|
Name |
Accession |
Description |
Interval |
E-value |
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
6-242 |
4.71e-125 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 363.63 E-value: 4.71e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 6 VLDVHDVYKDFKLPTEQATGLKQAVINWTKGIRGYRWqhVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKG 85
Cdd:COG1134 4 MIEVENVSKSYRLYHEPSRSLKELLLRRRRTRREEFW--ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 86 SVSVSGKLVPFIELGVGFNPELTGRENVYLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAI 165
Cdd:COG1134 82 RVEVNGRVSALLELGAGFHPELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVAT 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2222587728 166 KAQGDILVLDEVLAVGDEAFQRKCDDFFTQIRKDpTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETVADRY 242
Cdd:COG1134 162 AVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAAY 237
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
7-233 |
1.19e-107 |
|
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: 318.32 E-value: 1.19e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 7 LDVHDVYKDFKLPTEQATGLKQavINWTKGIRGYRWQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGS 86
Cdd:cd03220 1 IELENVSKSYPTYKGGSSSLKK--LGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 87 VSVSGKLVPFIELGVGFNPELTGRENVYLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIK 166
Cdd:cd03220 79 VTVRGRVSSLLGLGGGFNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2222587728 167 AQGDILVLDEVLAVGDEAFQRKCDDFFTQIRKDpTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYG 233
Cdd:cd03220 159 LEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
5-260 |
4.35e-51 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 174.23 E-value: 4.35e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 5 VVLDVHDVYKDFKLPTEQATGLKQAVINWTKGIRGYrwqhVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNK 84
Cdd:PRK13546 3 VSVNIKNVTKEYRIYRTNKERMKDALIPKHKNKTFF----ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 85 GSVSVSGKlVPFIELGVGFNPELTGRENVYLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVA 164
Cdd:PRK13546 79 GKVDRNGE-VSVIAISAGLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSIN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 165 IKAQGDILVLDEVLAVGDEAFQRKCDDFFTQIrKDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETVADRYT- 243
Cdd:PRK13546 158 ITVNPDILVIDEALSVGDQTFAQKCLDKIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKYEa 236
|
250
....*....|....*...
gi 2222587728 244 -LSNLEAERKKGEKQARK 260
Cdd:PRK13546 237 fLNDFKKKSKAEQKEFRN 254
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
12-272 |
2.45e-49 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 177.00 E-value: 2.45e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 12 VYKDFKLPTEQATGLKQAVINWTKGirgyRWQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSG 91
Cdd:PRK13545 10 VTKKYKMYNKPFDKLKDLFFRSKDG----EYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 92 KlVPFIELGVGFNPELTGRENVYLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDI 171
Cdd:PRK13545 86 S-AALIAISSGLNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 172 LVLDEVLAVGDEAFQRKCDDFFTQIrKDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETVAD-------RYTL 244
Cdd:PRK13545 165 LVIDEALSVGDQTFTKKCLDKMNEF-KEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDhydeflkKYNQ 243
|
250 260
....*....|....*....|....*...
gi 2222587728 245 SNLEAERKKGEKQARKAAQALAQKDEQG 272
Cdd:PRK13545 244 MSVEERKDFREEQISQFQHGLLQEDQTG 271
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
44-250 |
1.02e-42 |
|
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: 151.16 E-value: 1.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 44 HVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSG-----------KLVPFIELGVGFNPELTGREN 112
Cdd:COG4555 15 PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrkeprearRQIGVLPDERGLYDRLTVREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 113 VYLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRKCDDF 192
Cdd:COG4555 95 IRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2222587728 193 FTQIRKDPtKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETVADRYTLSNLEAE 250
Cdd:COG4555 175 LRALKKEG-KTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEENLEDA 231
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
39-233 |
1.18e-34 |
|
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: 128.78 E-value: 1.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 39 GYRWQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLV------PFIELGV--GFN---PEL 107
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIrtdrkaARQSLGYcpQFDalfDEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 108 TGRENVYLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQR 187
Cdd:cd03263 91 TVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRR 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2222587728 188 KCDDFFTQIRKDptKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYG 233
Cdd:cd03263 171 AIWDLILEVRKG--RSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
40-229 |
7.67e-33 |
|
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: 122.51 E-value: 7.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 40 YRWQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVP-----------FIELGVGFNPELT 108
Cdd:cd03230 10 YGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKkepeevkrrigYLPEEPSLYENLT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 109 GRENVYlncallgfdheqtdamyddivefaelgdfmdqklknYSSGMQVRLAFSVAIKAQGDILVLDEVLaVG-DEAFQR 187
Cdd:cd03230 90 VRENLK------------------------------------LSGGMKQRLALAQALLHDPELLILDEPT-SGlDPESRR 132
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2222587728 188 KCDDFFTQIRKDpTKTVILVTHDMGAVKRYCTRAMMIEDGKI 229
Cdd:cd03230 133 EFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
45-233 |
1.72e-31 |
|
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: 120.08 E-value: 1.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPF-IELGVGFNPELTG-------REN-VYL 115
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIaARNRIGYLPEERGlypkmkvIDQlVYL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 116 nCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRKCDDFFTQ 195
Cdd:cd03269 95 -AQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRE 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 2222587728 196 IRkDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYG 233
Cdd:cd03269 174 LA-RAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
9-233 |
3.10e-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: 120.13 E-value: 3.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 9 VHDVYKDFKLpTEQATGLKQAVINWTKgiRGYRWQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVS 88
Cdd:cd03267 3 VSNLSKSYRV-YSKEPGLIGSLKSLFK--RKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 89 VSGkLVPFIE-------LGVGFNP------ELTGRENVYLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGM 155
Cdd:cd03267 80 VAG-LVPWKRrkkflrrIGVVFGQktqlwwDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2222587728 156 QVRLAFSVAIKAQGDILVLDEVlAVGDEAF-QRKCDDFFTQIRKDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYG 233
Cdd:cd03267 159 RMRAEIAAALLHEPEILFLDEP-TIGLDVVaQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
46-233 |
4.41e-31 |
|
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: 119.40 E-value: 4.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 46 LRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSG-----------KLVPFIELGVGFNPELTGRENVY 114
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvreprevrRRIGIVFQDLSVDDELTGWENLY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 115 LNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRKCDDFFT 194
Cdd:cd03265 96 IHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIE 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 2222587728 195 QIRKDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYG 233
Cdd:cd03265 176 KLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
40-233 |
2.04e-30 |
|
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: 116.93 E-value: 2.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 40 YRWQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLV-----PFIELGV-----GFNPELTG 109
Cdd:cd03268 10 YGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYqknieALRRIGAlieapGFYPNLTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 110 RENVYLNCALLGFDHEQTdamyDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRKC 189
Cdd:cd03268 90 RENLRLLARLLGIRKKRI----DEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKEL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2222587728 190 DDFFTQIRKDpTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYG 233
Cdd:cd03268 166 RELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-242 |
4.15e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 119.42 E-value: 4.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 6 VLDVHDVYKDFKLPtEQATGLKQAVINWTKgiRGYRWQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKG 85
Cdd:COG4586 1 IIEVENLSKTYRVY-EKEPGLKGALKGLFR--REYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 86 SVSVSGkLVPF---IEL----GVGF------NPELTGRENVYLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYS 152
Cdd:COG4586 78 EVRVLG-YVPFkrrKEFarriGVVFgqrsqlWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 153 SGMQVRLAFSVAIKAQGDILVLDE------VLAvgdeafQRKCDDFFTQIRKDPTKTVILVTHDMGAVKRYCTRAMMIED 226
Cdd:COG4586 157 LGQRMRCELAAALLHRPKILFLDEptigldVVS------KEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDH 230
|
250
....*....|....*.
gi 2222587728 227 GKIVAYGDKETVADRY 242
Cdd:COG4586 231 GRIIYDGSLEELKERF 246
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
39-233 |
1.36e-29 |
|
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: 114.94 E-value: 1.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 39 GYRWQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPFIELGVGFNPE---------LTG 109
Cdd:cd03235 8 SYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGYVPQrrsidrdfpISV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 110 RENVYLNCAL-LGFDHEQTDAMYDDI---VEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAF 185
Cdd:cd03235 88 RDVVLMGLYGhKGLFRRLSKADKAKVdeaLERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2222587728 186 QRkcdDFFTQIR--KDPTKTVILVTHDMGAVKRYCTRAMMIeDGKIVAYG 233
Cdd:cd03235 168 QE---DIYELLRelRREGMTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
38-229 |
1.95e-29 |
|
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: 114.51 E-value: 1.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 38 RGYRWQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLV---PFIELG------VGF----- 103
Cdd:cd03255 12 GGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIsklSEKELAafrrrhIGFvfqsf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 104 N--PELTGRENVYLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVG 181
Cdd:cd03255 92 NllPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2222587728 182 DEAFQRKCDDFFTQIRKDPTKTVILVTHDMgAVKRYCTRAMMIEDGKI 229
Cdd:cd03255 172 DSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
45-228 |
2.86e-29 |
|
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: 114.10 E-value: 2.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLV---PFIELG--VGF---NPE-----LTGRE 111
Cdd:cd03225 16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLtklSLKELRrkVGLvfqNPDdqffgPTVEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 112 NVYLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRKCDD 191
Cdd:cd03225 96 EVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLE 175
|
170 180 190
....*....|....*....|....*....|....*..
gi 2222587728 192 FFTQIRKDPtKTVILVTHDMGAVKRYCTRAMMIEDGK 228
Cdd:cd03225 176 LLKKLKAEG-KTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
44-311 |
3.48e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 113.28 E-value: 3.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 44 HVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPFIEL-GVGFNPE-------LTGREN-VY 114
Cdd:COG4152 15 TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRrRIGYLPEerglypkMKVGEQlVY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 115 LncALL-GFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDE------VLAVgdeafqr 187
Cdd:COG4152 95 L--ARLkGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEpfsgldPVNV------- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 188 kcDDFFTQIR--KDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETVADRYTLSNLEAERKKGEKQARKAAQAL 265
Cdd:COG4152 166 --ELLKDVIRelAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRNTLRLEADGDAGWLRALPGVT 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2222587728 266 AQKDEQGKAVPVFPNGLNARvPILRTypigspLIDGTQPFRFGVEY 311
Cdd:COG4152 244 VVEEDGDGAELKLEDGADAQ-ELLRA------LLARGPVREFEEVR 282
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
44-233 |
9.10e-28 |
|
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: 110.15 E-value: 9.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 44 HVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLV---PF---IELGV-----GFNPELTGREN 112
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVvkePAearRRLGFvsdstGLYDRLTAREN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 113 VYLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRKCDDF 192
Cdd:cd03266 99 LEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREF 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2222587728 193 FTQIRkDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYG 233
Cdd:cd03266 179 IRQLR-ALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
37-210 |
1.27e-27 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 109.11 E-value: 1.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 37 IRGYRWqhVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPFIELGV-----------GFNP 105
Cdd:COG4133 11 RRGERL--LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYrrrlaylghadGLKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 106 ELTGRENVYLNCALLGFDHEQTDAmyDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAF 185
Cdd:COG4133 89 ELTVRENLRFWAALYGLRADREAI--DEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAG 166
|
170 180
....*....|....*....|....*
gi 2222587728 186 QRKCDDFFTQiRKDPTKTVILVTHD 210
Cdd:COG4133 167 VALLAELIAA-HLARGGAVLLTTHQ 190
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
39-233 |
1.63e-27 |
|
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: 108.29 E-value: 1.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 39 GYRWQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVpfielgvgfnPELTGREnVYLNCA 118
Cdd:cd03214 8 GYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDL----------ASLSPKE-LARKIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 119 LLgfdhEQtdAMyddivEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRKCDDFFTQIRK 198
Cdd:cd03214 77 YV----PQ--AL-----ELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLAR 145
|
170 180 190
....*....|....*....|....*....|....*
gi 2222587728 199 DPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYG 233
Cdd:cd03214 146 ERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-249 |
1.70e-27 |
|
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: 115.00 E-value: 1.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 2 DAPVVLDVHDVYKDFklpteqatglkqavinwtkGIRGYRWQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYY 81
Cdd:COG1123 256 AAEPLLEVRNLSKRY-------------------PVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLR 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 82 PNKGSVSVSGKLVPFIELG--------VG---------FNPELTGRENVYLNCALLG-FDHEQTDAMYDDIVEFAELG-D 142
Cdd:COG1123 317 PTSGSILFDGKDLTKLSRRslrelrrrVQmvfqdpyssLNPRMTVGDIIAEPLRLHGlLSRAERRERVAELLERVGLPpD 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 143 FMDQklknY----SSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRKCDDFFTQIRKDPTKTVILVTHDMGAVKRYC 218
Cdd:COG1123 397 LADR----YphelSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIA 472
|
250 260 270
....*....|....*....|....*....|....*
gi 2222587728 219 TRAMMIEDGKIVAYGDKETVADR----YTLSNLEA 249
Cdd:COG1123 473 DRVAVMYDGRIVEDGPTEEVFANpqhpYTRALLAA 507
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
40-228 |
1.74e-27 |
|
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: 107.33 E-value: 1.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 40 YRWQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKlvpfielGVGFNPELTGRENVYlncal 119
Cdd:cd00267 9 YGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGK-------DIAKLPLEELRRRIG----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 120 lgfdheqtdamyddivefaelgdFMDQklknYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRKCDDFFTQIRKD 199
Cdd:cd00267 77 -----------------------YVPQ----LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEE 129
|
170 180
....*....|....*....|....*....
gi 2222587728 200 pTKTVILVTHDMGAVKRYCTRAMMIEDGK 228
Cdd:cd00267 130 -GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
44-239 |
2.76e-27 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 109.06 E-value: 2.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 44 HVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLV----PF--IELGVG--------FnPELTG 109
Cdd:cd03219 14 VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDItglpPHeiARLGIGrtfqiprlF-PELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 110 RENV----------YLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLA 179
Cdd:cd03219 93 LENVmvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAA 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2222587728 180 -VGDEAFQRKCdDFFTQIRKDpTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETVA 239
Cdd:cd03219 173 gLNPEETEELA-ELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVR 231
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
46-176 |
3.66e-27 |
|
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: 106.19 E-value: 3.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 46 LRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPFI-------ELGV-----GFNPELTGRENV 113
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDerkslrkEIGYvfqdpQLFPRLTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2222587728 114 YLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNY----SSGMQVRLAFSVAIKAQGDILVLDE 176
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGERpgtlSGGQRQRVAIARALLTKPKLLLLDE 147
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
44-231 |
7.87e-27 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 107.82 E-value: 7.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 44 HVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVpfIELG-----------VGF-----N--P 105
Cdd:COG1136 22 TALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDI--SSLSerelarlrrrhIGFvfqffNllP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 106 ELTGRENVYLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDE--------- 176
Cdd:COG1136 100 ELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEptgnldskt 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2222587728 177 ---VLavgdeafqrkcdDFFTQIRKDPTKTVILVTHDMgAVKRYCTRAMMIEDGKIVA 231
Cdd:COG1136 180 geeVL------------ELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRIVS 224
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
44-238 |
1.72e-26 |
|
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: 106.90 E-value: 1.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 44 HVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPFI----------ELGV---GFN--PELT 108
Cdd:cd03258 19 TALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLsgkelrkarrRIGMifqHFNllSSRT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 109 GRENVYLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRK 188
Cdd:cd03258 99 VFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQS 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2222587728 189 CDDFFTQIRKDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETV 238
Cdd:cd03258 179 ILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
39-238 |
5.63e-26 |
|
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: 105.90 E-value: 5.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 39 GYRWQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLV---PFIELG--VGF-------NPE 106
Cdd:COG1120 10 GYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLaslSRRELArrIAYvpqeppaPFG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 107 LTGRENVYLNCA----LLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIkAQG-DILVLDEVLAVG 181
Cdd:COG1120 90 LTVRELVALGRYphlgLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARAL-AQEpPLLLLDEPTSHL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2222587728 182 DEAFQRKCDDFFTQIRKDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETV 238
Cdd:COG1120 169 DLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
30-233 |
4.00e-25 |
|
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: 102.97 E-value: 4.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 30 VINWTKGIR-GYRWQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVP------------- 95
Cdd:cd03257 4 VKNLSVSFPtGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLklsrrlrkirrke 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 96 ----FIELGVGFNPELTGRENVY--LNCALLGFDHEQTD-AMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQ 168
Cdd:cd03257 84 iqmvFQDPMSSLNPRMTIGEQIAepLRIHGKLSKKEARKeAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARALALN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2222587728 169 GDILVLDEVLAVGDEAFQRKCDDFFTQIRKDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYG 233
Cdd:cd03257 164 PKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
43-236 |
4.56e-25 |
|
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: 102.97 E-value: 4.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 43 QHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVP---FIEL-------GVGFN-----PEL 107
Cdd:cd03261 13 RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglsEAELyrlrrrmGMLFQsgalfDSL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 108 TGRENVylncALLGFDHEQ-TDAMYDDIV----EFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGD 182
Cdd:cd03261 93 TVFENV----AFPLREHTRlSEEEIREIVleklEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2222587728 183 EAFQRKCDDFFTQIRKDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKE 236
Cdd:cd03261 169 PIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPE 222
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
41-264 |
5.98e-25 |
|
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: 107.30 E-value: 5.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 41 RWQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPN---KGSVSVSGKLVP--------------FIELGVGF 103
Cdd:COG1123 17 GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLelsealrgrrigmvFQDPMTQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 104 NPeLTGRENVYLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDE 183
Cdd:COG1123 97 NP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 184 AFQRKCDDFFTQIRKDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETVADRYTLsnLEAERKKGEKQARKAAQ 263
Cdd:COG1123 176 TTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQA--LAAVPRLGAARGRAAPA 253
|
.
