|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-227 |
1.57e-97 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 286.96 E-value: 1.57e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPLAVKQAAGYLPD 85
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 86 AVGFYDSLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTS 165
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1345382048 166 GLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAELAAKV 227
Cdd:COG1131 161 GLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-233 |
5.95e-83 |
|
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: 250.16 E-value: 5.95e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 5 VIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPLAVKQAAGYLP 84
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 85 DAVGFYDSLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPT 164
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1345382048 165 SGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAELAAKVGGDALE 233
Cdd:COG4555 161 NGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEENLE 229
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-214 |
5.68e-73 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 222.27 E-value: 5.68e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPLAVKQAAGYLPD 85
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 86 AVGFYDSLTARENLaftarlagfadvdasgrigqalgrvrldgvadrkvgTFSRGMRQRLGLAELLMRDCQIMILDEPTS 165
Cdd:cd03230 81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1345382048 166 GLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRI 214
Cdd:cd03230 125 GLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-214 |
7.12e-73 |
|
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: 223.25 E-value: 7.12e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPLAVKQAaGYLPD 85
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRI-GALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 86 AVGFYDSLTARENLAFTARLAGFADvdasGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTS 165
Cdd:cd03268 80 APGFYPNLTARENLRLLARLLGIRK----KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1345382048 166 GLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRI 214
Cdd:cd03268 156 GLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-300 |
4.10e-71 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 221.91 E-value: 4.10e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 5 VIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKdPLRDplAVKQAAGYLP 84
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGE-PLDP--EDRRRIGYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 85 DAVGFYDSLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPT 164
Cdd:COG4152 78 EERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 165 SGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAELAAKVGGDALEIDLEAesfdAA 244
Cdd:COG4152 158 SGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRNTLRLEADG----DA 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1345382048 245 ARLSNLNGVDAVIGGDRRWRISASRDLRPEIAARVVESGGRLIALDAHRIGLGEAY 300
Cdd:COG4152 234 GWLRALPGVTVVEEDGDGAELKLEDGADAQELLRALLARGPVREFEEVRPSLNEIF 289
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-218 |
1.67e-63 |
|
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: 199.73 E-value: 1.67e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRNVVDGINLTVKQGeVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPLAVKQAAGYLPD 85
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 86 AVGFYDSLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTS 165
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1345382048 166 GLDPQSTEELLGFIADFAnEGRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVG 218
Cdd:cd03264 160 GLDPEERIRFRNLLSELG-EDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
13-300 |
3.31e-63 |
|
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: 201.85 E-value: 3.31e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 13 KAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPLAVKQAAGYLPDAVGFYDS 92
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 93 LTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQST 172
Cdd:TIGR01188 81 LTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 173 EELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAELAAKVGGDALEIDL-EAESFDAAARL---- 247
Cdd:TIGR01188 161 RAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGKDTLESRPrDIQSLKVEVSMliae 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1345382048 248 --SNLNGVDAVIGGDRRWRISASRDLR--PEIAARVVESGGRLIALDAHRIGLGEAY 300
Cdd:TIGR01188 241 lgETGLGLLAVTVDSDRIKILVPDGDEtvPEIVEAAIRNGIRIRSISTERPSLDDVF 297
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
6-218 |
2.91e-59 |
|
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: 189.12 E-value: 2.91e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAY----KGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPLAVKQAAG 81
Cdd:cd03266 2 ITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 82 YLPDAVGFYDSLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILD 161
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1345382048 162 EPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVG 218
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-194 |
6.42e-58 |
|
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: 184.99 E-value: 6.42e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 5 VIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPLAVKQAAGYLP 84
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 85 DAVGFYDSLTARENLAFTARLAGFADVDAsgRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPT 164
Cdd:COG4133 82 HADGLKPELTVRENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
170 180 190
....*....|....*....|....*....|
gi 1345382048 165 SGLDPQSTEELLGFIADFANEGRTVLVSSH 194
Cdd:COG4133 160 TALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-218 |
1.78e-57 |
|
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: 184.02 E-value: 1.78e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKdPLRDplAVKQAAGYLPD 85
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGK-PLDI--AARNRIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 86 AVGFYDSLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTS 165
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1345382048 166 GLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVG 218
Cdd:cd03269 158 GLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-223 |
3.75e-57 |
|
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: 183.48 E-value: 3.75e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKG--RNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPLAVKQAAGYL 83
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 84 PDAVGFYDSLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEP 163
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 164 TSGLDPQSTEELLGFIADFAnEGRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAEL 223
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-223 |
5.83e-56 |
|
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: 180.64 E-value: 5.83e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPLAVKQAAGYLPD 85
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 86 AVGFYDSLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTS 165
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1345382048 166 GLDPQSTEELLGFIADF-ANEGRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAEL 223
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-222 |
1.76e-53 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 174.89 E-value: 1.76e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 1 MSGTVIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPLAVkqaa 80
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRI---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 81 GYLPDAVGFYDS--LTARE----NLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRD 154
Cdd:COG1121 78 GYVPQRAEVDWDfpITVRDvvlmGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1345382048 155 CQIMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRIgFVGTLAE 222
Cdd:COG1121 158 PDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV-AHGPPEE 224
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-223 |
1.22e-51 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 169.82 E-value: 1.22e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAY-KGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPL-AVKQAAGYL 83
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLrELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 84 ---PDAVGFYDslTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMIL 160
Cdd:COG1122 81 fqnPDDQLFAP--TVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1345382048 161 DEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAEL 223
Cdd:COG1122 159 DEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
6-218 |
2.43e-50 |
|
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: 166.42 E-value: 2.43e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPLavkQAAGYLPD 85
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKDL---HKIGSLIE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 86 AVGFYDSLTARENLAFTARLAGFADvdasGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTS 165
Cdd:TIGR03740 78 SPPLYENLTARENLKVHTTLLGLPD----SRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTN 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1345382048 166 GLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVG 218
Cdd:TIGR03740 154 GLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLGYQG 206
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-213 |
6.77e-49 |
|
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: 162.25 E-value: 6.77e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 7 EARGLTKAYKGRN--VVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPLA-VKQAAGYL 83
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKeLRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 84 ---PDAVGFYDslTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMIL 160
Cdd:cd03225 81 fqnPDDQFFGP--TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1345382048 161 DEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGR 213
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-225 |
4.27e-47 |
|
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: 158.22 E-value: 4.27e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 1 MSGTVIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPLAVKQAA 80
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 81 ----GYLpdavgF-----YDSLTARENLAFTAR-LAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAEL 150
Cdd:COG1127 81 rrriGML-----FqggalFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1345382048 151 LMRDCQIMILDEPTSGLDPQSTEELLGFIADFANE-GRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAELAA 225
Cdd:COG1127 156 LALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-216 |
1.65e-45 |
|
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: 153.46 E-value: 1.65e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 7 EARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPLAVkqaaGYLP-- 84
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRI----GYVPqr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 85 DAVGFYDSLTARE--NLAFTARLAGFADVDASGR--IGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMIL 160
Cdd:cd03235 77 RSIDRDFPISVRDvvLMGLYGHKGLFRRLSKADKakVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1345382048 161 DEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRIGF 216
Cdd:cd03235 157 DEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTVVAS 212
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-223 |
3.21e-45 |
|
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: 154.05 E-value: 3.21e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 5 VIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDpLRDpLAVKQAA---G 81
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRD-LAS-LSRRELArriA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 82 YLPDAVGFYDSLTARENLAF--TARLAGFADVDASGR--IGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQI 157
Cdd:COG1120 79 YVPQEPPAPFGLTVRELVALgrYPHLGLFGRPSAEDReaVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1345382048 158 MILDEPTSGLDPQSTEELLGFIADFANE-GRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAEL 223
Cdd:COG1120 159 LLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-225 |
4.14e-45 |
|
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: 152.98 E-value: 4.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPLAVKQAAGylpd 85
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLG---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 86 aVG--F-----YDSLTARENL----------AFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLA 148
Cdd:cd03219 77 -IGrtFqiprlFPELTVLENVmvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1345382048 149 ELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAELAA 225
Cdd:cd03219 156 RALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-223 |
4.95e-45 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 159.68 E-value: 4.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 4 TVIEARGLTKAYKGRN-----VVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRdpLAVKQ 78
Cdd:COG1123 259 PLLEVRNLSKRYPVRGkggvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTK--LSRRS 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 79 AAGYLPDaVGF-----YDSL----TARENLAFTARLAGFAD-VDASGRIGQALGRVRLD-GVADRKVGTFSRGMRQRLGL 147
Cdd:COG1123 337 LRELRRR-VQMvfqdpYSSLnprmTVGDIIAEPLRLHGLLSrAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAI 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1345382048 148 AELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANE-GRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAEL 223
Cdd:COG1123 416 ARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEV 492
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-234 |
1.89e-44 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 153.42 E-value: 1.89e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 1 MSGTVIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKD-PLRDPLAvKQA 79
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPvPSRARHA-RQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 80 AGYLPDAVGFYDSLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMI 159
Cdd:PRK13537 82 VGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1345382048 160 LDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAEL-AAKVGGDALEI 234
Cdd:PRK13537 162 LDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALiESEIGCDVIEI 237
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-218 |
4.35e-44 |
|
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: 149.59 E-value: 4.35e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPlAVKQAAGYLPD 85
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVP-PERRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 86 AVGFYDSLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTS 165
Cdd:cd03259 80 DYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1345382048 166 GLDPQSTEELLGFIAD-FANEGRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVG 218
Cdd:cd03259 160 ALDAKLREELREELKElQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-214 |
3.18e-42 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 143.73 E-value: 3.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 7 EARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLR-DPLAVKQAAGYLPd 85
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlSPKELARKIAYVP- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 86 avgfydsltarenlaftarlagfadvdasgrigQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTS 165
Cdd:cd03214 80 ---------------------------------QALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1345382048 166 GLDPQSTEELLGFIADFANE-GRTVLVSSHLLDVVQTVCTRVALFNRGRI 214
Cdd:cd03214 127 HLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-225 |
3.05e-41 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 143.03 E-value: 3.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPLAVKQAA----G 81
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrrrmG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 82 YLPDAVGFYDSLTARENLAFTARLAG-FADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMIL 160
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTrLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1345382048 161 DEPTSGLDPQSTEELLGFIADFANE-GRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAELAA 225
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-223 |
2.10e-40 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 147.36 E-value: 2.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 4 TVIEARGLTKAYKG--RNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANA---GSVRLLDKDPLRDPLAV-- 76
Cdd:COG1123 3 PLLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALrg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 77 KQAAGYLPDAVGFYDSLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQ 156
Cdd:COG1123 83 RRIGMVFQDPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1345382048 157 IMILDEPTSGLDPQSTEELLGFIADFANE-GRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAEL 223
Cdd:COG1123 163 LLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
2-225 |
2.12e-40 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 141.33 E-value: 2.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 2 SGTVIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDplrdplavkqAAG 81
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRD----------ITG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 82 YLPDAV---G----F-----YDSLTARENLA----------FTARLAGF-----ADVDASGRIGQALGRVRLDGVADRKV 134
Cdd:COG0411 71 LPPHRIarlGiartFqnprlFPELTVLENVLvaaharlgrgLLAALLRLprarrEEREARERAEELLERVGLADRADEPA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 135 GTFSRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANE-GRTVLVSSHLLDVVQTVCTRVALFNRGR 213
Cdd:COG0411 151 GNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGR 230
|
250
....*....|..
gi 1345382048 214 IGFVGTLAELAA 225
Cdd:COG0411 231 VIAEGTPAEVRA 242
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-251 |
2.72e-40 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 146.71 E-value: 2.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 1 MSGTVIEARGLTKAYKGrnVV--DGINLTVKQGEVLGLLGPNGAGKTTtiLM--LMGLTEANAGSVRLLDKD-PLRDPlA 75
Cdd:COG3845 1 MMPPALELRGITKRFGG--VVanDDVSLTVRPGEIHALLGENGAGKST--LMkiLYGLYQPDSGEILIDGKPvRIRSP-R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 76 VKQAAGylpdaVG-----F--YDSLTARENLAFTARLAGFADVD---ASGRIGQALGRVRLDGVADRKVGTFSRGMRQRL 145
Cdd:COG3845 76 DAIALG-----IGmvhqhFmlVPNLTVAENIVLGLEPTKGGRLDrkaARARIRELSERYGLDVDPDAKVEDLSVGEQQRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 146 GLAELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRIgfVGT------ 219
Cdd:COG3845 151 EILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKV--VGTvdtaet 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1345382048 220 ----LAEL-------------AAKVGGDALEI-DLEAESFDAAARLSNLN 251
Cdd:COG3845 229 seeeLAELmvgrevllrvekaPAEPGEVVLEVeNLSVRDDRGVPALKDVS 278
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-225 |
8.66e-40 |
|
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: 138.72 E-value: 8.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKD--PLRDPLAVKQAAGYL 83
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDitGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 84 PDAVGFYDSLTARENLaftaRLAGFADVDASGRigQALGRV-----RLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIM 158
Cdd:cd03224 81 PEGRRIFPELTVEENL----LLGAYARRRAKRK--ARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1345382048 159 ILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAELAA 225
Cdd:cd03224 155 LLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-225 |
1.42e-39 |
|
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: 138.44 E-value: 1.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPlaVKQAA----G 81
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLP--MHKRArlgiG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 82 YLPDAVGFYDSLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILD 161
Cdd:cd03218 79 YLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1345382048 162 EPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAELAA 225
Cdd:cd03218 159 EPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-213 |
1.45e-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: 136.22 E-value: 1.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 7 EARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPL-AVKQAAGYLPD 85
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLeELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 86 avgfydsltarenlaftarlagfadvdasgrigqalgrvrldgvadrkvgtFSRGMRQRLGLAELLMRDCQIMILDEPTS 165
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1345382048 166 GLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGR 213
Cdd:cd00267 110 GLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-214 |
3.32e-39 |
|
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: 137.24 E-value: 3.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRN----VVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRdpLAVKQAAG 81
Cdd:cd03255 1 IELKNLSKTYGGGGekvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISK--LSEKELAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 82 YLPDAVGF----Y---DSLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRD 154
Cdd:cd03255 79 FRRRHIGFvfqsFnllPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1345382048 155 CQIMILDEPTSGLDPQSTEELLGFIADFANE-GRTVLVSSHLLDVVQTvCTRVALFNRGRI 214
Cdd:cd03255 159 PKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
5-225 |
7.20e-39 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 137.08 E-value: 7.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 5 VIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPLAvKQAA---G 81
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMH-KRARlgiG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 82 YLP-DAVGFYDsLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMIL 160
Cdd:COG1137 82 YLPqEASIFRK-LTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1345382048 161 DEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHllDVVQT--VCTRVALFNRGRIGFVGTLAELAA 225
Cdd:COG1137 161 DEPFAGVDPIAVADIQKIIRHLKERGIGVLITDH--NVRETlgICDRAYIISEGKVLAEGTPEEILN 225
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-223 |
7.88e-39 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 137.11 E-value: 7.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 4 TVIEARGLTKAYK-GRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPLAVKQAA-- 80
Cdd:COG3638 1 PMLELRNLSKRYPgGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 81 --GYLPDAVGFYDSLTAREN-----LAFTARLAGF------ADVDasgRIGQALGRVRLDGVADRKVGTFSRGMRQRLGL 147
Cdd:COG3638 81 riGMIFQQFNLVPRLSVLTNvlagrLGRTSTWRSLlglfppEDRE---RALEALERVGLADKAYQRADQLSGGQQQRVAI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1345382048 148 AELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANE-GRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAEL 223
Cdd:COG3638 158 ARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-233 |
1.90e-38 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 144.50 E-value: 1.90e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 2 SGTVIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDK--DPlRDpLAVKQA 79
Cdd:NF033858 263 DEPAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQpvDA-GD-IATRRR 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 80 AGYLPDAVGFYDSLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMI 159
Cdd:NF033858 341 VGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLI 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1345382048 160 LDEPTSGLDPQSTEELLGFIADFA-NEGRTVLVSSHLLDVVQTvCTRVALFNRGRIGFVGTLAELAAKVGGDALE 233
Cdd:NF033858 421 LDEPTSGVDPVARDMFWRLLIELSrEDGVTIFISTHFMNEAER-CDRISLMHAGRVLASDTPAALVAARGAATLE 494
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-165 |
3.11e-38 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 132.39 E-value: 3.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 21 VDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPL-AVKQAAGYLPDAVGFYDSLTARENL 99
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERkSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 100 AFTARLAGFADVDASGRIGQALGRVRLDGVADRKVG----TFSRGMRQRLGLAELLMRDCQIMILDEPTS 165
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-225 |
7.71e-38 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 134.55 E-value: 7.71e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRN----VVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKD-PLRDPLAVKQAA 80
Cdd:COG1124 2 LEVRNLSVSYGQGGrrvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPvTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 81 GYLP-DAvgfYDSL----TARENLAFTARLAGFADVDAsgRIGQALGRVRLD-GVADRKVGTFSRGMRQRLGLAELLMRD 154
Cdd:COG1124 82 QMVFqDP---YASLhprhTVDRILAEPLRIHGLPDREE--RIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARALILE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1345382048 155 CQIMILDEPTSGLDPQSTEELLGFIADFANE-GRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAELAA 225
Cdd:COG1124 157 PELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLA 228
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-213 |
8.78e-38 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 136.88 E-value: 8.78e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 1 MSGTVIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPLAVKQAA 80
Cdd:PRK13536 37 MSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 81 GYLPDAVGFYDSLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMIL 160
Cdd:PRK13536 117 GVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1345382048 161 DEPTSGLDPQST----EELLGFIAdfanEGRTVLVSSHLLDVVQTVCTRVALFNRGR 213
Cdd:PRK13536 197 DEPTTGLDPHARhliwERLRSLLA----RGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-214 |
9.75e-38 |
|
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: 133.42 E-value: 9.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDK---DPLRDPLAVKQAAGY 82
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLkltDDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 83 LPDAVGFYDSLTARENLAF---TARLAGFADVDASGRigQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMI 159
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLapiKVKGMSKAEAEERAL--ELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1345382048 160 LDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRI 214
Cdd:cd03262 159 FDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-223 |
5.29e-37 |
|
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: 131.93 E-value: 5.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 5 VIEARGLTKAYKGRN----VVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVR-------LLDKDPLRdp 73
Cdd:cd03258 1 MIELKNVSKVFGDTGgkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLvdgtdltLLSGKELR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 74 lAVKQAAGYLPDAVGFYDSLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMR 153
Cdd:cd03258 79 -KARRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1345382048 154 DCQIMILDEPTSGLDPQSTEELLGFIADFANE-GRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAEL 223
Cdd:cd03258 158 NPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-213 |
6.64e-37 |
|
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: 130.00 E-value: 6.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKD---PLRDPLAVKQAAGY 82
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDltdLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 83 LPDAVGFYDSLTARENLAFtaRLAGfadvdasgrigqalgrvrldgvadrkvgtfsrGMRQRLGLAELLMRDCQIMILDE 162
Cdd:cd03229 81 VFQDFALFPHLTVLENIAL--GLSG--------------------------------GQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1345382048 163 PTSGLDPQSTEELLGFIAD-FANEGRTVLVSSHLLDVVQTVCTRVALFNRGR 213
Cdd:cd03229 127 PTSALDPITRREVRALLKSlQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-214 |
8.27e-37 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 131.32 E-value: 8.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 1 MSgTVIEARGLTKAYKGRN----VVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRdpLAV 76
Cdd:COG1136 1 MS-PLLELRNLTKSYGTGEgevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISS--LSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 77 KQAAGYLPDAVGF-------YDSLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAE 149
Cdd:COG1136 78 RELARLRRRHIGFvfqffnlLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1345382048 150 LLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANE-GRTVLVSSHLLDVVQtVCTRVALFNRGRI 214
Cdd:COG1136 158 ALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELAA-RADRVIRLRDGRI 222
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-222 |
9.47e-37 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 131.74 E-value: 9.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 1 MSgTVIEARGLTKAYKGRN----------------------VVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEAN 58
Cdd:COG1134 1 MS-SMIEVENVSKSYRLYHepsrslkelllrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 59 AGSVRlldkdplRD-----PLAVkqaagylpdAVGFYDSLTARENLAFTARLAGF--ADVDAsgrigqalgrvRLDGVA- 130
Cdd:COG1134 80 SGRVE-------VNgrvsaLLEL---------GAGFHPELTGRENIYLNGRLLGLsrKEIDE-----------KFDEIVe 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 131 --------DRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTV 202
Cdd:COG1134 133 faelgdfiDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRL 212
|
250 260
....*....|....*....|
gi 1345382048 203 CTRVALFNRGRIGFVGTLAE 222
Cdd:COG1134 213 CDRAIWLEKGRLVMDGDPEE 232
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
5-225 |
1.94e-36 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 130.86 E-value: 1.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 5 VIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPLAVKQAAG--Y 82
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLGigY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 83 LPDAVGFYDSLTARENLafTARLAGFADVDASGRIGQA---LGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMI 159
Cdd:TIGR04406 81 LPQEASIFRKLTVEENI--MAVLEIRKDLDRAEREERLealLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFIL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1345382048 160 LDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAELAA 225
Cdd:TIGR04406 159 LDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVA 224
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-228 |
3.47e-36 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 136.43 E-value: 3.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 2 SGTVIEARGLTKAY-KGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVrLLDKDPLR--DPLAVKQ 78
Cdd:COG4988 333 GPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSI-LINGVDLSdlDPASWRR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 79 AAGYLP-DAVGFYDSLtaRENLAFTARLAGFADVDasgrigQALGRVRLDGVADR-------KVG----TFSRGMRQRLG 146
Cdd:COG4988 412 QIAWVPqNPYLFAGTI--RENLRLGRPDASDEELE------AALEAAGLDEFVAAlpdgldtPLGeggrGLSGGQAQRLA 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 147 LAELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFAnEGRTVLVSSHLLDVVqTVCTRVALFNRGRIGFVGTLAELAAK 226
Cdd:COG4988 484 LARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALL-AQADRILVLDDGRIVEQGTHEELLAK 561
|
..
