|
Name |
Accession |
Description |
Interval |
E-value |
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-246 |
1.46e-133 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 375.96 E-value: 1.46e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 1 MSVAIEFKNVTKRYPLYHHIGSGIKELIFNPRRAlsllSGRSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVM 80
Cdd:COG1134 1 MSSMIEVENVSKSYRLYHEPSRSLKELLLRRRRT----RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 81 KPSSGSVHVVGRVASMLELGGGFHPELTGRENIRLNATLLGLRRKELKQRLDKIIEFSELGEFIDEPIRVYSSGMLAKLG 160
Cdd:COG1134 77 EPTSGRVEVNGRVSALLELGAGFHPELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 161 FSVITQVDPDILIIDEVLAVGDISFQRKCLETINEFKKKGVTILFVSHNLRDIEKICDRVIWIENHKMKVMGEAHSVIAQ 240
Cdd:COG1134 157 FAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
....*.
gi 1699326967 241 YKEAMS 246
Cdd:COG1134 237 YEALLA 242
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
5-232 |
1.29e-108 |
|
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: 312.16 E-value: 1.29e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 5 IEFKNVTKRYPLYHHIGSGIKELifnpRRALSLLSGRSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSS 84
Cdd:cd03220 1 IELENVSKSYPTYKGGSSSLKKL----GILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 85 GSVHVVGRVASMLELGGGFHPELTGRENIRLNATLLGLRRKELKQRLDKIIEFSELGEFIDEPIRVYSSGMLAKLGFSVI 164
Cdd:cd03220 77 GTVTVRGRVSSLLGLGGGFNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1699326967 165 TQVDPDILIIDEVLAVGDISFQRKCLETINEFKKKGVTILFVSHNLRDIEKICDRVIWIENHKMKVMG 232
Cdd:cd03220 157 TALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1-243 |
2.61e-69 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 222.46 E-value: 2.61e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 1 MSVAIEFKNVTKRYPLYHHIGSGIKELIFNPRRalsllsGRSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVM 80
Cdd:PRK13545 1 MNYKVKFEHVTKKYKMYNKPFDKLKDLFFRSKD------GEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 81 KPSSGSVHVVGRvASMLELGGGFHPELTGRENIRLNATLLGLRRKELKQRLDKIIEFSELGEFIDEPIRVYSSGMLAKLG 160
Cdd:PRK13545 75 MPNKGTVDIKGS-AALIAISSGLNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 161 FSVITQVDPDILIIDEVLAVGDISFQRKCLETINEFKKKGVTILFVSHNLRDIEKICDRVIWIENHKMKVMGEAHSVIAQ 240
Cdd:PRK13545 154 FAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
...
gi 1699326967 241 YKE 243
Cdd:PRK13545 234 YDE 236
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1-243 |
2.65e-69 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 213.91 E-value: 2.65e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 1 MSVAIEFKNVTKRYPLYHHIGSGIKELIFnPRRAlsllsGRSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVM 80
Cdd:PRK13546 1 MNVSVNIKNVTKEYRIYRTNKERMKDALI-PKHK-----NKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 81 KPSSGSVHVVGRVaSMLELGGGFHPELTGRENIRLNATLLGLRRKELKQRLDKIIEFSELGEFIDEPIRVYSSGMLAKLG 160
Cdd:PRK13546 75 SPTVGKVDRNGEV-SVIAISAGLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 161 FSVITQVDPDILIIDEVLAVGDISFQRKCLETINEFKKKGVTILFVSHNLRDIEKICDRVIWIENHKMKVMGEAHSVIAQ 240
Cdd:PRK13546 154 FSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK 233
|
...
gi 1699326967 241 YKE 243
Cdd:PRK13546 234 YEA 236
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-241 |
2.50e-54 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 174.48 E-value: 2.50e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 5 IEFKNVTKRYplyhhigsgikelifnprralsllsgRSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSS 84
Cdd:COG1131 1 IEVRGLTKRY--------------------------GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTS 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 85 GSVHVVG------------RVASMLElGGGFHPELTGRENIRLNATLLGLRRKELKQRLDKIIEFSELGEFIDEPIRVYS 152
Cdd:COG1131 55 GEVRVLGedvardpaevrrRIGYVPQ-EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 153 SGMLAKLGF--SVITqvDPDILIIDEVlAVG-DISFQRKCLETINEFKKKGVTILFVSHNLRDIEKICDRVIWIENHKMK 229
Cdd:COG1131 134 GGMKQRLGLalALLH--DPELLILDEP-TSGlDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIV 210
|
250
....*....|..
gi 1699326967 230 VMGEAHSVIAQY 241
Cdd:COG1131 211 ADGTPDELKARL 222
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
45-244 |
2.21e-48 |
|
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: 159.64 E-value: 2.21e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRVA-----------SMLELGGGFHPELTGRENI 113
Cdd:COG4555 16 ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVrkeprearrqiGVLPDERGLYDRLTVRENI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 114 RLNATLLGLRRKELKQRLDKIIEFSELGEFIDEPIRVYSSGMLAK--LGFSVITqvDPDILIIDEVLAVGDISFQRKCLE 191
Cdd:COG4555 96 RYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKvaLARALVH--DPKVLLLDEPTNGLDVMARRLLRE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1699326967 192 TINEFKKKGVTILFVSHNLRDIEKICDRVIWIENHKMKVMGEAHSVIAQYKEA 244
Cdd:COG4555 174 ILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEE 226
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-228 |
2.08e-41 |
|
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: 139.46 E-value: 2.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 5 IEFKNVTKRYplyhhigsgikelifnprralsllsgRSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSS 84
Cdd:cd03230 1 IEVRNLSKRY--------------------------GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDS 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 85 GSVHVVG------------RVASMLElGGGFHPELTGRENIRlnatllglrrkelkqrldkiiefselgefidepirvYS 152
Cdd:cd03230 55 GEIKVLGkdikkepeevkrRIGYLPE-EPSLYENLTVRENLK------------------------------------LS 97
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1699326967 153 SGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKCLETINEFKKKGVTILFVSHNLRDIEKICDRVIWIENHKM 228
Cdd:cd03230 98 GGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
41-233 |
4.62e-38 |
|
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: 132.11 E-value: 4.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 41 RSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVG-----------RVASMLELGGGFHPELTG 109
Cdd:cd03266 16 KTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvkepaearRRLGFVSDSTGLYDRLTA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 110 RENIRLNATLLGLRRKELKQRLDKIIEFSELGEFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKC 189
Cdd:cd03266 96 RENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRAL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1699326967 190 LETINEFKKKGVTILFVSHNLRDIEKICDRVIWIenHKMKVMGE 233
Cdd:cd03266 176 REFIRQLRALGKCILFSTHIMQEVERLCDRVVVL--HRGRVVYE 217
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
5-223 |
1.90e-37 |
|
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: 131.30 E-value: 1.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 5 IEFKNVTKRYPLYHHiGSGIKEL---IFNPRRalsllsgRSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMK 81
Cdd:cd03267 1 IEVSNLSKSYRVYSK-EPGLIGSlksLFKRKY-------REVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 82 PSSGSVHVVGRV--------ASMLELGGGFHPEL----TGRENIRLNATLLGLRRKELKQRLDKIIEFSELGEFIDEPIR 149
Cdd:cd03267 73 PTSGEVRVAGLVpwkrrkkfLRRIGVVFGQKTQLwwdlPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1699326967 150 VYSSG--MLAKLGFSVITqvDPDILIIDEVLAVGDISFQRKCLETINEF-KKKGVTILFVSHNLRDIEKICDRVIWI 223
Cdd:cd03267 153 QLSLGqrMRAEIAAALLH--EPEILFLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVI 227
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
45-228 |
2.06e-37 |
|
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: 130.41 E-value: 2.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVG-----------RVASMLElGGGFHPELTGRENI 113
Cdd:cd03268 15 VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGksyqkniealrRIGALIE-APGFYPNLTARENL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 114 RLNATLLGLRrkelKQRLDKIIEFSELGEFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKCLETI 193
Cdd:cd03268 94 RLLARLLGIR----KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELI 169
|
170 180 190
....*....|....*....|....*....|....*
gi 1699326967 194 NEFKKKGVTILFVSHNLRDIEKICDRVIWIENHKM 228
Cdd:cd03268 170 LSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
42-232 |
3.86e-36 |
|