gi 2222587728 264 A 264
Cdd:COG1123 254 A 254
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
40-233 |
6.68e-25 |
|
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: 101.83 E-value: 6.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 40 YRWQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLV---PFIELGVGF-------NPELTG 109
Cdd:cd03259 10 YGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVtgvPPERRNIGMvfqdyalFPHLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 110 RENVYLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRKC 189
Cdd:cd03259 90 AENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREEL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2222587728 190 DDFFTQIRKDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYG 233
Cdd:cd03259 170 REELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
39-240 |
9.39e-25 |
|
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: 101.74 E-value: 9.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 39 GYRWQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLV----PF--IELGVGFNPE------ 106
Cdd:cd03224 9 GYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDItglpPHerARAGIGYVPEgrrifp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 107 -LTGRENVYLncALLGFDHEQTDAMYDDIVE-FAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEV---LA-- 179
Cdd:cd03224 89 eLTVEENLLL--GAYARRRAKRKARLERVYElFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPsegLApk 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2222587728 180 VGDEAFqrkcdDFFTQIRKDPTkTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETVAD 240
Cdd:cd03224 167 IVEEIF-----EAIRELRDEGV-TILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
3-238 |
6.86e-24 |
|
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: 100.11 E-value: 6.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 3 APVVLDVHDVYKDFKlpteqatGLKqavinwtkgirgyrwqhVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYP 82
Cdd:COG0411 1 SDPLLEVRGLTKRFG-------GLV-----------------AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRP 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 83 NKGSVSVSGK----LVPF--IELGVG--------FnPELTGRENVYL----------NCALLGF-----DHEQTDAMYDD 133
Cdd:COG0411 57 TSGRILFDGRditgLPPHriARLGIArtfqnprlF-PELTVLENVLVaaharlgrglLAALLRLprarrEEREARERAEE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 134 IVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAvG---DEAfqRKCDDFFTQIRKDPTKTVILVTHD 210
Cdd:COG0411 136 LLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAA-GlnpEET--EELAELIRRLRDERGITILLIEHD 212
|
250 260
....*....|....*....|....*...
gi 2222587728 211 MGAVKRYCTRAMMIEDGKIVAYGDKETV 238
Cdd:COG0411 213 MDLVMGLADRIVVLDFGRVIAEGTPAEV 240
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
39-211 |
9.57e-24 |
|
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: 99.08 E-value: 9.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 39 GYRWQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLV--PFIELGVGFN-----PELTGRE 111
Cdd:cd03293 13 GGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVtgPGPDRGYVFQqdallPWLTVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 112 NVYLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRKCDD 191
Cdd:cd03293 93 NVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQE 172
|
170 180
....*....|....*....|
gi 2222587728 192 FFTQIRKDPTKTVILVTHDM 211
Cdd:cd03293 173 ELLDIWRETGKTVLLVTHDI 192
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
38-229 |
1.06e-23 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 98.35 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 38 RGYRWQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPfielgvGFNPELTGRENVYL-- 115
Cdd:COG4619 8 FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLS------AMPPPEWRRQVAYVpq 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 116 NCALLG------------FDHEQTDamYDDIVE-FAELG---DFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLA 179
Cdd:COG4619 82 EPALWGgtvrdnlpfpfqLRERKFD--RERALElLERLGlppDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2222587728 180 VGDEAFQRKCDDFFTQIRKDPTKTVILVTHDMGAVKRYCTRAMMIEDGKI 229
Cdd:COG4619 160 ALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
43-240 |
1.56e-22 |
|
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: 96.20 E-value: 1.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 43 QHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVpfielgvgfnPELTGRE----------- 111
Cdd:COG1127 18 RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDI----------TGLSEKElyelrrrigml 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 112 ----------NVYLNCAL-LgfdHEQTD---AMYDDIV----EFAELGDFMDQK---LknySSGMQVRLAFSVAIKAQGD 170
Cdd:COG1127 88 fqggalfdslTVFENVAFpL---REHTDlseAEIRELVleklELVGLPGAADKMpseL---SGGMRKRVALARALALDPE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2222587728 171 ILVLDEVLA----VGDEAFqrkcDDFFTQIRKDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETVAD 240
Cdd:COG1127 162 ILLYDEPTAgldpITSAVI----DELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
40-233 |
1.60e-22 |
|
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: 95.34 E-value: 1.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 40 YRWQHVLRGISFQVHQGeFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSG-----------KLVPFIELGVGFNPELT 108
Cdd:cd03264 10 YGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqdvlkqpqklrRRIGYLPQEFGVYPNFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 109 GRENVYLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRK 188
Cdd:cd03264 89 VREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIR 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2222587728 189 CDDFFTQIRKDptKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYG 233
Cdd:cd03264 169 FRNLLSELGED--RIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
45-241 |
1.63e-22 |
|
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: 100.68 E-value: 1.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPFIELG--------VGFNPEL---TGRENv 113
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPAslrrqigvVLQDVFLfsgTIREN- 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 114 ylncaLLGFDHEQTDAMYDDIVEFAELGDF-------MDQKL----KNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGD 182
Cdd:COG2274 569 -----ITLGDPDATDEEIIEAARLAGLHDFiealpmgYDTVVgeggSNLSGGQRQRLAIARALLRNPRILILDEATSALD 643
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2222587728 183 EAFQRKCDDFFTQIRKDptKTVILVTHDMgAVKRYCTRAMMIEDGKIVAYGDKETVADR 241
Cdd:COG2274 644 AETEAIILENLRRLLKG--RTVIIIAHRL-STIRLADRIIVLDKGRIVEDGTHEELLAR 699
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
44-231 |
1.83e-22 |
|
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: 93.65 E-value: 1.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 44 HVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPF------IELGVGFNPELTGrenvylnc 117
Cdd:cd03216 14 KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFasprdaRRAGIAMVYQLSV-------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 118 allgfdheqtdamyddivefaelgdfmdqklknyssGMQVRLAFSVAIKAQGDILVLDE---VLAVgDEAfqrkcDDFFT 194
Cdd:cd03216 86 ------------------------------------GERQMVEIARALARNARLLILDEptaALTP-AEV-----ERLFK 123
|
170 180 190
....*....|....*....|....*....|....*....
gi 2222587728 195 QIR--KDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVA 231
Cdd:cd03216 124 VIRrlRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVG 162
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
44-238 |
1.88e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 99.71 E-value: 1.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 44 HVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPF------IELGVG-----FN--PELTGR 110
Cdd:COG1129 18 KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFrsprdaQAAGIAiihqeLNlvPNLSVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 111 ENVYLNcallgfdHEQT-------DAMYDDIVE-FAELG-DF-MDQKLKNYSSGMQ--VRLAFSVAIKAQgdILVLDE-- 176
Cdd:COG1129 98 ENIFLG-------REPRrgglidwRAMRRRARElLARLGlDIdPDTPVGDLSVAQQqlVEIARALSRDAR--VLILDEpt 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2222587728 177 -VLAvGDEAfqrkcDDFFTQIR--KDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETV 238
Cdd:COG1129 169 aSLT-EREV-----ERLFRIIRrlKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
45-238 |
1.94e-22 |
|
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: 95.48 E-value: 1.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGK---LVPFIELGVGFNPE---LTGRENVYLNCA 118
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditNLPPEKRDISYVPQnyaLFPHMTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 119 ----LLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRKCDDFFT 194
Cdd:cd03299 94 yglkKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELK 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2222587728 195 QIRKDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETV 238
Cdd:cd03299 174 KIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEV 217
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
29-233 |
4.35e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 96.41 E-value: 4.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 29 AVINWTKGIRGYRWQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVP----FIELGVG-- 102
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPsrarHARQRVGvv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 103 -----FNPELTGRENVYLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEV 177
Cdd:PRK13537 86 pqfdnLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2222587728 178 lAVGDEAFQRKCddFFTQIRK--DPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYG 233
Cdd:PRK13537 166 -TTGLDPQARHL--MWERLRSllARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEG 220
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
40-228 |
5.72e-22 |
|
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: 92.64 E-value: 5.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 40 YRWQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLV-------PFIELGVGF-------NP 105
Cdd:cd03229 10 YGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtdledelPPLRRRIGMvfqdfalFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 106 ELTGRENVYLncALlgfdheqtdamyddivefaelgdfmdqklknySSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAF 185
Cdd:cd03229 90 HLTVLENIAL--GL--------------------------------SGGQQQRVALARALAMDPDVLLLDEPTSALDPIT 135
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2222587728 186 QRKCDDFFTQIRKDPTKTVILVTHDMGAVKRYCTRAMMIEDGK 228
Cdd:cd03229 136 RREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
30-233 |
7.81e-22 |
|
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: 94.17 E-value: 7.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 30 VINWTKGIRGYRwqHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPFIELGV-------- 101
Cdd:cd03256 3 VENLSKTYPNGK--KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrrqi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 102 -----GFN--PELTGRENVylNCALLGF------------DHEQTDAMYddIVEFAELGDFMDQKLKNYSSGMQVRLAFS 162
Cdd:cd03256 81 gmifqQFNliERLSVLENV--LSGRLGRrstwrslfglfpKEEKQRALA--ALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2222587728 163 VAIKAQGDILVLDEVLAVGDEAFQRKCDDFFTQIRKDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYG 233
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDG 227
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
38-238 |
1.08e-21 |
|
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: 94.00 E-value: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 38 RGYRWqhVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKG-SVSVSGKlvpfiELG----------VGF-NP 105
Cdd:COG1119 13 RGGKT--ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGE-----RRGgedvwelrkrIGLvSP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 106 ELTGRENVYLNC---------ALLGFDHEQTDAMY---DDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILV 173
Cdd:COG1119 86 ALQLRFPRDETVldvvlsgffDSIGLYREPTDEQReraRELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2222587728 174 LDEVLAvG-DEAFQRKCDDFFTQIRKDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETV 238
Cdd:COG1119 166 LDEPTA-GlDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
46-227 |
2.46e-21 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 92.53 E-value: 2.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 46 LRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLV--PFIELGVGFN-----PELTGRENVYL--N 116
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQItePGPDRMVVFQnysllPWLTVRENIALavD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 117 CALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRKCDDFFTQI 196
Cdd:TIGR01184 81 RVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQI 160
|
170 180 190
....*....|....*....|....*....|.
gi 2222587728 197 RKDPTKTVILVTHDMGAVKRYCTRAMMIEDG 227
Cdd:TIGR01184 161 WEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
45-238 |
2.61e-21 |
|
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: 92.75 E-value: 2.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLV---PFIEL---------GVGFNPELTGREN 112
Cdd:cd03295 16 AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIreqDPVELrrkigyviqQIGLFPHMTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 113 VYLNCALLGFDHEQTDAMYDDIVEFAELGD--FMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRKCD 190
Cdd:cd03295 96 IALVPKLLKWPKEKIRERADELLALVGLDPaeFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQ 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2222587728 191 DFFTQIRKDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETV 238
Cdd:cd03295 176 EEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
46-231 |
3.63e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 95.86 E-value: 3.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 46 LRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPF------IELGVG-----FN--PELTGREN 112
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIrsprdaIALGIGmvhqhFMlvPNLTVAEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 113 VYLNCALLGFDHEQTDAMYDDIVEFAELGDF---MDQKLKNYSSGMQVRlafsVAI-KA--QG-DILVLDEVLAV--GDE 183
Cdd:COG3845 101 IVLGLEPTKGGRLDRKAARARIRELSERYGLdvdPDAKVEDLSVGEQQR----VEIlKAlyRGaRILILDEPTAVltPQE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2222587728 184 AfqrkcDDFFTQIR--KDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVA 231
Cdd:COG3845 177 A-----DELFEILRrlAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVG 221
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
38-233 |
7.84e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 93.36 E-value: 7.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 38 RGYRWQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVP----FIELGVG-------FNPE 106
Cdd:PRK13536 49 KSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPararLARARIGvvpqfdnLDLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 107 LTGRENVYLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVlAVGDEAFQ 186
Cdd:PRK13536 129 FTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEP-TTGLDPHA 207
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2222587728 187 RKCddFFTQIRKDPT--KTVILVTHDMGAVKRYCTRAMMIEDGKIVAYG 233
Cdd:PRK13536 208 RHL--IWERLRSLLArgKTILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
26-240 |
1.25e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 91.21 E-value: 1.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 26 LKQAVINWTKGIRGYRWQH--VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLV-----PFIE 98
Cdd:PRK13632 3 NKSVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIskenlKEIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 99 --LGVGF-NPE-----LT-------GRENvylNCallgFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSV 163
Cdd:PRK13632 83 kkIGIIFqNPDnqfigATveddiafGLEN---KK----VPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2222587728 164 AIKAQGDILVLDEVLAVGDEAFQRKCDDFFTQIRKDPTKTVILVTHDMG-AVKryCTRAMMIEDGKIVAYGD-KETVAD 240
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDeAIL--ADKVIVFSEGKLIAQGKpKEILNN 232
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
3-210 |
2.83e-20 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 90.15 E-value: 2.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 3 APVVLDVHDVYKDFKLPTEQatglkqavinwtkgirgyrwQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYP 82
Cdd:COG1116 4 AAPALELRGVSKRFPTGGGG--------------------VTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKP 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 83 NKGSVSVSGKLV--PFIELGVGF-NPEL----TGRENVYLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGM 155
Cdd:COG1116 64 TSGEVLVDGKPVtgPGPDRGVVFqEPALlpwlTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGM 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 156 QVRlafsVAIkAQG-----DILVLDEVLAVGDEAFQRKCDDFFTQIRKDPTKTVILVTHD 210
Cdd:COG1116 144 RQR----VAI-ARAlandpEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHD 198
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
44-238 |
6.57e-20 |
|
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: 88.39 E-value: 6.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 44 HVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYY-----PNKGSVSVSGKLV-----PFIEL--GVGF-----NP- 105
Cdd:cd03260 14 HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIydldvDVLELrrRVGMvfqkpNPf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 106 ELTGRENVYLNCALLGfdhEQTDAMYDDIVEF----AELGDFMDQKLKNY--SSGMQVRLAFSVAIKAQGDILVLDEVLA 179
Cdd:cd03260 94 PGSIYDNVAYGLRLHG---IKLKEELDERVEEalrkAALWDEVKDRLHALglSGGQQQRLCLARALANEPEVLLLDEPTS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2222587728 180 VGDEAFQRKCDDFFTQIRKDPtkTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETV 238
Cdd:cd03260 171 ALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
45-267 |
1.27e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 91.28 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLvpfiELGV-----GFNPELTGRENVY----- 114
Cdd:COG0488 13 LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL----RIGYlpqepPLDDDLTVLDTVLdgdae 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 115 LNCALLGFDH--EQTDAMYDDIVEFAEL--------------------------GDFMDQKLKNYSSGMQVRLAFSVAIK 166
Cdd:COG0488 89 LRALEAELEEleAKLAEPDEDLERLAELqeefealggweaearaeeilsglgfpEEDLDRPVSELSGGWRRRVALARALL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 167 AQGDILVLDEvlavgdeafqrkcddfftqirkdPT-------------------KTVILVTHDmgavkRY-----CTRAM 222
Cdd:COG0488 169 SEPDLLLLDE-----------------------PTnhldlesiewleeflknypGTVLVVSHD-----RYfldrvATRIL 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2222587728 223 MIEDGKIVAY-GD----KETVADRytlsnLEAERKKGEKQARKAAQALAQ 267
Cdd:COG0488 221 ELDRGKLTLYpGNysayLEQRAER-----LEQEAAAYAKQQKKIAKEEEF 265
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
49-233 |
2.60e-19 |
|
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: 86.19 E-value: 2.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 49 ISFQVhQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKL---------VPFIELGVGFN-------PELTGREN 112
Cdd:cd03297 17 IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkinLPPQQRKIGLVfqqyalfPHLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 113 vyLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRKCDDF 192
Cdd:cd03297 96 --LAFGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2222587728 193 FTQIRKDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYG 233
Cdd:cd03297 174 LKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
6-230 |
1.70e-18 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 85.24 E-value: 1.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 6 VLDVHDVYKDFklpteqATGLkqavINWTKGirgyrWQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKG 85
Cdd:TIGR02769 2 LLEVRDVTHTY------RTGG----LFGAKQ-----RAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 86 SVSVSG----KLVP-------------FIELGVGFNPELTGRENVYLNCA-LLGFDHEQTDAMYDDIVEFAELGDFMDQK 147
Cdd:TIGR02769 67 TVSFRGqdlyQLDRkqrrafrrdvqlvFQDSPSAVNPRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRSEDADK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 148 LKNYSSGMQV-RLAFSVAIKAQGDILVLDEVLAVGDEAFQRKCDDFFTQIRKDPTKTVILVTHDMGAVKRYCTRAMMIED 226
Cdd:TIGR02769 147 LPRQLSGGQLqRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDK 226
|
....
gi 2222587728 227 GKIV 230
Cdd:TIGR02769 227 GQIV 230
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
44-240 |
2.95e-18 |
|
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: 83.49 E-value: 2.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 44 HVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGK----LVPF--IELGVGFNPE-------LTGR 110
Cdd:COG0410 17 HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEditgLPPHriARLGIGYVPEgrrifpsLTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 111 ENVYLNcALLGFDHEQTDAMYDDIVE-FAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEV---LA--VGDEA 184
Cdd:COG0410 97 ENLLLG-AYARRDRAEVRADLERVYElFPRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPslgLAplIVEEI 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2222587728 185 FQRkcddfFTQIRKDPTkTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETVAD 240
Cdd:COG0410 176 FEI-----IRRLNREGV-TILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
48-243 |
6.21e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 86.39 E-value: 6.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 48 GISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSV--SGKLVPFIELGvgfnPELTGRENVYlncalLGFDHE 125
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvGDEWVDMTKPG----PDGRGRAKRY-----IGILHQ 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 126 Q-------------TDAMYDDI-VEFA--------ELGDFMDQKLKN--------YSSGMQVRLAFSVAIKAQGDILVLD 175
Cdd:TIGR03269 373 EydlyphrtvldnlTEAIGLELpDELArmkavitlKMVGFDEEKAEEildkypdeLSEGERHRVALAQVLIKEPRIVILD 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2222587728 176 EVLAVGDEAFQRKCDDFFTQIRKDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETVADRYT 243
Cdd:TIGR03269 453 EPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVEELT 520
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
43-230 |
6.74e-18 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 82.41 E-value: 6.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 43 QHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSG----KL----VPFI--ELGVGFN-----PEL 107
Cdd:COG2884 15 REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdlsRLkrreIPYLrrRIGVVFQdfrllPDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 108 TGRENVYLncAL--LGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAF 185
Cdd:COG2884 95 TVYENVAL--PLrvTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPET 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2222587728 186 QRKCDDFFTQIRKDPTkTVILVTHDMGAVKRYCTRAMMIEDGKIV 230
Cdd:COG2884 173 SWEIMELLEEINRRGT-TVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
44-241 |
8.07e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 83.25 E-value: 8.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 44 HVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLV-----PFIELGVGF---NPE-----LTGR 110
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVnaeneKWVRSKVGLvfqDPDdqvfsSTVW 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 111 ENVYLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRKCD 190
Cdd:PRK13647 99 DDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLM 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2222587728 191 DFFTQIRKDpTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETVADR 241
Cdd:PRK13647 179 EILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
44-234 |
1.41e-17 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 83.59 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 44 HVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLV---PFIEL-----GVG-----FNpeLTGR 110
Cdd:COG1135 19 TALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLtalSERELraarrKIGmifqhFN--LLSS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 111 ENVYLNCAL----LGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDE---------- 176
Cdd:COG1135 97 RTVAENVALpleiAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEatsaldpett 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 177 --VLAVGDEafqrkcddfftqIRKDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGD 234
Cdd:COG1135 177 rsILDLLKD------------INRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGP 224
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
46-238 |
3.49e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 81.60 E-value: 3.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 46 LRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKL-----VPFIELGVGF---NPE-----LTGREN 112
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVlseetVWDVRRQVGMvfqNPDnqfvgATVQDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 113 VYLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRKCDDF 192
Cdd:PRK13635 103 VAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLET 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2222587728 193 FTQIRKDPTKTVILVTHDMGAVKRyCTRAMMIEDGKIVAYGDKETV 238
Cdd:PRK13635 183 VRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEI 227
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
41-228 |
5.46e-17 |
|
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: 78.19 E-value: 5.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 41 RWQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPFIELgvgfnpeltgrENVYLNCALL 120
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDL-----------ESLRKNIAYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 121 gfdhEQTDAMYDDIVEFaelgdfmdqklkNYSSGMQV-RLAFSVAIKAQGDILVLDEVLAVGDEAFQRKCDDFFTQIRKD 199
Cdd:cd03228 82 ----PQDPFLFSGTIRE------------NILSGGQRqRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKG 145
|
170 180
....*....|....*....|....*....