gi 1345382048 227 VG 228
Cdd:COG4988 562 NG 563
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-214 |
3.67e-36 |
|
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: 129.55 E-value: 3.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 5 VIEARGLTKAYKGRN----VVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPLAVKQAA 80
Cdd:cd03257 1 LLEVKNLSVSFPTGGgsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 81 GYlpdAVGF-----YDSL----TARENLAFTARLAGFADVDASGRIGQALGRVRL---DGVADRKVGTFSRGMRQRLGLA 148
Cdd:cd03257 81 RK---EIQMvfqdpMSSLnprmTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1345382048 149 ELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANE-GRTVLVSSHLLDVVQTVCTRVALFNRGRI 214
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
11-228 |
3.76e-36 |
|
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: 138.22 E-value: 3.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 11 LTKAYKGRN--VVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPLAVKQAAGYLPDAVG 88
Cdd:TIGR01257 1943 LTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDA 2022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 89 FYDSLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTSGLD 168
Cdd:TIGR01257 2023 IDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMD 2102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 169 PQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAELAAKVG 228
Cdd:TIGR01257 2103 PQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFG 2162
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-227 |
1.43e-35 |
|
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: 128.45 E-value: 1.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYK-GRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLD----KDPLRDPLAVKQAA 80
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGtdinKLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 81 GYLPDAVGFYDSLTARENLaFTARLA---------GFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELL 151
Cdd:cd03256 81 GMIFQQFNLIERLSVLENV-LSGRLGrrstwrslfGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1345382048 152 MRDCQIMILDEPTSGLDPQSTEELLGFIADFANE-GRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAELAAKV 227
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEV 236
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
15-215 |
5.26e-35 |
|
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: 125.83 E-value: 5.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 15 YKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDplRDPLAVKQAAGYLPDAVG---FYD 91
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP--IKAKERRKSIGYVMQDVDyqlFTD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 92 SltARENLAFTARLAGfadvDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQS 171
Cdd:cd03226 88 S--VREELLLGLKELD----AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKN 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1345382048 172 TEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRIG 215
Cdd:cd03226 162 MERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-214 |
5.78e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 126.08 E-value: 5.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLR-DPLAVKQAAGYLP 84
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 85 -DAVGFYDslTARENLAFTARLAGFADVDAsgRIGQALGRVRLD-GVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDE 162
Cdd:COG4619 81 qEPALWGG--TVRDNLPFPFQLRERKFDRE--RALELLERLGLPpDILDKPVERLSGGERQRLALIRALLLQPDVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1345382048 163 PTSGLDPQSTEELLGFIADF-ANEGRTVLVSSHLLDVVQTVCTRVALFNRGRI 214
Cdd:COG4619 157 PTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-223 |
5.96e-35 |
|
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: 127.12 E-value: 5.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 4 TVIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGL---TEANagSVRLLDKDPLR-DPLAVKQA 79
Cdd:COG1119 2 PLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDlppTYGN--DVRLFGERRGGeDVWELRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 80 AGYL-PD-AVGFYDSLTARENL--AFTARLAGFADVDAS--GRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMR 153
Cdd:COG1119 80 IGLVsPAlQLRFPRDETVLDVVlsGFFDSIGLYREPTDEqrERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1345382048 154 DCQIMILDEPTSGLDPQSTEELLGFIADFANEGRT--VLVSSHLLDVVQTVcTRVALFNRGRIGFVGTLAEL 223
Cdd:COG1119 160 DPELLILDEPTAGLDLGARELLLALLDKLAAEGAPtlVLVTHHVEEIPPGI-THVLLLKDGRVVAAGPKEEV 230
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
4-225 |
2.00e-34 |
|
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: 125.09 E-value: 2.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 4 TVIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKD--PLRDPLAVKQAAG 81
Cdd:COG0410 2 PMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDitGLPPHRIARLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 82 YLPDAVGFYDSLTARENLaftaRLAGFAdVDASGRIGQALGRV-----RLDGVADRKVGTFSRGMRQRLGLAELLMRDCQ 156
Cdd:COG0410 82 YVPEGRRIFPSLTVEENL----LLGAYA-RRDRAEVRADLERVyelfpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1345382048 157 IMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAELAA 225
Cdd:COG0410 157 LLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
5-223 |
3.69e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 125.58 E-value: 3.69e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 5 VIEARGLTKAY-KGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVrLLDKDPL----RDPLAVKQA 79
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEV-LIKGEPIkydkKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 80 AGYL---PDAVGFydSLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQ 156
Cdd:PRK13639 80 VGIVfqnPDDQLF--APTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1345382048 157 IMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAEL 223
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-285 |
8.90e-34 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 126.37 E-value: 8.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 1 MSGTVIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPlavkqaa 80
Cdd:COG3842 1 MAMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLP------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 81 gylPDA--VGF----YD---SLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELL 151
Cdd:COG3842 74 ---PEKrnVGMvfqdYAlfpHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 152 MRDCQIMILDEPTSGLDPQSTEELLGFIADFANE-GRTVLVSSHLLDVVQTVCTRVALFNRGRI---------------- 214
Cdd:COG3842 151 APEPRVLLLDEPLSALDAKLREEMREELRRLQRElGITFIYVTHDQEEALALADRIAVMNDGRIeqvgtpeeiyerpatr 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1345382048 215 ---GFVGTLAELAAKV-GGDALEIDLEAESFDAAARLSNLNGVDAVIGgdrrwrisasrdLRPEiAARVVESGGR 285
Cdd:COG3842 231 fvaDFIGEANLLPGTVlGDEGGGVRTGGRTLEVPADAGLAAGGPVTVA------------IRPE-DIRLSPEGPE 292
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-228 |
9.74e-34 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 130.34 E-value: 9.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGR--NVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVrLLDKDPLR--DPLAVKQAAG 81
Cdd:COG2274 474 IELENVSFRYPGDspPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRI-LIDGIDLRqiDPASLRRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 82 YLP-DAVGFYDSLtaRENLAFTARLAGFADVDASGRIGQALGRV-RLDGVADRKVG----TFSRGMRQRLGLAELLMRDC 155
Cdd:COG2274 553 VVLqDVFLFSGTI--RENITLGDPDATDEEIIEAARLAGLHDFIeALPMGYDTVVGeggsNLSGGQRQRLAIARALLRNP 630
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1345382048 156 QIMILDEPTSGLDPQSTEELLGFIADFANeGRTVLVSSHLLDVVQtVCTRVALFNRGRIGFVGTLAELAAKVG 228
Cdd:COG2274 631 RILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTIR-LADRIIVLDKGRIVEDGTHEELLARKG 701
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
5-194 |
1.26e-33 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 122.22 E-value: 1.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 5 VIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPLAVKQAAGYLP 84
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 85 DAVGFYDSLTARENLAFTARLAGFADVDAsgrIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPT 164
Cdd:PRK13538 81 HQPGIKTELTALENLRFYQRLHGPGDDEA---LWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPF 157
|
170 180 190
....*....|....*....|....*....|
gi 1345382048 165 SGLDPQSTEELLGFIADFANEGRTVLVSSH 194
Cdd:PRK13538 158 TAIDKQGVARLEALLAQHAEQGGMVILTTH 187
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-190 |
1.45e-33 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 123.66 E-value: 1.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 1 MSGTVIEARGLTKAYKGRN----VVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKdPLRDPLA- 75
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGggvtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGK-PVTGPGPd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 76 ---VKQAAGYLPdavgfydSLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLM 152
Cdd:COG1116 82 rgvVFQEPALLP-------WLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALA 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 1345382048 153 RDCQIMILDEPTSGLDPQSTEELLGFIAD-FANEGRTVL 190
Cdd:COG1116 155 NDPEVLLMDEPFGALDALTRERLQDELLRlWQETGKTVL 193
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-215 |
1.69e-33 |
|
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: 122.20 E-value: 1.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRN----VVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVrLLDKDPLRDPLA----VK 77
Cdd:cd03293 1 LEVRNVSKTYGGGGgavtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEV-LVDGEPVTGPGPdrgyVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 78 QAAGYLPdavgfydSLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQI 157
Cdd:cd03293 80 QQDALLP-------WLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1345382048 158 MILDEPTSGLDPQSTEELLGFIADFANE-GRTVLVSSHLLDVVQTVCTRVALFNR--GRIG 215
Cdd:cd03293 153 LLLDEPFSALDALTREQLQEELLDIWREtGKTVLLVTHDIDEAVFLADRVVVLSArpGRIV 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
6-284 |
8.32e-33 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 124.03 E-value: 8.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKD----PLRDP-LA-VKQa 79
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDvtdlPPKDRnIAmVFQ- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 80 aGYlpdAVgfYDSLTARENLAFTARLAGF--ADVDAsgRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQI 157
Cdd:COG3839 83 -SY---AL--YPHMTVYENIAFPLKLRKVpkAEIDR--RVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 158 MILDEPTSGLDPQSTEELLGFIADFANE-GRTVLVSSHllDVVQ--TVCTRVALFNRGRI-------------------G 215
Cdd:COG3839 155 FLLDEPLSNLDAKLRVEMRAEIKRLHRRlGTTTIYVTH--DQVEamTLADRIAVMNDGRIqqvgtpeelydrpanlfvaG 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1345382048 216 FVGTLA--ELAAKVGGDALEIDleAESFDAAARLSNLNGVDAVIGgdrrwrisasrdLRPEiAARVVESGG 284
Cdd:COG3839 233 FIGSPPmnLLPGTVEGGGVRLG--GVRLPLPAALAAAAGGEVTLG------------IRPE-HLRLADEGD 288
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-222 |
1.08e-32 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 126.33 E-value: 1.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 4 TVIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKdplrdplaVKQaaGYL 83
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGET--------VKI--GYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 84 P-DAVGFYDSLTARENlaftarLAGFADVDASGRIGQALGRVRLDG-VADRKVGTFSRGMRQRLGLAELLMRDCQIMILD 161
Cdd:COG0488 384 DqHQEELDPDKTVLDE------LRDGAPGGTEQEVRGYLGRFLFSGdDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLD 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1345382048 162 EPTSGLDPQSTEELLGFIADFanEGrTVLVSSH---LLDvvqTVCTRVALFNRGRIG-FVGTLAE 222
Cdd:COG0488 458 EPTNHLDIETLEALEEALDDF--PG-TVLLVSHdryFLD---RVATRILEFEDGGVReYPGGYDD 516
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-281 |
1.72e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 122.50 E-value: 1.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 5 VIEARGLTKAYKGR---------------------NVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVR 63
Cdd:COG4586 1 IIEVENLSKTYRVYekepglkgalkglfrreyrevEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 64 LLDKDPLRDPLAVKQAAGylpdAV-G-----FYDsLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTF 137
Cdd:COG4586 81 VLGYVPFKRRKEFARRIG----VVfGqrsqlWWD-LPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 138 SRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQSTEELLGFIADF-ANEGRTVLVSSHLLDVVQTVCTRVALFNRGRIGF 216
Cdd:COG4586 156 SLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIY 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1345382048 217 VGTLAELAAKVGGDAlEIDLEAESFDAAARLSnlNGVDAVIGGDRRWRISASRDLR-PEIAARVVE 281
Cdd:COG4586 236 DGSLEELKERFGPYK-TIVLELAEPVPPLELP--RGGEVIEREGNRVRLEVDPRESlAEVLARLLA 298
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-223 |
1.83e-32 |
|
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: 120.03 E-value: 1.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPlAVKQAAGYLPD 85
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLP-PHKRPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 86 AVGFYDSLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTS 165
Cdd:cd03300 80 NYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1345382048 166 GLDPQSTEELLGFIADFANE-GRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAEL 223
Cdd:cd03300 160 ALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-222 |
2.38e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 120.22 E-value: 2.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 1 MSGTVIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPLAVKQAA 80
Cdd:COG4674 6 MHGPILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIARL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 81 GylpdaVG--F-----YDSLTARENL------------AFTARLAGfADVDasgRIGQALGRVRLDGVADRKVGTFSRGM 141
Cdd:COG4674 86 G-----IGrkFqkptvFEELTVFENLelalkgdrgvfaSLFARLTA-EERD---RIEEVLETIGLTDKADRLAGLLSHGQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 142 RQRLGLAELLMRDCQIMILDEPTSGLDPQSTE---ELLGFIAdfanEGRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVG 218
Cdd:COG4674 157 KQWLEIGMLLAQDPKLLLLDEPVAGMTDAETErtaELLKSLA----GKHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEG 232
|
....
gi 1345382048 219 TLAE 222
Cdd:COG4674 233 SLDE 236
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-223 |
2.45e-32 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 119.71 E-value: 2.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 5 VIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDK---DPLRDPLAVKQAag 81
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEdltDSKKDINKLRRK-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 82 ylpdaVGF-------YDSLTARENLAF---TARLAGFADVDASGRigQALGRVRLDGVADRKVGTFSRGMRQRLGLAELL 151
Cdd:COG1126 79 -----VGMvfqqfnlFPHLTVLENVTLapiKVKKMSKAEAEERAM--ELLERVGLADKADAYPAQLSGGQQQRVAIARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1345382048 152 MRDCQIMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAEL 223
Cdd:COG1126 152 AMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEF 223
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-228 |
3.02e-32 |
|
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: 125.65 E-value: 3.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 2 SGTVIEARGLTKAYKG--RNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLR-DPLAVKQ 78
Cdd:COG4987 330 GGPSLELEDVSFRYPGagRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDlDEDDLRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 79 AAGYLPDAVGFYDSlTARENLAFtarlagfADVDAS-GRIGQALGRVRLDGVADR-------KVG----TFSRGMRQRLG 146
Cdd:COG4987 410 RIAVVPQRPHLFDT-TLRENLRL-------ARPDATdEELWAALERVGLGDWLAAlpdgldtWLGeggrRLSGGERRRLA 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 147 LAELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFAnEGRTVLVSSHLLDVVQTVcTRVALFNRGRIGFVGTLAELAAK 226
Cdd:COG4987 482 LARALLRDAPILLLDEPTEGLDAATEQALLADLLEAL-AGRTVLLITHRLAGLERM-DRILVLEDGRIVEQGTHEELLAQ 559
|
..
gi 1345382048 227 VG 228
Cdd:COG4987 560 NG 561
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-223 |
7.06e-32 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 118.94 E-value: 7.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKG-RNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLR-DPLAVKQAAGYL 83
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREqDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 84 PDAVGFYDSLTARENLAFTARLAGFADVDASGRIGQALGRVRLD--GVADRKVGTFSRGMRQRLGLAELLMRDCQIMILD 161
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1345382048 162 EPTSGLDPQSTEELLGFIADFANE-GRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAEL 223
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-219 |
7.32e-32 |
|
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: 116.37 E-value: 7.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDplrdplavkqaagylpd 85
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKE----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 86 avgfYDSLTAREnlaftARLAGFAdvdasgRIGQalgrvrldgvadrkvgtFSRGMRQRLGLAELLMRDCQIMILDEPTS 165
Cdd:cd03216 64 ----VSFASPRD-----ARRAGIA------MVYQ-----------------LSVGERQMVEIARALARNARLLILDEPTA 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1345382048 166 GLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRIgfVGT 219
Cdd:cd03216 112 ALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV--VGT 163
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-214 |
1.04e-31 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 118.05 E-value: 1.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEAN-----AGSVRLLDKDPL---RDPLAVK 77
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGKDIYdldVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 78 QAAGYL---PDAVgfydSLTARENLAFTARLAGFADVDA-SGRIGQALGRVRLDG-VADR-KVGTFSRGMRQRLGLAELL 151
Cdd:cd03260 81 RRVGMVfqkPNPF----PGSIYDNVAYGLRLHGIKLKEElDERVEEALRKAALWDeVKDRlHALGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1345382048 152 MRDCQIMILDEPTSGLDPQSTEELLGFIADFANEgRTVLVSSHLLDVVQTVCTRVALFNRGRI 214
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-213 |
1.60e-31 |
|
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: 115.56 E-value: 1.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRN--VVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVrLLDKDPLR--DPLAVKQAAG 81
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEI-LIDGVDLRdlDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 82 YLP-DAVGFYDSLtaRENLaftarLagfadvdaSGriGQalgrvrldgvadrkvgtfsrgmRQRLGLAELLMRDCQIMIL 160
Cdd:cd03228 80 YVPqDPFLFSGTI--RENI-----L--------SG--GQ----------------------RQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1345382048 161 DEPTSGLDPQSTEELLGFIADFAnEGRTVLVSSHLLDVVQtVCTRVALFNRGR 213
Cdd:cd03228 121 DEATSALDPETEALILEALRALA-KGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
5-194 |
2.43e-31 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 116.51 E-value: 2.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 5 VIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPlRDPLAVKQAAgYLP 84
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI-DDPDVAEACH-YLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 85 DAVGFYDSLTARENLAFTARLAGfadvDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPT 164
Cdd:PRK13539 80 HRNAMKPALTVAENLEFWAAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPT 155
|
170 180 190
....*....|....*....|....*....|
gi 1345382048 165 SGLDPQSTEELLGFIADFANEGRTVLVSSH 194
Cdd:PRK13539 156 AALDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-214 |
2.47e-31 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 116.69 E-value: 2.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 5 VIEARGLTKAYK-GRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKD----PLRDPLAVKQA 79
Cdd:COG2884 1 MIRFENVSKRYPgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlsrlKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 80 AGY-------LPDavgfydsLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLM 152
Cdd:COG2884 81 IGVvfqdfrlLPD-------RTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1345382048 153 RDCQIMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRI 214
Cdd:COG2884 154 NRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
15-218 |
3.24e-31 |
|
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: 117.05 E-value: 3.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 15 YKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPL-RDPLAVKQAAGYLPDAVGFYDSL 93
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWkRRKKFLRRIGVVFGQKTQLWWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 94 TARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQSTE 173
Cdd:cd03267 111 PVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQE 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1345382048 174 ELLGFIADFANE-GRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVG 218
Cdd:cd03267 191 NIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
5-223 |
7.32e-31 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 115.96 E-value: 7.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 5 VIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVrLLD----KDPLRDPLAVKQAA 80
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDL-IVDglkvNDPKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 81 GYLPDAVGFYDSLTARENLAF-TARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMI 159
Cdd:PRK09493 80 GMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLML 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1345382048 160 LDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAEL 223
Cdd:PRK09493 160 FDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVL 223
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-214 |
1.77e-30 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 115.64 E-value: 1.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 4 TVIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKdPLRDPLAVKQAA--G 81
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGR-PLADWSPAELARrrA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 82 YLPDA--VGFydSLTARENLAFtARLAGFADVDASGRI-GQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLmrdCQ-- 156
Cdd:PRK13548 80 VLPQHssLSF--PFTVEEVVAM-GRAPHGLSRAEDDALvAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVL---AQlw 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1345382048 157 -------IMILDEPTSGLDPQSTEELLGFIADFANE-GRTVLVSSHLLDVVQTVCTRVALFNRGRI 214
Cdd:PRK13548 154 epdgpprWLLLDEPTSALDLAHQHHVLRLARQLAHErGLAVIVVLHDLNLAARYADRIVLLHQGRL 219
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
6-259 |
1.85e-30 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 117.53 E-value: 1.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMlMGLTEANAGsvrlldKDPLR------DPLAVKQA 79
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALP-AHV*GPDAG------RRPWRf*twcaNRRALRRT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 80 AG-YLPDAVGFYDSLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIM 158
Cdd:NF000106 87 IG*HRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 159 ILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAELAAKVGGDALEI-DLE 237
Cdd:NF000106 167 YLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGGRTLQIrPAH 246
|
250 260
....*....|....*....|..
gi 1345382048 238 AESFDAAARLSNLNGVDAVIGG 259
Cdd:NF000106 247 AAELDRMVGAIAQAGLDGIAGA 268
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-226 |
2.21e-30 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 117.10 E-value: 2.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRN----VVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRL-------LDKDPLRdpl 74
Cdd:COG1135 2 IELENLSKTFPTKGgpvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVdgvdltaLSERELR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 75 AVKQAAGYLPDAVGFYDSLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRD 154
Cdd:COG1135 79 AARRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1345382048 155 CQIMILDEPTSGLDPQSTEELLGFIADfANE--GRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAELAAK 226
Cdd:COG1135 159 PKVLLCDEATSALDPETTRSILDLLKD-INRelGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFAN 231
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
17-197 |
2.63e-30 |
|
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: 113.29 E-value: 2.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 17 GRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVrLLDKDPL----RDPLAVKQAAGYL---PDAVGF 89
Cdd:TIGR01166 4 GPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAV-LIDGEPLdysrKGLLERRQRVGLVfqdPDDQLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 90 YDSLTarENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTSGLDP 169
Cdd:TIGR01166 83 AADVD--QDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDP 160
|
170 180
....*....|....*....|....*...
gi 1345382048 170 QSTEELLGFIADFANEGRTVLVSSHLLD 197
Cdd:TIGR01166 161 AGREQMLAILRRLRAEGMTVVISTHDVD 188
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
6-208 |
4.78e-30 |
|
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: 112.97 E-value: 4.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPLAVKQAAGYLPD 85
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 86 AVGFYDSLTARENLAFtarlagFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTS 165
Cdd:cd03231 81 APGIKTTLSVLENLRF------WHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1345382048 166 GLDPQSTEELLGFIADFANEGRTVLVSSHL-LDVVQTVCTRVAL 208
Cdd:cd03231 155 ALDKAGVARFAEAMAGHCARGGMVVLTTHQdLGLSEAGARELDL 198
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-221 |
7.53e-30 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 118.20 E-value: 7.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 2 SGTVIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKD-PLRDPLAVkQAA 80
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPvRFRSPRDA-QAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 81 GylpdaVGF-------YDSLTARENLAFTARLAGFADVDASG---RIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAEL 150
Cdd:COG1129 80 G-----IAIihqelnlVPNLSVAENIFLGREPRRGGLIDWRAmrrRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1345382048 151 LMRDCQIMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRigFVGTLA 221
Cdd:COG1129 155 LSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGR--LVGTGP 223
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
8-225 |
1.57e-29 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 112.68 E-value: 1.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 8 ARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPL--AVKQAAGYLPD 85
Cdd:PRK10895 6 AKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhaRARRGIGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 86 AVGFYDSLTARENLafTARLAGFADVDASGRIGQA---LGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDE 162
Cdd:PRK10895 86 EASIFRRLSVYDNL--MAVLQIRDDLSAEQREDRAnelMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1345382048 163 PTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAELAA 225
Cdd:PRK10895 164 PFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6-194 |
1.81e-29 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 111.30 E-value: 1.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPLAVKQAAGYLPD 85
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 86 AVGFYDSLTARENLAFTARLAGFADVDASgrigQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTS 165
Cdd:TIGR01189 81 LPGLKPELSALENLHFWAAIHGGAQRTIE----DALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180
....*....|....*....|....*....
gi 1345382048 166 GLDPQSTEELLGFIADFANEGRTVLVSSH 194
Cdd:TIGR01189 157 ALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
6-214 |
2.05e-29 |
|
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: 111.53 E-value: 2.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKG--RNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVrLLDKDPLR--DPLAVKQAAG 81
Cdd:cd03245 3 IEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSV-LLDGTDIRqlDPADLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 82 YLP-DAVGFYDSLtaRENLAFTARLAGFADVDASGRIGQALGRVRLDGVA-DRKVG----TFSRGMRQRLGLAELLMRDC 155
Cdd:cd03245 82 YVPqDVTLFYGTL--RDNITLGAPLADDERILRAAELAGVTDFVNKHPNGlDLQIGergrGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1345382048 156 QIMILDEPTSGLDPQSTEELLGFIADFAnEGRTVLVSSH---LLDVVqtvcTRVALFNRGRI 214
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHrpsLLDLV----DRIIVMDSGRI 216
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
26-223 |
4.86e-29 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 110.71 E-value: 4.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 26 LTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPLAVkqaaGYLPDAVGF---------YDSLTAR 96
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKGWRHI----GYVPQRHEFawdfpisvaHTVMSGR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 97 ENLAFTARLAGFADVDAsgrIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQSTEELL 176
Cdd:TIGR03771 77 TGHIGWLRRPCVADFAA---VRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLT 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1345382048 177 GFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNrGRIGFVGTLAEL 223
Cdd:TIGR03771 154 ELFIELAGAGTAILMTTHDLAQAMATCDRVVLLN-GRVIADGTPQQL 199
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
5-223 |
5.08e-29 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 111.24 E-value: 5.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 5 VIEARGLTKAY-KGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKD----PLRDPLAVKQA 79
Cdd:TIGR02315 1 MLEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDitklRGKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 80 AGYLPDAVGFYDSLTARENLaFTARLAG----------FADVDASgRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAE 149
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENV-LHGRLGYkptwrsllgrFSEEDKE-RALSALERVGLADKAYQRADQLSGGQQQRVAIAR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1345382048 150 LLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANE-GRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAEL 223
Cdd:TIGR02315 159 ALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
12-218 |
5.11e-29 |
|
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: 110.82 E-value: 5.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 12 TKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTE--ANAGSVRLLDKDPlRDPLAVKQAAGYLPDAVGF 89
Cdd:cd03234 14 KNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEggGTTSGQILFNGQP-RKPDQFQKCVAYVRQDDIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 90 YDSLTARENLAFTARLAG---FAD-----VDASGRIGQ-ALGRVRldgvaDRKVGTFSRGMRQRLGLAELLMRDCQIMIL 160
Cdd:cd03234 93 LPGLTVRETLTYTAILRLprkSSDairkkRVEDVLLRDlALTRIG-----GNLVKGISGGERRRVSIAVQLLWDPKVLIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1345382048 161 DEPTSGLDPQSTEELLGFIADFANEGRTVLVSSH--------LLDvvqtvctRVALFNRGRIGFVG 218
Cdd:cd03234 168 DEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHqprsdlfrLFD-------RILLLSSGEIVYSG 226
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-223 |
5.57e-29 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 113.70 E-value: 5.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 1 MSgtvIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDpLAVKQAa 80
Cdd:COG1118 1 MS---IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTN-LPPRER- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 81 gylpdAVGF----YD---SLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMR 153
Cdd:COG1118 76 -----RVGFvfqhYAlfpHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1345382048 154 DCQIMILDEPTSGLDPQSTEE----LLGFIADFaneGRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAEL 223
Cdd:COG1118 151 EPEVLLLDEPFGALDAKVRKElrrwLRRLHDEL---GGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
15-218 |
1.64e-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: 109.54 E-value: 1.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 15 YKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLrdPLAVkqaagylpdAVGFYDSLT 94
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSS--LLGL---------GGGFNPELT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 95 ARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQSTEE 174
Cdd:cd03220 101 GRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEK 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1345382048 175 LLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVG 218
Cdd:cd03220 181 CQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-214 |
2.44e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 114.01 E-value: 2.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 8 ARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLlDKDpLRdplavkqaAGYLPDAV 87
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI-PKG-LR--------IGYLPQEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 88 GFYDSLTARENLA------------FTARLAGFADVDASG--------------------RIGQALGRVRLDGV-ADRKV 134
Cdd:COG0488 71 PLDDDLTVLDTVLdgdaelraleaeLEELEAKLAEPDEDLerlaelqeefealggweaeaRAEEILSGLGFPEEdLDRPV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 135 GTFSRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANegrTVLVSSH---LLDvvqTVCTRVALFNR 211
Cdd:COG0488 151 SELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPG---TVLVVSHdryFLD---RVATRILELDR 224
|
...