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: 127.49 E-value: 3.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 42 SYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHV---------------VGRVASMLELgggfHPE 106
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVaghdvvreprevrrrIGIVFQDLSV----DDE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 107 LTGRENIRLNATLLGLRRKELKQRLDKIIEFSELGEFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQ 186
Cdd:cd03265 88 LTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1699326967 187 RKCLETINEFKKK-GVTILFVSHNLRDIEKICDRVIWIENHKMKVMG 232
Cdd:cd03265 168 AHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-225 |
4.40e-36 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 129.82 E-value: 4.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 4 AIEFKNVTKRYPLYHHiGSGIKELI---FNPRRalsllsgRSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVM 80
Cdd:COG4586 1 IIEVENLSKTYRVYEK-EPGLKGALkglFRREY-------REVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGIL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 81 KPSSGSVHVVG------RVASMLELGGGF------HPELTGRENIRLNATLLGLRRKELKQRLDKIIEFSELGEFIDEPI 148
Cdd:COG4586 73 VPTSGEVRVLGyvpfkrRKEFARRIGVVFgqrsqlWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 149 RVYSSG--MLAKLGFSVITqvDPDILIIDE------VLAVGDIsfqRKCLETINefKKKGVTILFVSHNLRDIEKICDRV 220
Cdd:COG4586 153 RQLSLGqrMRCELAAALLH--RPKILFLDEptigldVVSKEAI---REFLKEYN--RERGTTILLTSHDMDDIEALCDRV 225
|
....*
gi 1699326967 221 IWIEN 225
Cdd:COG4586 226 IVIDH 230
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-232 |
1.60e-34 |
|
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: 122.77 E-value: 1.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 5 IEFKNVTKRYplyhhigsgikelifnprralsllsgRSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSS 84
Cdd:cd03269 1 LEVENVTKRF--------------------------GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDS 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 85 GSVHVVGRvaSMLELGG----------GFHPELTGRENIRLNATLLGLRRKELKQRLDKIIEFSELGEFIDEPIRVYSSG 154
Cdd:cd03269 55 GEVLFDGK--PLDIAARnrigylpeerGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKG 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1699326967 155 MLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKCLETINEFKKKGVTILFVSHNLRDIEKICDRVIWIENHKMKVMG 232
Cdd:cd03269 133 NQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-246 |
6.22e-34 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 121.67 E-value: 6.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 5 IEFKNVTKRYPlyhhigsgikelifnprralsllsgRSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSS 84
Cdd:COG1122 1 IELENLSFSYP-------------------------GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTS 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 85 GSVHVVGRVASMLELGG-----GF---HPEL-----TGRENIRLNATLLGLRRKELKQRLDKIIEFSELGEFIDEPI--- 148
Cdd:COG1122 56 GEVLVDGKDITKKNLRElrrkvGLvfqNPDDqlfapTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPhel 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 149 ------RVYSSGMLAklgfsvitqVDPDILIIDEVLAVGDISFQRKCLETINEFKKKGVTILFVSHNLRDIEKICDRVIW 222
Cdd:COG1122 136 sggqkqRVAIAGVLA---------MEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIV 206
|
250 260
....*....|....*....|....
gi 1699326967 223 IENHKMKVMGEAHSVIAQYKEAMS 246
Cdd:COG1122 207 LDDGRIVADGTPREVFSDYELLEE 230
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-232 |
6.44e-33 |
|
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: 119.15 E-value: 6.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 5 IEFKNVTKRYPlyhhigsgikelifnprralsllsGRSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSS 84
Cdd:cd03263 1 LQIRNLTKTYK------------------------KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTS 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 85 GSVHVVG------RVASMLELG-----GGFHPELTGRENIRLNATLLGLRRKELKQRLDKIIEFSELGEFIDEPIRVYSS 153
Cdd:cd03263 57 GTAYINGysirtdRKAARQSLGycpqfDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1699326967 154 GMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKCLETINEFkKKGVTILFVSHNLRDIEKICDRVIWIENHKMKVMG 232
Cdd:cd03263 137 GMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
47-227 |
1.46e-32 |
|
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: 117.58 E-value: 1.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 47 ENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRV---------ASMLELGG--GFHPELTGRENIRL 115
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPirdaredyrRRLAYLGHadGLKPELTVRENLRF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 116 NATLLGLRRKElkQRLDKIIEFSELGEFIDEPIRVYSSGM-----LAKLGFSvitqvDPDILIIDEVLAVGDISFQRKCL 190
Cdd:COG4133 99 WAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQkrrvaLARLLLS-----PAPLWLLDEPFTALDAAGVALLA 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 1699326967 191 ETINEFKKKGVTILFVSHNLRDIEkiCDRVIWIENHK 227
Cdd:COG4133 172 ELIAAHLARGGAVLLTTHQPLELA--AARVLDLGDFK 206
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
45-227 |
2.99e-32 |
|
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: 116.80 E-value: 2.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRVASMLELGG-----GF---HPE-----LTGRE 111
Cdd:cd03225 16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrrkvGLvfqNPDdqffgPTVEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 112 NIRLNATLLGLRRKELKQRLDKIIEFSELGEFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKCLE 191
Cdd:cd03225 96 EVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLE 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 1699326967 192 TINEFKKKGVTILFVSHNLRDIEKICDRVIWIENHK 227
Cdd:cd03225 176 LLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
42-226 |
2.78e-31 |
|
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: 114.55 E-value: 2.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 42 SYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRVASMLELGGGFHPE---------LTGREN 112
Cdd:cd03235 11 GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGYVPQrrsidrdfpISVRDV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 113 IRLNAT----LLGLRRKELKQRLDKIIEFSELGEFIDEPIRVYSSGMLAKLGFS-VITQvDPDILIIDEVLAVGDISFQR 187
Cdd:cd03235 91 VLMGLYghkgLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLArALVQ-DPDLLLLDEPFAGVDPKTQE 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 1699326967 188 KCLETINEFKKKGVTILFVSHNLRDIEKICDRVIWIENH 226
Cdd:cd03235 170 DIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-242 |
6.20e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 115.98 E-value: 6.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 4 AIEFKNVTKRYplyhhigsgikelifnprralsllsgRSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPS 83
Cdd:COG4152 1 MLELKGLTKRF--------------------------GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPD 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 84 SGSVHVVGRVASMLELGG-GFHPE-------LTGRENIRLNATLLGLRRKELKQRLDKIIEFSELGEFIDEPIRVYSSGM 155
Cdd:COG4152 55 SGEVLWDGEPLDPEDRRRiGYLPEerglypkMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 156 LAKLGF--SVITqvDPDILIIDE------VLAVGDISfqrkclETINEFKKKGVTILFVSHNLRDIEKICDRVIWIENHK 227
Cdd:COG4152 135 QQKVQLiaALLH--DPELLILDEpfsgldPVNVELLK------DVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGR 206
|
250
....*....|....*
gi 1699326967 228 MKVMGEAHSVIAQYK 242
Cdd:COG4152 207 KVLSGSVDEIRRQFG 221
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-226 |
1.39e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 113.65 E-value: 1.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 1 MSVAIEFKNVTKRYplyhhigsgikelifnprralsllsgRSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVM 80
Cdd:COG1121 3 MMPAIELENLTVSY--------------------------GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLL 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 81 KPSSGSVHVVGR-----------VASMLELGGGFhPeLTGRENIRLNAT----LLGLRRKELKQRLDKIIEFSELGEFID 145
Cdd:COG1121 57 PPTSGTVRLFGKpprrarrrigyVPQRAEVDWDF-P-ITVRDVVLMGRYgrrgLFRRPSRADREAVDEALERVGLEDLAD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 146 EPIRVYSSG-----MLAKlgfsVITQvDPDILIIDEVLAvG-DISFQRKCLETINEFKKKGVTILFVSHNLRDIEKICDR 219
Cdd:COG1121 135 RPIGELSGGqqqrvLLAR----ALAQ-DPDLLLLDEPFA-GvDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDR 208
|
....*..
