160 339 LTLNNVSFTYPdqPQPVLKGLSLQIKAGEKVALLGRTGCGKST----LLQLLTrawdPQQGEILLNGQPIADySEAALRQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 75 QIGYIPETPSLYEElTLREHIETVAMAYGIEQ-KVAFNRVEpLLKMFRLDQKLD-WF-----PVhfSKGMKQKVMIICAF 147
Cdd:PRK11160 415 AISVVSQRVHLFSA-TLRDNLLLAAPNASDEAlIEVLQQVG-LEKLLEDDKGLNaWLgeggrQL--SGGEQRRLGIARAL 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 577038301 148 VVDPSLFIVDEPFLGLDPLAIADLIQLLeVEKQKGKSILMSTHVLDSAEKMcDAFVILHKGEVRAQGNLQQL 219
Cdd:PRK11160 491 LHDAPLLLLDEPTEGLDAETERQILELL-AEHAQNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQEL 560
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-238 |
1.94e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 76.18 E-value: 1.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYVH-VPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLtlreDATNY------R 73
Cdd:PRK13644 1 MIRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGI----DTGDFsklqgiR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 74 KQIGYIPETPslyeeltlrehiETVAMAYGIEQKVAF-------------NRVEPLLKMFRLDQKLDWFPVHFSKGMKQK 140
Cdd:PRK13644 77 KLVGIVFQNP------------ETQFVGRTVEEDLAFgpenlclppieirKRVDRALAEIGLEKYRHRSPKTLSGGQGQC 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 141 VMIICAFVVDPSLFIVDEPFLGLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEkMCDAFVILHKGEVRAQGNlqqlr 220
Cdd:PRK13644 145 VALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELH-DADRIIVMDRGKIVLEGE----- 218
|
250 260
....*....|....*....|.
gi 577038301 221 evfdmPEASLNDI---YLALT 238
Cdd:PRK13644 219 -----PENVLSDVslqTLGLT 234
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-226 |
1.96e-16 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 75.89 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDATN-YRKQIGYI 79
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSReLAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 80 PETPSLYEELTLREHIetvamAYG----------------IEQKVAFNRVEPLLKMFrLDQkldwfpvhFSKGMKQKVMI 143
Cdd:COG4604 81 RQENHINSRLTVRELV-----AFGrfpyskgrltaedreiIDEAIAYLDLEDLADRY-LDE--------LSGGQRQRAFI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 144 ICAFVVDPSLFIVDEPFLGLDPLAIADLIQLL-EVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQQ---- 218
Cdd:COG4604 147 AMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLrRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEiitp 226
|
250
....*....|
gi 577038301 219 --LREVFDMP 226
Cdd:COG4604 227 evLSDIYDTD 236
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
20-226 |
2.60e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 75.35 E-value: 2.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 20 VSFTVESGQLVGLIGLNGAGKSTTINEIIGLLtPYSGEIKINGLTLRE-DATNYRKQIGYIPE--TPS----LYEELTLr 92
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAwSAAELARHRAYLSQqqTPPfampVFQYLTL- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 93 eHIETVAMAYGIEqkvafNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFV-VDPS------LFIVDEPFLGLDP 165
Cdd:PRK03695 93 -HQPDKTRTEAVA-----SALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLqVWPDinpagqLLLLDEPMNSLDV 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 577038301 166 LAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQQ------LREVFDMP 226
Cdd:PRK03695 167 AQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEvltpenLAQVFGVN 233
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
16-234 |
3.35e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 75.59 E-value: 3.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 16 VLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLRE-DATNYRKQIGYIPETPSLYEELTLReh 94
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARKVAYLPQQLPAAEGMTVR-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 95 iETVAMA----------YGIEQKvafNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGLD 164
Cdd:PRK10575 104 -ELVAIGrypwhgalgrFGAADR---EKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 577038301 165 PLAIADLIQLLE-VEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQQLrevfdMPEASLNDIY 234
Cdd:PRK10575 180 IAHQVDVLALVHrLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL-----MRGETLEQIY 245
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-192 |
4.89e-16 |
|
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: 76.63 E-value: 4.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYV-HVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLRE-DATNYRKQIGYI 79
Cdd:TIGR02868 335 LELRDLSAGYPgAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSlDQDEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 80 PETPSLYEElTLREHIEtVAMAYGIEQKV--AFNRV--EPLLKmfRLDQKLDwFPVH-----FSKGMKQKVMIICAFVVD 150
Cdd:TIGR02868 415 AQDAHLFDT-TVRENLR-LARPDATDEELwaALERVglADWLR--ALPDGLD-TVLGeggarLSGGERQRLALARALLAD 489
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 577038301 151 PSLFIVDEPFLGLDPLAIADLIQ-LLEVEkqKGKSILMSTHVL 192
Cdd:TIGR02868 490 APILLLDEPTEHLDAETADELLEdLLAAL--SGRTVVLITHHL 530
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
18-210 |
6.14e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 76.36 E-value: 6.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 18 KDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKING--LTLREDATNYRKQIGYIPETP---------SLY 86
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGkdISPRSPLDAVKKGMAYITESRrdngffpnfSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 87 EELTLREHIETVAM--AYGI-----EQKVAFNRVEPL-LKMFRLDQKLdwfpVHFSKGMKQKVMIICAFVVDPSLFIVDE 158
Cdd:PRK09700 360 QNMAISRSLKDGGYkgAMGLfhevdEQRTAENQRELLaLKCHSVNQNI----TELSGGNQQKVLISKWLCCCPEVIIFDE 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 577038301 159 PFLGLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEV 210
Cdd:PRK09700 436 PTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-99 |
6.76e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 76.26 E-value: 6.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKInGLTLRedatnyrkqIGYIP 80
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK---------IGYFD 384
|
90 100
....*....|....*....|
gi 577038301 81 -ETPSLYEELTLREHIETVA 99
Cdd:COG0488 385 qHQEELDPDKTVLDELRDGA 404
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
17-190 |
7.46e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 73.76 E-value: 7.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 17 LKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEI-----KINGLTLREdATNYRKQIGYIPETPSLYEELTL 91
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsghDITRLKNRE-VPFLRRQIGMIFQDHHLLMDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 92 REHIETVAMAYGIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDPLAIADL 171
Cdd:PRK10908 97 YDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGI 176
|
170
....*....|....*....
gi 577038301 172 IQLLEVEKQKGKSILMSTH 190
Cdd:PRK10908 177 LRLFEEFNRVGVTVLMATH 195
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-211 |
1.33e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 73.27 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTG----GYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTL----REDATNY 72
Cdd:PRK10584 6 IVEVHHLKKsvgqGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqmdEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 73 R-KQIGYIPETPSLYEELTLREHIETVAMAYGIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDP 151
Cdd:PRK10584 86 RaKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 577038301 152 SLFIVDEPFLGLDPLA---IADLiqLLEVEKQKGKSILMSTHVLDSAEKmCDAFVILHKGEVR 211
Cdd:PRK10584 166 DVLFADEPTGNLDRQTgdkIADL--LFSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQLQ 225
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-226 |
1.36e-15 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 73.68 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKING--LTLREDA--------- 69
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGeeIRLKPDRdgelvpadr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 70 ---TNYRKQIGYIPETPSLYEELTLREH-IETVAMAYGIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIIC 145
Cdd:COG4598 88 rqlQRIRTRLGMVFQSFNLWSHMTVLENvIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 146 AFVVDPSLFIVDEPFLGLDPlaiaDLIQllEVEK------QKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQql 219
Cdd:COG4598 168 ALAMEPEVMLFDEPTSALDP----ELVG--EVLKvmrdlaEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPA-- 239
|
....*..
gi 577038301 220 rEVFDMP 226
Cdd:COG4598 240 -EVFGNP 245
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
11-213 |
1.50e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 74.68 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 11 YVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGlTLREDATNYRKQIGYIPETPSLYEELT 90
Cdd:PRK11000 13 YGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGE-KRMNDVPPAERGVGMVFQSYALYPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 91 LREHietvaMAYG-----IEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDP 165
Cdd:PRK11000 92 VAEN-----MSFGlklagAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 577038301 166 -LAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVrAQ 213
Cdd:PRK11000 167 aLRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV-AQ 214
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-217 |
1.93e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 74.82 E-value: 1.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLR--EDATNYRKQIGY 78
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNklDHKLAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 79 IPETPSLYEELTLREHI-------ETVAMAYGIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDP 151
Cdd:PRK09700 85 IYQELSVIDELTVLENLyigrhltKKVCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 577038301 152 SLFIVDEPFLGLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQ 217
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVS 230
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
16-192 |
2.38e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 72.84 E-value: 2.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 16 VLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKingltlREDATnyrkQIGYIPETPSLYEELTLrehi 95
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK------RNGKL----RIGYVPQKLYLDTTLPL---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 96 eTVAMAYGIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGLD---PLAIADLI 172
Cdd:PRK09544 85 -TVNRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDvngQVALYDLI 163
|
170 180
....*....|....*....|
gi 577038301 173 QLLEVEkqKGKSILMSTHVL 192
Cdd:PRK09544 164 DQLRRE--LDCAVLMVSHDL 181
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-235 |
2.53e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 73.02 E-value: 2.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPY-----SGEIKINGLTL-REDATNYRKQ 75
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIfKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 76 IGYIPETPSLYEELTLrehIETVAMAYGIEQKVA-----FNRVEPLLKMFRL----DQKLDWFPVHFSKGMKQKVMIICA 146
Cdd:PRK14247 84 VQMVFQIPNPIPNLSI---FENVALGLKLNRLVKskkelQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 147 FVVDPSLFIVDEPFLGLDPLAIADlIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGnlqQLREVFDMP 226
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAK-IESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWG---PTREVFTNP 236
|
....*....