gi 1345382048 212 GRI 214
Cdd:COG0488 225 GKL 227
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-218 |
2.56e-28 |
|
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: 108.50 E-value: 2.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDpLRDPLAVKQAAGYLPD 85
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRD-VTDLPPKDRDIAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 86 AVGFYDSLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTS 165
Cdd:cd03301 80 NYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1345382048 166 GLDPQSTEELLGFIADFANE-GRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVG 218
Cdd:cd03301 160 NLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
24-225 |
2.62e-28 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 109.07 E-value: 2.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 24 INLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPLAVKqaagylPDAVGFYD-----SLTAREN 98
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAER------PVSMLFQEnnlfpHLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 99 LAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQSTEELLGF 178
Cdd:COG3840 92 IGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1345382048 179 IADFANE-GRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAELAA 225
Cdd:COG3840 172 VDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLD 219
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
6-214 |
2.97e-28 |
|
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: 108.26 E-value: 2.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRNV-VDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPlavKQAAGYLP 84
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLR---GRAIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 85 DAVG--FYDS-----LTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQI 157
Cdd:cd03292 78 RKIGvvFQDFrllpdRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1345382048 158 MILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRI 214
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-226 |
5.46e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 109.55 E-value: 5.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 1 MSGTVIEARGLTKAYK-GRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVrLLDKDPL----RDPLA 75
Cdd:PRK13636 1 MEDYILKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRI-LFDGKPIdysrKGLMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 76 VKQAAGYL---PDAVGFydSLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLM 152
Cdd:PRK13636 80 LRESVGMVfqdPDNQLF--SASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1345382048 153 RDCQIMILDEPTSGLDPQSTEELLGFIADFANE-GRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAELAAK 226
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
9-219 |
6.08e-28 |
|
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: 113.96 E-value: 6.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 9 RGLTKAYK--GRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPLAVKQAAGYLPDA 86
Cdd:TIGR01257 932 KNLVKIFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQH 1011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 87 VGFYDSLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTSG 166
Cdd:TIGR01257 1012 NILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSG 1091
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1345382048 167 LDPQSTEELLGFIADFaNEGRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGT 219
Cdd:TIGR01257 1092 VDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
6-223 |
7.76e-28 |
|
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: 108.20 E-value: 7.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPLAVKQaagylpd 85
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERN------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 86 aVGF-------YDSLTARENLAFTARLAGFADVDAS----GRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRD 154
Cdd:cd03296 76 -VGFvfqhyalFRHMTVFDNVAFGLRVKPRSERPPEaeirAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 155 CQIMILDEPTSGLDPQSTEELLGFIADFANE-GRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAEL 223
Cdd:cd03296 155 PKVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-218 |
1.16e-27 |
|
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: 105.86 E-value: 1.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRN--VVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPLAVKQAAGYL 83
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 84 PDAVGFYDSlTARENLaftarlagfadvdasgrigqalGRvrldgvadrkvgTFSRGMRQRLGLAELLMRDCQIMILDEP 163
Cdd:cd03247 81 NQRPYLFDT-TLRNNL----------------------GR------------RFSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1345382048 164 TSGLDPQSTEELLGFIADFAnEGRTVLVSSHLLDVVQTVcTRVALFNRGRIGFVG 218
Cdd:cd03247 126 TVGLDPITERQLLSLIFEVL-KDKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-222 |
2.03e-27 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 107.51 E-value: 2.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKD----PLRDpLAVKQAAg 81
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPlaawSPWE-LARRRAV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 82 yLPDA--VGFydSLTARENLAFtARLAGFAD-VDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLmrdCQI- 157
Cdd:COG4559 80 -LPQHssLAF--PFTVEEVVAL-GRAPHGSSaAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVL---AQLw 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1345382048 158 ---------MILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAE 222
Cdd:COG4559 153 epvdggprwLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
6-228 |
2.48e-27 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 111.41 E-value: 2.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAY-KGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVrLLDKDPLRD--PLAVKQAAGY 82
Cdd:COG1132 340 IEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRI-LIDGVDIRDltLESLRRQIGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 83 LP-DAVGFYDSLtaRENLAFTARLAGFADVDASGRIGQALGRVR-----LDGVADRKVGTFSRGMRQRLGLAELLMRDCQ 156
Cdd:COG1132 419 VPqDTFLFSGTI--RENIRYGRPDATDEEVEEAAKAAQAHEFIEalpdgYDTVVGERGVNLSGGQRQRIAIARALLKDPP 496
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1345382048 157 IMILDEPTSGLDPQSTEELLGFIADFAnEGRTVLVSSHLLDVVQTvCTRVALFNRGRIGFVGTLAELAAKVG 228
Cdd:COG1132 497 ILILDEATSALDTETEALIQEALERLM-KGRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHEELLARGG 566
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-221 |
2.92e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 110.88 E-value: 2.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 4 TVIEARGLTkaykGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKD-PLRDPL-AVKQAAG 81
Cdd:COG1129 255 VVLEVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPvRIRSPRdAIRAGIA 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 82 YLPD---AVGFYDSLTAREN--LAFTARLAGF------ADVDASGRIGQALgRVRLDGVaDRKVGTFSRGMRQRLGLAEL 150
Cdd:COG1129 331 YVPEdrkGEGLVLDLSIRENitLASLDRLSRGglldrrRERALAEEYIKRL-RIKTPSP-EQPVGNLSGGNQQKVVLAKW 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1345382048 151 LMRDCQIMILDEPTSGLDPQSTEELLGFIADFANEGRTVLV-SSHLLDVVQtVCTRVALFNRGRIgfVGTLA 221
Cdd:COG1129 409 LATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIViSSELPELLG-LSDRILVMREGRI--VGELD 477
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
15-226 |
3.97e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 107.02 E-value: 3.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 15 YKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVrLLDKDPL----RDPLAVKQAAGYL---PDAV 87
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAV-LWQGKPLdyskRGLLALRQQVATVfqdPEQQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 88 GFYDSLTAreNLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTSGL 167
Cdd:PRK13638 90 IFYTDIDS--DIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1345382048 168 DPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAELAAK 226
Cdd:PRK13638 168 DPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFAC 226
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-223 |
4.70e-27 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 108.77 E-value: 4.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 5 VIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVrLLDKDPLRDPLAVKQAAGYLP 84
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQI-MLDGVDLSHVPPYQRPINMMF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 85 DAVGFYDSLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPT 164
Cdd:PRK11607 98 QSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPM 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 165 SGLDPQSTEELLGFIADFANE-GRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAEL 223
Cdd:PRK11607 178 GALDKKLRDRMQLEVVDILERvGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-223 |
8.16e-27 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 105.84 E-value: 8.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 1 MSGTVIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKdplrdplavkQAA 80
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQ----------HIE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 81 GyLPDA-------------VGFYDSLTARENLAF-------TARLAGF--------ADVDASGRIGQALGRVRLDGVADR 132
Cdd:PRK11300 71 G-LPGHqiarmgvvrtfqhVRLFREMTVIENLLVaqhqqlkTGLFSGLlktpafrrAESEALDRAATWLERVGLLEHANR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 133 KVGTFSRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANE-GRTVLVSSHLLDVVQTVCTRVALFNR 211
Cdd:PRK11300 150 QAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQ 229
|
250
....*....|..
gi 1345382048 212 GRIGFVGTLAEL 223
Cdd:PRK11300 230 GTPLANGTPEEI 241
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-214 |
1.40e-26 |
|
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: 102.90 E-value: 1.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 4 TVIEARGLTkaykGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKD-PLRDPL-AVKQAAG 81
Cdd:cd03215 3 PVLEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPvTRRSPRdAIRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 82 YLPD---AVGFYDSLTARENLAFTARLAGfadvdasgrigqalgrvrldgvadrkvgtfsrGMRQRLGLAELLMRDCQIM 158
Cdd:cd03215 79 YVPEdrkREGLVLDLSVAENIALSSLLSG--------------------------------GNQQKVVLARWLARDPRVL 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1345382048 159 ILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRI 214
Cdd:cd03215 127 ILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
4-214 |
2.01e-26 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 104.45 E-value: 2.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 4 TVIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLD------------KDPLR 71
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDitidtarslsqqKGLIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 72 dplAVKQAAGYLPDAVGFYDSLTAREN-LAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAEL 150
Cdd:PRK11264 82 ---QLRQHVGFVFQNFNLFPHRTVLENiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1345382048 151 LMRDCQIMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRI 214
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-168 |
2.24e-26 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 106.96 E-value: 2.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 1 MSGTVIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKD----PL--RDPL 74
Cdd:PRK09452 10 SLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDithvPAenRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 75 AVKQAAGYLPdavgfydSLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRD 154
Cdd:PRK09452 90 TVFQSYALFP-------HMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNK 162
|
170
....*....|....
gi 1345382048 155 CQIMILDEPTSGLD 168
Cdd:PRK09452 163 PKVLLLDESLSALD 176
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
5-222 |
3.22e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 104.43 E-value: 3.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 5 VIEARGLTKAYK-GRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKD-PLRDPLAVKQAAGY 82
Cdd:PRK13647 4 IIEVEDLHFRYKdGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREvNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 83 L---PDAVGFydSLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMI 159
Cdd:PRK13647 84 VfqdPDDQVF--SSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1345382048 160 LDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRigfvgTLAE 222
Cdd:PRK13647 162 LDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGR-----VLAE 219
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
5-223 |
5.68e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 104.11 E-value: 5.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 5 VIEARGLTKAYKG-RNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRL----LDKDPLRDplaVKQA 79
Cdd:PRK13652 3 LIETRDLCYSYSGsKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIrgepITKENIRE---VRKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 80 AGYL---PDAVGFydSLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQ 156
Cdd:PRK13652 80 VGLVfqnPDDQIF--SPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1345382048 157 IMILDEPTSGLDPQSTEELLGFIADFANE-GRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAEL 223
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
9-227 |
5.74e-26 |
|
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: 107.20 E-value: 5.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 9 RGLTKAykgrnvVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRD-----PLA---VKQAA 80
Cdd:TIGR03269 294 RGVVKA------VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDmtkpgPDGrgrAKRYI 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 81 GYLPDAVGFYDSLTARENLA-----------------FTARLAGFADVDAsgrigqalgrvrlDGVADRKVGTFSRGMRQ 143
Cdd:TIGR03269 368 GILHQEYDLYPHRTVLDNLTeaiglelpdelarmkavITLKMVGFDEEKA-------------EEILDKYPDELSEGERH 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 144 RLGLAELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANE-GRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAE 222
Cdd:TIGR03269 435 RVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEE 514
|
....*
gi 1345382048 223 LAAKV 227
Cdd:TIGR03269 515 IVEEL 519
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
6-194 |
8.49e-26 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 106.99 E-value: 8.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGR-NVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRL-------LDKDPLRDPLA-V 76
Cdd:TIGR02857 322 LEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVngvpladADADSWRDQIAwV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 77 KQA----AGYLPDAVGFYDSLTARENLAFTARLAGFADVDASgrIGQALGRVrldgVADRKVGtFSRGMRQRLGLAELLM 152
Cdd:TIGR02857 402 PQHpflfAGTIAENIRLARPDASDAEIREALERAGLDEFVAA--LPQGLDTP----IGEGGAG-LSGGQAQRLALARAFL 474
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1345382048 153 RDCQIMILDEPTSGLDPQSTEELLGFIADFAnEGRTVLVSSH 194
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTH 515
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-223 |
1.24e-25 |
|
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: 102.91 E-value: 1.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAY-KG----RNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDP-------LRDp 73
Cdd:TIGR04521 1 IKLKNVSYIYqPGtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDItakkkkkLKD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 74 laVKQAAGYL---PDAVGFYDslTARENLAFTARLAGFADVDASGRIGQALGRVRLD-GVADRKVGTFSRGMRQRLGLAE 149
Cdd:TIGR04521 80 --LRKKVGLVfqfPEHQLFEE--TVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDeEYLERSPFELSGGQMRRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1345382048 150 LLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANE-GRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAEL 223
Cdd:TIGR04521 156 VLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEkGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREV 230
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-223 |
1.33e-25 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 106.29 E-value: 1.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 5 VIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLR-DPLAVKQAAGYL 83
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARlTPAKAHQLGIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 84 -PDAVGFYDSLTARENLAFtaRLAGFAdvDASGRIGQALGR--VRLD--------GVADRKVGTFSRGmrqrlglaelLM 152
Cdd:PRK15439 91 vPQEPLLFPNLSVKENILF--GLPKRQ--ASMQKMKQLLAAlgCQLDldssagslEVADRQIVEILRG----------LM 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1345382048 153 RDCQIMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAEL 223
Cdd:PRK15439 157 RDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6-222 |
1.71e-25 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 101.64 E-value: 1.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKgRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPlAVKQAAGYLPD 85
Cdd:cd03299 1 LKVENLSKDWK-EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLP-PEKRDISYVPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 86 AVGFYDSLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTS 165
Cdd:cd03299 79 NYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1345382048 166 GLDPQSTEELLGFIADFANE-GRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAE 222
Cdd:cd03299 159 ALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEE 216
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
25-218 |
3.62e-25 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 100.32 E-value: 3.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 25 NLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPlAVKQAAGYLPDAVGFYDSLTARENLAFTAR 104
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLA-PYQRPVSMLFQENNLFAHLTVRQNIGLGLH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 105 LAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFAN 184
Cdd:TIGR01277 97 PGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCS 176
|
170 180 190
....*....|....*....|....*....|....*
gi 1345382048 185 E-GRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVG 218
Cdd:TIGR01277 177 ErQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
14-199 |
3.80e-25 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 99.62 E-value: 3.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 14 AYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLrdplavkqaaGYLPDAVGFYDSL 93
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARV----------AYVPQRSEVPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 94 --TARE--NLAFTARLAGFADVDASGR--IGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTSGL 167
Cdd:NF040873 71 plTVRDlvAMGRWARRGLWRRLTRDDRaaVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190
....*....|....*....|....*....|..
gi 1345382048 168 DPQSTEELLGFIADFANEGRTVLVSSHLLDVV 199
Cdd:NF040873 151 DAESRERIIALLAEEHARGATVVVVTHDLELV 182
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
3-243 |
4.32e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 103.77 E-value: 4.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 3 GTVIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVrLLDKDPL--RDPLAVKQAA 80
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTV-LVAGDDVeaLSARAASRRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 81 GYLPD--AVGFYDSLTARENLAFTARLAGFADVDASGR--IGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQ 156
Cdd:PRK09536 80 ASVPQdtSLSFEFDVRQVVEMGRTPHRSRFDTWTETDRaaVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 157 IMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRIgfvgtlaeLAAKVGGDALEIDL 236
Cdd:PRK09536 160 VLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRV--------RAAGPPADVLTADT 231
|
....*..
gi 1345382048 237 EAESFDA 243
Cdd:PRK09536 232 LRAAFDA 238
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-214 |
4.78e-25 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 100.47 E-value: 4.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 1 MSgtvIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKD-PLRDPLAVKQA 79
Cdd:COG4161 1 MS---IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfDFSQKPSEKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 80 AGyLPDAVG-------FYDSLTARENL-AFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELL 151
Cdd:COG4161 78 RL-LRQKVGmvfqqynLWPHLTVMENLiEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1345382048 152 MRDCQIMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRI 214
Cdd:COG4161 157 MMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-214 |
6.05e-25 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 100.47 E-value: 6.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 1 MSgtvIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRL------LDKDP-LRDP 73
Cdd:PRK11124 1 MS---IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagnhfdFSKTPsDKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 74 LAVKQAAGYLPDAVGFYDSLTARENL-AFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLM 152
Cdd:PRK11124 78 RELRRNVGMVFQQYNLWPHLTVQQNLiEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1345382048 153 RDCQIMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRI 214
Cdd:PRK11124 158 MEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-214 |
1.43e-24 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 100.90 E-value: 1.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 5 VIEARGLTKAYKGRN----VVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANA---GSVRLLDKDPLRdpLAVK 77
Cdd:COG0444 1 LLEVRNLKVYFPTRRgvvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLK--LSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 78 QAAGYLPDAVGF-----YDSL----TARENLAFTARLAGFADV-DASGRIGQALGRVRLDG---VADRKVGTFSRGMRQR 144
Cdd:COG0444 79 ELRKIRGREIQMifqdpMTSLnpvmTVGDQIAEPLRIHGGLSKaEARERAIELLERVGLPDperRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1345382048 145 LGLAELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANE-GRTVLVSSHLLDVVQTVCTRVALFNRGRI 214
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRI 229
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-239 |
1.73e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 99.32 E-value: 1.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 4 TVIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKdPLRDpLAVKQAAGY- 82
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDK-PISM-LSSRQLARRl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 83 --LPDAVGFYDSLTARE--------NLAFTARLAGfadvDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLM 152
Cdd:PRK11231 79 alLPQHHLTPEGITVRElvaygrspWLSLWGRLSA----EDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 153 RDCQIMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGT-----LAELAAKV 227
Cdd:PRK11231 155 QDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTpeevmTPGLLRTV 234
|
250
....*....|..
gi 1345382048 228 ggdaleIDLEAE 239
Cdd:PRK11231 235 ------FDVEAE 240
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-212 |
1.92e-24 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 102.94 E-value: 1.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 1 MSGTVIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDK--DPLRDPLAVKQ 78
Cdd:PRK09700 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNInyNKLDHKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 79 AAGYLPDAVGFYDSLTARENLaFTARLA-----GFADVDAS---GRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAEL 150
Cdd:PRK09700 81 GIGIIYQELSVIDELTVLENL-YIGRHLtkkvcGVNIIDWRemrVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1345382048 151 LMRDCQIMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRG 212
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-233 |
2.02e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 100.12 E-value: 2.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 1 MSgtvIEARGLTKAY-KG----RNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDP------ 69
Cdd:PRK13637 1 MS---IKIENLTHIYmEGtpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdkkvk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 70 LRDplaVKQAAGYL---PDAVGFYDslTARENLAFTARLAGFADVDASGRIGQALGRVRLD--GVADRKVGTFSRGMRQR 144
Cdd:PRK13637 78 LSD---IRKKVGLVfqyPEYQLFEE--TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 145 LGLAELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANE-GRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAEL 223
Cdd:PRK13637 153 VAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
250
....*....|
gi 1345382048 224 AAKVggDALE 233
Cdd:PRK13637 233 FKEV--ETLE 240
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-219 |
2.49e-24 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 99.32 E-value: 2.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 4 TVIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGS---VRLLDKDP------LRDPL 74
Cdd:PRK09984 3 TIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAgshIELLGRTVqregrlARDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 75 AVKQAAGYLPDAVGFYDSLTARENLAFTAR---------LAGFADVDASgRIGQALGRVRLDGVADRKVGTFSRGMRQRL 145
Cdd:PRK09984 83 KSRANTGYIFQQFNLVNRLSVLENVLIGALgstpfwrtcFSWFTREQKQ-RALQALTRVGMVHFAHQRVSTLSGGQQQRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1345382048 146 GLAELLMRDCQIMILDEPTSGLDPQSTEELLGFIADF-ANEGRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGT 219
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
3-218 |
2.51e-24 |
|
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: 97.24 E-value: 2.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 3 GTVIEARGLTKAYKGRN------VVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANA--GSVRLLDKDplRDPL 74
Cdd:cd03213 1 GVTLSFRNLTVTVKSSPsksgkqLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRP--LDKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 75 AVKQAAGYLPDAVGFYDSLTARENLAFTARLAGFadvdaSGrigqalgrvrldgvadrkvgtfsrGMRQRLGLA-ELLMR 153
Cdd:cd03213 79 SFRKIIGYVPQDDILHPTLTVRETLMFAAKLRGL-----SG------------------------GERKRVSIAlELVSN 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1345382048 154 DcQIMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSH-LLDVVQTVCTRVALFNRGRIGFVG 218
Cdd:cd03213 130 P-SLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHqPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
16-228 |
6.38e-24 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 97.30 E-value: 6.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 16 KGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVrLLDKDPLRD-PLAV--KQAAGYLPDAVGFYDs 92
Cdd:cd03251 13 DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRI-LIDGHDVRDyTLASlrRQIGLVSQDVFLFND- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 93 lTARENLAFTARLAGFADVDASGRIGQALGRV-RLDGVADRKVG----TFSRGMRQRLGLAELLMRDCQIMILDEPTSGL 167
Cdd:cd03251 91 -TVAENIAYGRPGATREEVEEAARAANAHEFImELPEGYDTVIGergvKLSGGQRQRIAIARALLKDPPILILDEATSAL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1345382048 168 DPQStEELLGFIADFANEGRTVLVSSHLLDVVQTVcTRVALFNRGRIGFVGTLAELAAKVG 228
Cdd:cd03251 170 DTES-ERLVQAALERLMKNRTTFVIAHRLSTIENA-DRIVVLEDGKIVERGTHEELLAQGG 228
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-224 |
7.83e-24 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 101.14 E-value: 7.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 2 SGTVIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLlDKDPL-----RDPLA- 75
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILI-DGQEMrfastTAALAa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 76 ----VKQAAGYLPDavgfydsLTARENLaFTARL---AGFADV-DASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGL 147
Cdd:PRK11288 80 gvaiIYQELHLVPE-------MTVAENL-YLGQLphkGGIVNRrLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1345382048 148 AELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRigFVGTLAELA 224
Cdd:PRK11288 152 AKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGR--YVATFDDMA 226
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-237 |
9.51e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 97.78 E-value: 9.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 1 MSGTVIEARGLTKAYKG--RNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRL----LDKDPLRDpl 74
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVggmvLSEETVWD-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 75 aVKQAAGYL---PDA--VGfydsLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAE 149
Cdd:PRK13635 79 -VRRQVGMVfqnPDNqfVG----ATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 150 LLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANEGR-TVLVSSHLLDVVQTVcTRVALFNRGRIGFVGTLAELaAKVG 228
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQA-DRVIVMNKGEILEEGTPEEI-FKSG 231
|
....*....
gi 1345382048 229 GDALEIDLE 237
Cdd:PRK13635 232 HMLQEIGLD 240
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
6-227 |
1.00e-23 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 100.98 E-value: 1.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRN--VVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRlLDKDPLR--DPLAVKQAAG 81
Cdd:COG4618 331 LSVENLTVVPPGSKrpILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVR-LDGADLSqwDREELGRHIG 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 82 YLPDAVGFYDSlTARENlaftarLAGFADVDASgRIGQAlgrVRLDGVA----------DRKVG----TFSRGMRQRLGL 147
Cdd:COG4618 410 YLPQDVELFDG-TIAEN------IARFGDADPE-KVVAA---AKLAGVHemilrlpdgyDTRIGeggaRLSGGQRQRIGL 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 148 AELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQtVCTRVALFNRGRIGFVGTLAELAAKV 227
Cdd:COG4618 479 ARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLA-AVDKLLVLRDGRVQAFGPRDEVLARL 557
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
21-223 |
3.45e-23 |
|
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: 96.17 E-value: 3.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 21 VDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVrLLDKDPL------------RDPLA-VKQAAGYLPdav 87
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKV-LIDGQDIaamsrkelrelrRKKISmVFQSFALLP--- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 88 gfydSLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTSGL 167
Cdd:cd03294 116 ----HRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSAL 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 168 DP----QSTEELLGFIadfANEGRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAEL 223
Cdd:cd03294 192 DPlirrEMQDELLRLQ---AELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEI 248
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
16-228 |
3.90e-23 |
|
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: 94.98 E-value: 3.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 16 KGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVrLLDKDPLRD-PLAV--KQAAGYLPDAVGFYDS 92
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQI-LIDGIDIRDiSRKSlrSMIGVVLQDTFLFSGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 93 LtaRENLAFTARLAGFADVDASGRIGQALGRVR-----LDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTSGL 167
Cdd:cd03254 93 I--MENIRLGRPNATDEEVIEAAKEAGAHDFIMklpngYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNI 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1345382048 168 DPqSTEELLGFIADFANEGRTVLVSSHLLDVVQTVcTRVALFNRGRIGFVGTLAELAAKVG 228
Cdd:cd03254 171 DT-ETEKLIQEALEKLMKGRTSIIIAHRLSTIKNA-DKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-214 |
4.34e-23 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 97.18 E-value: 4.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 5 VIEARGLTKAYKGR----NVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRL-------LDKDPLRdp 73
Cdd:PRK11153 1 MIELKNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVdgqdltaLSEKELR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 74 LAVKQaagylpdaVG-----FY--DSLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLG 146
Cdd:PRK11153 79 KARRQ--------IGmifqhFNllSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1345382048 147 LAELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANE-GRTVLVSSHLLDVVQTVCTRVALFNRGRI 214
Cdd:PRK11153 151 IARALASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-233 |
8.47e-23 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 98.66 E-value: 8.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 5 VIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTtilmLMGLTeANA-----GSVRLLDKDpLRDPlAVKQA 79
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSS----LLSLI-AGArkiqqGRVEVLGGD-MADA-RHRRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 80 AG----YLPDAVG--FYDSLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMR 153
Cdd:NF033858 74 VCpriaYMPQGLGknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 154 DCQIMILDEPTSGLDPQSTEELLGFIADF--ANEGRTVLVSS----------HLldvvqtvctrVALfNRGRIGFVGTLA 221
Cdd:NF033858 154 DPDLLILDEPTTGVDPLSRRQFWELIDRIraERPGMSVLVATaymeeaerfdWL----------VAM-DAGRVLATGTPA 222
|
250
....*....|..