gi 2222587728 200 ptKTVILVTHDMGAVKRyCTRAMMIEDGK 228
Cdd:cd03228 146 --KTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
46-231 |
8.01e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 82.65 E-value: 8.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 46 LRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPF------IELGVG-------FNPELTGREN 112
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFasttaaLAAGVAiiyqelhLVPEMTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 113 VYLN--CALLGFDHEQTdAMYDDIVEFAELGDFMD--QKLKNYSSGMQ--VRLAFSVAIKAQgdILVLDE---VLAVgde 183
Cdd:PRK11288 100 LYLGqlPHKGGIVNRRL-LNYEAREQLEHLGVDIDpdTPLKYLSIGQRqmVEIAKALARNAR--VIAFDEptsSLSA--- 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2222587728 184 afqRKCDDFFTQIR--KDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVA 231
Cdd:PRK11288 174 ---REIEQLFRVIRelRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
34-245 |
1.46e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 79.35 E-value: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 34 TKGIRGYR-WQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSG------------------KLV 94
Cdd:PRK10419 15 HGGLSGKHqHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGeplaklnraqrkafrrdiQMV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 95 pFIELGVGFNPELTGRENVY--LNcALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQV-RLAFSVAIKAQGDI 171
Cdd:PRK10419 95 -FQDSISAVNPRKTVREIIRepLR-HLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLqRVCLARALAVEPKL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2222587728 172 LVLDEVLAVGDEAFQRKCDDFFTQIRKDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVaygDKETVADRYTLS 245
Cdd:PRK10419 173 LILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIV---ETQPVGDKLTFS 243
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
46-229 |
1.95e-16 |
|
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: 77.83 E-value: 1.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 46 LRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSG--------KLVPFI--ELGVGFN-----PELTGR 110
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqdvsdlrgRAIPYLrrKIGVVFQdfrllPDRNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 111 ENVYLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRKCD 190
Cdd:cd03292 97 ENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIM 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 2222587728 191 DFFTQIRKDPTkTVILVTHDMGAVKRYCTRAMMIEDGKI 229
Cdd:cd03292 177 NLLKKINKAGT-TVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
43-233 |
3.04e-16 |
|
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: 77.30 E-value: 3.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 43 QHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPFIE-----LGVGFN-----PELTGREN 112
Cdd:cd03301 13 VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPpkdrdIAMVFQnyalyPHMTVYDN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 113 VYLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRKCDDF 192
Cdd:cd03301 93 IAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2222587728 193 FTQIRKDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYG 233
Cdd:cd03301 173 LKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
39-238 |
4.69e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 77.75 E-value: 4.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 39 GYRWQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGK---------------LVPFIELgvgf 103
Cdd:PRK11231 11 GYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKpismlssrqlarrlaLLPQHHL---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 104 NPE-LTGRENV------YLNC--ALLGFDHEQTD-AMYD-DIVEFAelgdfmDQKLKNYSSGMQVRlAFSVAIKAQ-GDI 171
Cdd:PRK11231 87 TPEgITVRELVaygrspWLSLwgRLSAEDNARVNqAMEQtRINHLA------DRRLTDLSGGQRQR-AFLAMVLAQdTPV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2222587728 172 LVLDEVLAVGDEAFQRKCDDFFtQIRKDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETV 238
Cdd:PRK11231 160 VLLDEPTTYLDINHQVELMRLM-RELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
45-228 |
2.13e-15 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 74.81 E-value: 2.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKL-----VPFIELGvgfnpelTGRENVylncaL 119
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIayvsqEPWIQNG-------TIRENI-----L 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 120 LG--FDHEqtdaMYDDIVEFAEL---------GDFMD--QKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLA-----VG 181
Cdd:cd03250 88 FGkpFDEE----RYEKVIKACALepdleilpdGDLTEigEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSavdahVG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2222587728 182 DEAFQrKCddfFTQIRKDpTKTVILVTHDMGAVKrYCTRAMMIEDGK 228
Cdd:cd03250 164 RHIFE-NC---ILGLLLN-NKTRILVTHQLQLLP-HADQIVVLDNGR 204
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
43-237 |
2.86e-15 |
|
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: 78.26 E-value: 2.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 43 QHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPFIELG--------VGFNPEL---TGRE 111
Cdd:COG4988 350 RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAswrrqiawVPQNPYLfagTIRE 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 112 NVylncaLLGfDHEQTDAMYDDIVEFAELGDFMDQKLKNYS----------SGMQV-RLAFSVAIKAQGDILVLDEVLAV 180
Cdd:COG4988 430 NL-----RLG-RPDASDEELEAALEAAGLDEFVAALPDGLDtplgeggrglSGGQAqRLALARALLRDAPLLLLDEPTAH 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2222587728 181 GDEAFQRKCDDFFTQIRKDptKTVILVTHDMGAVKRyCTRAMMIEDGKIVAYGDKET 237
Cdd:COG4988 504 LDAETEAEILQALRRLAKG--RTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEE 557
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
43-210 |
4.54e-15 |
|
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: 74.20 E-value: 4.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 43 QHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKL---VPFIELGVG--FN-----PELTGREN 112
Cdd:cd03300 13 FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDitnLPPHKRPVNtvFQnyalfPHLTVFEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 113 VYLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRKCDDF 192
Cdd:cd03300 93 IAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLE 172
|
170
....*....|....*...
gi 2222587728 193 FTQIRKDPTKTVILVTHD 210
Cdd:cd03300 173 LKRLQKELGITFVFVTHD 190
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
40-241 |
4.71e-15 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 74.41 E-value: 4.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 40 YRWQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLV--------PFIELgvgFN-----PE 106
Cdd:COG3840 9 YRYGDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLtalppaerPVSML---FQennlfPH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 107 LTGRENVYL----NCALLGFDHEQTDAMyddivefAE---LGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLA 179
Cdd:COG3840 86 LTVAQNIGLglrpGLKLTAEQRAQVEQA-------LErvgLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2222587728 180 VGDEAFQRKCDDFFTQIRKDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETVADR 241
Cdd:COG3840 159 ALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDG 220
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
43-229 |
4.86e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 75.15 E-value: 4.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 43 QHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKL-----VPFIELGVGF---NPE-----LTG 109
Cdd:PRK13650 20 KYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLlteenVWDIRHKIGMvfqNPDnqfvgATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 110 RENVYLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRKC 189
Cdd:PRK13650 100 EDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLEL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2222587728 190 DDFFTQIRKDPTKTVILVTHDMGAVKrYCTRAMMIEDGKI 229
Cdd:PRK13650 180 IKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQV 218
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
39-240 |
5.07e-15 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 75.99 E-value: 5.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 39 GYRWQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGklvpfIEL-------------GVG--- 102
Cdd:PRK11153 14 GGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDG-----QDLtalsekelrkarrQIGmif 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 103 --FNpELTGR---ENVYLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEV 177
Cdd:PRK11153 89 qhFN-LLSSRtvfDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2222587728 178 LAVGDEAFQRKCDDFFTQIRKDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGdkeTVAD 240
Cdd:PRK11153 168 TSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQG---TVSE 227
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
45-241 |
6.37e-15 |
|
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: 74.06 E-value: 6.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPFI-------ELGVGFNPELTGRENVYLNC 117
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALAdpawlrrQVGVVLQENVLFNRSIRDNI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 118 ALlgfdhEQTDAMYDDIVEFAELG---DFMDQKLKNY-----------SSGMQVRLAFSVAIKAQGDILVLDEVLAVGDE 183
Cdd:cd03252 97 AL-----ADPGMSMERVIEAAKLAgahDFISELPEGYdtivgeqgaglSGGQRQRIAIARALIHNPRILIFDEATSALDY 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2222587728 184 AFQRKCDDFFTQIRKDptKTVILVTHDMGAVKRyCTRAMMIEDGKIVAYGDKETVADR 241
Cdd:cd03252 172 ESEHAIMRNMHDICAG--RTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
45-232 |
8.01e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 76.64 E-value: 8.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLvpfiELGvgfnpeltgrenvYLNCALLGFDH 124
Cdd:COG0488 330 LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETV----KIG-------------YFDQHQEELDP 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 125 EQTdaMYDDIVEFAE----------LGDFM------DQKLKNYSSGMQVRLAFSVAIKAQGDILVLDE-----------V 177
Cdd:COG0488 393 DKT--VLDELRDGAPggteqevrgyLGRFLfsgddaFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEptnhldietleA 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2222587728 178 LAvgdEAFQrkcdDFftqirkdpTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAY 232
Cdd:COG0488 471 LE---EALD----DF--------PGTVLLVSHDRYFLDRVATRILEFEDGGVREY 510
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
44-231 |
8.07e-15 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 73.62 E-value: 8.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 44 HVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKlvpfiELG--------------VGFN----- 104
Cdd:COG4181 26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQ-----DLFaldedararlrarhVGFVfqsfq 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 105 --PELTGRENVYLNCALLGFDHEQTDAMYddivEFAELGdfMDQKLKNY----SSGMQVRLAFSVAIKAQGDILVLDEVL 178
Cdd:COG4181 101 llPTLTALENVMLPLELAGRRDARARARA----LLERVG--LGHRLDHYpaqlSGGEQQRVALARAFATEPAILFADEPT 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2222587728 179 AVGDEAFQRKCDDFFTQIRKDPTKTVILVTHDMGAVKRyCTRAMMIEDGKIVA 231
Cdd:COG4181 175 GNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVE 226
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
43-229 |
8.63e-15 |
|
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: 72.95 E-value: 8.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 43 QHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPF-------IELGVG-----FN--PELT 108
Cdd:cd03262 13 FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkknineLRQKVGmvfqqFNlfPHLT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 109 GRENVYLncAL---LGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAF 185
Cdd:cd03262 93 VLENITL--APikvKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPEL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2222587728 186 QRKCDDFFTQIRKDPTkTVILVTHDMGAVKRYCTRAMMIEDGKI 229
Cdd:cd03262 171 VGEVLDVMKDLAEEGM-TMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
43-244 |
1.15e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 75.65 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 43 QHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSG------------KLVPFIELGVGFNPELTGR 110
Cdd:PRK09536 16 TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvealsaraasRRVASVPQDTSLSFEFDVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 111 ENVYL----NCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGD---- 182
Cdd:PRK09536 96 QVVEMgrtpHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDinhq 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2222587728 183 ----EAFQRKCDDfftqirkdpTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETVADRYTL 244
Cdd:PRK09536 176 vrtlELVRRLVDD---------GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTL 232
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
43-233 |
1.81e-14 |
|
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: 71.19 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 43 QHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPFIE------LGVgfnpeLTGRenVYLn 116
Cdd:cd03247 15 QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEkalsslISV-----LNQR--PYL- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 117 callgFDheqtDAMYDDivefaeLGdfmdqklKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRKCDDFFTQI 196
Cdd:cd03247 87 -----FD----TTLRNN------LG-------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEV 144
|
170 180 190
....*....|....*....|....*....|....*..
gi 2222587728 197 RKDptKTVILVTHDMGAVKRYcTRAMMIEDGKIVAYG 233
Cdd:cd03247 145 LKD--KTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
45-251 |
2.16e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 73.19 E-value: 2.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPF-----IE----LGVGF-NPE-----LTG 109
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYdkkslLEvrktVGIVFqNPDdqlfaPTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 110 RENVYLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRKC 189
Cdd:PRK13639 97 EEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQI 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2222587728 190 DDFFTQIRKDPTkTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGD-KETVADRYTL--SNLEAER 251
Cdd:PRK13639 177 MKLLYDLNKEGI-TIIISTHDVDLVPVYADKVYVMSDGKIIKEGTpKEVFSDIETIrkANLRLPR 240
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
40-248 |
2.50e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.99 E-value: 2.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 40 YRWQHV-LRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGK---------LVPFI----ELGVGFnP 105
Cdd:PRK15056 16 WRNGHTaLRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknLVAYVpqseEVDWSF-P 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 106 ELTgrENV-----YLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAV 180
Cdd:PRK15056 95 VLV--EDVvmmgrYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2222587728 181 GDEAFQRKCDDFFTQIRkDPTKTVILVTHDMGAVKRYCTRAMMIEdGKIVAYGDKETVadrYTLSNLE 248
Cdd:PRK15056 173 VDVKTEARIISLLRELR-DEGKTMLVSTHNLGSVTEFCDYTVMVK-GTVLASGPTETT---FTAENLE 235
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
40-233 |
2.89e-14 |
|
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: 71.76 E-value: 2.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 40 YRWQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPFIE-----LGVGFN-----PELTG 109
Cdd:cd03298 8 FSYGEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPpadrpVSMLFQennlfAHLTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 110 RENVYLNCAL-LGFDHEQTDAMyDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRK 188
Cdd:cd03298 88 EQNVGLGLSPgLKLTAEDRQAI-EVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2222587728 189 CDDFFTQIRKDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYG 233
Cdd:cd03298 167 MLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
38-209 |
3.48e-14 |
|
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: 71.24 E-value: 3.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 38 RGyrWQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPFIE---------LG--VGFNPE 106
Cdd:TIGR01189 10 RG--ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRdephenilyLGhlPGLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 107 LTGRENVYLNCAllgfDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAvgdeAFQ 186
Cdd:TIGR01189 88 LSALENLHFWAA----IHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTT----ALD 159
|
170 180
....*....|....*....|....*.
gi 2222587728 187 RKCDDFFTQIRKDPTKT---VILVTH 209
Cdd:TIGR01189 160 KAGVALLAGLLRAHLARggiVLLTTH 185
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
45-210 |
3.89e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 71.67 E-value: 3.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKlvPFIELG-------VGF---NPELTGrENVY 114
Cdd:PRK10247 22 ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGE--DISTLKpeiyrqqVSYcaqTPTLFG-DTVY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 115 LNCAL---LGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRKCDD 191
Cdd:PRK10247 99 DNLIFpwqIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNE 178
|
170
....*....|....*....
gi 2222587728 192 FFTQIRKDPTKTVILVTHD 210
Cdd:PRK10247 179 IIHRYVREQNIAVLWVTHD 197
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
45-247 |
4.50e-14 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 71.65 E-value: 4.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLV---PFIELG---------VGFNPELTGREn 112
Cdd:COG4604 16 VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVattPSRELAkrlailrqeNHINSRLTVRE- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 113 vylncaLLGF-------------DHEQTDAMyddiVEFAELGDFMDQKLKNYSSGmQVRLAFsVA-IKAQG-DILVLDEV 177
Cdd:COG4604 95 ------LVAFgrfpyskgrltaeDREIIDEA----IAYLDLEDLADRYLDELSGG-QRQRAF-IAmVLAQDtDYVLLDEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 178 L-------AVG-DEAFQRKCDDFftqirkdpTKTVILVTHDMGAVKRYCTR--AMmiEDGKIVAYGDKETVADRYTLSNL 247
Cdd:COG4604 163 LnnldmkhSVQmMKLLRRLADEL--------GKTVVIVLHDINFASCYADHivAM--KDGRVVAQGTPEEIITPEVLSDI 232
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
38-240 |
4.60e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 72.50 E-value: 4.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 38 RGYRWQHV-LRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSG---------KLVPFI--ELGVGFN- 104
Cdd:PRK13646 14 KGTPYEHQaIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdKYIRPVrkRIGMVFQf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 105 PE------------LTGRENVYLNCallgfdHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDIL 172
Cdd:PRK13646 94 PEsqlfedtvereiIFGPKNFKMNL------DEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDII 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2222587728 173 VLDEVLAVGDEAFQRKCDDFFTQIRKDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVA-------YGDKETVAD 240
Cdd:PRK13646 168 VLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSqtspkelFKDKKKLAD 242
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
44-238 |
5.19e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 74.05 E-value: 5.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 44 HVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSG----KLVPFI--ELGVGF-------NPELTGR 110
Cdd:PRK09700 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinynKLDHKLaaQLGIGIiyqelsvIDELTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 111 ENVYLNcallgfDHEQTDAMYDDIVEFAE-------------LGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEV 177
Cdd:PRK09700 99 ENLYIG------RHLTKKVCGVNIIDWREmrvraammllrvgLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2222587728 178 LAvgdEAFQRKCDDFF---TQIRKDpTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETV 238
Cdd:PRK09700 173 TS---SLTNKEVDYLFlimNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
45-228 |
9.10e-14 |
|
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: 68.24 E-value: 9.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPfielgvgfnpeltgrenVYLncallgfdh 124
Cdd:cd03221 15 LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKI-----------------GYF--------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 125 EQtdamyddivefaelgdfmdqklknYSSGMQVRLAFSVAIKAQGDILVLDE------VLAVgdEAFQrkcdDFFTQIRk 198
Cdd:cd03221 69 EQ------------------------LSGGEKMRLALAKLLLENPNLLLLDEptnhldLESI--EALE----EALKEYP- 117
|
170 180 190
....*....|....*....|....*....|
gi 2222587728 199 dptKTVILVTHDMGAVKRYCTRAMMIEDGK 228
Cdd:cd03221 118 ---GTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
46-287 |
1.12e-13 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 72.37 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 46 LRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSG----------------KLVPFIELGVGFNPELTG 109
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiakisdaelrevrrKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 110 RENVYLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRKC 189
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 190 DDFFTQIRKDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETVadrytLSNLEAERKKGEKQARKAAQALAQKD 269
Cdd:PRK10070 204 QDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI-----LNNPANDYVRTFFRGVDISQVFSAKD 278
|
250
....*....|....*...