gi 577038301 227 EASLNDIYL 235
Cdd:PRK14247 237 RHELTEKYV 245
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-224 |
3.19e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 72.50 E-value: 3.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLRE-DATNYRKQIGYI 79
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwSPAELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 80 PETPSLYEELTLREHIETVAMAYGIEQKvafnRVEPLL--KMFRLDqkLDwfpvHF--------SKGMKQKVMIicAFVV 149
Cdd:PRK13548 82 PQHSSLSFPFTVEEVVAMGRAPHGLSRA----EDDALVaaALAQVD--LA----HLagrdypqlSGGEQQRVQL--ARVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 150 --------DPSLFIVDEPFLGLDPLAIADLIQLL-EVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQQ-- 218
Cdd:PRK13548 150 aqlwepdgPPRWLLLDEPTSALDLAHQHHVLRLArQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEvl 229
|
250
....*....|
gi 577038301 219 ----LREVFD 224
Cdd:PRK13548 230 tpetLRRVYG 239
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-235 |
3.63e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 72.57 E-value: 3.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKST---TINEIIGL--LTPYSGEIKINGLTLRE---DATNYR 73
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTllrTFNRLLELneEARVEGEVRLFGRNIYSpdvDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 74 KQIGYIPETPSLYEELTLREHIETVAMAYGI--EQKVAFNRVEPLLKMFRL----DQKLDWFPVHFSKGMKQKVMIICAF 147
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 148 VVDPSLFIVDEPFLGLDPLAIADLIQLLeVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGnlqQLREVFDMPE 227
Cdd:PRK14267 165 AMKPKILLMDEPTANIDPVGTAKIEELL-FELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVG---PTRKVFENPE 240
|
....*...
gi 577038301 228 ASLNDIYL 235
Cdd:PRK14267 241 HELTEKYV 248
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-219 |
4.44e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 73.22 E-value: 4.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGltlrEDATNYRKQ---IGY 78
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDG----EDVTHRSIQqrdICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 79 IPETPSLYEELTLREHIetvamAYGIE-QKVA----FNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSL 153
Cdd:PRK11432 83 VFQSYALFPHMSLGENV-----GYGLKmLGVPkeerKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 577038301 154 FIVDEPFLGLDplaiADLIQLL-----EVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQQL 219
Cdd:PRK11432 158 LLFDEPLSNLD----ANLRRSMrekirELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
15-219 |
4.97e-15 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 73.90 E-value: 4.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 15 PVLKDVSFTVESGQLVGLIGLNGAGKSTtineIIGLLTPY----SGEIKINGLTLRE-DATNYRKQIGYIPETPSLY--- 86
Cdd:PRK11176 357 PALRNINFKIPAGKTVALVGRSGSGKST----IANLLTRFydidEGEILLDGHDLRDyTLASLRNQVALVSQNVHLFndt 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 87 ---------EELTLREHIETVA-MAYGIEqkvafnrvepllkmF--RLDQKLDWF----PVHFSKGMKQKVMIICAFVVD 150
Cdd:PRK11176 433 ianniayarTEQYSREQIEEAArMAYAMD--------------FinKMDNGLDTVigenGVLLSGGQRQRIAIARALLRD 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 577038301 151 PSLFIVDEPFLGLDPLAiADLIQLLEVEKQKGKSILMSTHVLDSAEKmCDAFVILHKGEVRAQGNLQQL 219
Cdd:PRK11176 499 SPILILDEATSALDTES-ERAIQAALDELQKNRTSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAEL 565
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
13-210 |
6.99e-15 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 71.35 E-value: 6.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 13 HVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLRE-DATNYRKQIGYIPETPSLYEElTL 91
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyEHKYLHSKVSLVGQEPVLFAR-SL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 92 REHIetvamAYGIeQKVAFNRVEPLLKMFRLDQKLDWFPVHF-----------SKGMKQKVMIICAFVVDPSLFIVDEPF 160
Cdd:cd03248 105 QDNI-----AYGL-QSCSFECVKEAAQKAHAHSFISELASGYdtevgekgsqlSGGQKQRVAIARALIRNPQVLILDEAT 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 577038301 161 LGLDPLAIADLIQLLEvEKQKGKSILMSTHVLDSAEKmCDAFVILHKGEV 210
Cdd:cd03248 179 SALDAESEQQVQQALY-DWPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
17-232 |
8.97e-15 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 71.39 E-value: 8.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 17 LKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGltlredatnyrkQIGYIPETPSLYEELTLREHIE 96
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG------------EVSVIAISAGLSGQLTGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 97 TVAMAYGIEQKvAFNRVEPLLKMFRLDQKLDWFPV-HFSKGMKQKVMIICAFVVDPSLFIVDEPF-LGLDPLAIADLIQL 174
Cdd:PRK13546 108 FKMLCMGFKRK-EIKAMTPKIIEFSELGEFIYQPVkKYSSGMRAKLGFSINITVNPDILVIDEALsVGDQTFAQKCLDKI 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 577038301 175 LEVeKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQqlrEVFDMPEASLND 232
Cdd:PRK13546 187 YEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELD---DVLPKYEAFLND 240
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
2-241 |
9.30e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 71.27 E-value: 9.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGgYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTP----YSGEIKINGLTLREDATNYRKqIG 77
Cdd:PRK10418 5 IELRNIAL-QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALRGRK-IA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 78 YIPETP-SLYEEL-TLREH-IETVAmAYGIEQKVAfnRVEPLLKMFRLDQK---LDWFPVHFSKGMKQKVMIICAFVVDP 151
Cdd:PRK10418 83 TIMQNPrSAFNPLhTMHTHaRETCL-ALGKPADDA--TLTAALEAVGLENAarvLKLYPFEMSGGMLQRMMIALALLCEA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 152 SLFIVDEPFLGLDPLAIADLIQLLE-VEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQqlrEVFDMPEAS- 229
Cdd:PRK10418 160 PFIIADEPTTDLDVVAQARILDLLEsIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVE---TLFNAPKHAv 236
|
250
....*....|....*
gi 577038301 230 ---LNDIYLALTKEE 241
Cdd:PRK10418 237 trsLVSAHLALYGME 251
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-67 |
1.18e-14 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 70.91 E-value: 1.18e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 577038301 1 MLEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLRE 67
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAA 67
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
17-190 |
1.43e-14 |
|
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: 69.58 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 17 LKDVSFTVESGQLVGLIGLNGAGKSTTIN-----EIIGLLTpysGEIKINGLTLREdatNYRKQIGYIPETPSLYEELTL 91
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDvlagrKTAGVIT---GEILINGRPLDK---NFQRSTGYVEQQDVHSPNLTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 92 REHIETVAMAYGIeqkvafnrvepllkmfrldqkldwfpvhfSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDPLAIADL 171
Cdd:cd03232 97 REALRFSALLRGL-----------------------------SVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNI 147
|
170
....*....|....*....
gi 577038301 172 IQLLEVEKQKGKSILMSTH 190
Cdd:cd03232 148 VRFLKKLADSGQAILCTIH 166
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-210 |
1.75e-14 |
|
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: 69.75 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYV-HVP-VLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLRE-DATNYRKQIGY 78
Cdd:cd03369 7 IEVENLSVRYApDLPpVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTiPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 79 IPETPSLYEElTLREHIETVAMaYGIEQkvafnrvepLLKMFRLDQKLDwfpvHFSKGMKQKVMIICAFVVDPSLFIVDE 158
Cdd:cd03369 87 IPQDPTLFSG-TIRSNLDPFDE-YSDEE---------IYGALRVSEGGL----NLSQGQRQLLCLARALLKRPRVLVLDE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 577038301 159 PFLGLDPLAIAdLIQLLEVEKQKGKSILMSTHVLDSAEKmCDAFVILHKGEV 210
Cdd:cd03369 152 ATASIDYATDA-LIQKTIREEFTNSTILTIAHRLRTIID-YDKILVMDAGEV 201
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-234 |
2.14e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 71.87 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLR----EDATNyrKQIG 77
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfastTAALA--AGVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 78 YIPETPSLYEELTLREHIETVAM--AYGIEQKVAFNRvEPLLKMFRLDQKLD-WFPV-HFSKGMKQKVMIICAFVVDPSL 153
Cdd:PRK11288 83 IIYQELHLVPEMTVAENLYLGQLphKGGIVNRRLLNY-EAREQLEHLGVDIDpDTPLkYLSIGQRQMVEIAKALARNARV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 154 FIVDEPFLGLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGE-VRAQGNLQQL-RE--VFDMPEAS 229
Cdd:PRK11288 162 IAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRyVATFDDMAQVdRDqlVQAMVGRE 241
|
....*
gi 577038301 230 LNDIY 234
Cdd:PRK11288 242 IGDIY 246
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
5-214 |
2.38e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 70.40 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 5 KKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDATN-YRKQIGYIPETP 83
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKeVARRIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 84 SLYEELTLREHI-------ETVAMAYGIEQKVAFNRVEPLLKMFRL-DQKLDwfpvHFSKGMKQKVMIICAFVVDPSLFI 155
Cdd:PRK10253 91 TTPGDITVQELVargryphQPLFTRWRKEDEEAVTKAMQATGITHLaDQSVD----TLSGGQRQRAWIAMVLAQETAIML 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 156 VDEPFLGLDPLAIADLIQLL-EVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQG 214
Cdd:PRK10253 167 LDEPTTWLDISHQIDLLELLsELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG 226
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-209 |
4.49e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 71.01 E-value: 4.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLT--PYSGEIKING--LTLREDATNYRKQI 76
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGspLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 77 GYIPETPSLYEELTLREHI----ETVAMAYGIEQKVAFNRVEPLLKMFRLDQKLDWFPV-HFSKGMKQKVMIICAFVVDP 151
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIflgnEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVgDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 577038301 152 SLFIVDEPFLGLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGE 209
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
14-210 |
4.69e-14 |
|