gi 1345382048 222 ELAAKVGGDALE 233
Cdd:NF033858 223 ELLARTGADTLE 234
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-168 |
1.17e-22 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 94.54 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 4 TVIEARGLTKAYKGRN----VVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLlDKDPLRDPLA---- 75
Cdd:COG4525 2 SMLTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITL-DGVPVTGPGAdrgv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 76 VKQAAGYLPdavgfydSLTARENLAFTARLAGfadVDASGRIGQA---LGRVRLDGVADRKVGTFSRGMRQRLGLAELLM 152
Cdd:COG4525 81 VFQKDALLP-------WLNVLDNVAFGLRLRG---VPKAERRARAeelLALVGLADFARRRIWQLSGGMRQRVGIARALA 150
|
170
....*....|....*.
gi 1345382048 153 RDCQIMILDEPTSGLD 168
Cdd:COG4525 151 ADPRFLLMDEPFGALD 166
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-213 |
1.62e-22 |
|
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: 90.97 E-value: 1.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLrdplavkqaaGYLPd 85
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKI----------GYFE- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 86 avgfydsltarenlaftarlagfadvdasgrigQalgrvrldgvadrkvgtFSRGMRQRLGLAELLMRDCQIMILDEPTS 165
Cdd:cd03221 70 ---------------------------------Q-----------------LSGGEKMRLALAKLLLENPNLLLLDEPTN 99
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1345382048 166 GLDPQSTEELLGFIADFAnegRTVLVSSHLLDVVQTVCTRVALFNRGR 213
Cdd:cd03221 100 HLDLESIEALEEALKEYP---GTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
29-224 |
1.93e-22 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 97.43 E-value: 1.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 29 KQGEVLGLLGPNGAGKTTTILMLMGLTEANA--GSVRLLDKDPLrDPLAVKQAAGYLPDAVGFYDSLTARENLAFTARLA 106
Cdd:TIGR00955 49 KPGELLAVMGSSGAGKTTLMNALAFRSPKGVkgSGSVLLNGMPI-DAKEMRAISAYVQQDDLFIPTLTVREHLMFQAHLR 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 107 GFADVDASG---RIGQALGRVRLDGVADRKVGT------FSRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQSTEELLG 177
Cdd:TIGR00955 128 MPRRVTKKEkreRVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQ 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1345382048 178 FIADFANEGRTVLV-----SSHLLDVVQTVCtrvaLFNRGRIGFVGTLAELA 224
Cdd:TIGR00955 208 VLKGLAQKGKTIICtihqpSSELFELFDKII----LMAEGRVAYLGSPDQAV 255
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
6-194 |
2.02e-22 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 94.00 E-value: 2.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLlDKDPLRDPLA----VKQAAG 81
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITL-DGKPVEGPGAergvVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 82 YLPdavgfydSLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILD 161
Cdd:PRK11248 81 LLP-------WRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLD 153
|
170 180 190
....*....|....*....|....*....|....*.
gi 1345382048 162 EPTSGLDPQSTE---ELLgfIADFANEGRTVLVSSH 194
Cdd:PRK11248 154 EPFGALDAFTREqmqTLL--LKLWQETGKQVLLITH 187
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
5-237 |
2.38e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 94.03 E-value: 2.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 5 VIEARGLTKAYKG---RNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVrLLDKDPL--RDPLAVKQA 79
Cdd:PRK13650 4 IIEVKNLTFKYKEdqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQI-IIDGDLLteENVWDIRHK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 80 AGYL---PDA--VGfydsLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRD 154
Cdd:PRK13650 83 IGMVfqnPDNqfVG----ATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 155 CQIMILDEPTSGLDPQSTEELLGFIADFANE-GRTVLVSSHLLDVVqTVCTRVALFNRGRIGFVGTLAELAAKvGGDALE 233
Cdd:PRK13650 159 PKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELFSR-GNDLLQ 236
|
....
gi 1345382048 234 IDLE 237
Cdd:PRK13650 237 LGLD 240
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
6-228 |
2.77e-22 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 96.71 E-value: 2.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRN--VVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVrLLDKDPLRDPLAV---KQAA 80
Cdd:TIGR02203 331 VEFRNVTFRYPGRDrpALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQI-LLDGHDLADYTLAslrRQVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 81 GYLPDAVGFYDSLTAreNLAFTARL-AGFADVDASGRIGQALGRV-RLDGVADRKVGT----FSRGMRQRLGLAELLMRD 154
Cdd:TIGR02203 410 LVSQDVVLFNDTIAN--NIAYGRTEqADRAEIERALAAAYAQDFVdKLPLGLDTPIGEngvlLSGGQRQRLAIARALLKD 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1345382048 155 CQIMILDEPTSGLDPQStEELLGFIADFANEGRTVLVSSHLLDVVQTVcTRVALFNRGRIGFVGTLAELAAKVG 228
Cdd:TIGR02203 488 APILILDEATSALDNES-ERLVQAALERLMQGRTTLVIAHRLSTIEKA-DRIVVMDDGRIVERGTHNELLARNG 559
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
6-196 |
4.33e-22 |
|
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: 96.28 E-value: 4.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRN-VVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLR-DPLAVKQAAGYL 83
Cdd:TIGR02868 335 LELRDLSAGYPGAPpVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSlDQDEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 84 PDAVGFYDSlTARENLAFTARLAGFADV-DASGRIGQALGRVRLDGVADRKVG----TFSRGMRQRLGLAELLMRDCQIM 158
Cdd:TIGR02868 415 AQDAHLFDT-TVRENLRLARPDATDEELwAALERVGLADWLRALPDGLDTVLGeggaRLSGGERQRLALARALLADAPIL 493
|
170 180 190
....*....|....*....|....*....|....*...
gi 1345382048 159 ILDEPTSGLDPQSTEELLGFIADfANEGRTVLVSSHLL 196
Cdd:TIGR02868 494 LLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-214 |
6.52e-22 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 93.64 E-value: 6.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 1 MSGTVIEARGLTKAYK------GRNV-----VDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKD- 68
Cdd:COG4608 3 MAEPLLEVRDLKKHFPvrgglfGRTVgvvkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 69 ---------PLR--------DPlavkqaagylpdavgfYDSL----TARENLAFTARLAGFADVDA-SGRIGQALGRVRL 126
Cdd:COG4608 83 tglsgrelrPLRrrmqmvfqDP----------------YASLnprmTVGDIIAEPLRIHGLASKAErRERVAELLELVGL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 127 D-GVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTSGLDP--QSteELLGFIADFANE-GRTVLVSSHLLDVVQTV 202
Cdd:COG4608 147 RpEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVsiQA--QVLNLLEDLQDElGLTYLFISHDLSVVRHI 224
|
250
....*....|..
gi 1345382048 203 CTRVALFNRGRI 214
Cdd:COG4608 225 SDRVAVMYLGKI 236
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
5-228 |
7.43e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 95.94 E-value: 7.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 5 VIEARGLTKAYKGR---NVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVrLLDKDPLRDPLAV---KQ 78
Cdd:TIGR00958 478 LIEFQDVSFSYPNRpdvPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQV-LLDGVPLVQYDHHylhRQ 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 79 AAGYLPDAVGFydSLTARENLAFTARLAGFADVDASGRIGQALGRVR-----LDGVADRKVGTFSRGMRQRLGLAELLMR 153
Cdd:TIGR00958 557 VALVGQEPVLF--SGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMefpngYDTEVGEKGSQLSGGQKQRIAIARALVR 634
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1345382048 154 DCQIMILDEPTSGLDPQStEELLGFIADFAneGRTVLVSSHLLDVVQTvCTRVALFNRGRIGFVGTLAELAAKVG 228
Cdd:TIGR00958 635 KPRVLILDEATSALDAEC-EQLLQESRSRA--SRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQG 705
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
17-219 |
1.33e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 91.97 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 17 GRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSV--RLLDK-DPLRDPLAVKQAAGYLPDAVGFYDSL 93
Cdd:PRK13644 14 GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlvSGIDTgDFSKLQGIRKLVGIVFQNPETQFVGR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 94 TARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQSTE 173
Cdd:PRK13644 94 TVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1345382048 174 ELLGFIADFANEGRTVLVSSHLLDVVQtVCTRVALFNRGRIGFVGT 219
Cdd:PRK13644 174 AVLERIKKLHEKGKTIVYITHNLEELH-DADRIIVMDRGKIVLEGE 218
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
4-213 |
3.53e-21 |
|
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: 89.80 E-value: 3.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 4 TVIEARGLTKAY-------KGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPL------ 70
Cdd:COG4778 3 TLLEVENLSKTFtlhlqggKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWvdlaqa 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 71 --RDPLAV-KQAAGY-------LPdavgfydSLTARENLAFTARLAGFADVDASGRIGQALGRVRLD----GVADrkvGT 136
Cdd:COG4778 83 spREILALrRRTIGYvsqflrvIP-------RVSALDVVAEPLLERGVDREEARARARELLARLNLPerlwDLPP---AT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1345382048 137 FSRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGR 213
Cdd:COG4778 153 FSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
26-218 |
3.65e-21 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 89.47 E-value: 3.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 26 LTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPLAVKQAAGYLPDAvGFYDSLTAREN--LAFTA 103
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQEN-NLFAHLTVEQNvgLGLSP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 104 RLAgFADVDaSGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFA 183
Cdd:cd03298 98 GLK-LTAED-RQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLH 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 1345382048 184 NE-GRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVG 218
Cdd:cd03298 176 AEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
31-218 |
5.15e-21 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 88.89 E-value: 5.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 31 GEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLlDKDPLRDP-----LAVKQ-AAGYLPDAVGFYDSLTARENLAFTAR 104
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVL-NGTVLFDSrkkinLPPQQrKIGLVFQQYALFPHLNVRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 105 laGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQSTEELLGFIADF-A 183
Cdd:cd03297 102 --RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIkK 179
|
170 180 190
....*....|....*....|....*....|....*
gi 1345382048 184 NEGRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVG 218
Cdd:cd03297 180 NLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-219 |
5.60e-21 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 91.68 E-value: 5.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 1 MSgtvIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPlAVKQAA 80
Cdd:PRK10851 1 MS---IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLH-ARDRKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 81 GYLPDAVGFYDSLTARENLAFTARL------AGFADVDAsgRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRD 154
Cdd:PRK10851 77 GFVFQHYALFRHMTVFDNIAFGLTVlprrerPNAAAIKA--KVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1345382048 155 CQIMILDEPTSGLDPQSTEELLGFIADFANEGR--TVLVsSHLLDVVQTVCTRVALFNRGRIGFVGT 219
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEELKftSVFV-THDQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
6-214 |
6.77e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 90.53 E-value: 6.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGR-----NVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSV-----------------R 63
Cdd:PRK13651 3 IKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekeK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 64 LLDKDPLRDPLA--VKQAAGyLPDAVG---------FYDSlTARENLAFTARLAGFADVDASGRIGQALGRVRLD-GVAD 131
Cdd:PRK13651 83 VLEKLVIQKTRFkkIKKIKE-IRRRVGvvfqfaeyqLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDeSYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 132 RKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNR 211
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKD 240
|
...
gi 1345382048 212 GRI 214
Cdd:PRK13651 241 GKI 243
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
2-233 |
1.20e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 89.08 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 2 SGTVIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVrLLDKDPLR--DPLAVKQA 79
Cdd:PRK10575 8 SDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEI-LLDAQPLEswSSKAFARK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 80 AGYLPDAVGFYDSLTARENLA-----FTARLAGFADVDASgRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRD 154
Cdd:PRK10575 87 VAYLPQQLPAAEGMTVRELVAigrypWHGALGRFGAADRE-KVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 155 CQIMILDEPTSGLDPQSTEELLGFIADFANE-GRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAELaakVGGDALE 233
Cdd:PRK10575 166 SRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL---MRGETLE 242
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-214 |
2.34e-20 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 86.12 E-value: 2.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRN--VVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLlDKDPLR--DPLAVKQAAG 81
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRL-DGADISqwDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 82 YLPDAVGFYDSlTARENLaftarlagfadvdasgrigqalgrvrldgvadrkvgtFSRGMRQRLGLAELLMRDCQIMILD 161
Cdd:cd03246 80 YLPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1345382048 162 EPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTvCTRVALFNRGRI 214
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
6-228 |
2.90e-20 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 87.67 E-value: 2.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYK-GRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVrLLDKDPLRDPL--AVKQAAGY 82
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSI-LIDGQDIREVTldSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 83 LP-DAVGFYDslTARENLAFTARLAGFADVDASGRIGQALGRV-RLDGVADRKVG----TFSRGMRQRLGLAELLMRDCQ 156
Cdd:cd03253 80 VPqDTVLFND--TIGYNIRYGRPDATDEEVIEAAKAAQIHDKImRFPDGYDTIVGerglKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1345382048 157 IMILDEPTSGLDPQSTEELLGFIADFANeGRTVLVSSHLLDVVQTvCTRVALFNRGRIGFVGTLAELAAKVG 228
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLAKGG 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-221 |
7.50e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 89.32 E-value: 7.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 4 TVIEARGLT-KAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLR-DPLAVKQA-A 80
Cdd:COG3845 256 VVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGlSPRERRRLgV 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 81 GYLPD------AVGfydSLTARENLAFT----ARLA--GFADVDASGRIGQALGR---VRLDGVaDRKVGTFSRGMRQRL 145
Cdd:COG3845 336 AYIPEdrlgrgLVP---DMSVAENLILGryrrPPFSrgGFLDRKAIRAFAEELIEefdVRTPGP-DTPARSLSGGNQQKV 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1345382048 146 GLAELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRIgfVGTLA 221
Cdd:COG3845 412 ILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRI--VGEVP 485
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
6-223 |
8.42e-20 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 86.68 E-value: 8.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKtTTILMLMG-LTEANAGSVRLLDKDPLRDP---LAVKQAAg 81
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGK-STLLSMISrLLPPDSGEVLVDGLDVATTPsreLAKRLAI- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 82 yLPDAVGFYDSLTARENLAF----------TArlagfADVDAsgrIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELL 151
Cdd:COG4604 80 -LRQENHINSRLTVRELVAFgrfpyskgrlTA-----EDREI---IDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1345382048 152 MRDCQIMILDEPTSGLDPQSTEELLGFIADFANE-GRTVLVSSHllDVVQTVC---TRVALFNrGRIGFVGTLAEL 223
Cdd:COG4604 151 AQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLH--DINFASCyadHIVAMKD-GRVVAQGTPEEI 223
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-225 |
1.28e-19 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 85.79 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 25 NLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPLAvKQAAGYLPDAVGFYDSLTARENLAF--- 101
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS-RRPVSMLFQENNLFSHLTVAQNIGLgln 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 102 -TARLagfaDVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQSTEELLGFIA 180
Cdd:PRK10771 98 pGLKL----NAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1345382048 181 DFANEGR-TVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAELAA 225
Cdd:PRK10771 174 QVCQERQlTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
36-223 |
1.31e-19 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 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. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 87.55 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 36 LLGPNGAGKTTTILMLMGLTEANAGSVrLLDKDPLRDPLAVKQAAGYLPDAVGFYDSLTARENLAFTARLAGFADVDASG 115
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSI-MLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 116 RIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANE-GRTVLVSSH 194
Cdd:TIGR01187 80 RVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQlGITFVFVTH 159
|
170 180
....*....|....*....|....*....
gi 1345382048 195 LLDVVQTVCTRVALFNRGRIGFVGTLAEL 223
Cdd:TIGR01187 160 DQEEAMTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
6-168 |
1.37e-19 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 87.85 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVrLLDKDPL-------RDPLAVKQ 78
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQI-FIDGEDVthrsiqqRDICMVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 79 AAGYLPdavgfydSLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIM 158
Cdd:PRK11432 86 SYALFP-------HMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVL 158
|
170
....*....|
gi 1345382048 159 ILDEPTSGLD 168
Cdd:PRK11432 159 LFDEPLSNLD 168
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
18-227 |
1.52e-19 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 88.56 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 18 RNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLlDKDPLR--DPLAVKQAAGYLPDAVGFYDSlTA 95
Cdd:TIGR01842 331 KPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRL-DGADLKqwDRETFGKHIGYLPQDVELFPG-TV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 96 RENLAFTARLAGFADVDASGRIGQALGRV-RLDGVADRKVG----TFSRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQ 170
Cdd:TIGR01842 409 AENIARFGENADPEKIIEAAKLAGVHELIlRLPDGYDTVIGpggaTLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEE 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1345382048 171 STEELLGFIADFANEGRTVLVSSHLLDVVQTVcTRVALFNRGRIGFVGTLAELAAKV 227
Cdd:TIGR01842 489 GEQALANAIKALKARGITVVVITHRPSLLGCV-DKILVLQDGRIARFGERDEVLAKL 544
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
6-228 |
1.52e-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: 85.67 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGR---NVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVrLLDKDPLRDpLAVKqaagY 82
Cdd:cd03249 1 IEFKNVSFRYPSRpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEI-LLDGVDIRD-LNLR----W 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 83 LPDAVGFYD------SLTARENLAFTARLAGFADVDASGRIGQALGRV-----RLDGVADRKVGTFSRGMRQRLGLAELL 151
Cdd:cd03249 75 LRSQIGLVSqepvlfDGTIAENIRYGKPDATDEEVEEAAKKANIHDFImslpdGYDTLVGERGSQLSGGQKQRIAIARAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1345382048 152 MRDCQIMILDEPTSGLDPQStEELLGFIADFANEGRTVLVSSHLLDVVQTvCTRVALFNRGRIGFVGTLAELAAKVG 228
Cdd:cd03249 155 LRNPKILLLDEATSALDAES-EKLVQEALDRAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDELMAQKG 229
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-214 |
1.81e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 88.30 E-value: 1.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 4 TVIEARGLTKAYKGRnvVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKD-PLRDPL-AVKQAAG 81
Cdd:PRK09700 264 TVFEVRNVTSRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDiSPRSPLdAVKKGMA 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 82 YLPDA---VGFYDSLTARENLAFTARLA--------GFADVDASGRIGQA---LGRVRLDGVaDRKVGTFSRGMRQRLGL 147
Cdd:PRK09700 342 YITESrrdNGFFPNFSIAQNMAISRSLKdggykgamGLFHEVDEQRTAENqreLLALKCHSV-NQNITELSGGNQQKVLI 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1345382048 148 AELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRI 214
Cdd:PRK09700 421 SKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
6-214 |
2.09e-19 |
|
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: 84.85 E-value: 2.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYK--GRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPL-AVKQAAGY 82
Cdd:cd03244 3 IEFKNVSLRYRpnLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLhDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 83 LP-DAVGFYDSLtaRENLAFtarLAGFADvdasGRIGQALGRVRLDGVADRKVGT-----------FSRGMRQRLGLAEL 150
Cdd:cd03244 83 IPqDPVLFSGTI--RSNLDP---FGEYSD----EELWQALERVGLKEFVESLPGGldtvveeggenLSVGQRQLLCLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1345382048 151 LMRDCQIMILDEPTSGLDPQSTEELLGFIAD-FANegRTVLVSSHLLDvvqTV--CTRVALFNRGRI 214
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDALIQKTIREaFKD--CTVLTIAHRLD---TIidSDRILVLDKGRV 215
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
6-206 |
2.21e-19 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 84.75 E-value: 2.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAY-------KGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRL--------LDKDPL 70
Cdd:TIGR02324 2 LEVEDLSKTFtlhqqggVRLPVLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRILVrhegawvdLAQASP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 71 RDPLAV-KQAAGYLPDAVGFYDSLTARENLAFTARLAGFADVDASGRIGQALGRVRLDG-VADRKVGTFSRGMRQRLGLA 148
Cdd:TIGR02324 82 REVLEVrRKTIGYVSQFLRVIPRVSALEVVAEPLLERGVPREAARARARELLARLNIPErLWHLPPATFSGGEQQRVNIA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1345382048 149 ELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRV 206
Cdd:TIGR02324 162 RGFIADYPILLLDEPTASLDAANRQVVVELIAEAKARGAALIGIFHDEEVRELVADRV 219
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-219 |
2.64e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 88.06 E-value: 2.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 1 MSGTVIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGL--------------TEANAGSVRlld 66
Cdd:PRK13549 1 MMEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVyphgtyegeiifegEELQASNIR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 67 kDPLRDPLA-VKQAAGYLPDavgfydsLTARENLAFTARL--AGFADVDA-SGRIGQALGRVRLDGVADRKVGTFSRGMR 142
Cdd:PRK13549 78 -DTERAGIAiIHQELALVKE-------LSVLENIFLGNEItpGGIMDYDAmYLRAQKLLAQLKLDINPATPVGNLGLGQQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1345382048 143 QRLGLAELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRigFVGT 219
Cdd:PRK13549 150 QLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR--HIGT 224
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
5-214 |
3.25e-19 |
|
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: 84.44 E-value: 3.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 5 VIEARGLTKAYKGR---NVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVrLLDKDPL---------RD 72
Cdd:cd03248 11 IVKFQNVTFAYPTRpdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQV-LLDGKPIsqyehkylhSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 73 PLAVKQaagylpDAVGFYDSLtaRENLAFTARLAGFADVDASGRIGQALGRVRL-----DGVADRKVGTFSRGMRQRLGL 147
Cdd:cd03248 90 VSLVGQ------EPVLFARSL--QDNIAYGLQSCSFECVKEAAQKAHAHSFISElasgyDTEVGEKGSQLSGGQKQRVAI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1345382048 148 AELLMRDCQIMILDEPTSGLDPQSTEELLGFIADfANEGRTVLVSSHLLDVVQTVcTRVALFNRGRI 214
Cdd:cd03248 162 ARALIRNPQVLILDEATSALDAESEQQVQQALYD-WPERRTVLVIAHRLSTVERA-DQILVLDGGRI 226
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
24-268 |
5.94e-19 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 85.93 E-value: 5.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 24 INLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVrLLDKDPLRDPLAV------KQAAGYLPDAVGFYDSLTARE 97
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEI-VLNGRTLFDSRKGiflppeKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 98 NLAFTARLAGFADVDAS-GRIGQALGrvrLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQSTEELL 176
Cdd:TIGR02142 95 NLRYGMKRARPSERRISfERVIELLG---IGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEIL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 177 GFIADFANEGRT-VLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAELAAKVGGDALE-------IDLEAESFDAAARLS 248
Cdd:TIGR02142 172 PYLERLHAEFGIpILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLAredqgslIEGVVAEHDQHYGLT 251
|
250 260
....*....|....*....|....*....
gi 1345382048 249 NL---------NGVDAVIGGDRRWRISAS 268
Cdd:TIGR02142 252 ALrlggghlwvPENLGPTGARLRLRVPAR 280
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
24-270 |
7.73e-19 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 85.54 E-value: 7.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 24 INLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDkDPLRDP-----LAV-KQAAGYLpdavgFYDS----- 92
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGG-EVLQDSargifLPPhRRRIGYV-----FQEArlfph 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 93 LTARENLAFTARlagfadvdasgRIGQALGRVRLDGVA---------DRKVGTFSRGMRQRLGLAELLMRDCQIMILDEP 163
Cdd:COG4148 92 LSVRGNLLYGRK-----------RAPRAERRISFDEVVellgighllDRRPATLSGGERQRVAIGRALLSSPRLLLMDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 164 TSGLDPQSTEELLGFIADFANEGRT-VLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAELAAKV------GGDALE--I 234
Cdd:COG4148 161 LAALDLARKAEILPYLERLRDELDIpILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPdllplaGGEEAGsvL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1345382048 235 DLEAESFDAAARLSNL---------NGVDAVIGGDRRWRISAsRD 270
Cdd:COG4148 241 EATVAAHDPDYGLTRLalgggrlwvPRLDLPPGTRVRVRIRA-RD 284
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-214 |
7.77e-19 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 86.66 E-value: 7.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 4 TVIEARGLTKAYKGR-----------NVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEAnAGSVRLLDKD---- 68
Cdd:COG4172 274 PLLEARDLKVWFPIKrglfrrtvghvKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS-EGEIRFDGQDldgl 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 69 ------PLR--------DPlavkqaagylpdavgfYDSLTAR--------ENLAFTARLAGFADVDAsgRIGQALGRVRL 126
Cdd:COG4172 353 srralrPLRrrmqvvfqDP----------------FGSLSPRmtvgqiiaEGLRVHGPGLSAAERRA--RVAEALEEVGL 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 127 D-GVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTSGLDpQSTE----ELLgfiADFANE-GRTVLVSSHLLDVVQ 200
Cdd:COG4172 415 DpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD-VSVQaqilDLL---RDLQREhGLAYLFISHDLAVVR 490
|
250
....*....|....