gi 2222587728 270 EQGKAvpvfPNGLNARVP 287
Cdd:PRK10070 279 IARRT----PNGLIRKTP 292
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
44-233 |
1.47e-13 |
|
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: 69.95 E-value: 1.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 44 HVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSG---KLVPFIEL--GVGFNPELTG------REN 112
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidiRDISRKSLrsMIGVVLQDTFlfsgtiMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 113 VYLN------------CALLGFDH--EQTDAMYDDIVefAELGdfmdqklKNYSSGMQVRLAFSVAIKAQGDILVLDEVL 178
Cdd:cd03254 97 IRLGrpnatdeevieaAKEAGAHDfiMKLPNGYDTVL--GENG-------GNLSQGERQLLAIARAMLRDPKILILDEAT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2222587728 179 AVGDEAFQRKCDDFFTQIRKDptKTVILVTHDMGAVKRyCTRAMMIEDGKIVAYG 233
Cdd:cd03254 168 SNIDTETEKLIQEALEKLMKG--RTSIIIAHRLSTIKN-ADKILVLDDGKIIEEG 219
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
45-233 |
1.56e-13 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 72.50 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGK---------------LVP---FIelgvgFNpe 106
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVdirdltleslrrqigVVPqdtFL-----FS-- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 107 LTGRENVylncaLLGfDHEQTDAMYDDIVEFAELGDF---MDQKL--------KNYSSGMQVRLAFSVAIKAQGDILVLD 175
Cdd:COG1132 428 GTIRENI-----RYG-RPDATDEEVEEAAKAAQAHEFieaLPDGYdtvvgergVNLSGGQRQRIAIARALLKDPPILILD 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2222587728 176 EVLA----VGDEAFQRKcddfFTQIRKDptKTVILVTHDMGAVKRyCTRAMMIEDGKIVAYG 233
Cdd:COG1132 502 EATSaldtETEALIQEA----LERLMKG--RTTIVIAHRLSTIRN-ADRILVLDDGRIVEQG 556
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
44-238 |
1.94e-13 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 70.19 E-value: 1.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 44 HVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLV---PFIEL-----------GVGFnPeLTG 109
Cdd:PRK13548 16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLadwSPAELarrravlpqhsSLSF-P-FTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 110 RENVYLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFS---VAIKAQGD---ILVLDEVLAVGDE 183
Cdd:PRK13548 94 EEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLArvlAQLWEPDGpprWLLLDEPTSALDL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2222587728 184 AFQRKCddffTQIRKDPTK----TVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETV 238
Cdd:PRK13548 174 AHQHHV----LRLARQLAHerglAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEV 228
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
45-229 |
2.05e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 69.42 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGK-LVPFIELG--------VGFN-------PELT 108
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQpLHQMDEEAraklrakhVGFVfqsfmliPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 109 GRENVYLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRK 188
Cdd:PRK10584 105 ALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDK 184
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2222587728 189 CDDFFTQIRKDPTKTVILVTHDMGAVKRyCTRAMMIEDGKI 229
Cdd:PRK10584 185 IADLLFSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQL 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
40-210 |
4.05e-13 |
|
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: 71.24 E-value: 4.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 40 YRW---QHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGklVPFIELG-------VGFNPE--- 106
Cdd:TIGR02868 342 AGYpgaPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDG--VPVSSLDqdevrrrVSVCAQdah 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 107 ---LTGRENVYLNCAllgfdhEQTDAMYDDIVEFAELGDF-------MDQKL----KNYSSGMQVRLAFSVAIKAQGDIL 172
Cdd:TIGR02868 420 lfdTTVRENLRLARP------DATDEELWAALERVGLADWlralpdgLDTVLgeggARLSGGERQRLALARALLADAPIL 493
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2222587728 173 VLDEV---LAVGDEAfqRKCDDFFTqirKDPTKTVILVTHD 210
Cdd:TIGR02868 494 LLDEPtehLDAETAD--ELLEDLLA---ALSGRTVVLITHH 529
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
40-209 |
5.93e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 67.67 E-value: 5.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 40 YRWQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVP-----------FIELGVGFNPELT 108
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKkdlctyqkqlcFVGHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 109 GRENVYlncallgFD-HEQTDAM-YDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEafq 186
Cdd:PRK13540 91 LRENCL-------YDiHFSPGAVgITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDE--- 160
|
170 180
....*....|....*....|....*
gi 2222587728 187 RKCDDFFTQIRKDPTK--TVILVTH 209
Cdd:PRK13540 161 LSLLTIITKIQEHRAKggAVLLTSH 185
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
43-244 |
6.49e-13 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 70.91 E-value: 6.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 43 QHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPFIE--------LGVGFNPELTG---RE 111
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDhhylhrqvALVGQEPVLFSgsvRE 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 112 NV-----------YLNCALLGFDHEQTDAMYDDI-VEFAELGDFMdqklknySSGMQVRLAFSVAIKAQGDILVLDEVLA 179
Cdd:TIGR00958 574 NIaygltdtpdeeIMAAAKAANAHDFIMEFPNGYdTEVGEKGSQL-------SGGQKQRIAIARALVRKPRVLILDEATS 646
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2222587728 180 VGDEAfqrkCDDFFTQIRKDPTKTVILVTHDMGAVKRyCTRAMMIEDGKIVAYGDKETVADRYTL 244
Cdd:TIGR00958 647 ALDAE----CEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQGC 706
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
40-238 |
7.13e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 68.33 E-value: 7.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 40 YRWQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPN-----KGSVSVSGKLV--PFI-------ELGVGFN- 104
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIysPDVdpievrrEVGMVFQy 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 105 ----PELTGRENVYLNCALLGFDHEQTDamYDDIVEFA--------ELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDIL 172
Cdd:PRK14267 94 pnpfPHLTIYDNVAIGVKLNGLVKSKKE--LDERVEWAlkkaalwdEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2222587728 173 VLDEVLAVGDEAFQRKCDDFFTQIRKDptKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETV 238
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKV 235
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
49-232 |
1.30e-12 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 69.83 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 49 ISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVP--------------------FIELGVGFNPELT 108
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTadnreayrqlfsavfsdfhlFDRLLGLDGEADP 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 109 GRENVYLncALLGFDHeqtdamyddIVEFAElGDFMDQKLknySSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRK 188
Cdd:COG4615 431 ARARELL--ERLELDH---------KVSVED-GRFSTTDL---SQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRRV 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2222587728 189 cddFFTQI---RKDPTKTVILVTHDmgavKRY---CTRAMMIEDGKIVAY 232
Cdd:COG4615 496 ---FYTELlpeLKARGKTVIAISHD----DRYfdlADRVLKMDYGKLVEL 538
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
44-252 |
1.57e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 69.49 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 44 HVLRG-ISFQVHQGEFFGIVGRNGGGKSTLLKIISQiYYPNKGSVSVSGklvpfIELG-------------VGFNPEL-- 107
Cdd:PRK11174 363 KTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKING-----IELReldpeswrkhlswVGQNPQLph 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 108 -TGRENVylncaLLGfDHEQTDAMYDDIVEFAELGDFMDQ-------KLKNYSSGMQV----RLAFSVAIKAQGDILVLD 175
Cdd:PRK11174 437 gTLRDNV-----LLG-NPDASDEQLQQALENAWVSEFLPLlpqgldtPIGDQAAGLSVgqaqRLALARALLQPCQLLLLD 510
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2222587728 176 EVLAVGDEAFQRKCDDFFTQIRKDptKTVILVTHDMGAVKRYCTRAMMiEDGKIVAYGDKET-VADRYTLSNLEAERK 252
Cdd:PRK11174 511 EPTASLDAHSEQLVMQALNAASRR--QTTLMVTHQLEDLAQWDQIWVM-QDGQIVQQGDYAElSQAGGLFATLLAHRQ 585
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
45-233 |
1.57e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 67.81 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSG-------------------------KLVPFI-E 98
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsdeenlwdirnkagmvfqnpdnQIVATIvE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 99 LGVGFNPeltgrENvylncalLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVL 178
Cdd:PRK13633 105 EDVAFGP-----EN-------LGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2222587728 179 AVGDEAFQRKCDDFFTQIRKDPTKTVILVTHDMG-AVKryCTRAMMIEDGKIVAYG 233
Cdd:PRK13633 173 AMLDPSGRREVVNTIKELNKKYGITIILITHYMEeAVE--ADRIIVMDSGKVVMEG 226
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
4-89 |
1.60e-12 |
|
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: 66.69 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 4 PVVLDVHDVYKDFKLPTEQATGLkqavinwtkgirgyrwqHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPN 83
Cdd:COG4778 2 TTLLEVENLSKTFTLHLQGGKRL-----------------PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPD 64
|
....*.
gi 2222587728 84 KGSVSV 89
Cdd:COG4778 65 SGSILV 70
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
45-176 |
2.20e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 66.05 E-value: 2.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPFIELGV---------GFNPELTGRENVYL 115
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEachylghrnAMKPALTVAENLEF 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2222587728 116 NCALLGfdheQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDE 176
Cdd:PRK13539 97 WAAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDE 153
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
45-236 |
2.30e-12 |
|
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: 66.49 E-value: 2.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPFIELG-----VG--------FNPelTGRE 111
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLAslrrqIGlvsqdvflFND--TVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 112 NVYLNcallgfDHEQTDAMYDDIVEFAELGDFMDQKLKNY-----------SSGMQVRLAFSVAIKAQGDILVLDEVLAV 180
Cdd:cd03251 95 NIAYG------RPGATREEVEEAARAANAHEFIMELPEGYdtvigergvklSGGQRQRIAIARALLKDPPILILDEATSA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2222587728 181 GDEAFQRKCDDFFTQIRKDptKTVILVTHDMGAVKRyCTRAMMIEDGKIVAYGDKE 236
Cdd:cd03251 169 LDTESERLVQAALERLMKN--RTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHE 221
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
45-233 |
3.20e-12 |
|
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: 65.98 E-value: 3.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLV------------------PFIELGvgfnpe 106
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDIskiglhdlrsrisiipqdPVLFSG------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 107 lTGRENvylncalLGFDHEQTDAMYDDIVEFAELGDFMDQKLK-----------NYSSGMQVRLAFSVAIKAQGDILVLD 175
Cdd:cd03244 93 -TIRSN-------LDPFGEYSDEELWQALERVGLKEFVESLPGgldtvveeggeNLSVGQRQLLCLARALLRKSKILVLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2222587728 176 EVLAV----GDEAFQRKCDDFFTQirkdptKTVILVTHDMGAVKRYcTRAMMIEDGKIVAYG 233
Cdd:cd03244 165 EATASvdpeTDALIQKTIREAFKD------CTVLTIAHRLDTIIDS-DRILVLDKGRVVEFD 219
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
40-241 |
3.77e-12 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 67.43 E-value: 3.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 40 YRWQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGK----LVPFiELGVG--------FnPEL 107
Cdd:COG3842 15 YGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRdvtgLPPE-KRNVGmvfqdyalF-PHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 108 TGRENV--YLNcaLLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQ--VRLAFSVAIKAqgDILVLDEVLA---- 179
Cdd:COG3842 93 TVAENVafGLR--MRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQqrVALARALAPEP--RVLLLDEPLSalda 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2222587728 180 -----VGDE--AFQRKcddffTQIrkdptkTVILVTHD------MG---AVkryctrammIEDGKIVAYGDKETVADR 241
Cdd:COG3842 169 klreeMREElrRLQRE-----LGI------TFIYVTHDqeealaLAdriAV---------MNDGRIEQVGTPEEIYER 226
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
41-210 |
3.97e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 68.07 E-value: 3.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 41 RWQHV-LRGISFQ--------------VHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLV------PFIEL 99
Cdd:PRK10522 319 DWQTLeLRNVTFAyqdngfsvgpinltIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVtaeqpeDYRKL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 100 gvgFNPELTgreNVYLNCALLGFDHEQTD-AMYDDIVEFAELGD---FMDQKLKN--YSSGMQVRLAFSVAIKAQGDILV 173
Cdd:PRK10522 399 ---FSAVFT---DFHLFDQLLGPEGKPANpALVEKWLERLKMAHkleLEDGRISNlkLSKGQKKRLALLLALAEERDILL 472
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2222587728 174 LDEVLAVGDEAFQRkcddFFTQI----RKDPTKTVILVTHD 210
Cdd:PRK10522 473 LDEWAADQDPHFRR----EFYQVllplLQEMGKTIFAISHD 509
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
53-225 |
5.02e-12 |
|
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: 68.50 E-value: 5.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 53 VHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKL----VPFIELGVGFNPE-------LTGRENVYLNCALLG 121
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiltnISDVHQNMGYCPQfdaiddlLTGREHLYLYARLRG 2041
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 122 FDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRKCDDFFTQIRKDpT 201
Cdd:TIGR01257 2042 VPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-G 2120
|
170 180
....*....|....*....|....*
gi 2222587728 202 KTVILVTHDMGAVKRYCTR-AMMIE 225
Cdd:TIGR01257 2121 RAVVLTSHSMEECEALCTRlAIMVK 2145
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
44-240 |
6.22e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 65.88 E-value: 6.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 44 HVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLV------------------PFIelgvGFNP 105
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtklpeykrakyigrvfqdPMM----GTAP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 106 ELTGREnvylNCAL-----------LGFDHEQTDaMYDDIVEFAELG--DFMDQKLKNYSSGmQvRLAFSV--AIKAQGD 170
Cdd:COG1101 96 SMTIEE----NLALayrrgkrrglrRGLTKKRRE-LFRELLATLGLGleNRLDTKVGLLSGG-Q-RQALSLlmATLTKPK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 171 ILVLDE------------VLAVGDEAFQRKcddfftQIrkdptkTVILVTHDMGAVKRYCTRAMMIEDGKIVA-YGDKE- 236
Cdd:COG1101 169 LLLLDEhtaaldpktaalVLELTEKIVEEN------NL------TTLMVTHNMEQALDYGNRLIMMHEGRIILdVSGEEk 236
|
....*..
gi 2222587728 237 ---TVAD 240
Cdd:COG1101 237 kklTVED 243
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
45-229 |
8.11e-12 |
|
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: 64.80 E-value: 8.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPFIE--------LGVGFNPELTGR---ENV 113
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEhkylhskvSLVGQEPVLFARslqDNI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 114 YLNCALLGFDH----EQTDAMYDDIVEFAELGDF-MDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRK 188
Cdd:cd03248 109 AYGLQSCSFECvkeaAQKAHAHSFISELASGYDTeVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQ 188
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2222587728 189 CDDfftQIRKDPT-KTVILVTHDMGAVKRyCTRAMMIEDGKI 229
Cdd:cd03248 189 VQQ---ALYDWPErRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
45-233 |
8.38e-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: 64.36 E-value: 8.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPFIELG--------VGFNPEL---TGRENv 113
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEdlrssltiIPQDPTLfsgTIRSN- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 114 ylncaLLGFDhEQTDAMYDDIVEFAELGDfmdqklkNYSSGMQVRLAFSVAIKAQGDILVLDEVLA----VGDEAFQRkc 189
Cdd:cd03369 102 -----LDPFD-EYSDEEIYGALRVSEGGL-------NLSQGQRQLLCLARALLKRPRVLVLDEATAsidyATDALIQK-- 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2222587728 190 ddfftQIRKDPTKTVIL-VTHDMGAVKRyCTRAMMIEDGKIVAYG 233
Cdd:cd03369 167 -----TIREEFTNSTILtIAHRLRTIID-YDKILVMDAGEVKEYD 205
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
40-239 |
1.01e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 64.60 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 40 YRWQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSG----KLVP--------FIElgvgfN--- 104
Cdd:PRK10771 9 WLYHHLPMRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGqdhtTTPPsrrpvsmlFQE-----Nnlf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 105 PELTGRENVYLNCAL-LGFDHEQTDAMyDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDE 183
Cdd:PRK10771 84 SHLTVAQNIGLGLNPgLKLNAAQREKL-HAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2222587728 184 AFQRKCDDFFTQIRKDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIvaYGDKETVA 239
Cdd:PRK10771 163 ALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRI--AWDGPTDE 216
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
48-238 |
1.12e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 65.01 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 48 GISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVP------FIELGVG--------FNpELTGRENV 113
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEglpghqIARMGVVrtfqhvrlFR-EMTVIENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 114 ------YLNCALL-------GFDHEQTDAMYDDIV--EFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVL 178
Cdd:PRK11300 102 lvaqhqQLKTGLFsgllktpAFRRAESEALDRAATwlERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 179 AVGDEAFQRKCDDFFTQIRKDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETV 238
Cdd:PRK11300 182 AGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 241
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
44-231 |
1.13e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 66.21 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 44 HVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKL---VPFIELGVG--FN-----PELTGRENV 113
Cdd:PRK11000 17 VISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRmndVPPAERGVGmvFQsyalyPHLSVAENM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 114 YLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRKCDDFF 193
Cdd:PRK11000 97 SFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEI 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 2222587728 194 TQIRKDPTKTVILVTHDMgavkrycTRAMMIEDgKIVA 231
Cdd:PRK11000 177 SRLHKRLGRTMIYVTHDQ-------VEAMTLAD-KIVV 206
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
40-211 |
1.25e-11 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 64.72 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 40 YRWQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLV--PFIELGVGFN-----PELTGREN 112
Cdd:PRK11248 11 YGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVegPGAERGVVFQnegllPWRNVQDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 113 VYLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDeAFQR-KCDD 191
Cdd:PRK11248 91 VAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD-AFTReQMQT 169
|
170 180
....*....|....*....|
gi 2222587728 192 FFTQIRKDPTKTVILVTHDM 211
Cdd:PRK11248 170 LLLKLWQETGKQVLLITHDI 189
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
45-229 |
1.43e-11 |
|
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: 63.00 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGklvpfIELGVgFNPELTGRENVYLncallgfdh 124
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDG-----ADISQ-WDPNELGDHVGYL--------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 125 eqtdaMYDDIVeFAelGDFMDqklkNYSSGMQV-RLAFSVAIKAQGDILVLDEVLAVGDEAFQRKCDDFFTQIRKDPTkT 203
Cdd:cd03246 82 -----PQDDEL-FS--GSIAE----NILSGGQRqRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGA-T 148
|
170 180
....*....|....*....|....*.