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: 70.99 E-value: 4.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 14 VPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKIN-----------GLTLREDATNYrkqIGYIPET 82
Cdd:TIGR03269 297 VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgdewvdmtkpGPDGRGRAKRY---IGILHQE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 83 PSLYeelTLREHIETVAMAYGIEQKVAFNRVEPL--LKMFRLDQK-----LDWFPVHFSKGMKQKVMIICAFVVDPSLFI 155
Cdd:TIGR03269 374 YDLY---PHRTVLDNLTEAIGLELPDELARMKAVitLKMVGFDEEkaeeiLDKYPDELSEGERHRVALAQVLIKEPRIVI 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 577038301 156 VDEPFLGLDPLAIADLIQ-LLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEV 210
Cdd:TIGR03269 451 LDEPTGTMDPITKVDVTHsILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-220 |
6.13e-14 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 70.15 E-value: 6.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAG--KSTTINEIIGlltPYSGEIKINGLTLREDATNYRKQIG-Y 78
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPWRF*TWCANRRALRRTIG*H 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 79 IPETPSLYEELTLREHIETVAMAYGIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDE 158
Cdd:NF000106 91 RPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 577038301 159 PFLGLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQQLR 220
Cdd:NF000106 171 PTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELK 232
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-210 |
6.34e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 68.96 E-value: 6.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLT----GGYVH-VPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGltlrEDATN---Y 72
Cdd:COG1101 1 MLELKNLSktfnPGTVNeKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDG----KDVTKlpeY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 73 R--KQIGYIPETPSL--YEELTLREHIetvAMAYGIEQKVAFNR---------VEPLLKMF------RLDQKLDwfpvHF 133
Cdd:COG1101 77 KraKYIGRVFQDPMMgtAPSMTIEENL---ALAYRRGKRRGLRRgltkkrrelFRELLATLglglenRLDTKVG----LL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 577038301 134 SKGMKQKVMIICAFVVDPSLFIVDEPFLGLDPlAIADLIQLL--EVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEV 210
Cdd:COG1101 150 SGGQRQALSLLMATLTKPKLLLLDEHTAALDP-KTAALVLELteKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
16-224 |
6.34e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 70.68 E-value: 6.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 16 VLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLL--TPYSGEIKINGltlREDATNYRKQIGYIPETPSLYEELTLRE 93
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIqgNNFTGTILANN---RKPTKQILKRTGFVTQDDILYPHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 94 HIETVAMA------YGIEQKVAFNRVEPLLKMFRLDQKL--DWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDP 165
Cdd:PLN03211 160 TLVFCSLLrlpkslTKQEKILVAESVISELGLTKCENTIigNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 166 LAIADLIQLLEVEKQKGKSILMSTHVLDS-AEKMCDAFVILHKGEVRAQGNLQQLREVFD 224
Cdd:PLN03211 240 TAAYRLVLTLGSLAQKGKTIVTSMHQPSSrVYQMFDSVLVLSEGRCLFFGKGSDAMAYFE 299
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-218 |
9.65e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 70.03 E-value: 9.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYVHvpvlkDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTL--REDATNYRKQIGYI 79
Cdd:PRK10762 258 LKVDNLSGPGVN-----DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvtRSPQDGLANGIVYI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 80 PET---PSLYEELTLREHIETVAMAYGIEQKVAFNR------VEPLLKMFR-----LDQKLDwfpvHFSKGMKQKVMIIC 145
Cdd:PRK10762 333 SEDrkrDGLVLGMSVKENMSLTALRYFSRAGGSLKHadeqqaVSDFIRLFNiktpsMEQAIG----LLSGGNQQKVAIAR 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 577038301 146 AFVVDPSLFIVDEPFLGLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQQ 218
Cdd:PRK10762 409 GLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTREQ 481
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
8-164 |
1.39e-13 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 68.99 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 8 TGGYVHVpvLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTL----REDATNYRKQIGYIPETP 83
Cdd:COG4608 27 TVGVVKA--VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDItglsGRELRPLRRRMQMVFQDP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 84 --SLYEELTLREHIETVAMAYGIEQKVAF-NRVEPLLKMFRLDQK-LDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEP 159
Cdd:COG4608 105 yaSLNPRMTVGDIIAEPLRIHGLASKAERrERVAELLELVGLRPEhADRYPHEFSGGQRQRIGIARALALNPKLIVCDEP 184
|
....*
gi 577038301 160 FLGLD 164
Cdd:COG4608 185 VSALD 189
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-219 |
2.19e-13 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 67.96 E-value: 2.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYVHV--PVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPySGEIKING-----LTLREdatnYRK 74
Cdd:cd03289 3 MTVKDLTAKYTEGgnAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGvswnsVPLQK----WRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 75 QIGYIPETPSLYEElTLREHIEtvamAYGIEQKVAFNRV--EPLLKMFrLDQ---KLDWFPVH----FSKGMKQKVMIIC 145
Cdd:cd03289 78 AFGVIPQKVFIFSG-TFRKNLD----PYGKWSDEEIWKVaeEVGLKSV-IEQfpgQLDFVLVDggcvLSHGHKQLMCLAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 577038301 146 AFVVDPSLFIVDEPFLGLDPLAIADLIQLLEvEKQKGKSILMSTHVLDsAEKMCDAFVILHKGEVRAQGNLQQL 219
Cdd:cd03289 152 SVLSKAKILLLDEPSAHLDPITYQVIRKTLK-QAFADCTVILSEHRIE-AMLECQRFLVIEENKVRQYDSIQKL 223
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-210 |
3.18e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 68.51 E-value: 3.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLT-GGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGltlrEDATN------YRK 74
Cdd:COG3845 258 LEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDG----EDITGlsprerRRL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 75 QIGYIPETP---------SLYEELTLREHIETVAMAYG-IEQKVAFNRVEPLLKMFR-----LDQKLDwfpvHFSKGMKQ 139
Cdd:COG3845 334 GVAYIPEDRlgrglvpdmSVAENLILGRYRRPPFSRGGfLDRKAIRAFAEELIEEFDvrtpgPDTPAR----SLSGGNQQ 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 577038301 140 KVMIICAFVVDPSLFIVDEPFLGLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEV 210
Cdd:COG3845 410 KVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-190 |
3.30e-13 |
|
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: 64.78 E-value: 3.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTlredatnyrkQIGYIPe 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV----------KIGYFE- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 82 tpslyeeltlrehietvamaygieqkvafnrvepllkmfrldqkldwfpvHFSKGMKQKVMIICAFVVDPSLFIVDEPFL 161
Cdd:cd03221 70 --------------------------------------------------QLSGGEKMRLALAKLLLENPNLLLLDEPTN 99
|
170 180
....*....|....*....|....*....
gi 577038301 162 GLDPLAIADLIQLLeveKQKGKSILMSTH 190
Cdd:cd03221 100 HLDLESIEALEEAL---KEYPGTVILVSH 125
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-211 |
3.83e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 66.98 E-value: 3.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTInEIIGLLTPYSGEIKING---------LTLREDATNY 72
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFL-KCLNRMNELESEVRVEGrveffnqniYERRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 73 RKQIGYIPETPSLYEeLTLREHIETVAMAYGIEQKVAFNR-VEPLLKMFRL----DQKLDWFPVHFSKGMKQKVMIICAF 147
Cdd:PRK14258 87 RRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKLEIDDiVESALKDADLwdeiKHKIHKSALDLSGGQQQRLCIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 577038301 148 VVDPSLFIVDEPFLGLDPLA---IADLIQLLEVEKQkgKSILMSTHVLDSAEKMCDAFVILHKGEVR 211
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDPIAsmkVESLIQSLRLRSE--LTMVIVSHNLHQVSRLSDFTAFFKGNENR 230
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-210 |
4.26e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 66.62 E-value: 4.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIkINGLTLREDATNyrkqigyipE 81
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLAEARE---------D 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 82 TPSLYEELTL---REHIETVAMayGIEQKVAFNRVEPLLKMFRLDQKLDWfPVHFSKGMKQKVMIICAFVVDPSLFIVDE 158
Cdd:PRK11247 83 TRLMFQDARLlpwKKVIDNVGL--GLKGQWRDAALQALAAVGLADRANEW-PAALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 577038301 159 PFLGLDPLAIADLIQLLE-VEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEV 210
Cdd:PRK11247 160 PLGALDALTRIEMQDLIEsLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
15-209 |
7.24e-13 |
|
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: 65.18 E-value: 7.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 15 PVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGltlredatnyrkQIGYIPETPSLYEElTLREH 94
Cdd:cd03250 19 FTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG------------SIAYVSQEPWIQNG-TIREN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 95 IetvamAYGIEqkvaFN--RVEPLLKMFRLDQKLDWFP-----------VHFSKGMKQKVMIICAFVVDPSLFIVDEPFL 161
Cdd:cd03250 86 I-----LFGKP----FDeeRYEKVIKACALEPDLEILPdgdlteigekgINLSGGQKQRISLARAVYSDADIYLLDDPLS 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 577038301 162 GLDPLAIADLIQ-LLEVEKQKGKSILMSTHVLDSAEKmCDAFVILHKGE 209
Cdd:cd03250 157 AVDAHVGRHIFEnCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
18-226 |
7.75e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 66.65 E-value: 7.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 18 KDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLR----EDATNYRKQIGYIPETP--SLYEELTL 91
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLgmkdDEWRAVRSDIQMIFQDPlaSLNPRMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 92 REHIETVAMAYGIE---QKVAfNRV-EPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDPLA 167
Cdd:PRK15079 118 GEIIAEPLRTYHPKlsrQEVK-DRVkAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSI 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 577038301 168 IADLIQLL-EVEKQKGKSILMSTHVLDSAEKMCDAFVILHKG-EVRaqgnLQQLREVFDMP 226
Cdd:PRK15079 197 QAQVVNLLqQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGhAVE----LGTYDEVYHNP 253
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
15-220 |