gi 1699326967 220 VIWIENH 226
Cdd:COG1121 209 VLLLNRG 215
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
45-225 |
7.16e-29 |
|
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: 108.29 E-value: 7.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGR-VASM-----LELGGGFHPE-------LTGRE 111
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRdITGLppherARAGIGYVPEgrrifpeLTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 112 NIRLNATLlgLRRKELKQRLDKIIE-FSELGEFIDEPIRVYSSG---MLAkLGFSVITqvDPDILIIDEV---LA---VG 181
Cdd:cd03224 95 NLLLGAYA--RRRAKRKARLERVYElFPRLKERRKQLAGTLSGGeqqMLA-IARALMS--RPKLLLLDEPsegLApkiVE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1699326967 182 DIsfqrkcLETINEFKKKGVTILFVSHNLRDIEKICDRVIWIEN 225
Cdd:cd03224 170 EI------FEAIRELRDEGVTILLVEQNARFALEIADRAYVLER 207
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
45-227 |
2.34e-28 |
|
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: 105.40 E-value: 2.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRvasmlelgggfhpeltgrenirlnatllGLRR 124
Cdd:cd00267 14 ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGK----------------------------DIAK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 125 KELKQRLDKIIEFSELgefidepirvySSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKCLETINEFKKKGVTIL 204
Cdd:cd00267 66 LPLEELRRRIGYVPQL-----------SGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVI 134
|
170 180
....*....|....*....|...
gi 1699326967 205 FVSHNLRDIEKICDRVIWIENHK 227
Cdd:cd00267 135 IVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-225 |
3.57e-27 |
|
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: 104.11 E-value: 3.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 5 IEFKNVTKRYPLyhhigsgikelifnprralsllSGRSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSS 84
Cdd:cd03255 1 IELKNLSKTYGG----------------------GGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTS 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 85 GSVHVVGRVASMLELGG--------------GFH--PELTGRENIRLNATLLGLRRKELKQRLDKIIEFSELGEFIDEPI 148
Cdd:cd03255 59 GEVRVDGTDISKLSEKElaafrrrhigfvfqSFNllPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 149 RVYSSGMLAKLGF--SVITqvDPDILIIDEVLAVGDISFQRKCLETINEF-KKKGVTILFVSHNlRDIEKICDRVIWIEN 225
Cdd:cd03255 139 SELSGGQQQRVAIarALAN--DPKIILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHD-PELAEYADRIIELRD 215
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
45-221 |
6.54e-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: 103.67 E-value: 6.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGR-VASMLE-----LGGG--------FhPELTGR 110
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEdITGLPPheiarLGIGrtfqiprlF-PELTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 111 ENIRLNA------TLLGLR----RKELKQRLDKIIEFSELGEFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLA- 179
Cdd:cd03219 94 ENVMVAAqartgsGLLLARarreEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAg 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1699326967 180 -----VGDIsfqrkcLETINEFKKKGVTILFVSHNLRDIEKICDRVI 221
Cdd:cd03219 174 lnpeeTEEL------AELIRELRERGITVLLVEHDMDVVMSLADRVT 214
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-239 |
8.96e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 104.89 E-value: 8.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 1 MSVA-IEFKNVTKRYplyhhigsGIKelifnprralsllsgrsyLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGV 79
Cdd:PRK13537 3 MSVApIDFRNVEKRY--------GDK------------------LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGL 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 80 MKPSSGSVHVVG-------RVASMlELG-----GGFHPELTGRENIRLNATLLGLRRKELKQRLDKIIEFSELGEFIDEP 147
Cdd:PRK13537 57 THPDAGSISLCGepvpsraRHARQ-RVGvvpqfDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 148 IRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKCLETINEFKKKGVTILFVSHNLRDIEKICDRVIWIENHK 227
Cdd:PRK13537 136 VGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
250
....*....|..
gi 1699326967 228 MKVMGEAHSVIA 239
Cdd:PRK13537 216 KIAEGAPHALIE 227
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
45-225 |
1.81e-26 |
|
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: 102.37 E-value: 1.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGR------VASMLELGGGFHPE-------LTGRE 111
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEditglpPHRIARLGIGYVPEgrrifpsLTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 112 NIRLnATLLGLRRKELKQRLDKIIE-FSELGEFIDEPIRVYSSG---MLAkLGFSVITqvDPDILIIDEV---LA---VG 181
Cdd:COG0410 98 NLLL-GAYARRDRAEVRADLERVYElFPRLKERRRQRAGTLSGGeqqMLA-IGRALMS--RPKLLLLDEPslgLApliVE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1699326967 182 DIsfqrkcLETINEFKKKGVTILFVSHNLRDIEKICDRVIWIEN 225
Cdd:COG0410 174 EI------FEIIRRLNREGVTILLVEQNARFALEIADRAYVLER 211
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
46-176 |
4.39e-26 |
|
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: 99.26 E-value: 4.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 46 IENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRVA------------SMLELGGGFHPELTGRENI 113
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLtdderkslrkeiGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1699326967 114 RLNATLLGLRRKELKQRLDKIIEFSELGEFIDEPIRVY----SSGMLAKLGFSVITQVDPDILIIDE 176
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGERpgtlSGGQRQRVAIARALLTKPKLLLLDE 147
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-221 |
4.10e-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: 103.06 E-value: 4.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 2 SVAIEFKNVTKRYPLYhhigsgikelifnprralsllSGRSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMK 81
Cdd:COG1123 258 EPLLEVRNLSKRYPVR---------------------GKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLR 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 82 PSSGSVHVVGR------VASMLELGGG-----------FHPELTGRENIRLNATLLG-LRRKELKQRLDKIIEFSELG-E 142
Cdd:COG1123 317 PTSGSILFDGKdltklsRRSLRELRRRvqmvfqdpyssLNPRMTVGDIIAEPLRLHGlLSRAERRERVAELLERVGLPpD 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 143 FIDEPIRVYSSG---------MLAklgfsvitqVDPDILIIDEVLAVGDISFQRKCLETINEFKKK-GVTILFVSHNLRD 212
Cdd:COG1123 397 LADRYPHELSGGqrqrvaiarALA---------LEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAV 467
|
....*....