gi 2222587728 204 VILVTHDMGAVKRyCTRAMMIEDGKI 229
Cdd:cd03246 149 RIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
46-241 |
1.58e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 64.85 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 46 LRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPF-----------IELGVGFN-PELTGRENV 113
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPetgnknlkklrKKVSLVFQfPEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 114 YLNCALLG---FDHEQTDAMYDDIVEFAELG---DFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQR 187
Cdd:PRK13641 103 VLKDVEFGpknFGFSEDEAKEKALKWLKKVGlseDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRK 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2222587728 188 KCDDFFTQIRKdPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGD-KETVADR 241
Cdd:PRK13641 183 EMMQLFKDYQK-AGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASpKEIFSDK 236
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
46-247 |
1.79e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 64.62 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 46 LRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSG-------KLVPFIEL-GVGF-NPE--LTGR---E 111
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtgdfsKLQGIRKLvGIVFqNPEtqFVGRtveE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 112 NVYLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEafqRKCDD 191
Cdd:PRK13644 98 DLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDP---DSGIA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2222587728 192 FFTQIRK--DPTKTVILVTHDMGAVkRYCTRAMMIEDGKIVAYGDKETVADRYTLSNL 247
Cdd:PRK13644 175 VLERIKKlhEKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDVSLQTL 231
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
44-244 |
1.90e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 64.48 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 44 HVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPFIELGVgfnpeLTGREN----------- 112
Cdd:PRK13636 20 HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGL-----MKLRESvgmvfqdpdnq 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 113 -----VYLNCAL----LGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDE 183
Cdd:PRK13636 95 lfsasVYQDVSFgavnLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2222587728 184 AFQRKCDDFFTQIRKDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGD-KETVADRYTL 244
Cdd:PRK13636 175 MGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNpKEVFAEKEML 236
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
45-234 |
2.13e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 64.72 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSV-----------------SVSGKLV---------PFIE 98
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekeKVLEKLViqktrfkkiKKIK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 99 -----LGVGFNP------ELTGRENVYLNCALLGFDHEQTDAMYDDIVEFAELG-DFMDQKLKNYSSGMQVRLAFSVAIK 166
Cdd:PRK13651 102 eirrrVGVVFQFaeyqlfEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDeSYLQRSPFELSGGQKRRVALAGILA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2222587728 167 AQGDILVLDEVLAVGDEAFQRKCDDFFTQIRKDpTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGD 234
Cdd:PRK13651 182 MEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGD 248
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
30-238 |
2.32e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 64.00 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 30 VINWTKGIRGyrwQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSG-------------KLVPF 96
Cdd:PRK11264 6 VKNLVKKFHG---QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDitidtarslsqqkGLIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 97 IELGVGFN-------PELTGRENVYLNCALL-GFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQ 168
Cdd:PRK11264 83 LRQHVGFVfqnfnlfPHRTVLENIIEGPVIVkGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2222587728 169 GDILVLDEVLAVGDEAFqrkCDDFFTQIRK--DPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETV 238
Cdd:PRK11264 163 PEVILFDEPTSALDPEL---VGEVLNTIRQlaQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
45-236 |
2.39e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 63.49 E-value: 2.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPFI-------------ELGVGFN-----PE 106
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSktpsdkairelrrNVGMVFQqynlwPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 107 LTGREN-VYLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAF 185
Cdd:PRK11124 97 LTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2222587728 186 QRKCDDFFTQIRKDPTKTVIlVTHDMGAVKRYCTRAMMIEDGKIVAYGDKE 236
Cdd:PRK11124 177 TAQIVSIIRELAETGITQVI-VTHEVEVARKTASRVVYMENGHIVEQGDAS 226
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
46-240 |
2.42e-11 |
|
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: 63.51 E-value: 2.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 46 LRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLV---PFIELGVGFN-------PELTGRENVYL 115
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAtdvPVQERNVGFVfqhyalfRHMTVFDNVAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 116 NC----ALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRKCDD 191
Cdd:cd03296 98 GLrvkpRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRR 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2222587728 192 FFTQIRKDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETVAD 240
Cdd:cd03296 178 WLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYD 226
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
46-238 |
2.47e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 64.30 E-value: 2.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 46 LRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSG-----KLVPFIEL----GVGFN-PELT-GRENVY 114
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdKKVKLSDIrkkvGLVFQyPEYQlFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 115 LNCAL----LGFDHEQTD-----AMydDIVEFaELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEaf 185
Cdd:PRK13637 103 KDIAFgpinLGLSEEEIEnrvkrAM--NIVGL-DYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP-- 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2222587728 186 qRKCDDFFTQIR---KDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETV 238
Cdd:PRK13637 178 -KGRDEILNKIKelhKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
46-231 |
2.77e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 65.34 E-value: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 46 LRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIyYPN---KGSVSVSGKLVPF-------------IELGVGFNPELTG 109
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEELQAsnirdteragiaiIHQELALVKELSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 110 RENVYLNCALLGFDHEQTDAMYDDIVE-FAELGDFMD--QKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAvgdeAFQ 186
Cdd:PRK13549 100 LENIFLGNEITPGGIMDYDAMYLRAQKlLAQLKLDINpaTPVGNLGLGQQQLVEIAKALNKQARLLILDEPTA----SLT 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2222587728 187 RKCDDFFTQIRKDPTK---TVILVTHDMGAVKRYCTRAMMIEDGKIVA 231
Cdd:PRK13549 176 ESETAVLLDIIRDLKAhgiACIYISHKLNEVKAISDTICVIRDGRHIG 223
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
40-238 |
3.33e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 63.45 E-value: 3.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 40 YRWQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPFI-----ELGVG------------ 102
Cdd:PRK10619 15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgQLKVAdknqlrllrtrl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 103 ------FN--PELTGRENVY-LNCALLGFdhEQTDAMYDDIVEFAELGDFMDQKLK---NYSSGMQVRLAFSVAIKAQGD 170
Cdd:PRK10619 95 tmvfqhFNlwSHMTVLENVMeAPIQVLGL--SKQEARERAVKYLAKVGIDERAQGKypvHLSGGQQQRVSIARALAMEPE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2222587728 171 ILVLDEVLAVGDEAFQRKCDDFFTQIRKDpTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETV 238
Cdd:PRK10619 173 VLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
46-277 |
3.54e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 63.61 E-value: 3.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 46 LRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSG---------KLVPFIELGVG----FNPELTGREN 112
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtlitstsknKDIKQIRKKVGlvfqFPESQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 113 VYLNCAL----LGFDHEQTDAMYDD---IVEFAElgDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAF 185
Cdd:PRK13649 103 VLKDVAFgpqnFGVSQEEAEALAREklaLVGISE--SLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 186 QRKCDDFFTQIRKDPTkTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETVADRYTLsnLEaERKKGEKQARKAAQAL 265
Cdd:PRK13649 181 RKELMTLFKKLHQSGM-TIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQDVDF--LE-EKQLGVPKITKFAQRL 256
|
250
....*....|..
gi 2222587728 266 AQKDEQGKAVPV 277
Cdd:PRK13649 257 ADRGISFSSLPI 268
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-240 |
3.95e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.07 E-value: 3.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 1 MDAPVVLDVHDVYKDFKlpteqatglkqavinwtkGIRgyrwqhVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIY 80
Cdd:PRK15439 6 TTAPPLLCARSISKQYS------------------GVE------VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIV 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 81 YPNKGSVSVSGK----------------LVP-----FielgvgfnPELTGRENVylncaLLGFDHEQTDA--MYDDIvef 137
Cdd:PRK15439 62 PPDSGTLEIGGNpcarltpakahqlgiyLVPqepllF--------PNLSVKENI-----LFGLPKRQASMqkMKQLL--- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 138 AELG------------DFMDQKLKNYSSGMqVRLAfsvaikaqgDILVLDEVLAVGDEAfqrKCDDFFTQIRKDPTKTV- 204
Cdd:PRK15439 126 AALGcqldldssagslEVADRQIVEILRGL-MRDS---------RILILDEPTASLTPA---ETERLFSRIRELLAQGVg 192
|
250 260 270
....*....|....*....|....*....|....*..
gi 2222587728 205 -ILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETVAD 240
Cdd:PRK15439 193 iVFISHKLPEIRQLADRISVMRDGTIALSGKTADLST 229
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
45-231 |
4.19e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 65.13 E-value: 4.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPFIE-----------LGVGFN-----PELT 108
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDadalaqlrrehFGFIFQryhllSHLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 109 GRENVYLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRK 188
Cdd:PRK10535 103 AAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEE 182
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2222587728 189 CDDFFTQIRkDPTKTVILVTHDmGAVKRYCTRAMMIEDGKIVA 231
Cdd:PRK10535 183 VMAILHQLR-DRGHTVIIVTHD-PQVAAQAERVIEIRDGEIVR 223
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
45-233 |
4.50e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 63.28 E-value: 4.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYP---NKGSVSVSG-----KLVPFIELGVGF---NPE-----LT 108
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGitltaKTVWDIREKVGIvfqNPDnqfvgAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 109 GRENVYLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRK 188
Cdd:PRK13640 102 VGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQ 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2222587728 189 CDDFFTQIRKDPTKTVILVTHDMGAVKrYCTRAMMIEDGKIVAYG 233
Cdd:PRK13640 182 ILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQG 225
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
40-216 |
4.60e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 63.13 E-value: 4.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 40 YRWQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIyYPNKGSVSVSGKLVPF----IELGVGFN----------- 104
Cdd:PRK14258 17 YDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM-NELESEVRVEGRVEFFnqniYERRVNLNrlrrqvsmvhp 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 105 -PEL---TGRENVYLNCALLGFdHEQTDamYDDIVEF----AELGDFMDQKLK----NYSSGMQVRLAFSVAIKAQGDIL 172
Cdd:PRK14258 96 kPNLfpmSVYDNVAYGVKIVGW-RPKLE--IDDIVESalkdADLWDEIKHKIHksalDLSGGQQQRLCIARALAVKPKVL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2222587728 173 VLDEVLAVGDEAFQRKCDDFFTQIRKDPTKTVILVTHDMGAVKR 216
Cdd:PRK14258 173 LMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSR 216
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
43-230 |
5.21e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 62.20 E-value: 5.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 43 QHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSG--------KLVPFIELGVGF---NPELTGRE 111
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhditrlknREVPFLRRQIGMifqDHHLLMDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 112 NVYLNCAL----LGFDHEQTDAMYDDIVEFAELGDfmdqKLKNY----SSGMQVRLAFSVAIKAQGDILVLDEVLAVGDE 183
Cdd:PRK10908 95 TVYDNVAIpliiAGASGDDIRRRVSAALDKVGLLD----KAKNFpiqlSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2222587728 184 AFQRKCDDFFTQIRKDPTkTVILVTHDMGAVKRYCTRAMMIEDGKIV 230
Cdd:PRK10908 171 ALSEGILRLFEEFNRVGV-TVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
44-238 |
7.30e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 62.90 E-value: 7.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 44 HVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVP---------FIELgVGFNPE-----LTG 109
Cdd:PRK13652 18 EALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITkenirevrkFVGL-VFQNPDdqifsPTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 110 RENVYLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRKC 189
Cdd:PRK13652 97 EQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKEL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2222587728 190 DDFFTQIRKDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETV 238
Cdd:PRK13652 177 IDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
39-238 |
1.07e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 61.93 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 39 GYRWQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPF-----IELGVGF------NP-E 106
Cdd:PRK10253 16 GYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyaskeVARRIGLlaqnatTPgD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 107 LTGRENV----YLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGD 182
Cdd:PRK10253 96 ITVQELVargrYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2222587728 183 EAFQRKCDDFFTQIRKDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYG-DKETV 238
Cdd:PRK10253 176 ISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGaPKEIV 232
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
40-239 |
1.31e-10 |
|
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: 61.40 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 40 YRWQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLV---PFIE---LGVGFNP-------E 106
Cdd:cd03218 10 YGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDItklPMHKrarLGIGYLPqeasifrK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 107 LTGRENVYLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDE------VLAV 180
Cdd:cd03218 90 LTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEpfagvdPIAV 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 181 GDeaFQRkcddfFTQIRKDpTKTVILVT-HDMGAVKRYCTRAMMIEDGKIVAYGDKETVA 239
Cdd:cd03218 170 QD--IQK-----IIKILKD-RGIGVLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
49-238 |
1.49e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 62.06 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 49 ISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPFI-----------ELGVGFN-PEL-----TGRE 111
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTskqkeikpvrkKVGVVFQfPESqlfeeTVLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 112 NVYLNCALLGFDHEQTDAMYDDIVEFAELG-DFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRKCD 190
Cdd:PRK13643 105 DVAFGPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMM 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2222587728 191 DFFTQIRKDpTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETV 238
Cdd:PRK13643 185 QLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDV 231
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
46-277 |
1.60e-10 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 63.06 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 46 LRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPFIEL-------GVGFNPEL----TGRENVY 114
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRaslrrniAVVFQDAGlfnrSIEDNIR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 115 LNCAllgfdhEQTDAMYDDIVEFAELGDFMDQKLKNY-----------SSGMQVRLAFSVAIKAQGDILVLDEVLAVGDE 183
Cdd:PRK13657 431 VGRP------DATDEEMRAAAERAQAHDFIERKPDGYdtvvgergrqlSGGERQRLAIARALLKDPPILILDEATSALDV 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 184 AFQRKCDDFFTQIRKDPTKTVIlvTHDMGAVkRYCTRAMMIEDGKIVAYGdketvadryTLSNLEAERKKGEKQARkaAQ 263
Cdd:PRK13657 505 ETEAKVKAALDELMKGRTTFII--AHRLSTV-RNADRILVFDNGRVVESG---------SFDELVARGGRFAALLR--AQ 570
|
250
....*....|....
gi 2222587728 264 ALAQKDEQGKAVPV 277
Cdd:PRK13657 571 GMLQEDERRKQPAA 584
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
32-238 |
1.65e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 62.55 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 32 NWTKGIRGyrwQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGK---LVPFIE--LGVGFN-- 104
Cdd:PRK11607 24 NLTKSFDG---QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVdlsHVPPYQrpINMMFQsy 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 105 ---PELTGRENVYLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVG 181
Cdd:PRK11607 101 alfPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGAL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2222587728 182 DEAFQRKCDDFFTQIRKDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETV 238
Cdd:PRK11607 181 DKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
43-237 |
2.07e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 62.92 E-value: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 43 QHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPF----------------IELgvgFNPE 106
Cdd:PRK11160 353 QPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADyseaalrqaisvvsqrVHL---FSAT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 107 LtgRENvylncaLLGFDHEQTDAMYDDIVEFAELGDFM--DQKLKNY--------SSGMQVRLAFSVAIKAQGDILVLDE 176
Cdd:PRK11160 430 L--RDN------LLLAAPNASDEALIEVLQQVGLEKLLedDKGLNAWlgeggrqlSGGEQRRLGIARALLHDAPLLLLDE 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2222587728 177 VLAVGDEAFQRKCDDFFTQIRKDptKTVILVTHDMGAVKRYcTRAMMIEDGKIVAYGDKET 237
Cdd:PRK11160 502 PTEGLDAETERQILELLAEHAQN--KTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQE 559
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
45-210 |
2.28e-10 |
|
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: 62.69 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSG-KLVPFIELG-------VGFNPEL---TGRENV 113
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGvPLADADADSwrdqiawVPQHPFLfagTIAENI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 114 YLNCAllgfdhEQTDAMYDDIVEFAELGDFMDQKLKNY-----------SSGMQVRLAFSVAIKAQGDILVLDEVLAVGD 182
Cdd:TIGR02857 417 RLARP------DASDAEIREALERAGLDEFVAALPQGLdtpigeggaglSGGQAQRLALARAFLRDAPLLLLDEPTAHLD 490
|
170 180
....*....|....*....|....*...
gi 2222587728 183 EAFQRKCDDFFTQIRKdpTKTVILVTHD 210
Cdd:TIGR02857 491 AETEAEVLEALRALAQ--GRTVLLVTHR 516
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
47-238 |
2.60e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 60.87 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 47 RGISFQVHQGEFFGIVGRNGGGKS----TLLKIISQIYYPNKGSV----------SVSGKLVPFIELG--VGFNPELTGR 110
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVlldgkpvapcALRGRKIATIMQNprSAFNPLHTMH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 111 ENVYLNCALLGfdHEQTDAMYDDIVEFAELGDfMDQKLKNY----SSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQ 186
Cdd:PRK10418 100 THARETCLALG--KPADDATLTAALEAVGLEN-AARVLKLYpfemSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2222587728 187 RKCDDFFTQIRKDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETV 238
Cdd:PRK10418 177 ARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
28-229 |
2.80e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 60.80 E-value: 2.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 28 QAVINWTKGIRGYRWQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKG----------SVSVSGKLVPFI 97
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSagshiellgrTVQREGRLARDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 98 -----ELGVGFNP-----ELTGRENVYLNC---------ALLGFDHEQTDAMYDDIVEFAeLGDFMDQKLKNYSSGMQVR 158
Cdd:PRK09984 82 rksraNTGYIFQQfnlvnRLSVLENVLIGAlgstpfwrtCFSWFTREQKQRALQALTRVG-MVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2222587728 159 LAFSVAIKAQGDILVLDEVLAVGDEAFQRKCDDFFTQIRKDPTKTVILVTHDMGAVKRYCTRAMMIEDGKI 229
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
61-177 |
2.90e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 59.50 E-value: 2.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 61 IVGRNGGGKSTLLKIISQIYYPNKGSV--------SVSGKLVPFIELGVGFNPELTGRENVYLNCALlgfdHEQTDAMYD 132
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIyykncninNIAKPYCTYIGHNLGLKLEMTVFENLKFWSEI----YNSAETLYA 106
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2222587728 133 DIVEFaELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEV 177
Cdd:PRK13541 107 AIHYF-KLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEV 150
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
45-241 |
3.15e-10 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 60.11 E-value: 3.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVP-------FIELGVG-----FN--PELTGR 110
Cdd:PRK09493 16 VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpkvderLIRQEAGmvfqqFYlfPHLTAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 111 ENVYLN-CALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRKC 189
Cdd:PRK09493 96 ENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEV 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2222587728 190 ddffTQIRKDPTK---TVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETVADR 241
Cdd:PRK09493 176 ----LKVMQDLAEegmTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKN 226
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
44-233 |
4.27e-10 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 61.24 E-value: 4.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 44 HVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLV---PFIELGVGF---N----PELTGRENV 113
Cdd:COG3839 17 EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVtdlPPKDRNIAMvfqSyalyPHMTVYENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 114 YLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDeAFQRkcddff 193
Cdd:COG3839 97 AFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLD-AKLR------ 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2222587728 194 TQIRKDPTK-------TVILVTHD------MGavkrycTRAMMIEDGKIVAYG 233
Cdd:COG3839 170 VEMRAEIKRlhrrlgtTTIYVTHDqveamtLA------DRIAVMNDGRIQQVG 216
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
49-233 |
4.84e-10 |
|
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: 62.34 E-value: 4.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 49 ISFqvHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVP----FIELGVGFNPE-------LTGRENVYLNC 117
Cdd:TIGR01257 951 ITF--YENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIEtnldAVRQSLGMCPQhnilfhhLTVAEHILFYA 1028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 118 ALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRKCDDFFTQIR 197
Cdd:TIGR01257 1029 QLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYR 1108
|
170 180 190
....*....|....*....|....*....|....*.