9.28e-13 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 67.24 E-value: 9.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 15 PVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGltlredatnyrkQIGYIPETPSLYEElTLREH 94
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG------------RISFSPQTSWIMPG-TIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 95 IetvamAYGIEQKVAfnRVEPLLKMFRLDQKLDWFP-----------VHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGL 163
Cdd:TIGR01271 507 I-----IFGLSYDEY--RYTSVIKACQLEEDIALFPekdktvlgeggITLSGGQRARISLARAVYKDADLYLLDSPFTHL 579
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 577038301 164 DPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKmCDAFVILHKGEVRAQGNLQQLR 220
Cdd:TIGR01271 580 DVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKK-ADKILLLHEGVCYFYGTFSELQ 635
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
14-227 |
1.61e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 66.42 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 14 VPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGL---TLREDATN-YRKQIGYIPETP--SLYE 87
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSPGKLQaLRRDIQFIFQDPyaSLDP 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 88 ELTLREHIETVAMAYGIEQ-KVAFNRVEPLLKMFRLDQKLDW-FPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDP 165
Cdd:PRK10261 417 RQTVGDSIMEPLRVHGLLPgKAAAARVAWLLERVGLLPEHAWrYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 577038301 166 LAIADLIQL-LEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGnlqQLREVFDMPE 227
Cdd:PRK10261 497 SIRGQIINLlLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG---PRRAVFENPQ 556
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
15-219 |
1.68e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.54 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 15 PVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPysgeikingltLREDATNYRKQIGYIPETPSLYEElTLREH 94
Cdd:PLN03232 631 PTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSH-----------AETSSVVIRGSVAYVPQVSWIFNA-TVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 95 IetvamAYGieQKVAFNRVEPLLKMFRLDQKLDWFP-----------VHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGL 163
Cdd:PLN03232 699 I-----LFG--SDFESERYWRAIDVTALQHDLDLLPgrdlteigergVNISGGQKQRVSMARAVYSNSDIYIFDDPLSAL 771
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 577038301 164 DPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMcDAFVILHKGEVRAQGNLQQL 219
Cdd:PLN03232 772 DAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAEL 826
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-213 |
1.75e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.11 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYV---HVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLT-PYSGEIKING--LTLREDATNYRK 74
Cdd:PRK13549 259 ILEVRNLTAWDPvnpHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGkpVKIRNPQQAIAQ 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 75 QIGYIPE-----------------TPSLYEELTLREHIETVAMAYGIEQKVAFNRVE---PLLKMFRLdqkldwfpvhfS 134
Cdd:PRK13549 339 GIAMVPEdrkrdgivpvmgvgkniTLAALDRFTGGSRIDDAAELKTILESIQRLKVKtasPELAIARL-----------S 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 577038301 135 KGMKQKVMIICAFVVDPSLFIVDEPFLGLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQ 213
Cdd:PRK13549 408 GGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLKGD 486
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
14-210 |
3.36e-12 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 64.86 E-value: 3.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 14 VPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKING--LTLREDA--------TNYrkqigyipetp 83
Cdd:PRK11650 17 TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGrvVNELEPAdrdiamvfQNY----------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 84 SLYEELTLREHietvaMAYG----------IEQkvafnRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSL 153
Cdd:PRK11650 86 ALYPHMSVREN-----MAYGlkirgmpkaeIEE-----RVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 154 FIVDEPFLGLDP-LAIADLIQLLEVEKQKGKSILMSTHvlDSAEKM--CDAFVILHKGEV 210
Cdd:PRK11650 156 FLFDEPLSNLDAkLRVQMRLEIQRLHRRLKTTSLYVTH--DQVEAMtlADRVVVMNGGVA 213
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-230 |
3.60e-12 |
|
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: 65.70 E-value: 3.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYVHV--PVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPySGEIKINGLTLRE-DATNYRKQIGY 78
Cdd:TIGR01271 1218 MDVQGLTAKYTEAgrAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST-EGEIQIDGVSWNSvTLQTWRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 79 IPETPSLYEElTLREHIETVAM-----AYGIEQKVAFNRVepllkMFRLDQKLDWFPVH----FSKGMKQKVMIICAFVV 149
Cdd:TIGR01271 1297 IPQKVFIFSG-TFRKNLDPYEQwsdeeIWKVAEEVGLKSV-----IEQFPDKLDFVLVDggyvLSNGHKQLMCLARSILS 1370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 150 DPSLFIVDEPFLGLDPLAIADLIQLLEvEKQKGKSILMSTHVLDSAEKmCDAFVILHKGEVRAQGNLQQLrevfdMPEAS 229
Cdd:TIGR01271 1371 KAKILLLDEPSAHLDPVTLQIIRKTLK-QSFSNCTVILSEHRVEALLE-CQQFLVIEGSSVKQYDSIQKL-----LNETS 1443
|
.
gi 577038301 230 L 230
Cdd:TIGR01271 1444 L 1444
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-209 |
7.14e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.57 E-value: 7.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLtP---YSGEIKINGLTLRedATNYR---- 73
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PhgtYEGEIIFEGEELQ--ASNIRdter 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 74 KQIGYIpetpslYEELTLREHIeTVA---------MAYGIEQKVAFN-RVEPLLKMFRLDQKLDwFPV-HFSKGMKQKVM 142
Cdd:PRK13549 82 AGIAII------HQELALVKEL-SVLeniflgneiTPGGIMDYDAMYlRAQKLLAQLKLDINPA-TPVgNLGLGQQQLVE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 577038301 143 IICAFVVDPSLFIVDEPFLGLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGE 209
Cdd:PRK13549 154 IAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-212 |
8.82e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 64.08 E-value: 8.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYV---HVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLT-PYSGEIKING--LTLREDATNYRK 74
Cdd:TIGR02633 257 ILEARNLTCWDVinpHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGkpVDIRNPAQAIRA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 75 QIGYIPE-----------------TPSLYEELTLREHIETVAMAYGIE---QKVAFNRVEPLLKMFRLdqkldwfpvhfS 134
Cdd:TIGR02633 337 GIAMVPEdrkrhgivpilgvgkniTLSVLKSFCFKMRIDAAAELQIIGsaiQRLKVKTASPFLPIGRL-----------S 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 577038301 135 KGMKQKVMIICAFVVDPSLFIVDEPFLGLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRA 212
Cdd:TIGR02633 406 GGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKG 483
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
15-210 |
1.45e-11 |
|
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: 61.51 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 15 PVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPY---SGEIKINGLTLREDATNYRKQIGYIPETPSLYEELTL 91
Cdd:cd03233 21 PILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTLTV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 92 REHIETVAMAYGIEqkvafnrvepllkMFRldqkldwfpvHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDPLAIADL 171
Cdd:cd03233 101 RETLDFALRCKGNE-------------FVR----------GISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 577038301 172 IQLL-EVEKQKGKSILMS-THVLDSAEKMCDAFVILHKGEV 210
Cdd:cd03233 158 LKCIrTMADVLKTTTFVSlYQASDEIYDLFDKVLVLYEGRQ 198
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-223 |
1.54e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 63.81 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 16 VLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDAT-NYRKQIGYIPETPSLYEElTLREH 94
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLhDLRFKITIIPQDPVLFSG-SLRMN 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 95 I--------ETVAMAYGIEQKVAFNRVEPLlkmfRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDpL 166
Cdd:TIGR00957 1380 LdpfsqysdEEVWWALELAHLKTFVSALPD----KLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVD-L 1454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 167 AIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFViLHKGEVR---AQGNLQQLREVF 223
Cdd:TIGR00957 1455 ETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIV-LDKGEVAefgAPSNLLQQRGIF 1513
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
13-232 |
1.86e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 63.19 E-value: 1.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 13 HVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGL---TLREDAtnYRKQIGYIPETPSLYEel 89
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIpltKLQLDS--WRSRLAVVSQTPFLFS-- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 90 tlrehiETVA--MAYG--------IEQKVAFNRV-EPLLkmfRLDQKLDW----FPVHFSKGMKQKVMIICAFVVDPSLF 154
Cdd:PRK10789 403 ------DTVAnnIALGrpdatqqeIEHVARLASVhDDIL---RLPQGYDTevgeRGVMLSGGQKQRISIARALLLNAEIL 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 155 IVDepflglDPLAIAD---LIQLLEVEKQ--KGKSILMSTHVLdSAEKMCDAFVILHKGEVRAQGNLQQLREVF----DM 225
Cdd:PRK10789 474 ILD------DALSAVDgrtEHQILHNLRQwgEGRTVIISAHRL-SALTEASEILVMQHGHIAQRGNHDQLAQQSgwyrDM 546
|
250
....*....|..
gi 577038301 226 -----PEASLND 232
Cdd:PRK10789 547 yryqqLEAALDD 558
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-220 |
3.03e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 61.54 E-value: 3.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLT---GGYVHVpvlKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIK-----INGLTLREDAtny 72
Cdd:PRK11300 5 LLSVSGLMmrfGGLLAV---NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILlrgqhIEGLPGHQIA--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 73 RKQIGYIPETPSLYEELTLRE--------HIETVAMAyGIEQKVAFNRVEpllkMFRLDQKLDWFPV------------H 132
Cdd:PRK11300 79 RMGVVRTFQHVRLFREMTVIEnllvaqhqQLKTGLFS-GLLKTPAFRRAE----SEALDRAATWLERvgllehanrqagN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 133 FSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDPLAIADLIQLL-EVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVR 211
Cdd:PRK11300 154 LAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIaELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPL 233
|
....*....