gi 1699326967 213 IEKICDRVI 221
Cdd:COG1123 468 VRYIADRVA 476
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-220 |
6.19e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 102.40 E-value: 6.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 1 MSVAIEFKNVTKRYPlyhhigsgikelifnPRRALSllsgrsylaieNISFQVKKGESVALIGRNGAGKSTSLGLVAGVM 80
Cdd:COG1129 1 AEPLLEMRGISKSFG---------------GVKALD-----------GVSLELRPGEVHALLGENGAGKSTLMKILSGVY 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 81 KPSSGSVHVVGRVASM------LELGGGF-H------PELTGRENIRLNATLLG---LRRKELKQRLDKIIEfsELGEFI 144
Cdd:COG1129 55 QPDSGEILLDGEPVRFrsprdaQAAGIAIiHqelnlvPNLSVAENIFLGREPRRgglIDWRAMRRRARELLA--RLGLDI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 145 D--EPIRVYSSGM-----LAKlgfsVITQvDPDILIIDE---VLAVGDIsfqRKCLETINEFKKKGVTILFVSHNLRDIE 214
Cdd:COG1129 133 DpdTPVGDLSVAQqqlveIAR----ALSR-DARVLILDEptaSLTEREV---ERLFRIIRRLKAQGVAIIYISHRLDEVF 204
|
....*.
gi 1699326967 215 KICDRV 220
Cdd:COG1129 205 EIADRV 210
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-221 |
1.47e-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: 97.16 E-value: 1.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 5 IEFKNVTKRYPLyhhigsgikelifnprralsllSGRSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSS 84
Cdd:cd03293 1 LEVRNVSKTYGG----------------------GGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTS 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 85 GSVHVVGRVASMLELGGGF-------HPELTGRENIRLNATLLGLRRKELKQRLDKIIEFSELGEFIDEPIRVYSSGM-- 155
Cdd:cd03293 59 GEVLVDGEPVTGPGPDRGYvfqqdalLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMrq 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1699326967 156 -------LAklgfsvitqVDPDILIIDEVLAVGDiSFQRKCL--ETINEFKKKGVTILFVSHNLRdiEKI--CDRVI 221
Cdd:cd03293 139 rvalaraLA---------VDPDVLLLDEPFSALD-ALTREQLqeELLDIWRETGKTVLLVTHDID--EAVflADRVV 203
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-221 |
5.53e-24 |
|
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: 95.65 E-value: 5.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 5 IEFKNVTKRYPLYhhigsgikelifnprralsllsGRSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSS 84
Cdd:cd03257 2 LEVKNLSVSFPTG----------------------GGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTS 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 85 GSV-----HVVGRVASMLELGGG------------FHPELTGRENIRLNATLLGLRRKELKQRLDKIIEFSELG---EFI 144
Cdd:cd03257 60 GSIifdgkDLLKLSRRLRKIRRKeiqmvfqdpmssLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGlpeEVL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1699326967 145 DEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKCLETINEFKKK-GVTILFVSHNLRDIEKICDRVI 221
Cdd:cd03257 140 NRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVA 217
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-221 |
8.90e-24 |
|
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: 8.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 5 IEFKNVTKRYPlyhhigsGIKelifnprralsllsgrsylAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSS 84
Cdd:cd03216 1 LELRGITKRFG-------GVK-------------------ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDS 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 85 GSVHVVGRVAS------MLELGGGFHPELTGREnirlnatllglrrkelKQRLdkiiefselgefidEPIRVYSSgmlak 158
Cdd:cd03216 55 GEILVDGKEVSfasprdARRAGIAMVYQLSVGE----------------RQMV--------------EIARALAR----- 99
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1699326967 159 lgfsvitqvDPDILIIDE---VLAVGDIsfqRKCLETINEFKKKGVTILFVSHNLRDIEKICDRVI 221
Cdd:cd03216 100 ---------NARLLILDEptaALTPAEV---ERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVT 153
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
46-228 |
1.11e-23 |
|
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: 93.65 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 46 IENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRvasmlelgggfhpeltgrenirlnaTLLGLRRK 125
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGK-------------------------DLASLSPK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 126 ELKQR---LDKIIEFSELGEFIDEPIRVYSSG-----MLAKlgfsVITQvDPDILIIDEVLAVGDISFQRKCLETINEF- 196
Cdd:cd03214 70 ELARKiayVPQALELLGLAHLADRPFNELSGGerqrvLLAR----ALAQ-EPPILLLDEPTSHLDIAHQIELLELLRRLa 144
|
170 180 190
....*....|....*....|....*....|..
gi 1699326967 197 KKKGVTILFVSHNLRDIEKICDRVIWIENHKM 228
Cdd:cd03214 145 RERGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-240 |
3.59e-23 |
|
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: 93.80 E-value: 3.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 5 IEFKNVTKRYPLyhhigsgikelifnprralsllSGRSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSS 84
Cdd:cd03258 2 IELKNVSKVFGD----------------------TGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTS 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 85 GSVHVVGRvaSMLELGG---------------GFH--PELTGRENIRLNATLLGLRRKELKQRLDKIIEFSELGEFIDEP 147
Cdd:cd03258 60 GSVLVDGT--DLTLLSGkelrkarrrigmifqHFNllSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 148 IRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKCLETINEFKKK-GVTILFVSHNLRDIEKICDRVIWIENH 226
Cdd:cd03258 138 PAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKG 217
|
250
....*....|....
gi 1699326967 227 KMKVMGEAHSVIAQ 240
Cdd:cd03258 218 EVVEEGTVEEVFAN 231
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-220 |
4.64e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 97.02 E-value: 4.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 1 MSVAIEFKNVTKRYPlyhhigsgikelifnprralsllsgrSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVM 80
Cdd:COG3845 2 MPPALELRGITKRFG--------------------------GVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLY 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 81 KPSSGSVHVVGRVASM------LELGGGF---H----PELTGRENIRL---NATLLGLRRKELKQRLDKIIEfsELGEFI 144
Cdd:COG3845 56 QPDSGEILIDGKPVRIrsprdaIALGIGMvhqHfmlvPNLTVAENIVLglePTKGGRLDRKAARARIRELSE--RYGLDV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 145 DEPIRVY--SSGM---------LAKlgfsvitqvDPDILIIDE---VLAVGDIsfqRKCLETINEFKKKGVTILFVSHNL 210
Cdd:COG3845 134 DPDAKVEdlSVGEqqrveilkaLYR---------GARILILDEptaVLTPQEA---DELFEILRRLAAEGKSIIFITHKL 201
|
250
....*....|
gi 1699326967 211 RDIEKICDRV 220
Cdd:COG3845 202 REVMAIADRV 211
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
45-221 |
1.39e-22 |
|
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: 91.81 E-value: 1.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRVA----------SMLELGGGFHPELTGRENIR 114
Cdd:cd03259 15 ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVtgvpperrniGMVFQDYALFPHLTVAENIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 115 LNATLLGLRRKELKQRLDKIIEFSELGEFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKCLETIN 194
Cdd:cd03259 95 FGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELK 174
|
170 180
....*....|....*....|....*...