gi 1345382048 201 TVCTRVALFNRGRI 214
Cdd:COG4172 491 ALAHRVMVMKDGKV 504
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
6-228 |
9.77e-19 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 83.30 E-value: 9.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYK--GRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKD-PLRDPLAVKQAAGY 82
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDlALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 83 -LPDAVGFYDSLtaRENLAFTARLAGFADVDASGRIGQALGRVRL--DG----VADRKVGtFSRGMRQRLGLAELLMRDC 155
Cdd:cd03252 81 vLQENVLFNRSI--RDNIALADPGMSMERVIEAAKLAGAHDFISElpEGydtiVGEQGAG-LSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1345382048 156 QIMILDEPTSGLDPQSTEELLGFIADFAnEGRTVLVSSHLLDVVQTVcTRVALFNRGRIGFVGTLAELAAKVG 228
Cdd:cd03252 158 RILIFDEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTVKNA-DRIIVMEKGRIVEQGSHDELLAENG 228
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
15-227 |
1.66e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 83.63 E-value: 1.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 15 YKGRNVVDgINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLD-----KDPLRDPLAVKQAAGYL---PDA 86
Cdd:PRK13643 17 FASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvssTSKQKEIKPVRKKVGVVfqfPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 87 VGFYDslTARENLAFTARLAGFADVDASGRIGQALGRVRLDG-VADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTS 165
Cdd:PRK13643 96 QLFEE--TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1345382048 166 GLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAELAAKV 227
Cdd:PRK13643 174 GLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEV 235
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-229 |
2.17e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 85.26 E-value: 2.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGR--NVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRL-------LDKDPLRDPLAV 76
Cdd:PRK11160 339 LTLNNVSFTYPDQpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLngqpiadYSEAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 77 KQAAGYLpdavgFYDSLtaRENLAFTARLAGfadvDAsgRIGQALGRVRLDGVADRKVG----------TFSRGMRQRLG 146
Cdd:PRK11160 419 VSQRVHL-----FSATL--RDNLLLAAPNAS----DE--ALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLG 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 147 LAELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFAnEGRTVLVSSHLLDVVQTVcTRVALFNRGRIGFVGTLAELAAK 226
Cdd:PRK11160 486 IARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQELLAQ 563
|
...
gi 1345382048 227 VGG 229
Cdd:PRK11160 564 QGR 566
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-192 |
2.53e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 82.58 E-value: 2.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANA-----GSVRLLDKD---PLRDPLAVK 77
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNiysPDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 78 QAAGYLPDAVGFYDSLTARENLAFTARLAGFAD--VDASGRIGQALGRVRL-DGVADR---KVGTFSRGMRQRLGLAELL 151
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKskKELDERVEWALKKAALwDEVKDRlndYPSNLSGGQRQRLVIARAL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1345382048 152 MRDCQIMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVS 192
Cdd:PRK14267 165 AMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVT 205
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-241 |
3.78e-18 |
|
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: 81.03 E-value: 3.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGL--TEANAGSVRLLDKDPLRDPLAVKQAAGYL 83
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 84 pdavgfydsltarenLAFtarlagfadvdasgrigQAlgRVRLDGV--AD--RKVG-TFSRGMRQRLGLAELLMRDCQIM 158
Cdd:cd03217 81 ---------------LAF-----------------QY--PPEIPGVknADflRYVNeGFSGGEKKRNEILQLLLLEPDLA 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 159 ILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSH---LLDVVQTvcTRVALFNRGRIgfvgtlaelaAKVGGDALEID 235
Cdd:cd03217 127 ILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHyqrLLDYIKP--DRVHVLYDGRI----------VKSGDKELALE 194
|
....*.
gi 1345382048 236 LEAESF 241
Cdd:cd03217 195 IEKKGY 200
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-214 |
4.09e-18 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 82.01 E-value: 4.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 4 TVIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTI--LMLMGLTEANA---GSVRLLDKD---PLRDPLA 75
Cdd:COG1117 10 PKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLrcLNRMNDLIPGArveGEILLDGEDiydPDVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 76 VKQAAGY-------LPdavgfydsLTARENLAFTARLAGFAD-VDASGRIGQALGRVRL-DGVADR--KVGT-FSRGMRQ 143
Cdd:COG1117 90 LRRRVGMvfqkpnpFP--------KSIYDNVAYGLRLHGIKSkSELDEIVEESLRKAALwDEVKDRlkKSALgLSGGQQQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1345382048 144 RLGLAELLMRDCQIMILDEPTSGLDPQST---EELlgfIADFANEgRTVLVSSHLLDVVQTVCTRVALFNRGRI 214
Cdd:COG1117 162 RLCIARALAVEPEVLLMDEPTSALDPISTakiEEL---ILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGEL 231
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-223 |
4.41e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 81.94 E-value: 4.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 1 MSGTVIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSV-----------------R 63
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIvvngqtinlvrdkdgqlK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 64 LLDKDPLRdplAVKQAAGYLPDAVGFYDSLTAREN-LAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGT-FSRGM 141
Cdd:PRK10619 81 VADKNQLR---LLRTRLTMVFQHFNLWSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVhLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 142 RQRLGLAELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLA 221
Cdd:PRK10619 158 QQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPE 237
|
..
gi 1345382048 222 EL 223
Cdd:PRK10619 238 QL 239
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
21-252 |
5.34e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 81.43 E-value: 5.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 21 VDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEAnAGSVRLLDKdPLRD----PLAVKQAagYLPD--------AVG 88
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGR-PLSDwsaaELARHRA--YLSQqqsppfamPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 89 FYDSLTARENLAFTArlagfadvdASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMR-------DCQIMILD 161
Cdd:COG4138 88 QYLALHQPAGASSEA---------VEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 162 EPTSGLD--PQSTeeLLGFIADFANEGRTVLVSSHllDVVQTV--CTRVALFNRGRIGFVGTLAELaakvggdaLEIDLE 237
Cdd:COG4138 159 EPMNSLDvaQQAA--LDRLLRELCQQGITVVMSSH--DLNHTLrhADRVWLLKQGKLVASGETAEV--------MTPENL 226
|
250
....*....|....*
gi 1345382048 238 AESFDAAARLSNLNG 252
Cdd:COG4138 227 SEVFGVKFRRLEVEG 241
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-223 |
5.58e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 81.50 E-value: 5.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 4 TVIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEAN-----AGSVRLLDKDPLRDPLAV-- 76
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIElr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 77 --KQAAGYLPDAVgfyDSLTARENLAFTARLAGFADVDAS--GRIGQALGRVRL-DGVADR---KVGTFSRGMRQRLGLA 148
Cdd:PRK14247 82 rrVQMVFQIPNPI---PNLSIFENVALGLKLNRLVKSKKElqERVRWALEKAQLwDEVKDRldaPAGKLSGGQQQRLCIA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1345382048 149 ELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVsSHLLDVVQTVCTRVALFNRGRIGFVGTLAEL 223
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLV-THFPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-218 |
6.42e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 83.90 E-value: 6.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 4 TVIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKD-PLRDPLAVKQAA-G 81
Cdd:PRK10762 3 ALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEvTFNGPKSSQEAGiG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 82 YLPDAVGFYDSLTARENL----AFTARLAG------FADVDAsgrigqALGRVRLDGVADRKVGTFSRGMRQRLGLAELL 151
Cdd:PRK10762 83 IIHQELNLIPQLTIAENIflgrEFVNRFGRidwkkmYAEADK------LLARLNLRFSSDKLVGELSIGEQQMVEIAKVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1345382048 152 MRDCQIMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGriGFVG 218
Cdd:PRK10762 157 SFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDG--QFIA 221
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
7-242 |
6.78e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 81.27 E-value: 6.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 7 EARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLT--EANAGSVRLLDKDPL------R------- 71
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILelspdeRaragifl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 72 ---DPLAVKqaaGylpdaVGFYDSLTArenlAFTARLAGFADV-DASGRIGQALGRVRLD-GVADRKV-GTFSRGMRQRL 145
Cdd:COG0396 82 afqYPVEIP---G-----VSVSNFLRT----ALNARRGEELSArEFLKLLKEKMKELGLDeDFLDRYVnEGFSGGEKKRN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 146 GLAELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSH---LLDVVqtVCTRVALFNRGRIgfvgtlae 222
Cdd:COG0396 150 EILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHyqrILDYI--KPDFVHVLVDGRI-------- 219
|
250 260
....*....|....*....|
gi 1345382048 223 laAKVGGDALEIDLEAESFD 242
Cdd:COG0396 220 --VKSGGKELALELEEEGYD 237
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
18-228 |
9.09e-18 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 83.47 E-value: 9.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 18 RNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRL-------LDKDPLRDPLA-VKQAAGYLpdavgf 89
Cdd:PRK13657 348 RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIdgtdirtVTRASLRRNIAvVFQDAGLF------ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 90 ydSLTARENLAFTARLAGFADVDASGRIGQALGRV-----RLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPT 164
Cdd:PRK13657 422 --NRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIerkpdGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEAT 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1345382048 165 SGLDPQsTEELLGFIADFANEGRTVLVSSHLLDVVQTVcTRVALFNRGRIGFVGTLAELAAKVG 228
Cdd:PRK13657 500 SALDVE-TEAKVKAALDELMKGRTTFIIAHRLSTVRNA-DRILVFDNGRVVESGSFDELVARGG 561
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-201 |
1.78e-17 |
|
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: 82.68 E-value: 1.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 5 VIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDK------DPLRDPLAvkq 78
Cdd:TIGR03719 322 VIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETvklayvDQSRDALD--- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 79 aagylpdavgfyDSLTARENLAFTARLAGFADVDASGRigQALGRVRLDGvAD--RKVGTFSRGMRQRLGLAELLMRDCQ 156
Cdd:TIGR03719 399 ------------PNKTVWEEISGGLDIIKLGKREIPSR--AYVGRFNFKG-SDqqKKVGQLSGGERNRVHLAKTLKSGGN 463
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1345382048 157 IMILDEPTSGLDPQSTEELLGFIADFANegrTVLVSSH---LLDVVQT 201
Cdd:TIGR03719 464 VLLLDEPTNDLDVETLRALEEALLNFAG---CAVVISHdrwFLDRIAT 508
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-213 |
1.79e-17 |
|
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: 82.57 E-value: 1.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 5 VIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGL--------------TEANAGSVRlldkDPL 70
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVyphgtwdgeiywsgSPLKASNIR----DTE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 71 RDPLAV-KQAAGYLPDavgfydsLTARENLAFTARL---AGFADVDASGRIGQALGR-VRLDGVAD-RKVGTFSRGMRQR 144
Cdd:TIGR02633 77 RAGIVIiHQELTLVPE-------LSVAENIFLGNEItlpGGRMAYNAMYLRAKNLLReLQLDADNVtRPVGDYGGGQQQL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1345382048 145 LGLAELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGR 213
Cdd:TIGR02633 150 VEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-250 |
4.91e-17 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 81.39 E-value: 4.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLL-------------------- 65
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSGRIIyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 66 ------------------DKDPLRDPLAvKQAAGYLPDAVGFYDSLTARENLAFTARLAGFADVDASGRIGQALGRVRLD 127
Cdd:TIGR03269 81 pcpvcggtlepeevdfwnLSDKLRRRIR-KRIAIMLQRTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 128 GVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQsTEELL--GFIADFANEGRTVLVSSHLLDVVQTVCTR 205
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQ-TAKLVhnALEEAVKASGISMVLTSHWPEVIEDLSDK 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1345382048 206 VALFNRGRIGFVGTLAELAAKV--GGDALEIDLEAESFDAAARLSNL 250
Cdd:TIGR03269 239 AIWLENGEIKEEGTPDEVVAVFmeGVSEVEKECEVEVGEPIIKVRNV 285
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
9-168 |
7.35e-17 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 80.07 E-value: 7.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 9 RGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVrLLDKDPLRDPLAVKQAAGYLPDAVG 88
Cdd:PRK11000 7 RNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDL-FIGEKRMNDVPPAERGVGMVFQSYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 89 FYDSLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTSGLD 168
Cdd:PRK11000 86 LYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-197 |
2.44e-16 |
|
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: 79.44 E-value: 2.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 27 TVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVrllDKDP-------------LRDPL----------AVK-QAAGY 82
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDY---DEEPswdevlkrfrgteLQDYFkklangeikvAHKpQYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 83 LPDAVgfydSLTARENLAftarlagfaDVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDE 162
Cdd:COG1245 172 IPKVF----KGTVRELLE---------KVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190
....*....|....*....|....*....|....*...
gi 1345382048 163 PTSGLDPQSTEELLGFIADFANEGRTVLVSSH---LLD 197
Cdd:COG1245 239 PSSYLDIYQRLNVARLIRELAEEGKYVLVVEHdlaILD 276
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-191 |
2.93e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 76.46 E-value: 2.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 1 MSGTVIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPLA--VKQ 78
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAkiMRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 79 AAGYLPDAVGFYDSLTARENLAftarLAG-FADVDasgRIGQALGRV-----RLDGVADRKVGTFSRGMRQRLGLAELLM 152
Cdd:PRK11614 81 AVAIVPEGRRVFSRMTVEENLA----MGGfFAERD---QFQERIKWVyelfpRLHERRIQRAGTMSGGEQQMLAIGRALM 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 1345382048 153 RDCQIMILDEPTSGLDPQSTEELLGFIADFANEGRTVLV 191
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFL 192
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
4-214 |
4.51e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 76.65 E-value: 4.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 4 TVIEARGLTKAYKG---------RNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRdpL 74
Cdd:PRK10419 2 TLLNVSGLSHHYAHgglsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAK--L 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 75 AVKQAAGYLPDA-VGFYDSLTA-------RENLAFTAR-LAGFADVDASGRIGQALGRVRLD-GVADRKVGTFSRGMRQR 144
Cdd:PRK10419 80 NRAQRKAFRRDIqMVFQDSISAvnprktvREIIREPLRhLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1345382048 145 LGLAELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANEGRTV-LVSSHLLDVVQTVCTRVALFNRGRI 214
Cdd:PRK10419 160 VCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTAcLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
12-222 |
5.78e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 78.38 E-value: 5.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 12 TKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEAN--AGSVRLLDKDPLRDPLavkQAAGYLPDAVGF 89
Cdd:PLN03211 75 TRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQIL---KRTGFVTQDDIL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 90 YDSLTARENLAFTA--RLAGFADVDASGRIGQA-LGRVRLDGVADRKVG-TFSRGM----RQRLGLAELLMRDCQIMILD 161
Cdd:PLN03211 152 YPHLTVRETLVFCSllRLPKSLTKQEKILVAESvISELGLTKCENTIIGnSFIRGIsggeRKRVSIAHEMLINPSLLILD 231
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1345382048 162 EPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDV-VQTVCTRVALFNRGRIGFVGTLAE 222
Cdd:PLN03211 232 EPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSrVYQMFDSVLVLSEGRCLFFGKGSD 293
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
5-194 |
5.86e-16 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 75.27 E-value: 5.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 5 VIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLlDKDPLRDPLAVKQAAgYLP 84
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQI-DGKTATRGDRSRFMA-YLG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 85 DAVGFYDSLTARENLAFTARLAGFadvDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPT 164
Cdd:PRK13543 89 HLPGLKADLSTLENLHFLCGLHGR---RAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPY 165
|
170 180 190
....*....|....*....|....*....|
gi 1345382048 165 SGLDPQSTEELLGFIADFANEGRTVLVSSH 194
Cdd:PRK13543 166 ANLDLEGITLVNRMISAHLRGGGAALVTTH 195
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-214 |
6.02e-16 |
|
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: 77.94 E-value: 6.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 5 VIEARGLTkAY----KGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTE-ANAGSVrLLDKDPL--RDPL-AV 76
Cdd:TIGR02633 257 ILEARNLT-CWdvinPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNV-FINGKPVdiRNPAqAI 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 77 KQAAGYLPD-----------AVGFYDSLTARENLAFTARLAGFADVDAsgrIGQALGRVRLDGVA-DRKVGTFSRGMRQR 144
Cdd:TIGR02633 335 RAGIAMVPEdrkrhgivpilGVGKNITLSVLKSFCFKMRIDAAAELQI---IGSAIQRLKVKTASpFLPIGRLSGGNQQK 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 145 LGLAELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRI 214
Cdd:TIGR02633 412 AVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-203 |
9.27e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 75.69 E-value: 9.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 1 MSGTVIEARGLTKAYK-GRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKdPLRDPLAvKQA 79
Cdd:PRK15056 2 MQQAGIVVNDVTVTWRnGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQ-PTRQALQ-KNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 80 AGYLPDAVGFYDSLTAR-ENLAFTARLA--GF---ADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMR 153
Cdd:PRK15056 80 VAYVPQSEEVDWSFPVLvEDVVMMGRYGhmGWlrrAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1345382048 154 DCQIMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVC 203
Cdd:PRK15056 160 QGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFC 209
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
5-223 |
9.58e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 75.80 E-value: 9.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 5 VIEARGLTKAYKG--RNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRL----LDKDPLRDplaVKQ 78
Cdd:PRK13632 7 MIKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIdgitISKENLKE---IRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 79 AAGYL---PDA--VGfydsLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMR 153
Cdd:PRK13632 84 KIGIIfqnPDNqfIG----ATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1345382048 154 DCQIMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVS-SHLLDVVqTVCTRVALFNRGRIGFVGTLAEL 223
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISiTHDMDEA-ILADKVIVFSEGKLIAQGKPKEI 229
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
21-228 |
9.63e-16 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 77.62 E-value: 9.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 21 VDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRlldkdplrdplaVKQAAGYLPDAVGFYDSLTARENLA 100
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVD------------IKGSAALIAISSGLNGQLTGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 101 FTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQSTEELLGFIA 180
Cdd:PRK13545 108 LKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMN 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1345382048 181 DFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAELAAKVG 228
Cdd:PRK13545 188 EFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYD 235
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
15-194 |
1.38e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 73.83 E-value: 1.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 15 YKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPLAVKQAAGYLPDAVGFYDSLT 94
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 95 ARENLAFTARLA-GFADVDASGRIgqalgrVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQSTE 173
Cdd:PRK13540 91 LRENCLYDIHFSpGAVGITELCRL------FSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLL 164
|
170 180
....*....|....*....|.
gi 1345382048 174 ELLGFIADFANEGRTVLVSSH 194
Cdd:PRK13540 165 TIITKIQEHRAKGGAVLLTSH 185
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
5-194 |
1.56e-15 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 74.31 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 5 VIEARGLTKAYK-GRN---VVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVrLLDKDPLRDPLAVKQAA 80
Cdd:TIGR02211 1 LLKCENLGKRYQeGKLdtrVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEV-LFNGQSLSKLSSNERAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 81 ------GY-------LPDavgfydsLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGL 147
Cdd:TIGR02211 80 lrnkklGFiyqfhhlLPD-------FTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAI 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1345382048 148 AELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANEGRT-VLVSSH 194
Cdd:TIGR02211 153 ARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTsFLVVTH 200
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-214 |
2.60e-15 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 74.19 E-value: 2.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 1 MSGTVIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKD-PLRDPLAVKQA 79
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgQLRDLYALSEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 80 AgylpdavgfyDSLTARENLAFT---ARLAGFADVDASGRIGQAL--------GRVR------LDGV---ADR---KVGT 136
Cdd:PRK11701 82 E----------RRRLLRTEWGFVhqhPRDGLRMQVSAGGNIGERLmavgarhyGDIRatagdwLERVeidAARiddLPTT 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1345382048 137 FSRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANE-GRTVLVSSHLLDVVQTVCTRVALFNRGRI 214
Cdd:PRK11701 152 FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-223 |
3.03e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 74.89 E-value: 3.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 3 GTVIEARGLTKAYKGRN-----VVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPLAVK 77
Cdd:PRK13631 19 DIILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 78 QAAGYLPDAVGFYDSL------------------TARENLAFTARLAGFADVDASGRIGQALGRVRLD-GVADRKVGTFS 138
Cdd:PRK13631 99 LITNPYSKKIKNFKELrrrvsmvfqfpeyqlfkdTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDdSYLERSPFGLS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 139 RGMRQRLGLAELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVG 218
Cdd:PRK13631 179 GGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTG 258
|
....*
gi 1345382048 219 TLAEL 223
Cdd:PRK13631 259 TPYEI 263
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-211 |
3.31e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.61 E-value: 3.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 4 TVIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRllDKDPLRdplavkqaAGYL 83
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK--RNGKLR--------IGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 84 PdavgfyDSLTARENLAFT-ARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDE 162
Cdd:PRK09544 73 P------QKLYLDTTLPLTvNRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDE 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1345382048 163 PTSGLDPQSTEELLGFIADFANE-GRTVLVSSHLLDVVQTVCTRVALFNR 211
Cdd:PRK09544 147 PTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4-214 |
3.77e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 75.74 E-value: 3.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 4 TVIEARGLT---KAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTE-ANAGSVrLLDKDPL--RDPL-AV 76
Cdd:PRK13549 258 VILEVRNLTawdPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEI-FIDGKPVkiRNPQqAI 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 77 KQAAGYLPD-----------AVGFYDSLTARENLAFTARLAGFADVDAsgrIGQALGRVRLD-GVADRKVGTFSRGMRQR 144
Cdd:PRK13549 337 AQGIAMVPEdrkrdgivpvmGVGKNITLAALDRFTGGSRIDDAAELKT---ILESIQRLKVKtASPELAIARLSGGNQQK 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 145 LGLAELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRI 214
Cdd:PRK13549 414 AVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
24-213 |
3.82e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 73.43 E-value: 3.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 24 INLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEAnAGSVRLLDKdPLRDPLAVKQAA--GYL------PDAVGFYDSLTA 95
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQ-PLEAWSAAELARhrAYLsqqqtpPFAMPVFQYLTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 96 reNLAFTARLAGFADVdasgrIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMR-------DCQIMILDEPTSGLD 168
Cdd:PRK03695 93 --HQPDKTRTEAVASA-----LNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1345382048 169 PQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGR 213
Cdd:PRK03695 166 VAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGK 210
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
21-223 |
4.26e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 75.07 E-value: 4.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 21 VDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRL-------LDKDPLRDPLAVKQAAGYlpDAVGFYDSL 93
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIdgvdiakISDAELREVRRKKIAMVF--QSFALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 94 TARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQSTE 173
Cdd:PRK10070 122 TVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1345382048 174 ELLGFIADF-ANEGRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAEL 223
Cdd:PRK10070 202 EMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
5-223 |
4.55e-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: 4.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 5 VIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTtILMLMGLTE-ANAGSVRL--------LDKDPLRDPLA 75
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKST-FLRCINLLEtPDSGEIRVggeeirlkPDRDGELVPAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 76 VKQAAgYLPDAVGF-------YDSLTARENLAFT-ARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGL 147
Cdd:COG4598 87 RRQLQ-RIRTRLGMvfqsfnlWSHMTVLENVIEApVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAI 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1345382048 148 AELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAEL 223
Cdd:COG4598 166 ARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEV 241
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
5-227 |
4.94e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 73.58 E-value: 4.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 5 VIEARGLTKAYKGRN------VVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRL--LDKDPLRDPLAV 76
Cdd:PRK13633 4 MIKCKNVSYKYESNEesteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVdgLDTSDEENLWDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 77 KQAAGYL---PDavgfyDSLTA---RENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAEL 150
Cdd:PRK13633 84 RNKAGMVfqnPD-----NQIVAtivEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 151 L-MR-DCqiMILDEPTSGLDPQSTEELLGFIADF-ANEGRTVLVSSHLLD-VVQTvcTRVALFNRGRIGFVGTLAELAAK 226
Cdd:PRK13633 159 LaMRpEC--IIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEeAVEA--DRIIVMDSGKVVMEGTPKEIFKE 234
|
.