gi 577038301 212 AQGNLQQLR 220
Cdd:PRK11300 234 ANGTPEEIR 242
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
15-223 |
4.59e-11 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 61.41 E-value: 4.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 15 PVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGltlredatnyrkQIGYIPETpSLYEELTLREH 94
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG------------RISFSSQF-SWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 95 IetvamAYGieqkVAFN--RVEPLLKMFRLDQKLDWFP-----------VHFSKGMKQKVMIICAFVVDPSLFIVDEPFL 161
Cdd:cd03291 118 I-----IFG----VSYDeyRYKSVVKACQLEEDITKFPekdntvlgeggITLSGGQRARISLARAVYKDADLYLLDSPFG 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 577038301 162 GLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKmCDAFVILHKGEVRAQGN---LQQLREVF 223
Cdd:cd03291 189 YLDVFTEKEIFESCVCKLMANKTRILVTSKMEHLKK-ADKILILHEGSSYFYGTfseLQSLRPDF 252
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-60 |
5.19e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 61.87 E-value: 5.19e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 577038301 2 LEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKI 60
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI 381
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
15-190 |
6.29e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 60.25 E-value: 6.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 15 PVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGL-TLREDATNYrkqIGYIPETPSLYEELTLRE 93
Cdd:PRK13543 25 PVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKtATRGDRSRF---MAYLGHLPGLKADLSTLE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 94 HIETVAMAYGIEQKVAFNRVeplLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDPLAIADLIQ 173
Cdd:PRK13543 102 NLHFLCGLHGRRAKQMPGSA---LAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNR 178
|
170
....*....|....*..
gi 577038301 174 LLEVEKQKGKSILMSTH 190
Cdd:PRK13543 179 MISAHLRGGGAALVTTH 195
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
15-219 |
1.04e-10 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 61.13 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 15 PVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLReDAT--NYRKQIGYIPETPSLYEElTLR 92
Cdd:PRK13657 349 QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIR-TVTraSLRRNIAVVFQDAGLFNR-SIE 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 93 EHI---------ETVAMAYGIEQKVAFnrvepllkmfrLDQKLDWFPVH-------FSKGMKQKVMIICAFVVDPSLFIV 156
Cdd:PRK13657 427 DNIrvgrpdatdEEMRAAAERAQAHDF-----------IERKPDGYDTVvgergrqLSGGERQRLAIARALLKDPPILIL 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 577038301 157 DEPFLGLDPLAIADLIQLLEvEKQKGKSILMSTHVLdSAEKMCDAFVILHKGEVRAQGNLQQL 219
Cdd:PRK13657 496 DEATSALDVETEAKVKAALD-ELMKGRTTFIIAHRL-STVRNADRILVFDNGRVVESGSFDEL 556
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
15-219 |
1.35e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.15 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 15 PVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLRE-DATNYRKQIGYIPETPSLYEElTLRE 93
Cdd:PLN03232 1250 PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfGLTDLRRVLSIIPQSPVLFSG-TVRF 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 94 HIETVAMAYGIEQKVAFNRVEplLK------MFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDpLA 167
Cdd:PLN03232 1329 NIDPFSEHNDADLWEALERAH--IKdvidrnPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVD-VR 1405
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 577038301 168 IADLIQLLEVEKQKGKSILMSTHVLDSAEKmCDAFVILHKGEVRAQGNLQQL 219
Cdd:PLN03232 1406 TDSLIQRTIREEFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQEL 1456
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
3-214 |
1.36e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 60.36 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 3 EIKK-LTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTL----REDATNYRKQIG 77
Cdd:PRK11308 16 PVKRgLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkadPEAQKLLRQKIQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 78 YIPETPslYEELTLREHIETVamaygIEQKVAFN-------RVEPLLKMFRL----DQKLDWFPVHFSKGMKQKVMIICA 146
Cdd:PRK11308 96 IVFQNP--YGSLNPRKKVGQI-----LEEPLLINtslsaaeRREKALAMMAKvglrPEHYDRYPHMFSGGQRQRIAIARA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 577038301 147 FVVDPSLFIVDEPFLGLDPLAIADLIQLL-EVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQG 214
Cdd:PRK11308 169 LMLDPDVVVADEPVSALDVSVQAQVLNLMmDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKG 237
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-200 |
1.92e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 59.02 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEI--IGLLTP---YSGEIKINGLTL---REDATNY 72
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGHNIyspRTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 73 RKQIGYIPETP-----SLYEELTLREHIEtvamayGIEQKVAFNR-VEPLLKMF----RLDQKLDWFPVHFSKGMKQKVM 142
Cdd:PRK14239 85 RKEIGMVFQQPnpfpmSIYENVVYGLRLK------GIKDKQVLDEaVEKSLKGAsiwdEVKDRLHDSALGLSGGQQQRVC 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 577038301 143 IICAFVVDPSLFIVDEPFLGLDPLAIADLIQLLEVEKQKgKSILMSTHVLDSAEKMCD 200
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISD 215
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-190 |
2.76e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 58.88 E-value: 2.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIG--LLTPYSGEIKINGLTLREDATNYRKQIG- 77
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERAHLGi 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 78 -----YIPETPSLYEELTLRehietvaMAYGIEQK-VAFNRVEPL---------LKMFRLDQKLDWFPVH--FSKGMKQK 140
Cdd:CHL00131 87 flafqYPIEIPGVSNADFLR-------LAYNSKRKfQGLPELDPLefleiinekLKLVGMDPSFLSRNVNegFSGGEKKR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 577038301 141 VMIICAFVVDPSLFIVDEPFLGLDPLA---IADLIQLLeveKQKGKSILMSTH 190
Cdd:CHL00131 160 NEILQMALLDSELAILDETDSGLDIDAlkiIAEGINKL---MTSENSIILITH 209
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
15-96 |
3.22e-10 |
|
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: 59.56 E-value: 3.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 15 PVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKingltLREDATnyrkqIGYIPETPSLYEELTLREH 94
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEAR-----PQPGIK-----VGYLPQEPQLDPTKTVREN 88
|
..
gi 577038301 95 IE 96
Cdd:TIGR03719 89 VE 90
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
13-227 |
3.54e-10 |
|
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: 59.31 E-value: 3.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 13 HVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLtPYSGEIKING---LTLREDA-TNYRKQIGYIPETP--SLY 86
Cdd:COG4172 298 HVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGqdlDGLSRRAlRPLRRRMQVVFQDPfgSLS 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 87 EELTLREHIETVAMAYGIEQKVA--FNRVEPLLKMFRLD-QKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGL 163
Cdd:COG4172 377 PRMTVGQIIAEGLRVHGPGLSAAerRARVAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSAL 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 577038301 164 DPLAIADLIQLL-EVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQQlreVFDMPE 227
Cdd:COG4172 457 DVSVQAQILDLLrDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQ---VFDAPQ 518
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
15-209 |
4.17e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 57.80 E-value: 4.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 15 PVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKING---LTLREDAtnYRKQIGYIPETPSLYEElTL 91
Cdd:PRK10247 21 KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGediSTLKPEI--YRQQVSYCAQTPTLFGD-TV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 92 REHIetvAMAYGI-EQKVAFNRVEPLLKMFRLDQKLDWFPVH-FSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDP---L 166
Cdd:PRK10247 98 YDNL---IFPWQIrNQQPDPAIFLDDLERFALPDTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALDEsnkH 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 577038301 167 AIADLIQLLevEKQKGKSILMSTHvlDSAE-KMCDAFVIL--HKGE 209
Cdd:PRK10247 175 NVNEIIHRY--VREQNIAVLWVTH--DKDEiNHADKVITLqpHAGE 216
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-210 |
4.88e-10 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 58.12 E-value: 4.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKST---TINEIIGlLTP---YSGEIKING---LTLREDATNY 72
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTllrCLNRMND-LIPgarVEGEILLDGediYDPDVDVVEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 73 RKQIGYIPETP-----SLYEELT--LREHietvamayGIEQKVAFN-RVEPLLKMFRL-----DqKLDWFPVHFSKGMKQ 139
Cdd:COG1117 91 RRRVGMVFQKPnpfpkSIYDNVAygLRLH--------GIKSKSELDeIVEESLRKAALwdevkD-RLKKSALGLSGGQQQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 577038301 140 KVMIICAFVVDPSLFIVDEPFLGLDPLA---IADLIQLLevekqKGK-SILMSTHVLDSAEKMCD--AFviLHKGEV 210
Cdd:COG1117 162 RLCIARALAVEPEVLLMDEPTSALDPIStakIEELILEL-----KKDyTIVIVTHNMQQAARVSDytAF--FYLGEL 231
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
15-166 |
5.51e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.87 E-value: 5.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 15 PVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGlLTP--YSgeikiNGLTL----R---EDATNYRKQIGYIpeTPSL 85
Cdd:PRK10938 274 PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPqgYS-----NDLTLfgrrRgsgETIWDIKKHIGYV--SSSL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 86 YEELTLREHIETVAM-----AYGIEQKVAfNRVEPL----LKMFRLDQKLDWFPVH-FSKGMKQKVMIICAFVVDPSLFI 155
Cdd:PRK10938 346 HLDYRVSTSVRNVILsgffdSIGIYQAVS-DRQQKLaqqwLDILGIDKRTADAPFHsLSWGQQRLALIVRALVKHPTLLI 424
|
170
....*....|.