gi 2222587728 198 KDptKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYG 233
Cdd:TIGR01257 1109 SG--RTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
45-238 |
5.10e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 60.06 E-value: 5.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPF-------------IELGVGFN-----PE 106
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFgkdifqidaiklrKEVGMVFQqpnpfPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 107 LTGRENVYLNCALLGF-DHEQTDAMYDDIVE----FAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVG 181
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIkEKREIKKIVEECLRkvglWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2222587728 182 DEAFQRKCDDFFTQIRKDptKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETV 238
Cdd:PRK14246 185 DIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
46-230 |
5.48e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 60.11 E-value: 5.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 46 LRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPF-------IELGVGF-NPE-----LTGREN 112
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAenvwnlrRKIGMVFqNPDnqfvgATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 113 VYLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRKCDDF 192
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRV 182
|
170 180 190
....*....|....*....|....*....|....*...
gi 2222587728 193 FTQIRKDPTKTVILVTHDMGAVKRyCTRAMMIEDGKIV 230
Cdd:PRK13642 183 IHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEII 219
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
45-233 |
5.68e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 59.54 E-value: 5.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQI--YYPN---KGSVSVSGKLV---PFIEL----GVGFN-----PEL 107
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEarvSGEVYLDGQDIfkmDVIELrrrvQMVFQipnpiPNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 108 TGRENVYLNCAL--LGFDHEQTDAMYDDIVEFAELGDFMDQKLK----NYSSGMQVRLAFSVAIKAQGDILVLDEVLAVG 181
Cdd:PRK14247 98 SIFENVALGLKLnrLVKSKKELQERVRWALEKAQLWDEVKDRLDapagKLSGGQQQRLCIARALAFQPEVLLADEPTANL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2222587728 182 DEAFQRKCDDFFTQIRKDptKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYG 233
Cdd:PRK14247 178 DPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWG 227
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
37-160 |
1.10e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 57.89 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 37 IRGyrwQHVL-RGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLV-----PFIE----LG--VGFN 104
Cdd:PRK13538 10 ERD---ERILfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIrrqrdEYHQdllyLGhqPGIK 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2222587728 105 PELTGRENVYLNCALLGfdhEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLA 160
Cdd:PRK13538 87 TELTALENLRFYQRLHG---PGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVA 139
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-243 |
1.30e-09 |
|
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: 59.30 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 6 VLDVHDVYKDFKLPTeqatglkqavinwtkgirgyRWQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPN-- 83
Cdd:COG0444 1 LLEVRNLKVYFPTRR--------------------GVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgi 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 84 -KGSVSVSGKLVpfieLGVG----------------------FNPELTGRENVYLncALLGFDHEQTDAMYDDIVE-FAE 139
Cdd:COG0444 61 tSGEILFDGEDL----LKLSekelrkirgreiqmifqdpmtsLNPVMTVGDQIAE--PLRIHGGLSKAEARERAIElLER 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 140 LG-DFMDQKLKNY----SSGMQVRLAFSVAIKAQGDILVLDE------------VLavgdeafqrkcdDFFTQIRKDPTK 202
Cdd:COG0444 135 VGlPDPERRLDRYphelSGGMRQRVMIARALALEPKLLIADEpttaldvtiqaqIL------------NLLKDLQRELGL 202
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2222587728 203 TVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETVADR----YT 243
Cdd:COG0444 203 AILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFENprhpYT 247
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
42-209 |
1.57e-09 |
|
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: 57.50 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 42 WQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPFIE-------LGVGFNPELTGRENVY 114
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRdsiarglLYLGHAPGIKTTLSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 115 LNCALLGFDHEqTDAMYDDIVEfAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAfqrKCDDFFT 194
Cdd:cd03231 92 ENLRFWHADHS-DEQVEEALAR-VGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA---GVARFAE 166
|
170
....*....|....*..
gi 2222587728 195 QIRKDPTK--TVILVTH 209
Cdd:cd03231 167 AMAGHCARggMVVLTTH 183
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
38-238 |
1.82e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 57.98 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 38 RGYRWQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPFIEL------GVGFNPE---LT 108
Cdd:PRK10895 11 KAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhararrGIGYLPQeasIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 109 GRENVYLNC-ALLGFDH----EQTDAMYDDIVE---FAELGDFMDQKLknySSGMQVRLAFSVAIKAQGDILVLDEVLAV 180
Cdd:PRK10895 91 RRLSVYDNLmAVLQIRDdlsaEQREDRANELMEefhIEHLRDSMGQSL---SGGERRRVEIARALAANPKFILLDEPFAG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2222587728 181 GDEAFQRKCDDFFTQIRkDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETV 238
Cdd:PRK10895 168 VDPISVIDIKRIIEHLR-DSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
45-234 |
2.06e-09 |
|
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: 57.93 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPFIELG--------VGFNPEL---TGRENV 113
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRwlrsqiglVSQEPVLfdgTIAENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 114 ylncaLLGfDHEQTDAMYDDIVEFAELGDFMDQKLKNY-----------SSGMQVRLAFSVAIKAQGDILVLDEVL---- 178
Cdd:cd03249 98 -----RYG-KPDATDEEVEEAAKKANIHDFIMSLPDGYdtlvgergsqlSGGQKQRIAIARALLRNPKILLLDEATsald 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2222587728 179 AVGDEAFQRKCDdfftQIRKDptKTVILVTHDMGAVkRYCTRAMMIEDGKIVAYGD 234
Cdd:cd03249 172 AESEKLVQEALD----RAMKG--RTTIVIAHRLSTI-RNADLIAVLQNGQVVEQGT 220
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
55-210 |
2.20e-09 |
|
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: 55.84 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 55 QGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVsvsgklvpfielgvgfnpeltgrenVYLNCallgfdheqtdAMYDDI 134
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV-------------------------IYIDG-----------EDILEE 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 135 VEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRK-----CDDFFTQIRKDPTKTVILVTH 209
Cdd:smart00382 45 VLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALlllleELRLLLLLKSEKNLTVILTTN 124
|
.
gi 2222587728 210 D 210
Cdd:smart00382 125 D 125
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
61-253 |
2.34e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 58.48 E-value: 2.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 61 IVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPF------------IELGVGFN-PEL-----TGRENVYLNCALLGF 122
Cdd:PRK13645 42 VIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkikevkrlrKEIGLVFQfPEYqlfqeTIEKDIAFGPVNLGE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 123 DHEQTDAMYDDIVEFAELG-DFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRKCDDFFTQIRKDPT 201
Cdd:PRK13645 122 NKQEAYKKVPELLKLVQLPeDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYK 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2222587728 202 KTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDK-ETVADRYTLSNLEAERKK 253
Cdd:PRK13645 202 KRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPfEIFSNQELLTKIEIDPPK 254
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
39-234 |
3.10e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 57.71 E-value: 3.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 39 GYRWQ--HVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPFIELG----------VGFNPE 106
Cdd:PRK13638 8 WFRYQdePVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGllalrqqvatVFQDPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 107 -----LTGRENVYLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVG 181
Cdd:PRK13638 88 qqifyTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2222587728 182 DEAFQRKCDDFFTQIRKDPTKtVILVTHDMGAVKRYCTRAMMIEDGKIVAYGD 234
Cdd:PRK13638 168 DPAGRTQMIAIIRRIVAQGNH-VIISSHDIDLIYEISDAVYVLRQGQILTHGA 219
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
45-229 |
5.46e-09 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 56.99 E-value: 5.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGsvsvsgklvpfiELgvgfnpeLTGRenvylncALLGFDH 124
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG------------EL-------LAGT-------APLAEAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 125 EQTDAMYDDivefAEL---------------GDFMDQKLK----------------NYSSGMQVRLAFSVAIKAQGDILV 173
Cdd:PRK11247 81 EDTRLMFQD----ARLlpwkkvidnvglglkGQWRDAALQalaavgladranewpaALSGGQKQRVALARALIHRPGLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2222587728 174 LDEVLAVGDEAFQRKCDDFFTQIRKDPTKTVILVTHDMGAVKRYCTRAMMIEDGKI 229
Cdd:PRK11247 157 LDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
46-245 |
6.38e-09 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 56.39 E-value: 6.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 46 LRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIyYPNKGSVSVSGKLVPFIELgvgfnPELTgRENVYLnC-------A 118
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSA-----AELA-RHRAYL-SqqqsppfA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 119 LLGF-----------DHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQ--VRLAFSV-----AIKAQGDILVLDEVLAV 180
Cdd:COG4138 84 MPVFqylalhqpagaSSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWqrVRLAAVLlqvwpTINPEGQLLLLDEPMNS 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2222587728 181 GDEAFQRKCDDFFTQIrKDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETVADRYTLS 245
Cdd:COG4138 164 LDVAQQAALDRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLS 227
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
45-234 |
6.56e-09 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 55.84 E-value: 6.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGS-VSVSGKLVPfielgVGFN----PELTGRENVYLNCAL 119
Cdd:PRK15177 2 VLDKTDFVMGYHEHIGILAAPGSGKTTLTRLLCGLDAPDEGDfIGLRGDALP-----LGANsfilPGLTGEENARMMASL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 120 LGFDHEQTDAMyddIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQ-RKCDDFFTQIRK 198
Cdd:PRK15177 77 YGLDGDEFSHF---CYQLTQLEQCYTDRVSEYSVTMKTHLAFAINLLLPCRLYIADGKLYTGDNATQlRMQAALACQLQQ 153
|
170 180 190
....*....|....*....|....*....|....*.
gi 2222587728 199 dptKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGD 234
Cdd:PRK15177 154 ---KGLIVLTHNPRLIKEHCHAFGVLLHGKITMCED 186
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
45-233 |
6.84e-09 |
|
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: 56.08 E-value: 6.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGK---------------LVP-----F---IELGV 101
Cdd:cd03253 16 VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQdirevtldslrraigVVPqdtvlFndtIGYNI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 102 GF-NPELTgRENVYlNCALLGFDHEQTDAM---YDDIVefAELGdfmdqkLKnYSSGMQVRLAFSVAIKAQGDILVLDEV 177
Cdd:cd03253 96 RYgRPDAT-DEEVI-EAAKAAQIHDKIMRFpdgYDTIV--GERG------LK-LSGGEKQRVAIARAILKNPPILLLDEA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2222587728 178 LAVGDEAFQRKCDDFFTQIRKDptKTVILVTHDMGAVKRyCTRAMMIEDGKIVAYG 233
Cdd:cd03253 165 TSALDTHTEREIQAALRDVSKG--RTTIVIAHRLSTIVN-ADKIIVLKDGRIVERG 217
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
46-240 |
8.29e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 56.47 E-value: 8.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 46 LRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSV---SGKLVPFIELGV-----------GF---NP--- 105
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDLYALSEaerrrllrtewGFvhqHPrdg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 106 ---ELTGRENVYLNCALLGFDHeqtdamYDDI----------VEFAElgDFMDQKLKNYSSGMQVRLAFSVAIKAQGDIL 172
Cdd:PRK11701 102 lrmQVSAGGNIGERLMAVGARH------YGDIratagdwlerVEIDA--ARIDDLPTTFSGGMQQRLQIARNLVTHPRLV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2222587728 173 VLDEVLAVGDEAFQRKCDDFFTQIRKDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETVAD 240
Cdd:PRK11701 174 FMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLD 241
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
46-233 |
1.45e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 56.95 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 46 LRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPFIELGVGFNPELTGRENVYL-------NCA 118
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLfndtianNIA 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 119 LLGFDHeqtdamY--DDIVEFAELGDFMD--QKLKN------------YSSGMQVRLAFSVAIKAQGDILVLDEVLAVGD 182
Cdd:PRK11176 439 YARTEQ------YsrEQIEEAARMAYAMDfiNKMDNgldtvigengvlLSGGQRQRIAIARALLRDSPILILDEATSALD 512
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2222587728 183 EAFQRKCDDFFTQIRKDptKTVILVTHDMGAVKRyCTRAMMIEDGKIVAYG 233
Cdd:PRK11176 513 TESERAIQAALDELQKN--RTSLVIAHRLSTIEK-ADEILVVEDGEIVERG 560
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
37-231 |
1.93e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 56.57 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 37 IRGYRWQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPF------IELGVGFNPE---- 106
Cdd:COG1129 259 VEGLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIrsprdaIRAGIAYVPEdrkg 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 107 ------LTGRENVYLncALL------GF-DHEQTDAMYDDIVEfaELG---DFMDQKLKNYSSGMQVRLAFSVAIKAQGD 170
Cdd:COG1129 339 eglvldLSIRENITL--ASLdrlsrgGLlDRRRERALAEEYIK--RLRiktPSPEQPVGNLSGGNQQKVVLAKWLATDPK 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2222587728 171 ILVLDE------VLAvgdeafqrKcDDFFTQIRK--DPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVA 231
Cdd:COG1129 415 VLILDEptrgidVGA--------K-AEIYRLIRElaAEGKAVIVISSELPELLGLSDRILVMREGRIVG 474
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
49-238 |
3.15e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 54.55 E-value: 3.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 49 ISFQVHQGEFFGIVGRNGGGKSTLLKIISQIyYPNKGSVSVSGKLVPFIELgvgfnPELtGRENVYLN------------ 116
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSA-----AEL-ARHRAYLSqqqtppfampvf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 117 --CALLGFDHEQTDAMYD---DIVEFAELGDFMDQKLKNYSSG--MQVRLAFSV-----AIKAQGDILVLDEVLAVGDEA 184
Cdd:PRK03695 88 qyLTLHQPDKTRTEAVASalnEVAEALGLDDKLGRSVNQLSGGewQRVRLAAVVlqvwpDINPAGQLLLLDEPMNSLDVA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2222587728 185 FQRKCDdffTQIRKDPTK--TVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETV 238
Cdd:PRK03695 168 QQAALD---RLLSELCQQgiAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
45-247 |
3.45e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 54.41 E-value: 3.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPfielgvGFNPELTGRENVYL--------- 115
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLE------SWSSKAFARKVAYLpqqlpaaeg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 116 --------------NCALLGF---DHEQTdamyDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVL 178
Cdd:PRK10575 100 mtvrelvaigrypwHGALGRFgaaDREKV----EEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPT 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2222587728 179 AVGDEAFQRKCDDFFTQIRKDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETVADRYTLSNL 247
Cdd:PRK10575 176 SALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQI 244
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
46-231 |
3.75e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.51 E-value: 3.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 46 LRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPF------IELGVGF-NPEL------TGREN 112
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFksskeaLENGISMvHQELnlvlqrSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 113 VYL-NCALLGF--DHeqtDAMYDDIVE-FAELGDFMDQKLK--NYS-SGMQ-VRLAFSVAIKAQgdILVLDEVLAVGDEa 184
Cdd:PRK10982 94 MWLgRYPTKGMfvDQ---DKMYRDTKAiFDELDIDIDPRAKvaTLSvSQMQmIEIAKAFSYNAK--IVIMDEPTSSLTE- 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2222587728 185 fqRKCDDFFTQIRK--DPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVA 231
Cdd:PRK10982 168 --KEVNHLFTIIRKlkERGCGIVYISHKMEEIFQLCDEITILRDGQWIA 214
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-72 |
5.58e-08 |
|
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: 55.08 E-value: 5.58e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2222587728 2 DAPVVLDVHDVYKDFKLPteqatglkqavinwtKGI--RGYRWQHVLRGISFQVHQGEFFGIVGRNGGGKSTL 72
Cdd:COG4172 271 DAPPLLEARDLKVWFPIK---------------RGLfrRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTL 328
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
43-209 |
6.26e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 53.04 E-value: 6.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 43 QHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYY--PNKGSVSvsgklVPFIElgvgFNPELTGRENVYLNCALL 120
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVD-----VPDNQ----FGREASLIDAIGRKGDFK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 121 gfdheqtDAMYddIVEFAELGD--FMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRKCDDFFTQIRK 198
Cdd:COG2401 114 -------DAVE--LLNAVGLSDavLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLAR 184
|
170
....*....|.
gi 2222587728 199 DPTKTVILVTH 209
Cdd:COG2401 185 RAGITLVVATH 195
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
45-210 |
8.64e-08 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 54.18 E-value: 8.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPFI-----ELGVGFN-----PELTGRENVY 114
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVpaenrHVNTVFQsyalfPHMTVFENVA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 115 LNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRKCDDFFT 194
Cdd:PRK09452 109 FGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELK 188
|
170
....*....|....*.