gi 1345382048 227 V 227
Cdd:PRK13633 235 V 235
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
6-228 |
5.18e-15 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 75.44 E-value: 5.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRNV--VDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVrLLD----KD----PLRDPLA 75
Cdd:PRK11176 342 IEFRNVTFTYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEI-LLDghdlRDytlaSLRNQVA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 76 VKQAAGYLpdavgFYDslTARENLAFtARLAGF--ADVDASGRIGQALGRV-RLDGVADRKVG----TFSRGMRQRLGLA 148
Cdd:PRK11176 421 LVSQNVHL-----FND--TIANNIAY-ARTEQYsrEQIEEAARMAYAMDFInKMDNGLDTVIGengvLLSGGQRQRIAIA 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 149 ELLMRDCQIMILDEPTSGLDPQStEELLGFIADFANEGRTVLVSSHLLDVVQTVcTRVALFNRGRIGFVGTLAELAAKVG 228
Cdd:PRK11176 493 RALLRDSPILILDEATSALDTES-ERAIQAALDELQKNRTSLVIAHRLSTIEKA-DEILVVEDGEIVERGTHAELLAQNG 570
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-214 |
6.24e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 73.63 E-value: 6.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 2 SGTVIEARGLTkaykgrnvvdGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPL-----RDPLAV 76
Cdd:PRK13649 14 AGTPFEGRALF----------DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsknKDIKQI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 77 KQAAGYL---PDAVGFYDslTARENLAFTARLAGFADVDASGRigqALGRVRLDGVA----DRKVGTFSRGMRQRLGLAE 149
Cdd:PRK13649 84 RKKVGLVfqfPESQLFEE--TVLKDVAFGPQNFGVSQEEAEAL---AREKLALVGISeslfEKNPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1345382048 150 LLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRI 214
Cdd:PRK13649 159 ILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKL 223
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
11-214 |
6.85e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 72.21 E-value: 6.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 11 LTKAY-KGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLR-----DPLAVKQAAGYLP 84
Cdd:PRK10908 7 VSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRlknreVPFLRRQIGMIFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 85 DAVGFYDSlTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPT 164
Cdd:PRK10908 87 DHHLLMDR-TVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1345382048 165 SGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRI 214
Cdd:PRK10908 166 GNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-228 |
8.66e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 74.50 E-value: 8.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLT-KAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMG-------LTeANAGSVRLLDKDPLRDPLA-V 76
Cdd:PRK11174 350 IEAEDLEiLSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGflpyqgsLK-INGIELRELDPESWRKHLSwV 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 77 KQAAgYLPDAvgfydslTARENLAFtarlagfADVDAS-GRIGQALGRVR-----------LDG-VADRKVGtFSRGMRQ 143
Cdd:PRK11174 429 GQNP-QLPHG-------TLRDNVLL-------GNPDASdEQLQQALENAWvseflpllpqgLDTpIGDQAAG-LSVGQAQ 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 144 RLGLAELLMRDCQIMILDEPTSGLDPQSTEELLGFIADfANEGRTVLVSSHLLDVVQTvCTRVALFNRGRIGFVGTLAEL 223
Cdd:PRK11174 493 RLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNA-ASRRQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQGDYAEL 570
|
....*
gi 1345382048 224 AAKVG 228
Cdd:PRK11174 571 SQAGG 575
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
20-194 |
9.19e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 74.76 E-value: 9.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 20 VVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPL---RDPLAV--KQAAGYLPDAVGFYDSLT 94
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVAtldADALAQlrREHFGFIFQRYHLLSHLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 95 ARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQSTEE 174
Cdd:PRK10535 103 AAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEE 182
|
170 180
....*....|....*....|
gi 1345382048 175 LLGFIADFANEGRTVLVSSH 194
Cdd:PRK10535 183 VMAILHQLRDRGHTVIIVTH 202
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-201 |
1.05e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 74.38 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 3 GTVIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDkdplrdplAVKqaagy 82
Cdd:PRK11819 322 DKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGE--------TVK----- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 83 lpdaVGFYDSltARENLAFTARLagFADVdaSG-----RIGQA-------LGRVRLDGvAD--RKVGTFSRGMRQRLGLA 148
Cdd:PRK11819 389 ----LAYVDQ--SRDALDPNKTV--WEEI--SGgldiiKVGNReipsrayVGRFNFKG-GDqqKKVGVLSGGERNRLHLA 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1345382048 149 ELLMRDCQIMILDEPTSGLDP---QSTEELLgfiADFANegrTVLVSSH---LLDVVQT 201
Cdd:PRK11819 458 KTLKQGGNVLLLDEPTNDLDVetlRALEEAL---LEFPG---CAVVISHdrwFLDRIAT 510
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
18-194 |
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: 70.74 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 18 RNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEanAGSVR---LLDKDPLRDPLAvkQAAGYLPDAVGFYDSLT 94
Cdd:cd03232 20 RQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKT--AGVITgeiLINGRPLDKNFQ--RSTGYVEQQDVHSPNLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 95 ARENLAFTARLAGFadvdasgrigqalgrvrldGVADRKvgtfsrgmrqRLGLAELLMRDCQIMILDEPTSGLDPQSTEE 174
Cdd:cd03232 96 VREALRFSALLRGL-------------------SVEQRK----------RLTIGVELAAKPSILFLDEPTSGLDSQAAYN 146
|
170 180
....*....|....*....|
gi 1345382048 175 LLGFIADFANEGRTVLVSSH 194
Cdd:cd03232 147 IVRFLKKLADSGQAILCTIH 166
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-197 |
3.61e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 72.92 E-value: 3.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 27 TVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSV-----------------------RLLDKDpLRdpLAVK-QAAGY 82
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYeeepswdevlkrfrgtelqnyfkKLYNGE-IK--VVHKpQYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 83 LPDAV-GfydslTARENLAftarlagfaDVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILD 161
Cdd:PRK13409 172 IPKVFkG-----KVRELLK---------KVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190
....*....|....*....|....*....|....*....
gi 1345382048 162 EPTSGLDPQSTEELLGFIADFAnEGRTVLVSSH---LLD 197
Cdd:PRK13409 238 EPTSYLDIRQRLNVARLIRELA-EGKYVLVVEHdlaVLD 275
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-214 |
5.24e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 70.90 E-value: 5.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEA-----NAGSVRLLDKDPL--RDPLAVKQ 78
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFnyRDVLEFRR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 79 AAGYLPDAVGFYdSLTARENLAFTARLAGFADVDASGRIGQA-LGRVRL-DGVADRKVGT---FSRGMRQRLGLAELLMR 153
Cdd:PRK14271 102 RVGMLFQRPNPF-PMSIMDNVLAGVRAHKLVPRKEFRGVAQArLTEVGLwDAVKDRLSDSpfrLSGGQQQLLCLARTLAV 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1345382048 154 DCQIMILDEPTSGLDPQSTEELLGFIADFANEgRTVLVSSHLLDVVQTVCTRVALFNRGRI 214
Cdd:PRK14271 181 NPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-194 |
5.78e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 72.29 E-value: 5.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 5 VIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDK------DPLRDPLAvkq 78
Cdd:PRK11147 319 VFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKlevayfDQHRAELD--- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 79 aagylPDAvgfydslTARENLAftarlAGFADVDASGRIGQALG----------RVRldgvadRKVGTFSRGMRQRLGLA 148
Cdd:PRK11147 396 -----PEK-------TVMDNLA-----EGKQEVMVNGRPRHVLGylqdflfhpkRAM------TPVKALSGGERNRLLLA 452
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1345382048 149 ELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFanEGrTVLVSSH 194
Cdd:PRK11147 453 RLFLKPSNLLILDEPTNDLDVETLELLEELLDSY--QG-TVLLVSH 495
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
3-214 |
6.06e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 70.63 E-value: 6.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 3 GTVIEARGLtkaykgrnvvDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDK-----------DPLR 71
Cdd:PRK13641 15 GTPMEKKGL----------DNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYhitpetgnknlKKLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 72 DPLAVkqaAGYLPDAVGFYDslTARENLAFTARLAGFADVDASGRIGQALGRVRL-DGVADRKVGTFSRGMRQRLGLAEL 150
Cdd:PRK13641 85 KKVSL---VFQFPEAQLFEN--TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1345382048 151 LMRDCQIMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRI 214
Cdd:PRK13641 160 MAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
10-194 |
6.16e-14 |
|
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: 71.89 E-value: 6.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 10 GLTKAY-KGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRL--------LDKDPLRDPLA----- 75
Cdd:TIGR03719 9 RVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPqpgikvgyLPQEPQLDPTKtvren 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 76 VKQAAGYLPDAVGFYDSLTAR---ENLAFTARLAGFA----DVDASG------RIGQALGRVRL-DGvaDRKVGTFSRGM 141
Cdd:TIGR03719 89 VEEGVAEIKDALDRFNEISAKyaePDADFDKLAAEQAelqeIIDAADawdldsQLEIAMDALRCpPW--DADVTKLSGGE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1345382048 142 RQRLGLAELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANegrTVLVSSH 194
Cdd:TIGR03719 167 RRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG---TVVAVTH 216
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1-209 |
7.95e-14 |
|
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: 71.74 E-value: 7.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 1 MSGTVIEARGLTKAYKG-RNVVDGinLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVrlldkdplrdPLAVKQA 79
Cdd:COG1245 337 EEETLVEYPDLTKSYGGfSLEVEG--GEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV----------DEDLKIS 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 80 agYLPDAVGFYDSLTARENLaftaRLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMI 159
Cdd:COG1245 405 --YKPQYISPDYDGTVEEFL----RSANTDDFGSSYYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYL 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1345382048 160 LDEPTSGLDPQSTEELLGFIADFA-NEGRTVLVSSHLLDVVQTVCTRVALF 209
Cdd:COG1245 479 LDEPSAHLDVEQRLAVAKAIRRFAeNRGKTAMVVDHDIYLIDYISDRLMVF 529
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1-214 |
8.00e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 70.02 E-value: 8.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 1 MSGTVIEARG--LTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVrLLDKDPLRDpLAVKQ 78
Cdd:PRK10253 1 MTESVARLRGeqLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHV-WLDGEHIQH-YASKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 79 AA---GYLPDAVGFYDSLTARENLA---------FTARLAgfADVDASGRIGQALGRVRLdgvADRKVGTFSRGMRQRLG 146
Cdd:PRK10253 79 VArriGLLAQNATTPGDITVQELVArgryphqplFTRWRK--EDEEAVTKAMQATGITHL---ADQSVDTLSGGQRQRAW 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1345382048 147 LAELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANE-GRTVLVSSHLLDVVQTVCTRVALFNRGRI 214
Cdd:PRK10253 154 IAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKI 222
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
21-226 |
9.16e-14 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 69.84 E-value: 9.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 21 VDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVrllDKDPLRDPLAVKqaagylpdaVGFYDSLTARENLA 100
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV---DRNGEVSVIAIS---------AGLSGQLTGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 101 FTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQSTEELLGFIA 180
Cdd:PRK13546 108 FKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIY 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1345382048 181 DFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAELAAK 226
Cdd:PRK13546 188 EFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-209 |
1.03e-13 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 69.36 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 27 TVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGsvrlldkdplrDPLAVKQAAGYLPDAVGFYDSLTARENLAFTARLA 106
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEG-----------DIEIELDTVSYKPQYIKADYEGTVRDLLSSITKDF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 107 G---FADVDasgrIGQALGrvrLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFA 183
Cdd:cd03237 90 YthpYFKTE----IAKPLQ---IEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFA 162
|
170 180
....*....|....*....|....*..
gi 1345382048 184 -NEGRTVLVSSHLLDVVQTVCTRVALF 209
Cdd:cd03237 163 eNNEKTAFVVEHDIIMIDYLADRLIVF 189
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
6-168 |
1.46e-13 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 70.26 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRN-VVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDK-----DP-LRDPLAVKQ 78
Cdd:PRK11650 4 LKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRvvnelEPaDRDIAMVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 79 aaGYlpdavGFYDSLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIM 158
Cdd:PRK11650 84 --NY-----ALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVF 156
|
170
....*....|
gi 1345382048 159 ILDEPTSGLD 168
Cdd:PRK11650 157 LFDEPLSNLD 166
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
6-228 |
1.50e-13 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 70.92 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYK-GRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRL-------LDKDPLRdplavk 77
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLngfslkdIDRHTLR------ 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 78 QAAGYLPDAVGFYDSlTARENLAFTARL-AGFADVDASGRIGQALGRVR-----LDGVADRKVGTFSRGMRQRLGLAELL 151
Cdd:TIGR01193 548 QFINYLPQEPYIFSG-SILENLLLGAKEnVSQDEIWAACEIAEIKDDIEnmplgYQTELSEEGSSISGGQKQRIALARAL 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 152 MRDCQIMILDEPTSGLD---PQSTEELLGFIADfanegRTVLVSSHLLDVVQTVcTRVALFNRGRIGFVGTLAELAAKVG 228
Cdd:TIGR01193 627 LTDSKVLILDESTSNLDtitEKKIVNNLLNLQD-----KTIIFVAHRLSVAKQS-DKIIVLDHGKIIEQGSHDELLDRNG 700
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-202 |
1.95e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 69.61 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 1 MSGTVIEARGLTKAY---KG-----RNV--VDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPL 70
Cdd:PRK11308 1 SQQPLLQAIDLKKHYpvkRGlfkpeRLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 71 R-DPLAVKQaagyLPDAVGF-----YDSLTARENLAFT--ARLAGFADVDASGRIGQALGRVRLDGV----ADRKVGTFS 138
Cdd:PRK11308 81 KaDPEAQKL----LRQKIQIvfqnpYGSLNPRKKVGQIleEPLLINTSLSAAERREKALAMMAKVGLrpehYDRYPHMFS 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1345382048 139 RGMRQRLGLAELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANE-GRTVLVSSHLLDVVQTV 202
Cdd:PRK11308 157 GGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHI 221
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
5-254 |
2.08e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 68.97 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 5 VIEARGLTKAYKGR---NVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLlDKDPL--RDPLAVKQA 79
Cdd:PRK13642 4 ILEVENLVFKYEKEsdvNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKI-DGELLtaENVWNLRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 80 AGYL---PDavGFYDSLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQ 156
Cdd:PRK13642 83 IGMVfqnPD--NQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 157 IMILDEPTSGLDPQSTEELLGFIADFANEGR-TVLVSSHLLDVVQTvCTRVALFNRGRIGFVGTLAELAAkVGGDALEID 235
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKYQlTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFA-TSEDMVEIG 238
|
250
....*....|....*....
gi 1345382048 236 LEAESFDAAARLSNLNGVD 254
Cdd:PRK13642 239 LDVPFSSNLMKDLRKNGFD 257
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-222 |
3.45e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 69.54 E-value: 3.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRlldkdplrdpLAVKQAAGYLPD 85
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK----------WSENANIGYYAQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 86 --AVGFYDSLTAREnlaFTARLAGFADVDASGRigQALGRVrLDGVAD--RKVGTFSRGMRQRLGLAELLMRDCQIMILD 161
Cdd:PRK15064 390 dhAYDFENDLTLFD---WMSQWRQEGDDEQAVR--GTLGRL-LFSQDDikKSVKVLSGGEKGRMLFGKLMMQKPNVLVMD 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1345382048 162 EPTSGLDPQSTEELLGFIADFanEGrTVLVSSHLLDVVQTVCTRV-ALFNRGRIGFVGTLAE 222
Cdd:PRK15064 464 EPTNHMDMESIESLNMALEKY--EG-TLIFVSHDREFVSSLATRIiEITPDGVVDFSGTYEE 522
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
6-214 |
3.73e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 69.55 E-value: 3.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLtkayKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKD-PLRDP-LAVKQAAGYL 83
Cdd:PRK11288 258 LRLDGL----KGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPiDIRSPrDAIRAGIMLC 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 84 PD---AVGFYDSLTARENLAFTAR---LAGFADVDASGRIGQALGRVRLDGV----ADRKVGTFSRGMRQRLGLAELLMR 153
Cdd:PRK11288 334 PEdrkAEGIIPVHSVADNINISARrhhLRAGCLINNRWEAENADRFIRSLNIktpsREQLIMNLSGGNQQKAILGRWLSE 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1345382048 154 DCQIMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRI 214
Cdd:PRK11288 414 DMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
24-215 |
4.60e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 69.31 E-value: 4.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 24 INLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPLAVKQAAG--YLPD---AVGFY-------- 90
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGlvYLPEdrqSSGLYldaplawn 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 91 -DSLTARENLAFTARLAGFADVDasgRIGQALGrVRLDGvADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTSGLDP 169
Cdd:PRK15439 362 vCALTHNRRGFWIKPARENAVLE---RYRRALN-IKFNH-AEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1345382048 170 QSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRIG 215
Cdd:PRK15439 437 SARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEIS 482
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3-227 |
5.92e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 67.40 E-value: 5.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 3 GTVIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVrLLDKDPL----RDPLAVKQ 78
Cdd:PRK11247 10 GTPLLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLaearEDTRLMFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 79 AAGYLP-----DAVGfydsLTARENLAFTARlagfadvdasgrigQALGRVrldGVADRKV---GTFSRGMRQRLGLAEL 150
Cdd:PRK11247 89 DARLLPwkkviDNVG----LGLKGQWRDAAL--------------QALAAV---GLADRANewpAALSGGQKQRVALARA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 151 LMRDCQIMILDEPTSGLDPQSTEELLGFIADFANE-GRTVLVSSHllDVVQTVCT--RVALFNRGRIGF----------- 216
Cdd:PRK11247 148 LIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQhGFTVLLVTH--DVSEAVAMadRVLLIEEGKIGLdltvdlprprr 225
|
250
....*....|...
gi 1345382048 217 VGT--LAELAAKV 227
Cdd:PRK11247 226 RGSarLAELEAEV 238
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
21-223 |
6.07e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 67.73 E-value: 6.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 21 VDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLD-KDP-----LRDPLAVKQAAGYL---PDAVGFYD 91
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyAIPanlkkIKEVKRLRKEIGLVfqfPEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 92 slTARENLAFTARLAGFADVDASGRIGQALGRVRL-DGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQ 170
Cdd:PRK13645 107 --TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPK 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1345382048 171 STEELLG-FIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAEL 223
Cdd:PRK13645 185 GEEDFINlFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEI 238
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
9-214 |
9.99e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 68.19 E-value: 9.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 9 RGLTKAYKGRN-VVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTeANAGSVrLLDKDPLRDpLAVKQaagYLP--- 84
Cdd:PRK15134 289 KGILKRTVDHNvVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEI-WFDGQPLHN-LNRRQ---LLPvrh 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 85 -DAVGFYD---SLTAR--------ENLAFTARLAGFADVDAsgRIGQALGRVRLDGVA-DRKVGTFSRGMRQRLGLAELL 151
Cdd:PRK15134 363 rIQVVFQDpnsSLNPRlnvlqiieEGLRVHQPTLSAAQREQ--QVIAVMEEVGLDPETrHRYPAEFSGGQRQRIAIARAL 440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1345382048 152 MRDCQIMILDEPTSGLDPQSTEELLGFIADFANEGR-TVLVSSHLLDVVQTVCTRVALFNRGRI 214
Cdd:PRK15134 441 ILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQlAYLFISHDLHVVRALCHQVIVLRQGEV 504
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
4-168 |
1.13e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 68.30 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 4 TVIEARGLTKAYkgrnvvDGINLTV-----KQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVrllDKDplrdplaVKQ 78
Cdd:PRK13409 339 TLVEYPDLTKKL------GDFSLEVeggeiYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV---DPE-------LKI 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 79 AagYLPDAVGFYDSLTARENLAFTARlagfaDVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIM 158
Cdd:PRK13409 403 S--YKPQYIKPDYDGTVEDLLRSITD-----DLGSSYYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLY 475
|
170
....*....|
gi 1345382048 159 ILDEPTSGLD 168
Cdd:PRK13409 476 LLDEPSAHLD 485
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
21-213 |
1.16e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 67.44 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 21 VDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEAN---AGSVRLLDKDPLRDP------LAVKQAAGYLPDA----- 86
Cdd:PRK09473 32 VNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPekelnkLRAEQISMIFQDPmtsln 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 87 ----VGfyDSLTarENLAFTARLAGFADVDASGRIgqalgrvrLDGV----ADRKVGT----FSRGMRQRLGLAELLMRD 154
Cdd:PRK09473 112 pymrVG--EQLM--EVLMLHKGMSKAEAFEESVRM--------LDAVkmpeARKRMKMypheFSGGMRQRVMIAMALLCR 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 155 CQIMILDEPTSGLDPQSTEELLGFIADFANEGRT-VLVSSHLLDVVQTVCTRVALFNRGR 213
Cdd:PRK09473 180 PKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGR 239
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-198 |
1.30e-12 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 66.62 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 27 TVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSV-----------------------RLLDKD--PLRDPLAVKQaag 81
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeildefrgselqnyftKLLEGDvkVIVKPQYVDL--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 82 yLPDAVgfydSLTARENLAftarlagfaDVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILD 161
Cdd:cd03236 99 -IPKAV----KGKVGELLK---------KKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFD 164
|
170 180 190
....*....|....*....|....*....|....*..
gi 1345382048 162 EPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDV 198
Cdd:cd03236 165 EPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAV 201
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
6-214 |
2.60e-12 |
|
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: 64.74 E-value: 2.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGR--NVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKD----PLRDplaVKQA 79
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDistiPLED---LRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 80 AGYLP-DAVGFydSLTARENLaftARLAGFADVDasgrIGQALgRVRLDGVadrkvgTFSRGMRQRLGLAELLMRDCQIM 158
Cdd:cd03369 84 LTIIPqDPTLF--SGTIRSNL---DPFDEYSDEE----IYGAL-RVSEGGL------NLSQGQRQLLCLARALLKRPRVL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1345382048 159 ILDEPTSGLDPQSTEELLGFI-ADFANEgrTVLVSSHLLdvvQTV--CTRVALFNRGRI 214
Cdd:cd03369 148 VLDEATASIDYATDALIQKTIrEEFTNS--TILTIAHRL---RTIidYDKILVMDAGEV 201
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
5-214 |
3.02e-12 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 65.49 E-value: 3.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 5 VIEARGLTkAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEAN----AGSVRLLDKdplrdPLAVKQAA 80
Cdd:PRK10418 4 QIELRNIA-LQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGK-----PVAPCALR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 81 GYLPDAV------GFYDSLTARENLAFTARLAGFADVDAsgRIGQALGRVRLDG---VADRKVGTFSRGMRQRLGLAELL 151
Cdd:PRK10418 78 GRKIATImqnprsAFNPLHTMHTHARETCLALGKPADDA--TLTAALEAVGLENaarVLKLYPFEMSGGMLQRMMIALAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1345382048 152 MRDCQIMILDEPTSGLDPQSTEELLGFIADFANE-GRTVLVSSHLLDVVQTVCTRVALFNRGRI 214
Cdd:PRK10418 156 LCEAPFIIADEPTTDLDVVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
18-195 |
3.36e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 64.12 E-value: 3.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 18 RNVVDgINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSV--RLLDKDPLRDPLAvkqaaGYLPDAVGFYDSLTA 95
Cdd:PRK13541 14 KNLFD-LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIyyKNCNINNIAKPYC-----TYIGHNLGLKLEMTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 96 RENLAFTARLagfadVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQSTEEL 175
Cdd:PRK13541 88 FENLKFWSEI-----YNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLL 162
|
170 180
....*....|....*....|
gi 1345382048 176 LGFIADFANEGRTVLVSSHL 195
Cdd:PRK13541 163 NNLIVMKANSGGIVLLSSHL 182
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
21-226 |
3.38e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 65.57 E-value: 3.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 21 VDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLD-------KDPLRDPlaVKQAAGYL---PDAVGFY 90
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktKDKYIRP--VRKRIGMVfqfPESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 91 DSLTaREnLAFTARLAGFaDVDA----SGRIGQALGRVRldGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTSG 166
Cdd:PRK13646 101 DTVE-RE-IIFGPKNFKM-NLDEvknyAHRLLMDLGFSR--DVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1345382048 167 LDPQSTEELLGFIADFA-NEGRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAELAAK 226
Cdd:PRK13646 176 LDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-194 |
4.18e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 67.06 E-value: 4.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 18 RNVVDGINLTVKQGEVLGLLGPNGAGKTTTILML-----MGLTEanaGSVRLLDKDPLRDPLA-----VKQAAGYLPDAv 87
Cdd:TIGR00956 776 RVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLaervtTGVIT---GGDRLVNGRPLDSSFQrsigyVQQQDLHLPTS- 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 88 gfydslTARENLAFTARLAGFADVDASGR---IGQALGRVRLDGVADRKVGTFSRGM----RQRLGLA-ELLMRDCQIMI 159
Cdd:TIGR00956 852 ------TVRESLRFSAYLRQPKSVSKSEKmeyVEEVIKLLEMESYADAVVGVPGEGLnveqRKRLTIGvELVAKPKLLLF 925
|
170 180 190
....*....|....*....|....*....|....*
gi 1345382048 160 LDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSH 194
Cdd:TIGR00956 926 LDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIH 960
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-176 |
4.36e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 65.11 E-value: 4.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKA-YKG----RNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRdpLAVKQAA 80
Cdd:COG1101 2 LELKNLSKTfNPGtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTK--LPEYKRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 81 GYlpdaVG--FYD-------SLTARENLAFtarlagfadvdASGR-----IGQALGRVRLD-----------GVADR--- 132
Cdd:COG1101 80 KY----IGrvFQDpmmgtapSMTIEENLAL-----------AYRRgkrrgLRRGLTKKRRElfrellatlglGLENRldt 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1345382048 133 KVGTFSRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQSTEELL 176
Cdd:COG1101 145 KVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVL 188
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-223 |
6.01e-12 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 65.86 E-value: 6.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 1 MSGTVIEARGLTKAYKG----RNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANA----GSVRLLDKDPLRD 72
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAahpsGSILFDGQDLLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 73 PLAVKQAA-GylpDAVG--FYDSLTA-----------RENLAFTARLAGFAdvdASGRIGQALGRVRLDGvADRKVGTF- 137
Cdd:COG4172 82 SERELRRIrG---NRIAmiFQEPMTSlnplhtigkqiAEVLRLHRGLSGAA---ARARALELLERVGIPD-PERRLDAYp 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 138 ---SRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANE-GRTVLVSSHLLDVVQTVCTRVALFNRGR 213
Cdd:COG4172 155 hqlSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLGVVRRFADRVAVMRQGE 234
|
250
....*....|
gi 1345382048 214 IGFVGTLAEL 223
Cdd:COG4172 235 IVEQGPTAEL 244
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
18-228 |
7.33e-12 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 65.89 E-value: 7.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 18 RNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRL-------LDKDPLRDPLAVKQAAGYLpdavgFY 90
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFhdipltkLQLDSWRSRLAVVSQTPFL-----FS 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 91 DSLTAreNLAFTARLAGFADVDASGRIGQALGRV-RLDGVADRKVG----TFSRGMRQRLGLAELLMRDCQIMILDEPTS 165
Cdd:PRK10789 403 DTVAN--NIALGRPDATQQEIEHVARLASVHDDIlRLPQGYDTEVGergvMLSGGQKQRISIARALLLNAEILILDDALS 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1345382048 166 GLDPQSTEELLGFIADFAnEGRTVLVSSHLLDVVqTVCTRVALFNRGRIGFVGTLAELAAKVG 228
Cdd:PRK10789 481 AVDGRTEHQILHNLRQWG-EGRTVIISAHRLSAL-TEASEILVMQHGHIAQRGNHDQLAQQSG 541
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
5-223 |
9.34e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 64.08 E-value: 9.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 5 VIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMG-LTEANA-GSVRL-----LDKDPLR--DPLA 75
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGApRGARVtgdvtLNGEPLAaiDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 76 VKQAAGYLPDAVGFYDSLTARENLAFT----ARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELL 151
Cdd:PRK13547 81 LARLRAVLPQAAQPAFAFSAREIVLLGryphARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 152 ---------MRDCQIMILDEPTSGLDPQSTEELLGFIADFANEGRT-VLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLA 221
Cdd:PRK13547 161 aqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHDPNLAARHADRIAMLADGAIVAHGAPA 240
|
..