gi 577038301 156 VDEPFLGLDPL 166
Cdd:PRK10938 425 LDEPLQGLDPL 435
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-81 |
5.70e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 58.75 E-value: 5.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINgltlrEDAtnyrkQIGYIPE 81
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWS-----ENA-----NIGYYAQ 389
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-214 |
7.19e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 57.63 E-value: 7.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIK----------INGLTLREDAT 70
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHyrmrdgqlrdLYALSEAERRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 71 NYRKQIGYIPETPslyeELTLREHIETVA------MA-----YG-IEQKVAF--NRVEpllkmfrLDQ-KLDWFPVHFSK 135
Cdd:PRK11701 86 LLRTEWGFVHQHP----RDGLRMQVSAGGnigerlMAvgarhYGdIRATAGDwlERVE-------IDAaRIDDLPTTFSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 136 GMKQKVMIICAFVVDPSLFIVDEPFLGLDPLAIADLIQLL-EVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQG 214
Cdd:PRK11701 155 GMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLrGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-236 |
9.86e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 57.41 E-value: 9.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 7 LTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKST---TINEIIGLLT--PYSGEIKINGLTL--REDATNYRKQIGYI 79
Cdd:PRK14271 27 LTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTflrTLNRMNDKVSgyRYSGDVLLGGRSIfnYRDVLEFRRRVGML 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 80 PETPSLYEeLTLREHIETVAMAYGIEQK-----VAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLF 154
Cdd:PRK14271 107 FQRPNPFP-MSIMDNVLAGVRAHKLVPRkefrgVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 155 IVDEPFLGLDPLAIADLIQLLEVEKQKgKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQQLrevFDMPEASLNDIY 234
Cdd:PRK14271 186 LLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL---FSSPKHAETARY 261
|
..
gi 577038301 235 LA 236
Cdd:PRK14271 262 VA 263
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
15-114 |
1.33e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.82 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 15 PVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKIngltlredATNYRkqIGYIPETPSLYEELTLREH 94
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP--------APGIK--VGYLPQEPQLDPEKTVREN 90
|
90 100
....*....|....*....|
gi 577038301 95 IETvAMAygiEQKVAFNRVE 114
Cdd:PRK11819 91 VEE-GVA---EVKAALDRFN 106
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
15-86 |
1.34e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.83 E-value: 1.34e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 577038301 15 PVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLRE-DATNYRKQIGYIPETPSLY 86
Cdd:PLN03130 1253 PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKfGLMDLRKVLGIIPQAPVLF 1325
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-190 |
1.64e-09 |
|
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: 55.61 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGL--LTPYSGEIKINGLTLREDATNYRKQIG-- 77
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARLGif 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 78 ----YIPETPSLYEELTLREhietvaMAYGieqkvafnrvepllkmfrldqkldwfpvhFSKGMKQKVMIICAFVVDPSL 153
Cdd:cd03217 81 lafqYPPEIPGVKNADFLRY------VNEG-----------------------------FSGGEKKRNEILQLLLLEPDL 125
|
170 180 190
....*....|....*....|....*....|....*..
gi 577038301 154 FIVDEPFLGLDPLAIADLIQLLEVEKQKGKSILMSTH 190
Cdd:cd03217 126 AILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITH 162
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
15-103 |
1.95e-09 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 57.14 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 15 PVLKDVSFTVESGQLVGLIGLNGAGKSTtineIIGLLT----PYSGEIKINGLTLRE-DATNYRKQIGYIPETPSLYEEl 89
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKST----LARLLFrfydVTSGRILIDGQDIRDvTQASLRAAIGIVPQDTVLFND- 446
|
90
....*....|....
gi 577038301 90 TLREHIetvamAYG 103
Cdd:COG5265 447 TIAYNI-----AYG 455
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-60 |
3.08e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.67 E-value: 3.08e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 577038301 2 LEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKI 60
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
129-221 |
9.99e-09 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 54.53 E-value: 9.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 129 FPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDPLAIADLIQLLE-VEKQKGKSILMSTHVLDSAEKMCDAFVILHK 207
Cdd:COG4170 155 YPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLArLNQLQGTSILLISHDLESISQWADTITVLYC 234
|
90
....*....|....
gi 577038301 208 GEVRAQGNLQQLRE 221
Cdd:COG4170 235 GQTVESGPTEQILK 248
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-219 |
3.39e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 53.57 E-value: 3.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYVH-VPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLRE-DATNYRKQIGYI 79
Cdd:PRK10790 341 IDIDNVSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSlSHSVLRQGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 80 PETP-----SLYEELTLREHI--ETVAMAYGIEQKVAFNRVEPLLKMFRLDQKLDwfpvHFSKGMKQKVMIICAFVVDPS 152
Cdd:PRK10790 421 QQDPvvladTFLANVTLGRDIseEQVWQALETVQLAELARSLPDGLYTPLGEQGN----NLSVGQKQLLALARVLVQTPQ 496
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 153 LFIVDEPFLGLDP---LAIADLIQLLevekQKGKSILMSTHVLdSAEKMCDAFVILHKGEVRAQGNLQQL 219
Cdd:PRK10790 497 ILILDEATANIDSgteQAIQQALAAV----REHTTLVVIAHRL-STIVEADTILVLHRGQAVEQGTHQQL 561
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
15-219 |
5.32e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.20 E-value: 5.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 15 PVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYS-GEIKINGltlredatnyrkQIGYIPETPSLYEElTLRE 93
Cdd:PLN03130 631 PTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRG------------TVAYVPQVSWIFNA-TVRD 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 94 HIetvamAYGIEQKVAfnRVEPLLKMFRLDQKLDWFP-----------VHFSKGMKQKVMIICAFVVDPSLFIVDEPFLG 162
Cdd:PLN03130 698 NI-----LFGSPFDPE--RYERAIDVTALQHDLDLLPggdlteigergVNISGGQKQRVSMARAVYSNSDVYIFDDPLSA 770
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 163 LDPLAIADLIQLLEVEKQKGKSILMST---HVLDSAEKMcdafVILHKGEVRAQGNLQQL 219
Cdd:PLN03130 771 LDAHVGRQVFDKCIKDELRGKTRVLVTnqlHFLSQVDRI----ILVHEGMIKEEGTYEEL 826
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1-210 |
6.63e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.42 E-value: 6.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGgyVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDATNYRKQIGYip 80
Cdd:PRK10982 250 ILEVRNLTS--LRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHGF-- 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 81 etpslyeELTLREHIETVAMAYgieQKVAFNRVEP----------LLKMFRLDQKLDWF--------PVH------FSKG 136
Cdd:PRK10982 326 -------ALVTEERRSTGIYAY---LDIGFNSLISnirnyknkvgLLDNSRMKSDTQWVidsmrvktPGHrtqigsLSGG 395
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 577038301 137 MKQKVMIICAFVVDPSLFIVDEPFLGLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEV 210
Cdd:PRK10982 396 NQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-182 |
6.72e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.71 E-value: 6.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 21 SFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEiKINGLTlREDATNYRKQIGYIPET--------PSLYEELTLR 92
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGE-RQSQFS-HITRLSFEQLQKLVSDEwqrnntdmLSPGEDDTGR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 93 ehieTVAMAYGIEQKVAfNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDPLAIADLI 172
Cdd:PRK10938 101 ----TTAEIIQDEVKDP-ARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLA 175
|
170
....*....|
gi 577038301 173 QLLEVEKQKG 182
Cdd:PRK10938 176 ELLASLHQSG 185
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-219 |
8.76e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.22 E-value: 8.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYVHVPVlkdvSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLR--------------- 66
Cdd:PRK11288 258 LRLDGLKGPGLREPI----SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDirsprdairagimlc 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 67 -EDatnyRKQIGYIPeTPSLYEELTL--REHIETVAMAY--GIEQKVAFNRVEPL-LKMFRLDQKLdwfpVHFSKGMKQK 140
Cdd:PRK11288 334 pED----RKAEGIIP-VHSVADNINIsaRRHHLRAGCLInnRWEAENADRFIRSLnIKTPSREQLI----MNLSGGNQQK 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 141 VMIICAFVVDPSLFIVDEPFLGLDPLAIADLIQLLEVEKQKGKSILMSTHvlDSAEKM--CDAFVILHKGEV-----RAQ 213
Cdd:PRK11288 405 AILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSS--DLPEVLgvADRIVVMREGRIagelaREQ 482
|
....*.