gi 1699326967 195 E-FKKKGVTILFVSHNLRDIEKICDRVI 221
Cdd:cd03259 175 ElQRELGITTIYVTHDQEEALALADRIA 202
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
45-239 |
2.00e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 92.74 E-value: 2.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVG-------RVASMLELGGGF--HPE--LTGR--- 110
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtgdfsKLQGIRKLVGIVfqNPEtqFVGRtve 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 111 ENIRLNATLLGLRRKELKQRLDKIIEFSELGEFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKCL 190
Cdd:PRK13644 97 EDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1699326967 191 ETINEFKKKGVTILFVSHNLRDIEkICDRVIWIENHKMKVMGEAHSVIA 239
Cdd:PRK13644 177 ERIKKLHEKGKTIVYITHNLEELH-DADRIIVMDRGKIVLEGEPENVLS 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-240 |
2.02e-22 |
|
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: 95.36 E-value: 2.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 1 MSVAIEFKNVTKRYPlyhhigsgikelifnprralsllsGRSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVM 80
Cdd:COG1123 1 MTPLLEVRDLSVRYP------------------------GGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLL 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 81 KPS---SGSVHVVGRV---ASMLELGGG-----------FHPeLTGRENIRLNATLLGLRRKELKQRLDKIIEFSELGEF 143
Cdd:COG1123 57 PHGgriSGEVLLDGRDlleLSEALRGRRigmvfqdpmtqLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 144 IDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKCLETINEFKKK-GVTILFVSHNLRDIEKICDRVIW 222
Cdd:COG1123 136 LDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVV 215
|
250
....*....|....*...
gi 1699326967 223 IENHKMKVMGEAHSVIAQ 240
Cdd:COG1123 216 MDDGRIVEDGPPEEILAA 233
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
46-238 |
3.79e-22 |
|
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: 91.64 E-value: 3.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 46 IENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGR---------VASML-----ELGGGFHpeLTGRE 111
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRdlaslsrreLARRIayvpqEPPAPFG--LTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 112 NIRLNAT----LLGLRRKELKQRLDKIIEFSELGEFIDEPIRVYSSG-----MLAKlgfsVITQvDPDILIIDEVLAVGD 182
Cdd:COG1120 95 LVALGRYphlgLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGerqrvLIAR----ALAQ-EPPLLLLDEPTSHLD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1699326967 183 ISFQRKCLETINEF-KKKGVTILFVSHNLRDIEKICDRVIWIENHKMKVMGEAHSVI 238
Cdd:COG1120 170 LAHQLEVLELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
44-176 |
4.72e-22 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 94.42 E-value: 4.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 44 LAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVG--------------RVASMLE-LGGGFHPELT 108
Cdd:NF033858 15 VALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGgdmadarhrravcpRIAYMPQgLGKNLYPTLS 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 109 GRENIRLNATLLGLRRKELKQRLDKIIEFSELGEFIDEPIRVYSSGMLAKLGF--SVITqvDPDILIIDE 176
Cdd:NF033858 95 VFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLccALIH--DPDLLILDE 162
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
45-221 |
7.39e-22 |
|
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: 90.87 E-value: 7.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGR---------VASM--------LELgggFhPEL 107
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRditglpphrIARLgiartfqnPRL---F-PEL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 108 TGRENIRL----------NATLLGLRR-----KELKQRLDKIIEFSELGEFIDEPIRVYSSGMLAKLGFSVITQVDPDIL 172
Cdd:COG0411 95 TVLENVLVaaharlgrglLAALLRLPRarreeREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1699326967 173 IIDEVLA------VGDIsfqrkcLETINEFKKK-GVTILFVSHNLRDIEKICDRVI 221
Cdd:COG0411 175 LLDEPAAglnpeeTEEL------AELIRRLRDErGITILLIEHDMDLVMGLADRIV 224
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-225 |
9.10e-22 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 90.25 E-value: 9.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 4 AIEFKNVTKRYPLYHHigsgikelifnPRRALSllsgrsylaieNISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPS 83
Cdd:COG1124 1 MLEVRNLSVSYGQGGR-----------RVPVLK-----------DVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPW 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 84 SGSVHVVGRVASMLELG--------------GGFHPELTGREniRLNATLLGLRRKELKQRLDKIIEFSELG-EFIDE-P 147
Cdd:COG1124 59 SGEVTFDGRPVTRRRRKafrrrvqmvfqdpyASLHPRHTVDR--ILAEPLRIHGLPDREERIAELLEQVGLPpSFLDRyP 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1699326967 148 IRVySSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKCLETINEFKKK-GVTILFVSHNLRDIEKICDRVIWIEN 225
Cdd:COG1124 137 HQL-SGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQN 214
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-232 |
1.14e-21 |
|
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: 89.17 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 5 IEFKNVTKRYPlyhhigsgikelifnPRRALSllsgrsylaieNISFQVKKGESvALIGRNGAGKSTSLGLVAGVMKPSS 84
Cdd:cd03264 1 LQLENLTKRYG---------------KKRALD-----------GVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSS 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 85 GSVHVVGR--VASMLELGG---------GFHPELTGRENIRLNATLLGLRRKELKQRLDKIIEFSELGEFIDEPIRVYSS 153
Cdd:cd03264 54 GTIRIDGQdvLKQPQKLRRrigylpqefGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 154 GMLAKLGfsvITQV---DPDILIIDEVLAVGD----ISFqRKCLETINEfkkkGVTILFVSHNLRDIEKICDRVIWIENH 226
Cdd:cd03264 134 GMRRRVG---IAQAlvgDPSILIVDEPTAGLDpeerIRF-RNLLSELGE----DRIVILSTHIVEDVESLCNQVAVLNKG 205
|
....*.
gi 1699326967 227 KMKVMG 232
Cdd:cd03264 206 KLVFEG 211
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-238 |
2.93e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 90.66 E-value: 2.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 2 SVAIEFKNVTKRYplyhhigsgikelifnprralsllsgRSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMK 81
Cdd:PRK13536 39 TVAIDLAGVSKSY--------------------------GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 82 PSSGSVHVVG-------RVASMlELG-----GGFHPELTGRENIRLNATLLGLRRKELKQRLDKIIEFSELGEFIDEPIR 149
Cdd:PRK13536 93 PDAGKITVLGvpvparaRLARA-RIGvvpqfDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 150 VYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKCLETINEFKKKGVTILFVSHNLRDIEKICDRVIWIENHKMK 229
Cdd:PRK13536 172 DLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKI 251
|
....*....