gi 2222587728 195 QIRKDPTKTVILVTHD 210
Cdd:PRK09452 189 ALQRKLGITFVFVTHD 204
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
44-230 |
8.98e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 52.96 E-value: 8.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 44 HVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVP------FIELGVGFNPE---LTGRENVY 114
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITdwqtakIMREAVAIVPEgrrVFSRMTVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 115 LNCALLGF--DHEQTDAMYDDIVE-FAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDE-VLAVGDEAFQRKCD 190
Cdd:PRK11614 99 ENLAMGGFfaERDQFQERIKWVYElFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEpSLGLAPIIIQQIFD 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2222587728 191 DfFTQIRKDPTkTVILVTHDMGAVKRYCTRAMMIEDGKIV 230
Cdd:PRK11614 179 T-IEQLREQGM-TIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
61-238 |
1.31e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 53.34 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 61 IVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPFIELGVGFNPELTGRENVYLNCALlgFDH------------EQTD 128
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLPPEKRRIGYVFQDARL--FPHykvrgnlrygmaKSMV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 129 AMYDDIVEFaeLGdfMDQKLKNY----SSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRKCDDFFTQIRKDpTKTV 204
Cdd:PRK11144 107 AQFDKIVAL--LG--IEPLLDRYpgslSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLARE-INIP 181
|
170 180 190
....*....|....*....|....*....|....*
gi 2222587728 205 IL-VTHDMGAVKRYCTRAMMIEDGKIVAYGDKETV 238
Cdd:PRK11144 182 ILyVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
46-238 |
1.94e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 52.33 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 46 LRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSV------SGK----LVPFIE-LGVGFN-PELT-GREN 112
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKknkkLKPLRKkVGIVFQfPEHQlFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 113 VYLNCAL----LGFDHEQTDAMYDDIVEFAELG-DFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQR 187
Cdd:PRK13634 103 VEKDICFgpmnFGVSEEDAKQKAREMIELVGLPeELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRK 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2222587728 188 KCDDFFTQIRKDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETV 238
Cdd:PRK13634 183 EMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
45-179 |
2.15e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 51.39 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGK---------LVPFIELGVGFNPELTGRENVYL 115
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKtatrgdrsrFMAYLGHLPGLKADLSTLENLHF 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2222587728 116 NCALLGFDHEQTDAMYDDIVefaELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLA 179
Cdd:PRK13543 106 LCGLHGRRAKQMPGSALAIV---GLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYA 166
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
45-255 |
2.38e-07 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 52.78 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPFI---ELGVGFnpeltgrenVYLNCALLG 121
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLharDRKVGF---------VFQHYALFR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 122 ----FD-----------HEQTDAMYDD-----IVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVG 181
Cdd:PRK10851 88 hmtvFDniafgltvlprRERPNAAAIKakvtqLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2222587728 182 DEAFQRKCDDFFTQIRKDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETV----ADRYTLSNL-EAERKKGE 255
Cdd:PRK10851 168 DAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVwrepATRFVLEFMgEVNRLQGT 246
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
46-238 |
2.46e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 52.90 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 46 LRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYyPN---KGSVSVSG-------------KLVPFIELGVGFNPELTG 109
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGsplkasnirdterAGIVIIHQELTLVPELSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 110 RENVYLNcallgfdHEQT--------DAMY---DDIVEFAELGDFMDQK-LKNYSSGMQVRLAFSVAIKAQGDILVLDEV 177
Cdd:TIGR02633 96 AENIFLG-------NEITlpggrmayNAMYlraKNLLRELQLDADNVTRpVGDYGGGQQQLVEIAKALNKQARLLILDEP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2222587728 178 LAvgdeAFQRKCDDFFTQIRKDPTK---TVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETV 238
Cdd:TIGR02633 169 SS----SLTEKETEILLDIIRDLKAhgvACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTM 228
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
44-243 |
3.15e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.79 E-value: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 44 HVLRGISFQVHQGEFFGIVGRNGGGKST----LLKIIsqiyyPNKGSVSVSG---------KLVPF-IELGVGF---NPE 106
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGqplhnlnrrQLLPVrHRIQVVFqdpNSS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 107 LTGRENVYLNCAL-LGFDHEQTDAMYDD---IVEFAELGdfMDQKLKN-----YSSGMQVRLAFSVAIKAQGDILVLDEV 177
Cdd:PRK15134 375 LNPRLNVLQIIEEgLRVHQPTLSAAQREqqvIAVMEEVG--LDPETRHrypaeFSGGQRQRIAIARALILKPSLIILDEP 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 178 LAVGDEAFQRKCDDFFTQIRKDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETV----ADRYT 243
Cdd:PRK15134 453 TSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVfaapQQEYT 522
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
40-238 |
4.64e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 50.94 E-value: 4.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 40 YRWQHV--LRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPFIELG--------------VGF 103
Cdd:PRK15112 21 FRRQTVeaVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSyrsqrirmifqdpsTSL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 104 NPeltgRENV--------YLNCALLGFDHEQtdAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLD 175
Cdd:PRK15112 101 NP----RQRIsqildfplRLNTDLEPEQREK--QIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIAD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2222587728 176 EVLAVGDEAFQRKCDDFFTQIRKDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETV 238
Cdd:PRK15112 175 EALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADV 237
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
45-233 |
4.99e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 52.64 E-value: 4.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPFIEL-GVGFNPELTGRENVYLNCAL-LGF 122
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLhDLRFKITIIPQDPVLFSGSLrMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 123 D--HEQTDAMYDDIVEFAELGDFMD---QKL--------KNYSSGMQVRLAFSVAIKAQGDILVLDEVLAvgdeAFQRKC 189
Cdd:TIGR00957 1381 DpfSQYSDEEVWWALELAHLKTFVSalpDKLdhecaeggENLSVGQRQLVCLARALLRKTKILVLDEATA----AVDLET 1456
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2222587728 190 DDFF-TQIRKD-PTKTVILVTHDMGAVKRYcTRAMMIEDGKIVAYG 233
Cdd:TIGR00957 1457 DNLIqSTIRTQfEDCTVLTIAHRLNTIMDY-TRVIVLDKGEVAEFG 1501
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
40-238 |
5.19e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 50.93 E-value: 5.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 40 YRWQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQ--------------------IYYPNKGSVSVSGklvpfiEL 99
Cdd:PRK14239 15 YNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRmndlnpevtitgsivynghnIYSPRTDTVDLRK------EI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 100 GVGF---NP-ELTGRENVYLNCALLGfdhEQTDAMYDDIVE--------FAELGDFMDQKLKNYSSGMQVRLAFSVAIKA 167
Cdd:PRK14239 89 GMVFqqpNPfPMSIYENVVYGLRLKG---IKDKQVLDEAVEkslkgasiWDEVKDRLHDSALGLSGGQQQRVCIARVLAT 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2222587728 168 QGDILVLDEVLAVGDEAFQRKCDDFFTQIRKDptKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETV 238
Cdd:PRK14239 166 SPKIILLDEPTSALDPISAGKIEETLLGLKDD--YTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
35-176 |
5.68e-07 |
|
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: 50.35 E-value: 5.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 35 KGIRGYRWqhVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIIS---QIYYPNKGSVSVSG---------KLVPFIELGVG 102
Cdd:cd03234 14 KNWNKYAR--ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISgrvEGGGTTSGQILFNGqprkpdqfqKCVAYVRQDDI 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2222587728 103 FNPELTGRENVYLnCALLGFDHEQTDAMYDDIVEFAELGDFMD-----QKLKNYSSGMQVRLAFSVAIKAQGDILVLDE 176
Cdd:cd03234 92 LLPGLTVRETLTY-TAILRLPRKSSDAIRKKRVEDVLLRDLALtriggNLVKGISGGERRRVSIAVQLLWDPKVLILDE 169
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
46-115 |
6.40e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.54 E-value: 6.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 46 LRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPFI------ELGVG-----FN--PELTGREN 112
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNgpkssqEAGIGiihqeLNliPQLTIAEN 99
|
...
gi 2222587728 113 VYL 115
Cdd:PRK10762 100 IFL 102
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
44-176 |
6.90e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 52.05 E-value: 6.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 44 HVlrgiSFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPFIELG----VGFNP-------ELTGREN 112
Cdd:NF033858 284 HV----SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIAtrrrVGYMSqafslygELTVRQN 359
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2222587728 113 VYLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDE 176
Cdd:NF033858 360 LELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDE 423
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
45-251 |
7.63e-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: 50.63 E-value: 7.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKlvpfielgVGFNPEL------TGRENVYLNCA 118
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--------ISFSSQFswimpgTIKENIIFGVS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 119 LLGFDHE---QTDAMYDDIVEFAELGD-FMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRKCddFFT 194
Cdd:cd03291 124 YDEYRYKsvvKACQLEEDITKFPEKDNtVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEI--FES 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2222587728 195 QIRK-DPTKTVILVTHDMGAVKRyCTRAMMIEDGKIVAYGdketvadryTLSNLEAER 251
Cdd:cd03291 202 CVCKlMANKTRILVTSKMEHLKK-ADKILILHEGSSYFYG---------TFSELQSLR 249
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
46-255 |
7.98e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 51.39 E-value: 7.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 46 LRGISFQVHQGEFFGIVGRNGGGKS----TLLKIISQiyypNKGSVSVSGKLV-----PFIELG---------------- 100
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQ----AGGLVQCDKMLLrrrsrQVIELSeqsaaqmrhvrgadma 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 101 -------VGFNPELTGRENVYLNCAL-LGFDHEqtDAMYD-----DIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKA 167
Cdd:PRK10261 108 mifqepmTSLNPVFTVGEQIAESIRLhQGASRE--EAMVEakrmlDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSC 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 168 QGDILVLDEVLAVGDEAFQRKCDDFFTQIRKDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETV----ADRYT 243
Cdd:PRK10261 186 RPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIfhapQHPYT 265
|
250
....*....|..
gi 2222587728 244 LSNLEAERKKGE 255
Cdd:PRK10261 266 RALLAAVPQLGA 277
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
52-211 |
8.31e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 51.32 E-value: 8.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 52 QVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVS----VSGK---LVPFIELGVGFNPELTGRENVylncallgfdh 124
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDedlkISYKpqyISPDYDGTVEEFLRSANTDDF----------- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 125 eQTDAMYDDIVEFAELGDFMDQKLKNYSSG-MQvRLAFSVAIKAQGDILVLDEVLAVGD--------EAFQRkcddfFTQ 195
Cdd:COG1245 431 -GSSYYKTEIIKPLGLEKLLDKNVKDLSGGeLQ-RVAIAACLSRDADLYLLDEPSAHLDveqrlavaKAIRR-----FAE 503
|
170
....*....|....*.
gi 2222587728 196 IRKdptKTVILVTHDM 211
Cdd:COG1245 504 NRG---KTAMVVDHDI 516
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
45-275 |
8.54e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.90 E-value: 8.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPFIELG--------VGFNPEL---TGRENV 113
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTdlrrvlsiIPQSPVLfsgTVRFNI 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 114 ylncallgfD--HEQTDAMYDDIVEFAELGDFMDQKL-----------KNYSSGMQVRLAFSVAIKAQGDILVLDEVLAV 180
Cdd:PLN03232 1331 ---------DpfSEHNDADLWEALERAHIKDVIDRNPfgldaevseggENFSVGQRQLLSLARALLRRSKILVLDEATAS 1401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 181 ----GDEAFQRKCDDFFTQIrkdptkTVILVTHDMGAVKRyCTRAMMIEDGKIVAYGDKETVADRYTLSNLEAERKKGEK 256
Cdd:PLN03232 1402 vdvrTDSLIQRTIREEFKSC------TMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTGPA 1474
|
250
....*....|....*....
gi 2222587728 257 QARKAAQALAQKDEQGKAV 275
Cdd:PLN03232 1475 NAQYLSNLVFERRENGMSL 1493
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
45-214 |
9.92e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 50.11 E-value: 9.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLvpfielGVGFNPEltgreNVYLNCAL----L 120
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKL------RIGYVPQ-----KLYLDTTLpltvN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 121 GFDHEQTDAMYDDI------VEFAELGDFMDQKLknySSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRKCDDFFT 194
Cdd:PRK09544 88 RFLRLRPGTKKEDIlpalkrVQAGHLIDAPMQKL---SGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLID 164
|
170 180
....*....|....*....|
gi 2222587728 195 QIRKDPTKTVILVTHDMGAV 214
Cdd:PRK09544 165 QLRRELDCAVLMVSHDLHLV 184
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
45-311 |
1.04e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 51.32 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVsvsgklvpFIELGVGFNPELTGRENVYLNCALLGFDH 124
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV--------WAERSIAYVPQQAWIMNATVRGNILFFDE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 125 EQTDAMYDDI------VEFAELGDFMD----QKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGD----EAFQRKCd 190
Cdd:PTZ00243 747 EDAARLADAVrvsqleADLAQLGGGLEteigEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDahvgERVVEEC- 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 191 dFFTQIRkdpTKTVILVTHDMGAVKRY-CTRAMmiEDGKIVAYGDKETVADRYTLSNLEAERK--KGEKQARKAAQALAQ 267
Cdd:PTZ00243 826 -FLGALA---GKTRVLATHQVHVVPRAdYVVAL--GDGRVEFSGSSADFMRTSLYATLAAELKenKDSKEGDADAEVAEV 899
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2222587728 268 KDEQGKAV-----PVFPNGLNARVPILRTYPIGSPLI------DGTQPFRFGVEY 311
Cdd:PTZ00243 900 DAAPGGAVdheppVAKQEGNAEGGDGAALDAAAGRLMtreekaSGSVPWSTYVAY 954
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
46-211 |
1.10e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 50.13 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 46 LRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVP---FIEL----GVGF-NPeltgrENVYLNC 117
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITddnFEKLrkhiGIVFqNP-----DNQFVGS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 118 AL---LGFDHEQTDAMYDDIVEF-------AELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQR 187
Cdd:PRK13648 100 IVkydVAFGLENHAVPYDEMHRRvsealkqVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQ 179
|
170 180
....*....|....*....|....
gi 2222587728 188 KCDDFFTQIRKDPTKTVILVTHDM 211
Cdd:PRK13648 180 NLLDLVRKVKSEHNITIISITHDL 203
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
37-106 |
1.13e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 50.80 E-value: 1.13e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2222587728 37 IRGYRWQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVP------FIELGVGFNPE 106
Cdd:COG3845 265 VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITglspreRRRLGVAYIPE 340
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
45-229 |
1.16e-06 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 49.43 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPFI-----------ELGVGFN-----PELT 108
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaakaelrnqKLGFIYQfhhllPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 109 GRENVYLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDeafQRK 188
Cdd:PRK11629 104 ALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD---ARN 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2222587728 189 CDDFFT---QIRKDPTKTVILVTHDMGAVKRYcTRAMMIEDGKI 229
Cdd:PRK11629 181 ADSIFQllgELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRL 223
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
30-251 |
1.27e-06 |
|
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: 50.57 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 30 VINWTKGIRGYRwqhVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQI--YYPNKGSV----------------SVSG 91
Cdd:TIGR03269 3 VKNLTKKFDGKE---VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpSKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 92 KLVP-----FIELGVGF-NPE--------------------LTGRENVYLNC--ALLGFDHEQTDAMYD--DIVEFAELG 141
Cdd:TIGR03269 80 EPCPvcggtLEPEEVDFwNLSdklrrrirkriaimlqrtfaLYGDDTVLDNVleALEEIGYEGKEAVGRavDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 142 DFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRKCDDFFTQIRKDPTKTVILVTHDMGAVKRYCTRA 221
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKA 239
|
250 260 270
....*....|....*....|....*....|..
gi 2222587728 222 MMIEDGKIVAYGDKETVADRY--TLSNLEAER 251
Cdd:TIGR03269 240 IWLENGEIKEEGTPDEVVAVFmeGVSEVEKEC 271
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
45-92 |
1.52e-06 |
|
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: 48.68 E-value: 1.52e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIIS--QIYYPNKGSVSVSGK 92
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMghPKYEVTEGEILFKGE 64
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
45-251 |
1.69e-06 |
|
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: 50.68 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKL-----VPFIELGvgfnpelTGRENVYLNcal 119
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRIsfspqTSWIMPG-------TIKDNIIFG--- 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 120 LGFDHEQTDA------MYDDIVEFAELGD--FMDQKLkNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGD-----EAFQ 186
Cdd:TIGR01271 511 LSYDEYRYTSvikacqLEEDIALFPEKDKtvLGEGGI-TLSGGQRARISLARAVYKDADLYLLDSPFTHLDvvtekEIFE 589
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2222587728 187 RKCDDFFTqirkdpTKTVILVTHDMGAVKRyCTRAMMIEDGKIVAYGdketvadryTLSNLEAER 251
Cdd:TIGR01271 590 SCLCKLMS------NKTRILVTSKLEHLKK-ADKILLLHEGVCYFYG---------TFSELQAKR 638
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
45-246 |
1.74e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.89 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGklVPFIELG-------VGFNPEL------TGRE 111
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDG--CDISKFGlmdlrkvLGIIPQApvlfsgTVRF 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 112 NvylncaLLGFDhEQTDAMYDDIVEFAELGDF-------MDQKL----KNYSSGMQVRLAFSVAIKAQGDILVLDEVLA- 179
Cdd:PLN03130 1332 N------LDPFN-EHNDADLWESLERAHLKDVirrnslgLDAEVseagENFSVGQRQLLSLARALLRRSKILVLDEATAa 1404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 180 --VGDEAFQRKcddfftQIRKD-PTKTVILVTHDMGAVKRyCTRAMMIEDGKIVAYGDKETVadrytLSN 246
Cdd:PLN03130 1405 vdVRTDALIQK------TIREEfKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENL-----LSN 1462
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
25-209 |
1.77e-06 |
|
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: 48.32 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 25 GLKQAVINWTKGIRGYRWQH---VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIIS--QIYYPNKGSVSVSGKLVPFIEL 99
Cdd:cd03213 1 GVTLSFRNLTVTVKSSPSKSgkqLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLDKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 100 G--VGF-------NPELTGRENVYlncallgfdheqtdamyddiveFAelgdfmdQKLKNYSSGMQVRLAFSVAIKAQGD 170
Cdd:cd03213 81 RkiIGYvpqddilHPTLTVRETLM----------------------FA-------AKLRGLSGGERKRVSIALELVSNPS 131
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2222587728 171 ILVLDEVLAvGDEAFQrkCDDFFTQIRK--DPTKTVILVTH 209
Cdd:cd03213 132 LLFLDEPTS-GLDSSS--ALQVMSLLRRlaDTGRTIICSIH 169
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
44-149 |
1.90e-06 |
|
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: 50.32 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 44 HVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIyypnkgSVSVSGKLVPFIELGVGF-------NPELTGRENVYLN 116
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV------DKDFNGEARPQPGIKVGYlpqepqlDPTKTVRENVEEG 92
|
90 100 110
....*....|....*....|....*....|....*.