gi 577038301 214 GNLQQL 219
Cdd:PRK11288 483 ATERQA 488
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
17-193 |
1.35e-07 |
|
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: 50.87 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 17 LKDVSFTVESG-----QLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTlredatnyrkqIGYIPETPSLYEELTL 91
Cdd:cd03237 10 LGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT-----------VSYKPQYIKADYEGTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 92 REHIETVAMAYGIEqkvAFNRVEpLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDP---LAI 168
Cdd:cd03237 79 RDLLSSITKDFYTH---PYFKTE-IAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVeqrLMA 154
|
170 180 190
....*....|....*....|....*....|
gi 577038301 169 ADLIQLLEVEKQKG-----KSILMSTHVLD 193
Cdd:cd03237 155 SKVIRRFAENNEKTafvveHDIIMIDYLAD 184
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
55-190 |
2.74e-07 |
|
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: 50.47 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 55 SGEIKINGLTLREDATNYRKQIGYIPETPSLYEELTLREHIETVAMAYGIEQKVAFNRVEPLLKMFRLDQKLDWFpvHFS 134
Cdd:pfam13304 161 LLLEDWAVLDLAADLALFPDLKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGELPAF--ELS 238
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 577038301 135 KGMKQKVMIICAFVVD---PSLFIVDEPFLGLDPLAIADLIQLLEVEKQKGKSILMSTH 190
Cdd:pfam13304 239 DGTKRLLALLAALLSAlpkGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
16-190 |
3.08e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.00 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 16 VLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTP--YSGEIKINGLTLREDatNYRKQIGYIPETPSLYEELTLRE 93
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISGFPKKQE--TFARISGYCEQNDIHSPQVTVRE 972
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 94 HIETVAM-----AYGIEQKVAF-NRVEPLLKMFRLDQKLDWFP--VHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDP 165
Cdd:PLN03140 973 SLIYSAFlrlpkEVSKEEKMMFvDEVMELVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA 1052
|
170 180
....*....|....*....|....*
gi 577038301 166 LAIADLIQLLEVEKQKGKSILMSTH 190
Cdd:PLN03140 1053 RAAAIVMRTVRNTVDTGRTVVCTIH 1077
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
17-202 |
4.39e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 49.40 E-value: 4.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 17 LKDVSFTVESGQLVGLIGLNGAGKSTTI---NEIIGLLTPYSGEIKI-----NGLTLREDATNYRKQIGYIPETP----- 83
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILrcfNRLNDLIPGFRVEGKVtfhgkNLYAPDVDPVEVRRRIGMVFQKPnpfpk 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 84 SLYEELTLREHI--------ETVAMAygIEQKVAFNRVEPLLKMFRLDqkldwfpvhFSKGMKQKVMIICAFVVDPSLFI 155
Cdd:PRK14243 106 SIYDNIAYGARIngykgdmdELVERS--LRQAALWDEVKDKLKQSGLS---------LSGGQQQRLCIARAIAVQPEVIL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 577038301 156 VDEPFLGLDP---LAIADLIQllEVEKQkgKSILMSTHVLDSAEKMCD--AF 202
Cdd:PRK14243 175 MDEPCSALDPistLRIEELMH--ELKEQ--YTIIIVTHNMQQAARVSDmtAF 222
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
17-190 |
4.54e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 49.97 E-value: 4.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 17 LKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTL-REDATNYRKQIGYIPETPSLYEELTLREhi 95
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVtAEQPEDYRKLFSAVFTDFHLFDQLLGPE-- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 96 etvamayGIEQKVAfnRVEPLLKMFRLDQKL---DWF--PVHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDPLAIAD 170
Cdd:PRK10522 417 -------GKPANPA--LVEKWLERLKMAHKLeleDGRisNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRRE 487
|
170 180
....*....|....*....|.
gi 577038301 171 LIQ-LLEVEKQKGKSILMSTH 190
Cdd:PRK10522 488 FYQvLLPLLQEMGKTIFAISH 508
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
12-190 |
6.03e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 48.80 E-value: 6.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 12 VHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLL--TPYSGEIKINGLTlredatnyrkqigyipetpsLYEEL 89
Cdd:COG2401 41 VERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQ--------------------FGREA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 90 TLrehIETVAMAYGIEQKVAF-NRV---EPLLkMFRLdqkldwfPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDP 165
Cdd:COG2401 101 SL---IDAIGRKGDFKDAVELlNAVglsDAVL-WLRR-------FKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDR 169
|
170 180
....*....|....*....|....*..
gi 577038301 166 LaIADLI--QLLEVEKQKGKSILMSTH 190
Cdd:COG2401 170 Q-TAKRVarNLQKLARRAGITLVVATH 195
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-230 |
9.47e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 49.23 E-value: 9.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGltlREDATNYRKQ----- 75
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG---KEVTFNGPKSsqeag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 76 IGYIPETPSLYEELTLREHI----ETVAMAYGIEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDP 151
Cdd:PRK10762 81 IGIIHQELNLIPQLTIAENIflgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFES 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 577038301 152 SLFIVDEPFLGLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQgnlqqlREVFDMPEASL 230
Cdd:PRK10762 161 KVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAE------REVADLTEDSL 233
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-190 |
1.22e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.95 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 16 VLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTP---YSGEIKINGltlREDATNYRKQIGYIPETPSLYEELTLR 92
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNG---RPLDSSFQRSIGYVQQQDLHLPTSTVR 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 93 EHIETVAM-----AYGIEQKVAFnrVEPLLKMFRLDQKLDWFPVHFSKGM----KQKVMIICAFVVDPSLFI-VDEPFLG 162
Cdd:TIGR00956 855 ESLRFSAYlrqpkSVSKSEKMEY--VEEVIKLLEMESYADAVVGVPGEGLnveqRKRLTIGVELVAKPKLLLfLDEPTSG 932
|
170 180
....*....|....*....|....*...
gi 577038301 163 LDPLAIADLIQLLEVEKQKGKSILMSTH 190
Cdd:TIGR00956 933 LDSQTAWSICKLMRKLADHGQAILCTIH 960
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-209 |
1.32e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 48.26 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYVH----VPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGL------LTPYS---GEIKINGLTLRE 67
Cdd:PRK15093 3 LLDIRNLTIEFKTsdgwVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnwrVTADRmrfDDIDLLRLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 68 DatnyRKQIGYI-------PET---PSLYEELTLREHIETVAMAYGIEQKVAFNR---VEPLLKMFRLDQK--LDWFPVH 132
Cdd:PRK15093 83 R----RKLVGHNvsmifqePQScldPSERVGRQLMQNIPGWTYKGRWWQRFGWRKrraIELLHRVGIKDHKdaMRSFPYE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 577038301 133 FSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDPLAIADLIQLL-EVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGE 209
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLtRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQ 236
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-87 |
1.49e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.62 E-value: 1.49e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 577038301 16 VLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKING-----LTLREdatnYRKQIGYIPETPSLYE 87
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGreigaYGLRE----LRRQFSMIPQDPVLFD 1397
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
5-192 |
1.79e-06 |
|
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: 47.33 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 5 KKLTGGYV----HVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDATNY-----RKQ 75
Cdd:cd03290 1 VQVTNGYFswgsGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEAtrsrnRYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 76 IGYIPETPSLYEElTLREHIetvamAYGieqkVAFN--RVEPLLKMFRLDQKLDWFP-----------VHFSKGMKQKVM 142
Cdd:cd03290 81 VAYAAQKPWLLNA-TVEENI-----TFG----SPFNkqRYKAVTDACSLQPDIDLLPfgdqteigergINLSGGQRQRIC 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 577038301 143 IICAFVVDPSLFIVDEPFLGLDPLAIADLIQ--LLEVEKQKGKSILMSTHVL 192
Cdd:cd03290 151 VARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKL 202
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
16-190 |
1.82e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.17 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 16 VLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDATNYrkqIGYIPETPSLYEELTLREHI 95
Cdd:PRK13541 15 NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPY---CTYIGHNLGLKLEMTVFENL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 96 ETVAMAYgieqkvafNRVEPL---LKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDPLAIADLI 172
Cdd:PRK13541 92 KFWSEIY--------NSAETLyaaIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLN 163
|
170
....*....|....*...
gi 577038301 173 QLLEVEKQKGKSILMSTH 190
Cdd:PRK13541 164 NLIVMKANSGGIVLLSSH 181
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-58 |
1.83e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.24 E-value: 1.83e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 577038301 1 MLEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEI 58
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI 369
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
15-219 |
1.88e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 48.40 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 15 PVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGltlredatnyrkQIGYIPETpSLYEELTLREH 94
Cdd:TIGR00957 652 PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG------------SVAYVPQQ-AWIQNDSLREN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 95 IetvamAYGieQKVAFNRVEPLLKMFRLDQKLDWFP-----------VHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGL 163
Cdd:TIGR00957 719 I-----LFG--KALNEKYYQQVLEACALLPDLEILPsgdrteigekgVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAV 791
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 577038301 164 DPLAIADLIQLLEVEKQ--KGKSILMSTHVLdSAEKMCDAFVILHKGEVRAQGNLQQL 219
Cdd:TIGR00957 792 DAHVGKHIFEHVIGPEGvlKNKTRILVTHGI-SYLPQVDVIIVMSGGKISEMGSYQEL 848
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1-208 |
5.80e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 46.71 E-value: 5.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLtP---YSGEIKINGLTLREDATNYRKQIG 77
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PhgsYEGEILFDGEVCRFKDIRDSEALG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 78 Y--IPETPSLYEELTLREHI----ETVamAYG-IEQKVAFNRVEPLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVD 150
Cdd:NF040905 80 IviIHQELALIPYLSIAENIflgnERA--KRGvIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 577038301 151 PSLFIVDEPFLGL---DPLAIADLiqLLEVEKQKGKSILMStHVLDSAEKMCDAFVILHKG 208
Cdd:NF040905 158 VKLLILDEPTAALneeDSAALLDL--LLELKAQGITSIIIS-HKLNEIRRVADSITVLRDG 215
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-70 |
6.03e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 46.36 E-value: 6.03e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTpysGEIKINGLTLREDAT 70
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLT---GGGAPRGARVTGDVT 67
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
17-59 |
1.12e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.10 E-value: 1.12e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 577038301 17 LKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIK 59
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH 377
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
14-86 |
1.94e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.41 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 14 VPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINgltlreDATN--------YRKQIGYIPETPSL 85
Cdd:PTZ00265 398 VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN------DSHNlkdinlkwWRSKIGVVSQDPLL 471
|
.
gi 577038301 86 Y 86
Cdd:PTZ00265 472 F 472
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
15-173 |
2.94e-05 |
|
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: 44.13 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 15 PVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLRE-DATNYRKQIGYIPETPSLYEElTLRE 93
Cdd:cd03288 35 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKlPLHTLRSRLSIILQDPILFSG-SIRF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 94 HIETvamaygiEQKVAFNRVEPLLKMFRLDQKLDWFP-----------VHFSKGMKQKVMIICAFVVDPSLFIVDEPFLG 162
Cdd:cd03288 114 NLDP-------ECKCTDDRLWEALEIAQLKNMVKSLPggldavvteggENFSVGQRQLFCLARAFVRKSSILIMDEATAS 186
|
170
....*....|.