gi 1699326967 230 VMGEAHSVI 238
Cdd:PRK13536 252 AEGRPHALI 260
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
48-225 |
7.07e-21 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 87.50 E-value: 7.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 48 NISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVG----------RVASMLelgggFH-----PELTGREN 112
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGqdltalppaeRPVSML-----FQennlfPHLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 113 IrlnatLLGLR-----RKELKQRLDKIIEFSELGEFIDEPIRVYSSG-----MLAKlgfsVITQVDPdILIIDEVLAVGD 182
Cdd:COG3840 92 I-----GLGLRpglklTAEQRAQVEQALERVGLAGLLDRLPGQLSGGqrqrvALAR----CLVRKRP-ILLLDEPFSALD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1699326967 183 ISFQRKCLETINEF-KKKGVTILFVSHNLRDIEKICDRVIWIEN 225
Cdd:COG3840 162 PALRQEMLDLVDELcRERGLTVLMVTHDPEDAARIADRVLLVAD 205
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
46-229 |
2.00e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.35 E-value: 2.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 46 IENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVhvvgRVASMLELG------GGFHPELTGRENIRLNATl 119
Cdd:COG0488 331 LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV----KLGETVKIGyfdqhqEELDPDKTVLDELRDGAP- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 120 lGLRRKELKQRLDKIIeFSelGEFIDEPIRVYSSG-----MLAKLGFSvitqvDPDILIIDE-----------VLavgdi 183
Cdd:COG0488 406 -GGTEQEVRGYLGRFL-FS--GDDAFKPVGVLSGGekarlALAKLLLS-----PPNVLLLDEptnhldietleAL----- 471
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1699326967 184 sfqrkcLETINEFkkKGvTILFVSHNlRD-IEKICDRVIWIENHKMK 229
Cdd:COG0488 472 ------EEALDDF--PG-TVLLVSHD-RYfLDRVATRILEFEDGGVR 508
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
5-228 |
2.68e-20 |
|
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: 85.54 E-value: 2.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 5 IEFKNVTKRYPlyhhigsgikelifnprralsllsgRSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSS 84
Cdd:cd03292 1 IEFINVTKTYP-------------------------NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTS 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 85 GSVHVVGRVASML----------ELGGGFH-----PELTGRENIRLNATLLGLRRKELKQRLDKIIEFSELGEFIDEPIR 149
Cdd:cd03292 56 GTIRVNGQDVSDLrgraipylrrKIGVVFQdfrllPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPA 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1699326967 150 VYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKCLETINEFKKKGVTILFVSHNLRDIEKICDRVIWIENHKM 228
Cdd:cd03292 136 ELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
46-213 |
4.52e-20 |
|
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: 85.91 E-value: 4.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 46 IENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSG-SVHVVGR---------------VASMlELGGGFHPELTG 109
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGErrggedvwelrkrigLVSP-ALQLRFPRDETV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 110 RENIR--LNATlLGLRRK---ELKQRLDKIIEFSELGEFIDEPIRVYSSG-----MLAKlgfSVITqvDPDILIIDEVLA 179
Cdd:COG1119 98 LDVVLsgFFDS-IGLYREptdEQRERARELLELLGLAHLADRPFGTLSQGeqrrvLIAR---ALVK--DPELLILDEPTA 171
|
170 180 190
....*....|....*....|....*....|....*
gi 1699326967 180 VGDISFQRKCLETINEF-KKKGVTILFVSHNLRDI 213
Cdd:COG1119 172 GLDLGARELLLALLDKLaAEGAPTLVLVTHHVEEI 206
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-232 |
1.09e-19 |
|
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: 84.66 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 5 IEFKNVTKRYplyhhiGSGIKelifnprralsllsgrsylAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSS 84
Cdd:cd03295 1 IEFENVTKRY------GGGKK-------------------AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTS 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 85 GSVHVVGRvaSMLELGG--------------GFHPELTGRENIRLNATLLGLRRKELKQRLDKIIEFSEL--GEFIDEPI 148
Cdd:cd03295 56 GEIFIDGE--DIREQDPvelrrkigyviqqiGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 149 RVYSSGMLAKLGFSVITQVDPDILIIDEVL-AVGDISfqRKCLEtiNEFKK----KGVTILFVSHNLRDIEKICDRVIWI 223
Cdd:cd03295 134 HELSGGQQQRVGVARALAADPPLLLMDEPFgALDPIT--RDQLQ--EEFKRlqqeLGKTIVFVTHDIDEAFRLADRIAIM 209
|
....*....
gi 1699326967 224 ENHKMKVMG 232
Cdd:cd03295 210 KNGEIVQVG 218
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-240 |
1.18e-19 |
|
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: 87.58 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 4 AIEFKNVTKRYPlyhhigsgikelifnprralsllsGRSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPS 83
Cdd:COG2274 473 DIELENVSFRYP------------------------GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPT 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 84 SGSVHVVGRVASMLELGG-----GF---HPEL---TGRENIRLNATLLGLrrkelkQRLDKIIEFSELGEFIDE-Pirvy 151
Cdd:COG2274 529 SGRILIDGIDLRQIDPASlrrqiGVvlqDVFLfsgTIRENITLGDPDATD------EEIIEAARLAGLHDFIEAlP---- 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 152 sSGMLAKLG-----FS------------VITqvDPDILIIDEVLAVGDISFQRKCLETINEFkKKGVTILFVSHNLRDIe 214
Cdd:COG2274 599 -MGYDTVVGeggsnLSggqrqrlaiaraLLR--NPRILILDEATSALDAETEAIILENLRRL-LKGRTVIIIAHRLSTI- 673
|
250 260
....*....|....*....|....*.
gi 1699326967 215 KICDRVIWIENHKMKVMGEAHSVIAQ 240
Cdd:COG2274 674 RLADRIIVLDKGRIVEDGTHEELLAR 699
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
46-220 |
1.48e-19 |
|
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: 84.13 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 46 IENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRVASMLE------LGGGFHP-------ELTGREN 112
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPmhkrarLGIGYLPqeasifrKLTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 113 IRLNATLLGLRRKELKQRLDKIIEFSELGEFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDE------VLAVGDISfq 186
Cdd:cd03218 96 ILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEpfagvdPIAVQDIQ-- 173
|
170 180 190
....*....|....*....|....*....|....
gi 1699326967 187 rkclETINEFKKKGVTILFVSHNLRDIEKICDRV 220
Cdd:cd03218 174 ----KIIKILKDRGIGVLITDHNVRETLSITDRA 203
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
40-232 |
2.42e-19 |
|
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: 82.36 E-value: 2.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 40 GRSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVhvvgrvasmleLGGGFHPeltgrenirlnATL 119
Cdd:cd03247 12 EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI-----------TLDGVPV-----------SDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 120 LGLRRKELKQRLDKIIEFSE-LGEFIDEPirvYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKCLETINEFkK 198
Cdd:cd03247 70 EKALSSLISVLNQRPYLFDTtLRNNLGRR---FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEV-L 145
|
170 180 190
....*....|....*....|....*....|....