gi 2222587728 117 CAllgfdhEQTDAM--YDDIVE-FAELGDFMDQKLK 149
Cdd:TIGR03719 93 VA------EIKDALdrFNEISAkYAEPDADFDKLAA 122
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
52-176 |
1.98e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.19 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 52 QVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSvsgklvpfIELGVGFNP-------ELTgrenVYlncALLGFDH 124
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD--------PELKISYKPqyikpdyDGT----VE---DLLRSIT 425
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2222587728 125 EQTDAMY--DDIVEFAELGDFMDQKLKNYSSG-MQvRLAFSVAIKAQGDILVLDE 176
Cdd:PRK13409 426 DDLGSSYykSEIIKPLQLERLLDKNVKDLSGGeLQ-RVAIAACLSRDADLYLLDE 479
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
45-92 |
2.52e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.16 E-value: 2.52e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGK 92
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGR 1372
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
26-241 |
2.70e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 50.33 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 26 LKQAVINWTKGIrgyrwQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKlvpfielgVGFNP 105
Cdd:TIGR00957 639 VHNATFTWARDL-----PPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--------VAYVP 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 106 EL------TGRENVYLNCALLGFDHEQTD---AMYDDIvEFAELGDFMD--QKLKNYSSGMQVRLAFSVAIKAQGDILVL 174
Cdd:TIGR00957 706 QQawiqndSLRENILFGKALNEKYYQQVLeacALLPDL-EILPSGDRTEigEKGVNLSGGQKQRVSLARAVYSNADIYLF 784
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2222587728 175 DEVL-AVGDEAFQRKCDDFFTQIRKDPTKTVILVTHDMGAVKRyCTRAMMIEDGKIVAYGDKETVADR 241
Cdd:TIGR00957 785 DDPLsAVDAHVGKHIFEHVIGPEGVLKNKTRILVTHGISYLPQ-VDVIIVMSGGKISEMGSYQELLQR 851
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
46-229 |
3.05e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 49.62 E-value: 3.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 46 LRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLV----PFIEL------------GVGFNPELTG 109
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvtrsPQDGLangivyisedrkRDGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 110 RENVYLnCALLGFDHEQTDAMYDDivEFAELGDF----------MDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEV-- 177
Cdd:PRK10762 348 KENMSL-TALRYFSRAGGSLKHAD--EQQAVSDFirlfniktpsMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPtr 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2222587728 178 -LAVG--DEAFQrkcddFFTQIRKDPTkTVILVTHDMGAVKRYCTRAMMIEDGKI 229
Cdd:PRK10762 425 gVDVGakKEIYQ-----LINQFKAEGL-SIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
45-234 |
3.92e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 48.69 E-value: 3.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSV----SGKLVPFIELGVGFNPELTGRENVYLNCALL 120
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKNNHELITNPYSKKIKNFKELRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 121 GF---------DHEQTDAMYDDI------VEFAELG-----------DFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVL 174
Cdd:PRK13631 121 VFqfpeyqlfkDTIEKDIMFGPValgvkkSEAKKLAkfylnkmglddSYLERSPFGLSGGQKRRVAIAGILAIQPEILIF 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 175 DEVLAVGDEAFQRKCDDFFTQIRKDpTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGD 234
Cdd:PRK13631 201 DEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKILKTGT 259
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
45-250 |
4.64e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 48.94 E-value: 4.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPFIELG--------VGFNPELTGrENVYLN 116
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDswrsrlavVSQTPFLFS-DTVANN 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 117 CALlgfdhEQTDAMYDDIVEFAELGDFMDQKLK---NY-----------SSGMQVRLAFSVAIKAQGDILVLDEVLAVGD 182
Cdd:PRK10789 409 IAL-----GRPDATQQEIEHVARLASVHDDILRlpqGYdtevgergvmlSGGQKQRISIARALLLNAEILILDDALSAVD 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2222587728 183 EAFQRKCDDFFTQIRKDptKTVILVTHDMGAVKRyCTRAMMIEDGKIVAYGDKETVA-------DRYTLSNLEAE 250
Cdd:PRK10789 484 GRTEHQILHNLRQWGEG--RTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAqqsgwyrDMYRYQQLEAA 555
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
51-263 |
5.93e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.79 E-value: 5.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 51 FQVHQGEFFGIVGRNGGGKSTLLKIIS--------QIYYPNKGSVS---------VSGKLVPFIELGVGFNPELTGRENV 113
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNgevllddgRIIYEQDLIVArlqqdpprnVEGTVYDFVAEGIEEQAEYLKRYHD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 114 YLNcaLLG-----------------FDHE---QTDAMYDDIVEfaELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILV 173
Cdd:PRK11147 104 ISH--LVEtdpseknlnelaklqeqLDHHnlwQLENRINEVLA--QLGLDPDAALSSLSGGWLRKAALGRALVSNPDVLL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 174 LDE------VLAVgdeafqrkcdDFFTQIRKDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAY-GDketvADRYTLSN 246
Cdd:PRK11147 180 LDEptnhldIETI----------EWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYpGN----YDQYLLEK 245
|
250 260
....*....|....*....|
gi 2222587728 247 LEAERKKGEKQA---RKAAQ 263
Cdd:PRK11147 246 EEALRVEELQNAefdRKLAQ 265
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
45-236 |
7.22e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 47.33 E-value: 7.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIIS--QIYYPNKGSVSVSGKLVPFIE------LGV--GF-NP-ELTGREN 112
Cdd:CHL00131 22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAghPAYKILEGDILFKGESILDLEpeerahLGIflAFqYPiEIPGVSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 113 V-YLNCALLGFDHEQTDAMYDDIvEFAELgdfMDQKLKnySSGMQ-------VRLAFSVAIKAQGDIL---VLDEVLAVG 181
Cdd:CHL00131 102 AdFLRLAYNSKRKFQGLPELDPL-EFLEI---INEKLK--LVGMDpsflsrnVNEGFSGGEKKRNEILqmaLLDSELAIL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 182 DEAFQRKCDDFFTQIR------KDPTKTVILVTHdmgavkrYcTRAM---------MIEDGKIVAYGDKE 236
Cdd:CHL00131 176 DETDSGLDIDALKIIAeginklMTSENSIILITH-------Y-QRLLdyikpdyvhVMQNGKIIKTGDAE 237
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
45-249 |
9.31e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 47.13 E-value: 9.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIIS----QIYYPN----KGSVSVSGKLVPFIE----------LGVGFNP- 105
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgdltGGGAPRgarvTGDVTLNGEPLAAIDaprlarlravLPQAAQPa 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 106 -ELTGRENVYLNC----ALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAI-------KAQGD--I 171
Cdd:PRK13547 96 fAFSAREIVLLGRyphaRRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphDAAQPprY 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2222587728 172 LVLDEVLAVGDEAFQRKCDDFFTQIRKDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGdkeTVADRYTLSNLEA 249
Cdd:PRK13547 176 LLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHG---APADVLTPAHIAR 250
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
46-80 |
1.01e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.86 E-value: 1.01e-05
10 20 30
....*....|....*....|....*....|....*
gi 2222587728 46 LRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIY 80
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY 51
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
27-232 |
1.31e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.58 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 27 KQAVI--NWTKGirgYRWQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVpfielgVGFN 104
Cdd:PRK15064 317 RNALEveNLTKG---FDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENAN------IGYY 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 105 PELTGREnvylncallgFDHEQT--DAMY-------DDIVEFAELG------DFMDQKLKNYSSGMQVRLAFSVAIKAQG 169
Cdd:PRK15064 388 AQDHAYD----------FENDLTlfDWMSqwrqegdDEQAVRGTLGrllfsqDDIKKSVKVLSGGEKGRMLFGKLMMQKP 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2222587728 170 DILVLDEVLAVGD----EAFQRKCDDFftqirkdpTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAY 232
Cdd:PRK15064 458 NVLVMDEPTNHMDmesiESLNMALEKY--------EGTLIFVSHDREFVSSLATRIIEITPDGVVDF 516
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
49-262 |
1.42e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 47.04 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 49 ISFQVHQGEFFGIVGRNGGGKS-TLLKIISQIYYPNKgsvsVSGKLVPF------------------IELGVGFNPELTG 109
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPGR----VMAEKLEFngqdlqrisekerrnlvgAEVAMIFQDPMTS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 110 renvyLN-CALLGFD-------HE--QTDAMYDDIVEFAELGDFMD--QKLKNY----SSGMQVRLAFSVAIKAQGDILV 173
Cdd:PRK11022 102 -----LNpCYTVGFQimeaikvHQggNKKTRRQRAIDLLNQVGIPDpaSRLDVYphqlSGGMSQRVMIAMAIACRPKLLI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 174 LDEVLAVGDEAFQRKCDDFFTQIRKDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETV--ADR--YTLSNLEA 249
Cdd:PRK11022 177 ADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIfrAPRhpYTQALLRA 256
|
250
....*....|...
gi 2222587728 250 ERKKGEKQARKAA 262
Cdd:PRK11022 257 LPEFAQDKARLAS 269
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
44-145 |
2.16e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.04 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 44 HVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNkgsvsvSGKLVPFIELGVGF-------NPELTGRENVYLN 116
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEF------EGEARPAPGIKVGYlpqepqlDPEKTVRENVEEG 94
|
90 100 110
....*....|....*....|....*....|..
gi 2222587728 117 CAllgfdhEQTDAM--YDDI-VEFAELGDFMD 145
Cdd:PRK11819 95 VA------EVKAALdrFNEIyAAYAEPDADFD 120
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
45-91 |
2.34e-05 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 46.74 E-value: 2.34e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSG 91
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDG 419
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
38-236 |
3.01e-05 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 45.53 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 38 RGYRwqHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVP---------------------- 95
Cdd:PRK11831 17 RGNR--CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPamsrsrlytvrkrmsmlfqsga 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 96 -FIELGVGFNPELTGRENVYLNCALLgfdhEQTDAMYDDIVEFAELGDFMDQKLknySSGMQVRLAFSVAIKAQGDILVL 174
Cdd:PRK11831 95 lFTDMNVFDNVAYPLREHTQLPAPLL----HSTVMMKLEAVGLRGAAKLMPSEL---SGGMARRAALARAIALEPDLIMF 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2222587728 175 DEVLAVGDEAFQRKCDDFFTQIRKDPTKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKE 236
Cdd:PRK11831 168 DEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQ 229
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
102-233 |
3.69e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.88 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 102 GFNPELTGRENVYLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVG 181
Cdd:NF000106 96 GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGL 175
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2222587728 182 DEAFQRKCDDFFTQIRKDPTkTVILVTHDMGAVKRYCTRAMMIEDGKIVAYG 233
Cdd:NF000106 176 DPRTRNEVWDEVRSMVRDGA-TVLLTTQYMEEAEQLAHELTVIDRGRVIADG 226
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
45-76 |
4.54e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 45.60 E-value: 4.54e-05
10 20 30
....*....|....*....|....*....|..
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKII 76
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMV 50
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
44-238 |
4.78e-05 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 45.03 E-value: 4.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 44 HVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIY--YPN---KGSV-----SVSGKLVPFIEL----GVGF---NP- 105
Cdd:COG1117 25 QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlIPGarvEGEIlldgeDIYDPDVDVVELrrrvGMVFqkpNPf 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 106 ELTGRENVylncaLLGF-DHEQTD-AMYDDIVEFA--------ELGDfmdqKLKNY----SSGMQVRL--AFSVAIKAqg 169
Cdd:COG1117 105 PKSIYDNV-----AYGLrLHGIKSkSELDEIVEESlrkaalwdEVKD----RLKKSalglSGGQQQRLciARALAVEP-- 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2222587728 170 DILVLDEVLAVGDEAFQRKCDDFFTQIRKDptKTVILVTHDMGAVKRYCTRAMMIEDGKIVAYGDKETV 238
Cdd:COG1117 174 EVLLMDEPTSALDPISTAKIEELILELKKD--YTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQI 240
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
3-238 |
5.05e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 45.10 E-value: 5.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 3 APVVLDVHDVYKDFKLPTeqatGLKQAVinwtkgirgyrwqhvlRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYP 82
Cdd:PRK09473 9 ADALLDVKDLRVTFSTPD----GDVTAV----------------NDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 83 N---KGSVSVSGKLV---PFIELG---------------VGFNPELTGRENVyLNCALL--GFDH----EQTDAMYDdIV 135
Cdd:PRK09473 69 NgriGGSATFNGREIlnlPEKELNklraeqismifqdpmTSLNPYMRVGEQL-MEVLMLhkGMSKaeafEESVRMLD-AV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 136 EFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRKCDDFFTQIRKDPTKTVILVTHDMGAVK 215
Cdd:PRK09473 147 KMPEARKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVA 226
|
250 260
....*....|....*....|...
gi 2222587728 216 RYCTRAMMIEDGKIVAYGDKETV 238
Cdd:PRK09473 227 GICDKVLVMYAGRTMEYGNARDV 249
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
55-211 |
6.17e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 45.55 E-value: 6.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 55 QGEFFGIVGRNGGGKSTLLKIISQIYYPN------------------------------KGSVSVSGK--LVPFIelgvg 102
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNlgdydeepswdevlkrfrgtelqdyfkklaNGEIKVAHKpqYVDLI----- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 103 fnPEL---TGREnvylncaLLgfdhEQTD--AMYDDIVEFAELGDFMDQKLKNYSSG-MQvRLAFSVAIKAQGDILVLDE 176
Cdd:COG1245 173 --PKVfkgTVRE-------LL----EKVDerGKLDELAEKLGLENILDRDISELSGGeLQ-RVAIAAALLRDADFYFFDE 238
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2222587728 177 V---LAVgdeaFQR----KCddfftqIRK--DPTKTVILVTHDM 211
Cdd:COG1245 239 PssyLDI----YQRlnvaRL------IRElaEEGKYVLVVEHDL 272
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
55-176 |
6.64e-05 |
|
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: 44.32 E-value: 6.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 55 QGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPF----IElgvgfnPELTGRenVYlncALLgfdHEQTDAM 130
Cdd:cd03237 24 ESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYkpqyIK------ADYEGT--VR---DLL---SSITKDF 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2222587728 131 YD------DIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDE 176
Cdd:cd03237 90 YThpyfktEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDE 141
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-70 |
1.37e-04 |
|
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: 44.29 E-value: 1.37e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 1 MDAPVVLDVHDVYKDFKlpteqatglkqavinwtkgiRGYRWQHVLRGISFQVHQGEFFGIVGRNGGGKS 70
Cdd:COG4172 1 MMSMPLLSVEDLSVAFG--------------------QGGGTVEAVKGVSFDIAAGETLALVGESGSGKS 50
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
48-89 |
1.41e-04 |
|
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: 44.16 E-value: 1.41e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2222587728 48 GISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSV 89
Cdd:TIGR03719 340 DLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI 381
|
|
| Wzt_C-like |
cd10147 |
C-Terminal domain of O-antigenic polysaccharide transporter protein Wzt and related proteins; ... |
296-407 |
2.07e-04 |
|
C-Terminal domain of O-antigenic polysaccharide transporter protein Wzt and related proteins; The Escherichia coli ABC protein Wzt consists of 2 domains, a conventional ABC domain that binds ATP and utilizes its energy to transport molecules across membranes, and a C terminal domain which is responsible for its target molecule specificity. Wzt is part of the ATP-binding-cassette (ABC) transporter complex, responsible for the transport of the O-antigenic polysaccharide (O-PS) portion of lipopolysaccharide (LPS), a major component of the outer membrane of Gram-negative bacteria. This CD includes Wzt proteins from two Escherichia coli serotypes O8 and O9a, WztO8 and WztO9a; these proteins are specific for their cognate polysaccharides (O8 or O9a O-PS).
Pssm-ID: 199902 Cd Length: 144 Bit Score: 41.58 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 296 SPLIDGTQPFRFGVEYQFDEP-GDFYIAIALHDMSR----GGITYDSGSKTFRITKKGHHRLEFELPVDqFNDGEFSLFT 370
Cdd:cd10147 25 VNTFRSGEPVTLRIEYEVNEDiEDPVVGFTIKDRDGqdvfGTNTLLLGGVLPSLKAGGEGEVEFTFPLP-LNPGEYSLSV 103
|
90 100 110
....*....|....*....|....*....|....*..
gi 2222587728 371 SLrvpnASDPGATDLVAVAIDAnsCSFVVRNPRNRQY 407
Cdd:cd10147 104 AL----ADGDGHHEVLDWIDDA--LSFEVESSSKSLF 134
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
45-230 |
2.07e-04 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 43.55 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGK--------------------LVPFIELGvgfn 104
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEdvthrsiqqrdicmvfqsyaLFPHMSLG---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 105 peltgrENVYLNCALLGFDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEA 184
Cdd:PRK11432 97 ------ENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDAN 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2222587728 185 FQRKCDDFFTQIRKDPTKTVILVTHDMgavkrycTRAMMIEDGKIV 230
Cdd:PRK11432 171 LRRSMREKIRELQQQFNITSLYVTHDQ-------SEAFAVSDTVIV 209
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
55-211 |
2.51e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 43.64 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 55 QGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVS------------------------VSGKLVP-----FIELGvgfnP 105
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEeepswdevlkrfrgtelqnyfkklYNGEIKVvhkpqYVDLI----P 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 106 EL---TGREnvylncaLLgfdhEQTD--AMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDEV--- 177
Cdd:PRK13409 174 KVfkgKVRE-------LL----KKVDerGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPtsy 242
|
170 180 190
....*....|....*....|....*....|....*
gi 2222587728 178 LAVGdeafQR-KCDDFFTQIRKDptKTVILVTHDM 211
Cdd:PRK13409 243 LDIR----QRlNVARLIRELAEG--KYVLVVEHDL 271
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
36-77 |
2.85e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.08 E-value: 2.85e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2222587728 36 GIRGYRWQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIIS 77
Cdd:PRK10938 266 GVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLIT 307
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
45-90 |
3.54e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.48 E-value: 3.54e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVS 90
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN 445
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
46-92 |
6.14e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 41.87 E-value: 6.14e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2222587728 46 LRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGK 92
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQ 77
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
49-106 |
6.31e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 42.21 E-value: 6.31e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2222587728 49 ISFQVHQGE---FFGIVgrnGGGKSTLLKIISQIYYPNKGSVSVSGKLVPF------IELGVGFNPE 106
Cdd:PRK11288 272 ISFSVRAGEivgLFGLV---GAGRSELMKLLYGATRRTAGQVYLDGKPIDIrsprdaIRAGIMLCPE 335
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
152-238 |
7.48e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 41.23 E-value: 7.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 152 SSGMQVRLAFSVAIKAQGDILVLDEVLAVGDEAFQRKCDDFFTQIRKdpTKTVILVTHDMGAVKRYCTRAMMIEDGKIVA 231
Cdd:PRK14271 165 SGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLAD--RLTVIIVTHNLAQAARISDRAALFFDGRLVE 242
|
....*..
gi 2222587728 232 YGDKETV 238
Cdd:PRK14271 243 EGPTEQL 249
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
48-89 |
1.80e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 40.87 E-value: 1.80e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2222587728 48 GISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSV 89
Cdd:PRK11819 342 DLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
39-176 |
2.16e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.54 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 39 GYRWQHVLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSG--KLVPFIELGVGFnpeLTGRENVYLN 116
Cdd:PRK10636 321 GYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKgiKLGYFAQHQLEF---LRADESPLQH 397
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587728 117 CALLGfDHEQTDAMYDDIVEFAELGDFMDQKLKNYSSGMQVRLAFSVAIKAQGDILVLDE 176
Cdd:PRK10636 398 LARLA-PQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDE 456
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
58-112 |
2.60e-03 |
|
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: 39.68 E-value: 2.60e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2222587728 58 FFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGKLVPFIELGVGFNPELTGREN 112
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTDERSRNGGIGGIPSLLNGIDPK 55
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
45-91 |
3.84e-03 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 39.07 E-value: 3.84e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYpNKGSVSVSG 91
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDG 64
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
46-93 |
4.37e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 39.55 E-value: 4.37e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2222587728 46 LRGISFQVHQGEFFGIVGRNGGGKSTLLKI-ISQIyYPNKGSVSVSGKL 93
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLmLGQL-QADSGRIHCGTKL 382
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
48-92 |
7.58e-03 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 38.53 E-value: 7.58e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2222587728 48 GISFQVHQGEFFGIVGRNGGGKSTLLKIISQIYYPNKGSVSVSGK 92
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGK 83
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
45-91 |
8.95e-03 |
|
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: 38.74 E-value: 8.95e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2222587728 45 VLRGISFQVHQGEFFGIVGRNGGGKSTLLKIISQIyYPNKGSVSVSG 91
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDG 1279
|
|
| |