gi 577038301 163 LDpLAIADLIQ 173
Cdd:cd03288 187 ID-MATENILQ 196
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
26-96 |
3.13e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 42.75 E-value: 3.13e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 577038301 26 SGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIK-INGLTLREDATNYRKQIGYIPETPSLYEELTLREHIE 96
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALA 72
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
15-190 |
3.31e-05 |
|
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: 42.91 E-value: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 15 PVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGltlredatnyRKQIGYIPETPSLYeELTLREh 94
Cdd:cd03223 15 VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE----------GEDLLFLPQRPYLP-LGTLRE- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 95 ietvAMAYgieqkvafnrvePllkmfrldqkldWFPVhFSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDPLAIADLIQL 174
Cdd:cd03223 83 ----QLIY------------P------------WDDV-LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQL 133
|
170
....*....|....*.
gi 577038301 175 LeveKQKGKSILMSTH 190
Cdd:cd03223 134 L---KELGITVISVGH 146
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-221 |
3.80e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 43.63 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTGGYVHVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGL--LTPYSGEIKINGLTLREDATNYRKQIG- 77
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 78 -----YIPETPSLYEELTLREHIETVAMAYGIEQKVAF---NRVEPLLKMFRLDQKLDWFPVH--FSKGMKQKVMIICAF 147
Cdd:PRK09580 81 fmafqYPVEIPGVSNQFFLQTALNAVRSYRGQEPLDRFdfqDLMEEKIALLKMPEDLLTRSVNvgFSGGEKKRNDILQMA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 148 VVDPSLFIVDEPFLGLDPLAIADLIQLLEVEKQKGKSILMSTH---VLDSAEKmcDAFVILHKGEVRAQGN---LQQLRE 221
Cdd:PRK09580 161 VLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHyqrILDYIKP--DYVHVLYQGRIVKSGDftlVKQLEE 238
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-99 |
7.74e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.56 E-value: 7.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 16 VLKDVSFTVESGQLVGLIGLNGAGKST----TINEIIGLLTPYSGEIKINGLTLREDATNYRKQIGYIPETPSLYEELTL 91
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTllktIASNTDGFHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVHFPHLTV 155
|
....*...
gi 577038301 92 REHIETVA 99
Cdd:TIGR00956 156 GETLDFAA 163
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
17-190 |
8.59e-05 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 43.07 E-value: 8.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 17 LKDVSFTVESGqLVGLIGLNGAGKSTTINEIIGLLTPYSG-----------------EIKInGLTLREDATNYRKQIGYI 79
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSrkfdeedfylgddpdlpEIEI-ELTFGSLLSRLLRLLLKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 80 PETPSLYEEL----------------TLREHIETVAMAYGIEQKVAFNRVEPLLKMFRLDQKlDWFPVHFSK-GMKQKVM 142
Cdd:COG3593 92 EDKEELEEALeelneelkealkalneLLSEYLKELLDGLDLELELSLDELEDLLKSLSLRIE-DGKELPLDRlGSGFQRL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 577038301 143 IICAFVV---------DPSLFIVDEPFLGLDPLAIADLIQLLEVEKQKGKSILMSTH 190
Cdd:COG3593 171 ILLALLSalaelkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTH 227
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
14-219 |
1.49e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.41 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 14 VPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGltlredatnyrKQIGYIPETPSL-------Y 86
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQG-----------KEIDFKSSKEALengismvH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 87 EELTL-REHIETVAMAYG--------IEQKVAFNRVEPLLKmfRLDQKLDwfP----VHFSKGMKQKVMIICAFVVDPSL 153
Cdd:PRK10982 80 QELNLvLQRSVMDNMWLGryptkgmfVDQDKMYRDTKAIFD--ELDIDID--PrakvATLSVSQMQMIEIAKAFSYNAKI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 577038301 154 FIVDEPFLGLDPLAIADLIQLLEVEKQKGKSILMSTHVLDSAEKMCDAFVILHKGEVRAQGNLQQL 219
Cdd:PRK10982 156 VIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGL 221
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
17-164 |
2.46e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 41.72 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 17 LKDVSFTVESGQL-----VGLIGLNGAGKSTTINEIIGLLTPYSGEIKInglTLRedatnyrkqIGYIPETPSLYEELTL 91
Cdd:PRK13409 350 LGDFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP---ELK---------ISYKPQYIKPDYDGTV 417
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 577038301 92 REHIETVAMAYGieqkVAFNRVEpLLKMFRLDQKLDWFPVHFSKGMKQKVMIICAFVVDPSLFIVDEPFLGLD 164
Cdd:PRK13409 418 EDLLRSITDDLG----SSYYKSE-IIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-224 |
3.07e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.55 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 2 LEIKKLTGGYV---HVPVLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEIKINGLTLREDATNYRKQIGY 78
Cdd:PTZ00265 1166 IEIMDVNFRYIsrpNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIVFKNEHTNDMTNEQDYQGD 1245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 79 IPETPSL------------------------------------YEELTLREHIETVAMA-----YGIEQKVAFNR----- 112
Cdd:PTZ00265 1246 EEQNVGMknvnefsltkeggsgedstvfknsgkilldgvdicdYNLKDLRNLFSIVSQEpmlfnMSIYENIKFGKedatr 1325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 113 --VEPLLKMFRLDQKLDWFPVHF-----------SKGMKQKVMIICAFVVDPSLFIVDEPFLGLDPLAiADLIQ--LLEV 177
Cdd:PTZ00265 1326 edVKRACKFAAIDEFIESLPNKYdtnvgpygkslSGGQKQRIAIARALLREPKILLLDEATSSLDSNS-EKLIEktIVDI 1404
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 577038301 178 EKQKGKSILMSTHVLDSAeKMCDAFVILHKGE-----VRAQGNLQQLREVFD 224
Cdd:PTZ00265 1405 KDKADKTIITIAHRIASI-KRSDKIVVFNNPDrtgsfVQAHGTHEELLSVQD 1455
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1-210 |
3.47e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 41.31 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 1 MLEIKKLTggyVHVP------VLKDVSFTVESGQLVGLIGLNGAGKSTTINEIIGllTPY----SGEIKINGLTLR---- 66
Cdd:NF040905 257 VFEVKNWT---VYHPlhperkVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFG--RSYgrniSGTVFKDGKEVDvstv 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 67 EDA--------TNYRKQIGYI-----------PETPSLYEELTLREHIET-VAMAY---------GIEQKVAfnrvepll 117
Cdd:NF040905 332 SDAidaglayvTEDRKGYGLNliddikrnitlANLGKVSRRGVIDENEEIkVAEEYrkkmniktpSVFQKVG-------- 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 118 kmfrldqKLdwfpvhfSKGMKQKVMIICAFVVDPSLFIVDEPFLGLDPLA---IADLIQLLEVEkqkGKSILMSTHVLDS 194
Cdd:NF040905 404 -------NL-------SGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAkyeIYTIINELAAE---GKGVIVISSELPE 466
|
250
....*....|....*.
gi 577038301 195 AEKMCDAFVILHKGEV 210
Cdd:NF040905 467 LLGMCDRIYVMNEGRI 482
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
17-200 |
3.48e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 40.00 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 17 LKDVSFTVESGQLVGLIGLNGAGKSTTINEIIglltpysgeikingltlredatnYRKQIGYIPETPSLYEELTLrehie 96
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL-----------------------YASGKARLISFLPKFSRNKL----- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 97 tvamaygieqkVAFNRVEPLLKM----FRLDQKLDwfpvHFSKGMKQKVMIICAFVVDP--SLFIVDEPFLGLDPlaiAD 170
Cdd:cd03238 63 -----------IFIDQLQFLIDVglgyLTLGQKLS----TLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQ---QD 124
|
170 180 190
....*....|....*....|....*....|....*.
gi 577038301 171 LIQLLEVEK---QKGKSILMSTH---VLDSAEKMCD 200
Cdd:cd03238 125 INQLLEVIKgliDLGNTVILIEHnldVLSSADWIID 160
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
10-190 |
4.69e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.00 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 10 GYVHVPVL-KDVSFTVESGQLVGLIGLNGAGKSTTINEIIGLLTPYSGEI--------------KINGLTLREDATNYRK 74
Cdd:PLN03073 517 GYPGGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVfrsakvrmavfsqhHVDGLDLSSNPLLYMM 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038301 75 QIgyIPETPslyeELTLREHIETvamaYGIEQKVAfnrvepLLKMFRLdqkldwfpvhfSKGMKQKVMIICAFVVDPSLF 154
Cdd:PLN03073 597 RC--FPGVP----EQKLRAHLGS----FGVTGNLA------LQPMYTL-----------SGGQKSRVAFAKITFKKPHIL 649
|
170 180 190
....*....|....*....|....*....|....*.
gi 577038301 155 IVDEPFLGLDPLAIADLIQLLeVEKQKGksILMSTH 190
Cdd:PLN03073 650 LLDEPSNHLDLDAVEALIQGL-VLFQGG--VLMVSH 682
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
23-53 |
2.78e-03 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 38.61 E-value: 2.78e-03
10 20 30
....*....|....*....|....*....|.
gi 577038301 23 TVESGQLVGLIGLNGAGKSTTINEIIGLLTP 53
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKP 125
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
7-42 |
3.98e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 38.01 E-value: 3.98e-03
10 20 30
....*....|....*....|....*....|....*....
gi 577038301 7 LTGGYV---HVPVLKDVSFTVESGQLVGLIGLNGAGKST 42
Cdd:PRK11147 6 IHGAWLsfsDAPLLDNAELHIEDNERVCLVGRNGAGKST 44
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
23-53 |
5.16e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 37.87 E-value: 5.16e-03
10 20 30
....*....|....*....|....*....|.
gi 577038301 23 TVESGQLVGLIGLNGAGKSTTINEIIGLLTP 53
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIP 125
|
|
| PTZ00226 |
PTZ00226 |
fumarate hydratase; Provisional |
216-238 |
6.40e-03 |
|
fumarate hydratase; Provisional
Pssm-ID: 240319 [Multi-domain] Cd Length: 570 Bit Score: 37.33 E-value: 6.40e-03
|
| |