gi 1699326967 199 KGVTILFVSHNLRDIEKIcDRVIWIENHKMKVMG 232
Cdd:cd03247 146 KDKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
5-231 |
9.87e-19 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 83.62 E-value: 9.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 5 IEFKNVTKRYplyhhigsgikelifnprralsllsGRSYLaIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSS 84
Cdd:PRK11432 7 VVLKNITKRF-------------------------GSNTV-IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTE 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 85 GSVHVVG----------RVASMLELGGGFHPELTGRENIRLNATLLGLRRKELKQRLDKIIEFSELGEFIDEPIRVYSSG 154
Cdd:PRK11432 61 GQIFIDGedvthrsiqqRDICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1699326967 155 MLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKCLETINEFKKK-GVTILFVSHNLRDIEKICDRVIWIenHKMKVM 231
Cdd:PRK11432 141 QQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVM--NKGKIM 216
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
50-232 |
2.23e-18 |
|
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: 80.61 E-value: 2.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 50 SFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVG----------RVASMLELGGGFHPELTGRENIRLnATL 119
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvdvtaappadRPVSMLFQENNLFAHLTVEQNVGL-GLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 120 LGLR-RKELKQRLDKIIEFSELGEFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKCLETINEF-K 197
Cdd:cd03298 97 PGLKlTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLhA 176
|
170 180 190
....*....|....*....|....*....|....*
gi 1699326967 198 KKGVTILFVSHNLRDIEKICDRVIWIENHKMKVMG 232
Cdd:cd03298 177 ETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-228 |
3.23e-18 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 80.10 E-value: 3.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 5 IEFKNVTKRYPlyhhigsgikelifNPRRALSllsgrsylaieNISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSS 84
Cdd:COG2884 2 IRFENVSKRYP--------------GGREALS-----------DVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTS 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 85 GSVHVVGR-VASM---------LELG-----GGFHPELTGRENIRLNATLLGLRRKELKQRLDKIIEFSELGEFIDEPIR 149
Cdd:COG2884 57 GQVLVNGQdLSRLkrreipylrRRIGvvfqdFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPH 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 150 VYSSG-----MLAKlgfSVITqvDPDILIIDEVLA------VGDIsfqrkcLETINEFKKKGVTILFVSHNLRDIEKICD 218
Cdd:COG2884 137 ELSGGeqqrvAIAR---ALVN--RPELLLADEPTGnldpetSWEI------MELLEEINRRGTTVLIATHDLELVDRMPK 205
|
250
....*....|
gi 1699326967 219 RVIWIENHKM 228
Cdd:COG2884 206 RVLELEDGRL 215
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
39-243 |
4.34e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 80.90 E-value: 4.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 39 SGRSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGR-------------------------- 92
Cdd:PRK13633 19 ESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLdtsdeenlwdirnkagmvfqnpdnqi 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 93 VASMLELGGGFHPeltgrENirlnatlLGLRRKELKQRLDKIIEFSELGEFIDEPIRVYSSGMLAKLGFSVITQVDPDIL 172
Cdd:PRK13633 99 VATIVEEDVAFGP-----EN-------LGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECI 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1699326967 173 IIDEVLAVGDISFQRKCLETINEFKKK-GVTILFVSHNLRDIEKiCDRVIWIENHKMKVMGEAHSVIAQYKE 243
Cdd:PRK13633 167 IFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKEVEM 237
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
45-244 |
8.77e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 80.48 E-value: 8.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVG-----RVASMLEL----GGGF-HPEL-----TG 109
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdKKVKLSDIrkkvGLVFqYPEYqlfeeTI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 110 RENIRLNATLLGLRRKELKQRLDKIIEFSELG--EFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQR 187
Cdd:PRK13637 102 EKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1699326967 188 KCLETINEF-KKKGVTILFVSHNLRDIEKICDRVIWIENHKMKVMGEAHSViaqYKEA 244
Cdd:PRK13637 182 EILNKIKELhKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV---FKEV 236
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
33-221 |
1.40e-17 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 79.35 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 33 RALSLLSGRSYLAI-ENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRVASMLELG----------- 100
Cdd:PRK10419 14 AHGGLSGKHQHQTVlNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAqrkafrrdiqm 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 101 ------GGFHPELTGRENIRLNAT-LLGLRRKELKQRLDKIIEFSELG-EFIDEPIRVYSSGMLAKLGFSVITQVDPDIL 172
Cdd:PRK10419 94 vfqdsiSAVNPRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1699326967 173 IIDEVLAVGDISFQRKCLETINEFKKK-GVTILFVSHNLRDIEKICDRVI 221
Cdd:PRK10419 174 ILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVM 223
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
45-225 |
2.12e-17 |
|
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: 77.23 E-value: 2.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRVASMLELG--------------GGFHPELTGR 110
Cdd:cd03229 15 VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElpplrrrigmvfqdFALFPHLTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 111 ENIRlnatlLGLrrkelkqrldkiiefselgefidepirvySSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKCL 190
Cdd:cd03229 95 ENIA-----LGL-----------------------------SGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVR 140
|
170 180 190
....*....|....*....|....*....|....*.
gi 1699326967 191 ETINEFKKK-GVTILFVSHNLRDIEKICDRVIWIEN 225
Cdd:cd03229 141 ALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-227 |
2.52e-17 |
|
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: 75.95 E-value: 2.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 5 IEFKNVTKRYPlyhhigsgiKELIFNprralsllsgrsylaieNISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSS 84
Cdd:cd03221 1 IELENLSKTYG---------GKLLLK-----------------DISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDE 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 85 GSVHV--VGRVASMLELGGGfhpeltgrENIRLnatllglrrkelkqrldkiiefselgefidepirvyssgMLAKLGFS 162
Cdd:cd03221 55 GIVTWgsTVKIGYFEQLSGG--------EKMRL---------------------------------------ALAKLLLE 87
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1699326967 163 vitqvDPDILIIDEVLAVGDISFQRKCLETINEFKKkgvTILFVSHNLRDIEKICDRVIWIENHK 227
Cdd:cd03221 88 -----NPNLLLLDEPTNHLDLESIEALEEALKEYPG---TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-230 |
5.92e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 79.34 E-value: 5.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 7 FKNVTKRYplyhhigsGIKELIfnprralsllsgrsylaiENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGS 86
Cdd:COG0488 1 LENLSKSF--------GGRPLL------------------DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGE 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 87 VHVVG--RVAsMLELGGGFHPELTGRENIrlnatLLGLRR-KELKQRLDKI-----------IEFSELGEFIDE------ 146
Cdd:COG0488 55 VSIPKglRIG-YLPQEPPLDDDLTVLDTV-----LDGDAElRALEAELEELeaklaepdedlERLAELQEEFEAlggwea 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 147 --------------------PIRVYSSGM-----LAKLGFSvitqvDPDILIIDEV---LavgDIsfqrkclETI----N 194
Cdd:COG0488 129 earaeeilsglgfpeedldrPVSELSGGWrrrvaLARALLS-----EPDLLLLDEPtnhL---DL-------ESIewleE 193
|
250 260 270
....*....|....*....|....*....|....*..
gi 1699326967 195 EFKKKGVTILFVSHNlRD-IEKICDRVIWIENHKMKV 230
Cdd:COG0488 194 FLKNYPGTVLVVSHD-RYfLDRVATRILELDRGKLTL 229
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-240 |
6.08e-17 |
|
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: 79.42 E-value: 6.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 2 SVAIEFKNVTKRYPlyhhigsgikelifnPRRAlsllsgrsylAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMK 81
Cdd:COG4988 334 PPSIELEDVSFSYP---------------GGRP----------ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLP 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 82 PSSGSVHVVGRVASMLELGG--------GFHPEL---TGRENIRL---NATllglrrkelKQRLDKIIEFSELGEFIDEp 147
Cdd:COG4988 389 PYSGSILINGVDLSDLDPASwrrqiawvPQNPYLfagTIRENLRLgrpDAS---------DEELEAALEAAGLDEFVAA- 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 148 irvYSSGMLAKLG-----FSV-------ITQV---DPDILIIDEVLAVGDISFQRKCLETINEFkKKGVTILFVSHNLRD 212
Cdd:COG4988 459 ---LPDGLDTPLGeggrgLSGgqaqrlaLARAllrDAPLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHRLAL 534
|
250 260
....*....|....*....|....*...