gi 1345382048 222 EL 223
Cdd:PRK13547 241 DV 242
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
19-181 |
1.16e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 63.26 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 19 NVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRdpLAVKQAAGYLPDAVGFY-------D 91
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQ--MDEEARAKLRAKHVGFVfqsfmliP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 92 SLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQS 171
Cdd:PRK10584 102 TLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQT 181
|
170
....*....|
gi 1345382048 172 TEEllgfIAD 181
Cdd:PRK10584 182 GDK----IAD 187
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
9-213 |
1.43e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 64.75 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 9 RGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKdplrdPLAVKQAAGYLPDAVg 88
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGK-----EIDFKSSKEALENGI- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 89 fydSLTARE-NLAFTARL------------AGFADVDASGRIGQAL-GRVRLDGVADRKVGTFSRGMRQRLGLAELLMRD 154
Cdd:PRK10982 76 ---SMVHQElNLVLQRSVmdnmwlgryptkGMFVDQDKMYRDTKAIfDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYN 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1345382048 155 CQIMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGR 213
Cdd:PRK10982 153 AKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-215 |
1.91e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 63.13 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANA-----GSVRLLDKDPLRDPLAV---- 76
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERRVNLnrlr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 77 KQAAGYLPDAVGFydSLTARENLAFTARLAGF-ADVDASGRIGQALGRVRL-DGVAD---RKVGTFSRGMRQRLGLAELL 151
Cdd:PRK14258 88 RQVSMVHPKPNLF--PMSVYDNVAYGVKIVGWrPKLEIDDIVESALKDADLwDEIKHkihKSALDLSGGQQQRLCIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1345382048 152 MRDCQIMILDEPTSGLDPQSTEELLGFIADFANEGR-TVLVSSHLLDVVQTVCTRVALF--NRGRIG 215
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNLHQVSRLSDFTAFFkgNENRIG 232
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-223 |
2.16e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 63.14 E-value: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 18 RNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANA------GSVRLLDKDPLR-DPLAVKQAAGYLPDAVGFY 90
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDskikvdGKVLYFGKDIFQiDAIKLRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 91 DSLTARENLAFTARLAGFADVDASGRI-GQALGRVRL-DGVADR---KVGTFSRGMRQRLGLAELLMRDCQIMILDEPTS 165
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHGIKEKREIKKIvEECLRKVGLwKEVYDRlnsPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1345382048 166 GLDPQSTEELLGFIADFANEGRTVLVsSHLLDVVQTVCTRVALFNRGRIGFVGTLAEL 223
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNEIAIVIV-SHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
20-199 |
3.03e-11 |
|
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: 61.72 E-value: 3.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 20 VVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVrlldkdplrdplavkqaagYLPDAVGFYD------SL 93
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV-------------------SVPGSIAYVSqepwiqNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 94 TARENLAFTAR------------------LAGFADVDASgRIGQalgrvrlDGVadrkvgTFSRGMRQRLGLAELLMRDC 155
Cdd:cd03250 81 TIRENILFGKPfdeeryekvikacalepdLEILPDGDLT-EIGE-------KGI------NLSGGQKQRISLARAVYSDA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1345382048 156 QIMILDEPTSGLDPQsTEE------LLGFIADfaneGRTVLVSSHLLDVV 199
Cdd:cd03250 147 DIYLLDDPLSAVDAH-VGRhifencILGLLLN----NKTRILVTHQLQLL 191
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-212 |
3.53e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 62.10 E-value: 3.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 1 MSGTVIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEAN-----AGSVRLLDKD---PLRD 72
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNiysPRTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 73 PLAVKQAAGYL---PDAVGFydslTARENLAFTARLAGFAD-------VDASGRIGQALGRVRlDGVADRKVGtFSRGMR 142
Cdd:PRK14239 81 TVDLRKEIGMVfqqPNPFPM----SIYENVVYGLRLKGIKDkqvldeaVEKSLKGASIWDEVK-DRLHDSALG-LSGGQQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1345382048 143 QRLGLAELLMRDCQIMILDEPTSGLDPQST----EELLGFIADFanegrTVLVSSHLLDVVQTVCTRVALFNRG 212
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALDPISAgkieETLLGLKDDY-----TMLLVTRSMQQASRISDRTGFFLDG 223
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
6-194 |
3.56e-11 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 63.66 E-value: 3.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRN-----VVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRlLDKDPLRDplavKQAA 80
Cdd:COG4615 328 LELRGVTYRYPGEDgdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEIL-LDGQPVTA----DNRE 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 81 GYlpdavgfydsltaRENlaFTA---------RLAGFADVDASGRIGQALGRVRLDG---VADRKVGT--FSRGMRQRLG 146
Cdd:COG4615 403 AY-------------RQL--FSAvfsdfhlfdRLLGLDGEADPARARELLERLELDHkvsVEDGRFSTtdLSQGQRKRLA 467
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1345382048 147 LAELLMRDCQIMILDEPTSGLDPQS----TEELLGfiaDFANEGRTVLVSSH 194
Cdd:COG4615 468 LLVALLEDRPILVFDEWAADQDPEFrrvfYTELLP---ELKARGKTVIAISH 516
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
24-226 |
5.66e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 61.96 E-value: 5.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 24 INLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLD---------KD--PLRDPLA-VKQaagyLPDAVGFYD 91
Cdd:PRK13634 26 VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGErvitagkknKKlkPLRKKVGiVFQ----FPEHQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 92 slTARENLAFTARLAGFADVDASGRIGQALGRVRLD-GVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQ 170
Cdd:PRK13634 102 --TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPeELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1345382048 171 STEELLGFIADFANEGR--TVLVsSHLLDVVQTVCTRVALFNRGRIGFVGTLAELAAK 226
Cdd:PRK13634 180 GRKEMMEMFYKLHKEKGltTVLV-THSMEDAARYADQIVVMHKGTVFLQGTPREIFAD 236
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
3-176 |
7.43e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 62.52 E-value: 7.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 3 GTVIEARGLT-KAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLrdpLAVKQAAg 81
Cdd:COG4178 360 DGALALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARV---LFLPQRP- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 82 YLPDAvgfydslTARENLAFTARLAGFADvdasGRIGQALGRVRLDGVADR--------KVgtFSRGMRQRLGLAELLMR 153
Cdd:COG4178 436 YLPLG-------TLREALLYPATAEAFSD----AELREALEAVGLGHLAERldeeadwdQV--LSLGEQQRLAFARLLLH 502
|
170 180
....*....|....*....|...
gi 1345382048 154 DCQIMILDEPTSGLDPQSTEELL 176
Cdd:COG4178 503 KPDWLFLDEATSALDEENEAALY 525
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
21-218 |
7.67e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 62.57 E-value: 7.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 21 VDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSV----RLLDKDPLRDPLAVKQAAGYL---PdavgfYDSL 93
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIifngQRIDTLSPGKLQALRRDIQFIfqdP-----YASL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 94 TARENLAFTA----RLAGFADVDASG-RIGQALGRVRLDGV-ADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTSGL 167
Cdd:PRK10261 415 DPRQTVGDSImeplRVHGLLPGKAAAaRVAWLLERVGLLPEhAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1345382048 168 DPQSTEELLGFIADFANE-GRTVLVSSHLLDVVQTVCTRVALFNRGRIGFVG 218
Cdd:PRK10261 495 DVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
4-210 |
8.51e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 61.34 E-value: 8.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 4 TVIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTtilMLMGLTEAN--------AGSVRLLDK---DPLRD 72
Cdd:PRK14243 9 TVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKST---ILRCFNRLNdlipgfrvEGKVTFHGKnlyAPDVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 73 PLAVKQAAGYL-----PDAVGFYDsltareNLAFTARLAGFaDVDASGRIGQALGRVRL-DGVAD--RKVG-TFSRGMRQ 143
Cdd:PRK14243 86 PVEVRRRIGMVfqkpnPFPKSIYD------NIAYGARINGY-KGDMDELVERSLRQAALwDEVKDklKQSGlSLSGGQQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 144 RLGLAELLMRDCQIMILDEPTSGLDPQST---EELLGFIAdfanEGRTVLVSSHLLDVVQTVCTRVALFN 210
Cdd:PRK14243 159 RLCIARAIAVQPEVILMDEPCSALDPISTlriEELMHELK----EQYTIIIVTHNMQQAARVSDMTAFFN 224
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-228 |
9.75e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.33 E-value: 9.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 21 VDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKD-PLRDPL-AVKQAAGYLPD---AVGFYDSLTA 95
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEvVTRSPQdGLANGIVYISEdrkRDGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 96 RENLAFTArLAGFADvdASGRIG-----QALGR-VRLDGV----ADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTS 165
Cdd:PRK10762 348 KENMSLTA-LRYFSR--AGGSLKhadeqQAVSDfIRLFNIktpsMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTR 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 166 GLDPQSTEELLGFIADFANEGRT-VLVSSHLLDVVqTVCTRVALFNRGRIG--FVGTLAE----LAAKVG 228
Cdd:PRK10762 425 GVDVGAKKEIYQLINQFKAEGLSiILVSSEMPEVL-GMSDRILVMHEGRISgeFTREQATqeklMAAAVG 493
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
4-194 |
9.89e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 61.32 E-value: 9.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 4 TVIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVrLLDKDPL----RDPL-AVKQ 78
Cdd:PRK11831 6 NLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEI-LFDGENIpamsRSRLyTVRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 79 AAGYLPDAVGFYDSLTARENLAFTAR-LAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQI 157
Cdd:PRK11831 85 RMSMLFQSGALFTDMNVFDNVAYPLReHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDL 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 1345382048 158 MILDEPTSGLDPQSTEELLGFIADFANE-GRTVLVSSH 194
Cdd:PRK11831 165 IMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSH 202
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-197 |
1.10e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 60.97 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 1 MSGTVIEARGLTKAYKG--RNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMG--LTEANAGSVRLLDKDPLRDPLA- 75
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGllLPDDNPNSKITVDGITLTAKTVw 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 76 -VKQAAGYL---PDA--VGfydsLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAE 149
Cdd:PRK13640 81 dIREKVGIVfqnPDNqfVG----ATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1345382048 150 LLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANE-GRTVLVSSHLLD 197
Cdd:PRK13640 157 ILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDID 205
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
17-221 |
1.88e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 61.34 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 17 GRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEAN--AGSVRLLDKD-PLRD-PLAVKQAAGY---------- 82
Cdd:NF040905 272 ERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSYGRniSGTVFKDGKEvDVSTvSDAIDAGLAYvtedrkgygl 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 83 -LPDavgfydslTAREN--LAFTARLAGFADVDASGRIGQALG-----RVRLDGVaDRKVGTFSRGMRQRLGLAELLMRD 154
Cdd:NF040905 352 nLID--------DIKRNitLANLGKVSRRGVIDENEEIKVAEEyrkkmNIKTPSV-FQKVGNLSGGNQQKVVLSKWLFTD 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1345382048 155 CQIMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRIgfVGTLA 221
Cdd:NF040905 423 PDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRI--TGELP 487
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
5-199 |
2.15e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.59 E-value: 2.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 5 VIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMG--LTEANAGSVRLLDKDPLRD-PLAvkqaag 81
Cdd:COG2401 30 VLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVPDNQFGREaSLI------ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 82 ylpDAVG-FYDSLTARENLAftarLAGFADVdasgrigqALGRvrldgvadRKVGTFSRGMRQRLGLAELLMRDCQIMIL 160
Cdd:COG2401 104 ---DAIGrKGDFKDAVELLN----AVGLSDA--------VLWL--------RRFKELSTGQKFRFRLALLLAERPKLLVI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1345382048 161 DEPTSGLDPQSTEELLGFIADFANE-GRTVLVSSHLLDVV 199
Cdd:COG2401 161 DEFCSHLDRQTAKRVARNLQKLARRaGITLVVATHHYDVI 200
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
21-206 |
2.24e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 60.49 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 21 VDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLR------------------DPLAVKQAAGY 82
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGmkddewravrsdiqmifqDPLASLNPRMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 83 LPDAVG-----FYDSLTAREnlaftarlagfadvdASGRIGQALGRVRL-DGVADRKVGTFSRGMRQRLGLAELLMRDCQ 156
Cdd:PRK15079 117 IGEIIAeplrtYHPKLSRQE---------------VKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPK 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1345382048 157 IMILDEPTSGLDPQSTEELLGFIADFANE-GRTVLVSSHLLDVVQTVCTRV 206
Cdd:PRK15079 182 LIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRV 232
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1-228 |
2.28e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 61.27 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 1 MSGTvIEARGLTKAY-KGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRL-------LDKDPLRD 72
Cdd:PRK10790 337 QSGR-IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLdgrplssLSHSVLRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 73 PLA-VKQAAGYLPDAvgFYDSLTARENLAftarlagfadvdaSGRIGQALGRVRL--------DGVADR---KVGTFSRG 140
Cdd:PRK10790 416 GVAmVQQDPVVLADT--FLANVTLGRDIS-------------EEQVWQALETVQLaelarslpDGLYTPlgeQGNNLSVG 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 141 MRQRLGLAELLMRDCQIMILDEPTSGLDP---QSTEELLGFIadfaNEGRTVLVSSHLLDVVQTVCTRVALfNRGRIGFV 217
Cdd:PRK10790 481 QKQLLALARVLVQTPQILILDEATANIDSgteQAIQQALAAV----REHTTLVVIAHRLSTIVEADTILVL-HRGQAVEQ 555
|
250
....*....|.
gi 1345382048 218 GTLAELAAKVG 228
Cdd:PRK10790 556 GTHQQLLAAQG 566
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
9-194 |
3.30e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.52 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 9 RGLTKAY-KGRNVVDGINLTVKQGEVLGLLGPNGAGKTTtILMLM-GLTEANAGSVRL--------LDKDPLRDPL---- 74
Cdd:PRK11819 10 NRVSKVVpPKKQILKDISLSFFPGAKIGVLGLNGAGKST-LLRIMaGVDKEFEGEARPapgikvgyLPQEPQLDPEktvr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 75 -AVKQAAGYLPDAVGFYDSLTAR---ENLAFTARLAGFADV----DASG------RIGQALGRVRLDGvADRKVGTFSRG 140
Cdd:PRK11819 89 eNVEEGVAEVKAALDRFNEIYAAyaePDADFDALAAEQGELqeiiDAADawdldsQLEIAMDALRCPP-WDAKVTKLSGG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1345382048 141 MRQRLGLAELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANegrTVLVSSH 194
Cdd:PRK11819 168 ERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPG---TVVAVTH 218
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-228 |
1.08e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 59.57 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 20 VVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRL----LDKDPLRDplaVKQAAGYLP-DAVGFYDSLt 94
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIdglnIAKIGLHD---LRFKITIIPqDPVLFSGSL- 1376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 95 aRENL-AFT-------------ARLAGFADVDASGrigqalgrvrLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMIL 160
Cdd:TIGR00957 1377 -RMNLdPFSqysdeevwwalelAHLKTFVSALPDK----------LDHECAEGGENLSVGQRQLVCLARALLRKTKILVL 1445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1345382048 161 DEPTSGLDPQsTEELLGFIADFANEGRTVLVSSHLLDVVQTVcTRVALFNRGRIGFVGTLAELAAKVG 228
Cdd:TIGR00957 1446 DEATAAVDLE-TDNLIQSTIRTQFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEVAEFGAPSNLLQQRG 1511
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
5-206 |
3.54e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 57.49 E-value: 3.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 5 VIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTtiLM--LMGLTEanAGSVR---LLDKDP-----LRDPL 74
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKST--LMkvLSGVYP--HGSYEgeiLFDGEVcrfkdIRDSE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 75 AV-----KQAAGYLPDavgfydsLTARENLaF----TARlAGFADVDAS-GRIGQALGRVRLDGVADRKVGTFSRGMRQR 144
Cdd:NF040905 77 ALgiviiHQELALIPY-------LSIAENI-FlgneRAK-RGVIDWNETnRRARELLAKVGLDESPDTLVTDIGVGKQQL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1345382048 145 LGLAELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRV 206
Cdd:NF040905 148 VEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSI 209
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-242 |
4.25e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 56.19 E-value: 4.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 1 MSGTVIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMG-----LTEanaGSV-----RLLDKDP- 69
Cdd:CHL00131 3 KNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpaykILE---GDIlfkgeSILDLEPe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 70 LRDPLAVKQAAGYLPDAVGFYDSLTARenLAFTARLA--GFADVDA---SGRIGQALGRVRLDGV-ADRKVGT-FSRGMR 142
Cdd:CHL00131 80 ERAHLGIFLAFQYPIEIPGVSNADFLR--LAYNSKRKfqGLPELDPlefLEIINEKLKLVGMDPSfLSRNVNEgFSGGEK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 143 QRLGLAELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSH---LLDVVQTvcTRVALFNRGRIgfvgt 219
Cdd:CHL00131 158 KRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHyqrLLDYIKP--DYVHVMQNGKI----- 230
|
250 260
....*....|....*....|...
gi 1345382048 220 laelaAKVGGDALEIDLEAESFD 242
Cdd:CHL00131 231 -----IKTGDAELAKELEKKGYD 248
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
19-196 |
5.59e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 55.59 E-value: 5.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 19 NVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVrLLDKDPLRDPLAVKQAA------GY-------LPD 85
Cdd:PRK11629 23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDV-IFNGQPMSKLSSAAKAElrnqklGFiyqfhhlLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 86 avgfydsLTARENLAFTARLAGFADVDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTS 165
Cdd:PRK11629 102 -------FTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTG 174
|
170 180 190
....*....|....*....|....*....|....
gi 1345382048 166 GLDPQSTE---ELLGFIAdfANEGRTVLVSSHLL 196
Cdd:PRK11629 175 NLDARNADsifQLLGELN--RLQGTAFLVVTHDL 206
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-223 |
5.62e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.17 E-value: 5.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 2 SGTVIEARGLTKAYKGRN----VVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSV---RLLDKDPLRDPL 74
Cdd:PRK10261 9 ARDVLAVENLNIAFMQEQqkiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdKMLLRRRSRQVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 75 AV-KQAAGYLPDAVG------FYDSLTAR-------ENLAFTARL-AGFADVDASGRIGQALGRVRL---DGVADRKVGT 136
Cdd:PRK10261 89 ELsEQSAAQMRHVRGadmamiFQEPMTSLnpvftvgEQIAESIRLhQGASREEAMVEAKRMLDQVRIpeaQTILSRYPHQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 137 FSRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANE-GRTVLVSSHLLDVVQTVCTRVALFNRGRIG 215
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
....*...
gi 1345382048 216 FVGTLAEL 223
Cdd:PRK10261 249 ETGSVEQI 256
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-214 |
9.42e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.52 E-value: 9.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 20 VVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPLA-VKQAAGYLPDAVGFYdSLTAREN 98
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTdLRRVLSIIPQSPVLF-SGTVRFN 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 99 LAftarlaGFADVDASGrIGQALGRVRLDGVADRKV-----------GTFSRGMRQRLGLAELLMRDCQIMILDEPTSGL 167
Cdd:PLN03232 1330 ID------PFSEHNDAD-LWEALERAHIKDVIDRNPfgldaevseggENFSVGQRQLLSLARALLRRSKILVLDEATASV 1402
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1345382048 168 DPQsTEELLGFIADFANEGRTVLVSSHLLDVVQTvCTRVALFNRGRI 214
Cdd:PLN03232 1403 DVR-TDSLIQRTIREEFKSCTMLVIAHRLNTIID-CDKILVLSSGQV 1447
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
24-224 |
1.22e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.14 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 24 INLTVKQGEVLGLLGPNGAGKTTTILMLMG-LTEANAGSVrlldkdplrdplAVKQAAGYLPDAVGFYDSlTARENLAFT 102
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSV------------VIRGSVAYVPQVSWIFNA-TVRENILFG 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 103 ARLAgfadvdaSGRIGQAL-------------GRVRLDgVADRKVgTFSRGMRQRLGLAELLMRDCQIMILDEPTSGLDP 169
Cdd:PLN03232 703 SDFE-------SERYWRAIdvtalqhdldllpGRDLTE-IGERGV-NISGGQKQRVSMARAVYSNSDIYIFDDPLSALDA 773
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1345382048 170 QSTEELLGFIADFANEGRT-VLVSS--HLLDVVQtvctRVALFNRGRIGFVGTLAELA 224
Cdd:PLN03232 774 HVAHQVFDSCMKDELKGKTrVLVTNqlHFLPLMD----RIILVSEGMIKEEGTFAELS 827
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-197 |
1.55e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 54.76 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 1 MSGTVIEARGLTKAYKGRN--VVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSV----RLLDKDPLRDpl 74
Cdd:PRK13648 3 DKNSIIVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnQAITDDNFEK-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 75 aVKQAAGYL---PDA--VGF---YDSLTARENLAFTARlagfadvDASGRIGQALGRVRLDGVADRKVGTFSRGMRQRLG 146
Cdd:PRK13648 81 -LRKHIGIVfqnPDNqfVGSivkYDVAFGLENHAVPYD-------EMHRRVSEALKQVDMLERADYEPNALSGGQKQRVA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1345382048 147 LAELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVS-SHLLD 197
Cdd:PRK13648 153 IAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISiTHDLS 204
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
121-201 |
2.91e-08 |
|
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: 52.71 E-value: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 121 LGRVRLDgvadRKVGTFSRGMRQRLGLAELLMRDCQ--IMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDV 198
Cdd:cd03238 76 LGYLTLG----QKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDV 151
|
...
gi 1345382048 199 VQT 201
Cdd:cd03238 152 LSS 154
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
17-176 |
3.23e-08 |
|
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: 52.16 E-value: 3.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 17 GRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVrllDKDPLRDPLAVKQAaGYLPDAvgfydslTAR 96
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---GMPEGEDLLFLPQR-PYLPLG-------TLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 97 ENLAFtarlagfadvdasgrigqALGRVrldgvadrkvgtFSRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQSTEELL 176
Cdd:cd03223 82 EQLIY------------------PWDDV------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLY 131
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-213 |
5.59e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 53.94 E-value: 5.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 18 RNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEAN-----AGSVR-----LLDKDP--LRDPLAVKQAAGYLPD 85
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRfhgesLLHASEqtLRGVRGNKIAMIFQEP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 86 AVGFYDSLTARENLAFTARL-AGFADVDASGRIGQALGRVRLDGVADRkVGTF----SRGMRQRLGLAELLMRDCQIMIL 160
Cdd:PRK15134 102 MVSLNPLHTLEKQLYEVLSLhRGMRREAARGEILNCLDRVGIRQAAKR-LTDYphqlSGGERQRVMIAMALLTRPELLIA 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1345382048 161 DEPTSGLDPQSTEELLGFIADFANE-GRTVLVSSHLLDVVQTVCTRVALFNRGR 213
Cdd:PRK15134 181 DEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
31-194 |
5.78e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 54.08 E-value: 5.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 31 GEVLGLLGPNGAGKTTTILMLMGLTEAN--AGSVRLLDKDPLRDPLAvkQAAGYLPDAVGFYDSLTARENLAFTARLAGF 108
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFPKKQETFA--RISGYCEQNDIHSPQVTVRESLIYSAFLRLP 983
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 109 ADVDASGR---IGQALGRVRLDGVADRKVGT-----FSRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQSTEELLGFIA 180
Cdd:PLN03140 984 KEVSKEEKmmfVDEVMELVELDNLKDAIVGLpgvtgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVR 1063
|
170
....*....|....
gi 1345382048 181 DFANEGRTVLVSSH 194
Cdd:PLN03140 1064 NTVDTGRTVVCTIH 1077
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
11-196 |
8.43e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 53.25 E-value: 8.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 11 LTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLrdplavkqaaGYLpdAVGFY 90
Cdd:PRK10636 318 VSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKL----------GYF--AQHQL 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 91 DSLTAREN-LAFTARLagfADVDASGRIGQALGR--VRLDGVADrKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTSGL 167
Cdd:PRK10636 386 EFLRADESpLQHLARL---APQELEQKLRDYLGGfgFQGDKVTE-ETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHL 461
|
170 180 190
....*....|....*....|....*....|.
gi 1345382048 168 DPQSTEELLGFIADFanEGRTVLVS--SHLL 196
Cdd:PRK10636 462 DLDMRQALTEALIDF--EGALVVVShdRHLL 490
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
137-197 |
1.13e-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: 52.39 E-value: 1.13e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1345382048 137 FSRGMRQRLGLAELLMRDCQ---IMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSH---LLD 197
Cdd:pfam13304 237 LSDGTKRLLALLAALLSALPkggLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHsplLLD 303
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-194 |
1.22e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 52.99 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 2 SGTVIEARGLTKAYK--GRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANaGSVRLldkDPLR-DPLAVKQ 78
Cdd:TIGR01271 1214 SGGQMDVQGLTAKYTeaGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQI---DGVSwNSVTLQT 1289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 79 ---AAGYLPDAVgFYDSLTARENLAFTARLAG------FADVDASGRIGQALGrvRLDGVADRKVGTFSRGMRQRLGLAE 149
Cdd:TIGR01271 1290 wrkAFGVIPQKV-FIFSGTFRKNLDPYEQWSDeeiwkvAEEVGLKSVIEQFPD--KLDFVLVDGGYVLSNGHKQLMCLAR 1366
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1345382048 150 LLMRDCQIMILDEPTSGLDPQSTEELLGFIAD-FANegRTVLVSSH 194
Cdd:TIGR01271 1367 SILSKAKILLLDEPSAHLDPVTLQIIRKTLKQsFSN--CTVILSEH 1410
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
4-168 |
1.26e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 51.71 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 4 TVIEARGLTKAYKGR---------NVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVrLLDKDPL---- 70
Cdd:PRK15112 3 TLLEVRNLSKTFRYRtgwfrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGEL-LIDDHPLhfgd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 71 ------------RDP---LAVKQAAGYLPDavgfydsLTARENLAFTARlagfadvDASGRIGQALGRVRL-DGVADRKV 134
Cdd:PRK15112 82 ysyrsqrirmifQDPstsLNPRQRISQILD-------FPLRLNTDLEPE-------QREKQIIETLRQVGLlPDHASYYP 147
|
170 180 190
....*....|....*....|....*....|....
gi 1345382048 135 GTFSRGMRQRLGLAELLMRDCQIMILDEPTSGLD 168
Cdd:PRK15112 148 HMLAPGQKQRLGLARALILRPKVIIADEALASLD 181
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
131-248 |
1.31e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 52.91 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 131 DRKVGTFSRGMRQRLGLAELLMRDCQ-IM-ILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSH------LLDVVQTV 202
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHLGAELIgITyILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHdeqmisLADRIIDI 550
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1345382048 203 CTRVALFNrGRIGFVGTLAE-------LAAKVGGDALEIDLEAESFDAAARLS 248
Cdd:PRK00635 551 GPGAGIFG-GEVLFNGSPREflaksdsLTAKYLRQELTIPIPEKRTNSLGTLT 602
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
22-214 |
1.51e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 52.65 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 22 DGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRL--------LDKDPLR-------DPLA--VKQAAGYLP 84
Cdd:PRK11147 20 DNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYeqdlivarLQQDPPRnvegtvyDFVAegIEEQAEYLK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 85 DavgfYDSLTAR-------ENLAFTARLAgfADVDASG------RIGQALGRVRLDgvADRKVGTFSRGMRQRLGLAELL 151
Cdd:PRK11147 100 R----YHDISHLvetdpseKNLNELAKLQ--EQLDHHNlwqlenRINEVLAQLGLD--PDAALSSLSGGWLRKAALGRAL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1345382048 152 MRDCQIMILDEPTSGLDPQSTEELLGFIADFanEGRTVLVsSHLLDVVQTVCTRVALFNRGRI 214
Cdd:PRK11147 172 VSNPDVLLLDEPTNHLDIETIEWLEGFLKTF--QGSIIFI-SHDRSFIRNMATRIVDLDRGKL 231
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
18-168 |
1.51e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.48 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 18 RNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPL-----RDPLAVKQAAGYLPDAVGFYDS 92
Cdd:PRK10636 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLawvnqETPALPQPALEYVIDGDREYRQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 93 LTARENLAfTARLAGFADVDASGRIG-------QALGRVRLDGVA------DRKVGTFSRGMRQRLGLAELLMRDCQIMI 159
Cdd:PRK10636 94 LEAQLHDA-NERNDGHAIATIHGKLDaidawtiRSRAASLLHGLGfsneqlERPVSDFSGGWRMRLNLAQALICRSDLLL 172
|
....*....
gi 1345382048 160 LDEPTSGLD 168
Cdd:PRK10636 173 LDEPTNHLD 181
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
108-201 |
1.53e-07 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 51.46 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 108 FADVDASGRIGQALGRVRLDGVadrKVG----TFSRGMRQRLGLA-ELLMRDC--QIMILDEPTSGLDPQSTEELLGFIA 180
Cdd:cd03271 140 FENIPKIARKLQTLCDVGLGYI---KLGqpatTLSGGEAQRIKLAkELSKRSTgkTLYILDEPTTGLHFHDVKKLLEVLQ 216
|
90 100
....*....|....*....|.
gi 1345382048 181 DFANEGRTVLVSSHLLDVVQT 201
Cdd:cd03271 217 RLVDKGNTVVVIEHNLDVIKC 237
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
20-229 |
1.54e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.82 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 20 VVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPLA-VKQAAGYLPDA-VGFydSLTARE 97
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMdLRKVLGIIPQApVLF--SGTVRF 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 98 NL-AFTARlagfADVDasgrIGQALGRVRLDGVADRK-VG----------TFSRGMRQRLGLAELLMRDCQIMILDEPTS 165
Cdd:PLN03130 1332 NLdPFNEH----NDAD----LWESLERAHLKDVIRRNsLGldaevseageNFSVGQRQLLSLARALLRRSKILVLDEATA 1403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1345382048 166 GLDP------QST--EELlgfiadfanEGRTVLVSSHLLDVVQTvCTRVALFNRGRIGFVGTLAELAAKVGG 229
Cdd:PLN03130 1404 AVDVrtdaliQKTirEEF---------KSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLSNEGS 1465
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
138-200 |
1.87e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 50.05 E-value: 1.87e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1345382048 138 SRGMRQRLGLAELL----MRDCQIMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQ 200
Cdd:cd03227 79 SGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAE 145
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-226 |
1.91e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 52.61 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 20 VVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLrDPLAVKQAAGYLPDAVGF---YDSLTAR 96
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISF-SPQTSWIMPGTIKDNIIFglsYDEYRYT 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 97 ENL---AFTARLAGFADVDASgrigqalgrVRLDGVAdrkvgTFSRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQSTE 173
Cdd:TIGR01271 520 SVIkacQLEEDIALFPEKDKT---------VLGEGGI-----TLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEK 585
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1345382048 174 ELLG--FIADFANEGRtVLVSSHLLDVVQTvcTRVALFNRGRIGFVGTLAELAAK 226
Cdd:TIGR01271 586 EIFEscLCKLMSNKTR-ILVTSKLEHLKKA--DKILLLHEGVCYFYGTFSELQAK 637
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
20-223 |
2.59e-07 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 51.01 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 20 VVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLrdplaVKQAAGYLPDavgfydslTARENL 99
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISF-----SSQFSWIMPG--------TIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 100 AFTAR------------------LAGFADVDASgrigqALGRvrlDGVadrkvgTFSRGMRQRLGLAELLMRDCQIMILD 161
Cdd:cd03291 119 IFGVSydeyryksvvkacqleedITKFPEKDNT-----VLGE---GGI------TLSGGQRARISLARAVYKDADLYLLD 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1345382048 162 EPTSGLDPQSTEELLG--FIADFANEGRtVLVSSHLLDVVQTvcTRVALFNRGRIGFVGTLAEL 223
Cdd:cd03291 185 SPFGYLDVFTEKEIFEscVCKLMANKTR-ILVTSKMEHLKKA--DKILILHEGSSYFYGTFSEL 245
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
17-193 |
2.76e-07 |
|
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: 49.95 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 17 GRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANA---GSVRLLDKDPLRDPLAVKQAAGYLPDAVGFYDSL 93
Cdd:cd03233 19 KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 94 TARENLAFTARLAGfadvdasgrigqalgrvrldgvaDRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQSTE 173
Cdd:cd03233 99 TVRETLDFALRCKG-----------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTAL 155
|
170 180
....*....|....*....|
gi 1345382048 174 ELLGFIADFANEGRTVLVSS 193
Cdd:cd03233 156 EILKCIRTMADVLKTTTFVS 175
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
6-170 |
3.02e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 51.51 E-value: 3.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRNV-VDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVrLLDKDPL--RDPLAVKQAAGY 82
Cdd:PRK10522 323 LELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEI-LLDGKPVtaEQPEDYRKLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 83 LPDAVGFYDSLTARENLAftarlAGFADVDASGRIGQALGRVRLDG--VADRKvgtFSRGMRQRLGL--AELLMRDcqIM 158
Cdd:PRK10522 402 VFTDFHLFDQLLGPEGKP-----ANPALVEKWLERLKMAHKLELEDgrISNLK---LSKGQKKRLALllALAEERD--IL 471
|
170
....*....|..
gi 1345382048 159 ILDEPTSGLDPQ 170
Cdd:PRK10522 472 LLDEWAADQDPH 483
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
6-194 |
3.90e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.17 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 6 IEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMG-LTEANAGSVRLLDK-----DPLRDplaVKQA 79
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdHPQGYSNDLTLFGRrrgsgETIWD---IKKH 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 80 AGYLPDAV----------------GFYDSLTAREnlAFTARLAGFADvdasgrigQALGRVRLDG-VADRKVGTFSRGmR 142
Cdd:PRK10938 338 IGYVSSSLhldyrvstsvrnvilsGFFDSIGIYQ--AVSDRQQKLAQ--------QWLDILGIDKrTADAPFHSLSWG-Q 406
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1345382048 143 QRLGL-AELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANEGRTVL--VSSH 194
Cdd:PRK10938 407 QRLALiVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLlfVSHH 461
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
28-209 |
9.98e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 48.34 E-value: 9.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 28 VKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPLAVKQAAGYLpdavgfydsltarenlaftarlag 107
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQYIDLSGGEL------------------------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 108 fadvdasgrigqalgrvrldgvadrkvgtfsrgmrQRLGLAELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANEG- 186
Cdd:cd03222 78 -----------------------------------QRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGk 122
|
170 180
....*....|....*....|...
gi 1345382048 187 RTVLVSSHLLDVVQTVCTRVALF 209
Cdd:cd03222 123 KTALVVEHDLAVLDYLSDRIHVF 145
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-211 |
1.01e-06 |
|
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: 47.75 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 30 QGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDplavkqaagylpdavgfydsltarenlaftarlagfa 109
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILE------------------------------------- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 110 dvdasgrigqALGRVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFAN----- 184
Cdd:smart00382 44 ----------EVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLlllks 113
|
170 180
....*....|....*....|....*...
gi 1345382048 185 -EGRTVLVSSHLLDVVQTVCTRVALFNR 211
Cdd:smart00382 114 eKNLTVILTTNDEKDLGPALLRRRFDRR 141
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4-226 |
1.09e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.73 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 4 TVIEARGLTkAYKGRNVVDgINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKdplrdplAVKQAAGYL 83
Cdd:PRK10982 249 VILEVRNLT-SLRQPSIRD-VSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGK-------KINNHNANE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 84 PDAVGFYDSLTARENLAFTARLA-GFADVDASgrIGQALGRVRLdgVADRK----------------------VGTFSRG 140
Cdd:PRK10982 320 AINHGFALVTEERRSTGIYAYLDiGFNSLISN--IRNYKNKVGL--LDNSRmksdtqwvidsmrvktpghrtqIGSLSGG 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 141 MRQRLGLAELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQTVCTRVALFNRGRI-GFVGT 219
Cdd:PRK10982 396 NQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVaGIVDT 475
|
250
....*....|....
gi 1345382048 220 -------LAELAAK 226
Cdd:PRK10982 476 ktttqneILRLASL 489
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
137-213 |
2.07e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 49.26 E-value: 2.07e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1345382048 137 FSRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQSTEELLGFIADF-ANEGRTVLVSSHLLDVVQTVCTRVALFNRGR 213
Cdd:PTZ00265 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRITIIIAHRLSTIRYANTIFVLSNRER 657
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
17-168 |
2.48e-06 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 47.79 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 17 GRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLR-DPLAVKQAAGYLPDA-VGFYDslT 94
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTlKPEIYRQQVSYCAQTpTLFGD--T 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1345382048 95 ARENLAFTARLAGFA-DVDAsgrIGQALGRVRL-DGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTSGLD 168
Cdd:PRK10247 97 VYDNLIFPWQIRNQQpDPAI---FLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
24-222 |
2.93e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 48.33 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 24 INLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKdPLRDP-----LAV-KQAAGYLpdavgFYDS----- 92
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGR-VLFDAekgicLPPeKRRIGYV-----FQDArlfph 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 93 LTARENLAFtarlaGFADVDAS--GRIGQALGrvrLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQ 170
Cdd:PRK11144 91 YKVRGNLRY-----GMAKSMVAqfDKIVALLG---IEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1345382048 171 STEELLGFIADFANEGRT-VLVSSHLLDVVQTVCTRVALFNRGRIGFVGTLAE 222
Cdd:PRK11144 163 RKRELLPYLERLAREINIpILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
24-225 |
3.24e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.62 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 24 INLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVrlldkdplrdpLAVKQAAgYLPDAVGFYDSlTARENLAF-- 101
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-----------WAERSIA-YVPQQAWIMNA-TVRGNILFfd 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 102 ---TARLAgfadvDASgRIGQALGRVR-LDGVADRKVG----TFSRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQSTE 173
Cdd:PTZ00243 746 eedAARLA-----DAV-RVSQLEADLAqLGGGLETEIGekgvNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGE 819
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1345382048 174 E-----LLGFIAdfaneGRTVLVSSHLLDVVQTVCTRVALfNRGRIGFVGTLAELAA 225
Cdd:PTZ00243 820 RvveecFLGALA-----GKTRVLATHQVHVVPRADYVVAL-GDGRVEFSGSSADFMR 870
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
144-213 |
3.93e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 46.83 E-value: 3.93e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1345382048 144 RLGLAELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANE--GRTVLVSSH---LLDVVQTVCtRVALFNRGR 213
Cdd:cd03240 129 RLALAETFGSNCGILALDEPTTNLDEENIEESLAEIIEERKSqkNFQLIVITHdeeLVDAADHIY-RVEKDGRQK 202
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
121-201 |
7.50e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 47.32 E-value: 7.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 121 LGRVRLDgvadRKVGTFSRGMRQRLGLA-ELLMRDC--QIMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLD 197
Cdd:TIGR00630 818 LGYIRLG----QPATTLSGGEAQRIKLAkELSKRSTgrTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLD 893
|
....
gi 1345382048 198 VVQT 201
Cdd:TIGR00630 894 VIKT 897
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
24-196 |
8.28e-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: 46.17 E-value: 8.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 24 INLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPLAVKQAAGYLPDAVGFYDS----LTARENL 99
Cdd:cd03290 20 INIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPwllnATVEENI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 100 AFtarlagfadvdasgriGQALGRVRLDGVAD----------------RKVG----TFSRGMRQRLGLAELLMRDCQIMI 159
Cdd:cd03290 100 TF----------------GSPFNKQRYKAVTDacslqpdidllpfgdqTEIGergiNLSGGQRQRICVARALYQNTNIVF 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 1345382048 160 LDEPTSGLDPQSTEELL--GFIADFANEGRTVLVSSHLL 196
Cdd:cd03290 164 LDDPFSALDIHLSDHLMqeGILKFLQDDKRTLVLVTHKL 202
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
21-168 |
9.65e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 46.66 E-value: 9.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 21 VDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTE----ANAGSVRLLDKDPLRDPLAVKQAAGYLPDAVGFYDSLTAR 96
Cdd:PRK11022 23 VDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRISEKERRNLVGAEVAMIFQDPMTSL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 97 eNLAFTarlAGFADVDA---------SGRIGQALGRVRLDGVAD--RKVGTF----SRGMRQRLGLAELLMRDCQIMILD 161
Cdd:PRK11022 103 -NPCYT---VGFQIMEAikvhqggnkKTRRQRAIDLLNQVGIPDpaSRLDVYphqlSGGMSQRVMIAMAIACRPKLLIAD 178
|
....*..
gi 1345382048 162 EPTSGLD 168
Cdd:PRK11022 179 EPTTALD 185
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
5-70 |
1.70e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 45.17 E-value: 1.70e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1345382048 5 VIEARGLTKAYKGRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLT--EANAGSVRLLDKDPL 70
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLL 68
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
131-223 |
2.27e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.18 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 131 DRKVGTF----SRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANEG-RTVLVSSHLLDVVQTVCTR 205
Cdd:PTZ00265 1349 DTNVGPYgkslSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASIKRSDKI 1428
|
90 100
....*....|....*....|..
gi 1345382048 206 VALFNRGRIG-FV---GTLAEL 223
Cdd:PTZ00265 1429 VVFNNPDRTGsFVqahGTHEEL 1450
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
21-192 |
3.64e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.48 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 21 VDGInltVKQGEVLGLLGPNGAGKTTTILMLMGLTEA---NAGSVRLLDKDPLRDplAVKQAAG---YLPDAVGFYDSLT 94
Cdd:TIGR00956 80 MDGL---IKPGELTVVLGRPGSGCSTLLKTIASNTDGfhiGVEGVITYDGITPEE--IKKHYRGdvvYNAETDVHFPHLT 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 95 ARENLAFTARLAGFA--------DVDASGRIGQALGRVRLDGVADRKVGT-FSRGM----RQRLGLAELLMRDCQIMILD 161
Cdd:TIGR00956 155 VGETLDFAARCKTPQnrpdgvsrEEYAKHIADVYMATYGLSHTRNTKVGNdFVRGVsggeRKRVSIAEASLGGAKIQCWD 234
|
170 180 190
....*....|....*....|....*....|....
gi 1345382048 162 EPTSGLDPQSTEEL---LGFIADFANEgrTVLVS 192
Cdd:TIGR00956 235 NATRGLDSATALEFiraLKTSANILDT--TPLVA 266
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
131-200 |
4.80e-05 |
|
ATP-binding cassette domain I 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: 213237 [Multi-domain] Cd Length: 226 Bit Score: 43.79 E-value: 4.80e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1345382048 131 DRKVGTFSRGMRQRLGLAELLMRDCQ--IMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQ 200
Cdd:cd03270 132 SRSAPTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIR 203
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
20-214 |
5.55e-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: 43.74 E-value: 5.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 20 VVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLRDPLAVKQA--AGYLPDAVGFYDSLtaRE 97
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSrlSIILQDPILFSGSI--RF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 98 NLAFTARLAGFADVDASgRIGQALGRVR-----LDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTSGLDpQST 172
Cdd:cd03288 114 NLDPECKCTDDRLWEAL-EIAQLKNMVKslpggLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASID-MAT 191
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1345382048 173 EELLGFIADFANEGRTVLVSSHLLDVVQTVcTRVALFNRGRI 214
Cdd:cd03288 192 ENILQKVVMTAFADRTVVTIAHRVSTILDA-DLVLVLSRGIL 232
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
131-194 |
1.27e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.46 E-value: 1.27e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1345382048 131 DRKVGTFSRGMRQRLGLAEllmrdcQI--------MILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSH 194
Cdd:TIGR00630 483 SRAAGTLSGGEAQRIRLAT------QIgsgltgvlYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEH 548
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
119-201 |
2.14e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 119 QALGRVRLDGVA-DRKVGTFSRGMRQRLGLA-ELL--MRDCQIMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSH 194
Cdd:PRK00635 791 HALCSLGLDYLPlGRPLSSLSGGEIQRLKLAyELLapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEH 870
|
....*..
gi 1345382048 195 LLDVVQT 201
Cdd:PRK00635 871 NMHVVKV 877
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
17-169 |
2.20e-04 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 42.81 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 17 GRNVVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGsvrLLDKDPlrdplavKQAAGYLPDAVgfYDSL-TA 95
Cdd:TIGR00954 464 GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGG---RLTKPA-------KGKLFYVPQRP--YMTLgTL 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 96 RENLAFTARLAGFADVDASGR-IGQALGRVRLDGVADRKVG---------TFSRGMRQRLGLAELLMRDCQIMILDEPTS 165
Cdd:TIGR00954 532 RDQIIYPDSSEDMKRRGLSDKdLEQILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTS 611
|
....
gi 1345382048 166 GLDP 169
Cdd:TIGR00954 612 AVSV 615
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
17-206 |
5.45e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.38 E-value: 5.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 17 GRNVVDGINLTVKQGEVLGLLGPNGAGKTT-----------------------------TILMLMGLTEANAGSVRLLDK 67
Cdd:PLN03073 189 GRDLIVDASVTLAFGRHYGLVGRNGTGKTTflrymamhaidgipkncqilhveqevvgdDTTALQCVLNTDIERTQLLEE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 68 DPlrdPLAVKQAAGYLPDAVGFY--DSLTARENLAFTARLAG------FADVD-ASGRIGQALGRVRLDG-VADRKVGTF 137
Cdd:PLN03073 269 EA---QLVAQQRELEFETETGKGkgANKDGVDKDAVSQRLEEiykrleLIDAYtAEARAASILAGLSFTPeMQVKATKTF 345
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1345382048 138 SRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFAnegRTVLVSSHLLDVVQTVCTRV 206
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP---KTFIVVSHAREFLNTVVTDI 411
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
119-201 |
6.74e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.21 E-value: 6.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 119 QALGRVRLDGVadrKVG----TFSRGMRQRLGLA-ELLMRDC--QIMILDEPTSGLDPQSTEELLGFIADFANEGRTVLV 191
Cdd:PRK00349 812 QTLVDVGLGYI---KLGqpatTLSGGEAQRVKLAkELSKRSTgkTLYILDEPTTGLHFEDIRKLLEVLHRLVDKGNTVVV 888
|
90
....*....|
gi 1345382048 192 SSHLLDVVQT 201
Cdd:PRK00349 889 IEHNLDVIKT 898
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
131-191 |
2.45e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 39.23 E-value: 2.45e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1345382048 131 DRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQSTEELLGFIADFANEGRT-VLV 191
Cdd:PRK10938 130 DRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITlVLV 191
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
24-225 |
2.65e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 39.72 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 24 INLTVKQGEVLGLLGPNGAGKTTTILMLMG-LTEANAGSVrlldkdplrdplAVKQAAGYLPDaVGFYDSLTARENLAF- 101
Cdd:PLN03130 636 INLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASV------------VIRGTVAYVPQ-VSWIFNATVRDNILFg 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 102 ----TARLAGFADVDASGRIGQALGRVRLDGVADRKVgTFSRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQSTEELLG 177
Cdd:PLN03130 703 spfdPERYERAIDVTALQHDLDLLPGGDLTEIGERGV-NISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFD 781
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1345382048 178 FIADFANEGRT-VLVSS--HLLDVVQtvctRVALFNRGRIGFVGTLAELAA 225
Cdd:PLN03130 782 KCIKDELRGKTrVLVTNqlHFLSQVD----RIILVHEGMIKEEGTYEELSN 828
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
136-201 |
4.31e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.85 E-value: 4.31e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1345382048 136 TFSRGMRQRLGLA-ELLMRDCQ--IMILDEPTSGLDPQSTEELLGFIADFANEGRTVLVSSHLLDVVQT 201
Cdd:COG0178 826 TLSGGEAQRVKLAsELSKRSTGktLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHNLDVIKT 894
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
20-71 |
5.67e-03 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 37.96 E-value: 5.67e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1345382048 20 VVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEAN----AGSVRLLDKDPLR 71
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtADRFRWNGIDLLK 77
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
20-242 |
8.37e-03 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 36.96 E-value: 8.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 20 VVDGINLTVKQGEVLGLLGPNGAGKTTTILMLMGLTEANAGSVRLLDKDPLrdPLAVKqaAGYLPdavgfydSLTARENL 99
Cdd:PRK15177 2 VLDKTDFVMGYHEHIGILAAPGSGKTTLTRLLCGLDAPDEGDFIGLRGDAL--PLGAN--SFILP-------GLTGEENA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1345382048 100 AFTARLAGFaDVDASGRIGQALgrVRLDGVADRKVGTFSRGMRQRLGLAELLMRDCQIMILDEPTSGLDPQSTEELLGFI 179
Cdd:PRK15177 71 RMMASLYGL-DGDEFSHFCYQL--TQLEQCYTDRVSEYSVTMKTHLAFAINLLLPCRLYIADGKLYTGDNATQLRMQAAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1345382048 180 A-DFANEGRTVLvsSHLLDVVQTVCTRVALFNRGRIGFVGTLAELAA---KVGGDALEIDLEAESFD 242
Cdd:PRK15177 148 AcQLQQKGLIVL--THNPRLIKEHCHAFGVLLHGKITMCEDLAQATAlfeQYQSNQATIQTEDYSFD 212
|
|
| |