gi 1699326967 213 IeKICDRVIWIENHKMKVMGEAHSVIAQ 240
Cdd:COG4988 535 L-AQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
44-221 |
1.46e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 76.98 E-value: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 44 LAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRVAS-------MLELGGGF-HPE-----LTGR 110
Cdd:PRK13635 21 YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSeetvwdvRRQVGMVFqNPDnqfvgATVQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 111 ENIRLNATLLGLRRKELKQRLDKIIEFSELGEFID-EPIRVySSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKC 189
Cdd:PRK13635 101 DDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNrEPHRL-SGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREV 179
|
170 180 190
....*....|....*....|....*....|...
gi 1699326967 190 LETINEFK-KKGVTILFVSHNLRDIEKiCDRVI 221
Cdd:PRK13635 180 LETVRQLKeQKGITVLSITHDLDEAAQ-ADRVI 211
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
46-221 |
1.51e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 76.35 E-value: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 46 IENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGR-VASM--LELGG-----------GFhPeLTGRE 111
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRpLADWspAELARrravlpqhsslSF-P-FTVEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 112 NIRLNATLLGLRRKELKQRLDKIIEFSELGEFIDEPIRVYSSG-----MLAKlgfsVITQV-----DPDILIIDEVLAVG 181
Cdd:PRK13548 96 VVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGeqqrvQLAR----VLAQLwepdgPPRWLLLDEPTSAL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1699326967 182 DISFQRKCLETINEF-KKKGVTILFVSHNLRDIEKICDRVI 221
Cdd:PRK13548 172 DLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIV 212
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-240 |
1.63e-16 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 77.43 E-value: 1.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 5 IEFKNVTKRYPLyhhigsgikelifnprralsllSGRSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSS 84
Cdd:COG1135 2 IELENLSKTFPT----------------------KGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTS 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 85 GSVHVVGRVasMLELGGG------------F-HPEL----TGRENIRLNATLLGLRRKELKQRLDKIIEFSELGEFIDep 147
Cdd:COG1135 60 GSVLVDGVD--LTALSERelraarrkigmiFqHFNLlssrTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKAD-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 148 irVY----SSGM---------LAklgfsvitqVDPDILIIDE------------VLAVgdisfqrkcLETINefKKKGVT 202
Cdd:COG1135 136 --AYpsqlSGGQkqrvgiaraLA---------NNPKVLLCDEatsaldpettrsILDL---------LKDIN--RELGLT 193
|
250 260 270
....*....|....*....|....*....|....*...
gi 1699326967 203 ILFVSHNLRDIEKICDRVIWIENHKMKVMGEAHSVIAQ 240
Cdd:COG1135 194 IVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFAN 231
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
48-224 |
2.35e-16 |
|
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: 75.02 E-value: 2.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 48 NISFQVKkGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRV---------ASMLELGGGF-------HPELTGRE 111
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkinLPPQQRKIGLvfqqyalFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 112 NIRLNatLLGLRRKELKQRLDKIIEFSELGEFIDEPIRVYSSGMLAK--LGFSVITQvdPDILIIDEVLAVGDISFQRKC 189
Cdd:cd03297 95 NLAFG--LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRvaLARALAAQ--PELLLLDEPFSALDRALRLQL 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 1699326967 190 LETINEFKKK-GVTILFVSHNLRDIEKICDRVIWIE 224
Cdd:cd03297 171 LPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVME 206
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-225 |
2.76e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 75.93 E-value: 2.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 1 MSVAIEFKNVTKRYPlyhhigSGIKelifnprralsllsgrsylAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVM 80
Cdd:PRK13647 1 MDNIIEVEDLHFRYK------DGTK-------------------ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIY 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 81 KPSSGSVHVVGRVASML-------ELGGGFH-PE-----LTGRENIRLNATLLGLRRKELKQRLDKIIEFSELGEFIDEP 147
Cdd:PRK13647 56 LPQRGRVKVMGREVNAEnekwvrsKVGLVFQdPDdqvfsSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKP 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1699326967 148 IRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKCLETINEFKKKGVTILFVSHNLRDIEKICDRVIWIEN 225
Cdd:PRK13647 136 PYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKE 213
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-232 |
3.21e-16 |
|
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: 75.02 E-value: 3.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 1 MSVAIEFKNVTKRyplyhhigsgikeliFNPRRALsllsgrsylaiENISFQVKKGESVALIGRNGAGKSTSLGLVAGVM 80
Cdd:COG1127 2 SEPMIEVRNLTKS---------------FGDRVVL-----------DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLL 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 81 KPSSGSVHVVGR-VASM-----LEL---------GGGFHPELTGRENIrlnatLLGLR------RKELKQRLDKIIEFSE 139
Cdd:COG1127 56 RPDSGEILVDGQdITGLsekelYELrrrigmlfqGGALFDSLTVFENV-----AFPLRehtdlsEAEIRELVLEKLELVG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 140 LGEFIDEpirvY----SSGM-----LAKlgfSVITqvDPDILIIDEV------LAVGDISfqrkclETINEFKKK-GVTI 203
Cdd:COG1127 131 LPGAADK----MpselSGGMrkrvaLAR---ALAL--DPEILLYDEPtagldpITSAVID------ELIRELRDElGLTS 195
|
250 260
....*....|....*....|....*....
gi 1699326967 204 LFVSHNLRDIEKICDRVIWIENHKMKVMG 232
Cdd:COG1127 196 VVVTHDLDSAFAIADRVAVLADGKIIAEG 224
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
40-229 |
3.49e-16 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 74.22 E-value: 3.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 40 GRSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRVAS-----------MLELGGGFHPElT 108
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKakerrksigyvMQDVDYQLFTD-S 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 109 GRENIRLNATLLGLRRKELKQRLDKIiefsELGEFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRK 188
Cdd:cd03226 89 VREELLLGLKELDAGNEQAETVLKDL----DLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMER 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1699326967 189 CLETINEFKKKGVTILFVSHNLRDIEKICDRVIWIENHKMK 229
Cdd:cd03226 165 VGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-220 |
4.04e-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: 74.21 E-value: 4.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 5 IEFKNVTKRYPlyhhigsgikelifnprralsllsgrSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSS 84
Cdd:cd03301 1 VELENVTKRFG--------------------------NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTS 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 85 GSVHVVGRVASMLE-----LGGGF-----HPELTGRENIRLNATLLGLRRKELKQRLDKIIEFSELGEFIDEPIRVYSSG 154
Cdd:cd03301 55 GRIYIGGRDVTDLPpkdrdIAMVFqnyalYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGG 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1699326967 155 MLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKCLETINEFKKK-GVTILFVSHNLRDIEKICDRV 220
Cdd:cd03301 135 QRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRI 201
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
20-232 |
4.14e-16 |
|
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: 77.36 E-value: 4.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 20 IGSGIKELIFNPRRALSLLSGRSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRVA----S 95
Cdd:TIGR01257 1929 ISGGNKTDILRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIltniS 2008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 96 MLELGGGFHPE-------LTGRENIRLNATLLGLRRKELKQRLDKIIEFSELGEFIDEPIRVYSSGMLAKLGFSVITQVD 168
Cdd:TIGR01257 2009 DVHQNMGYCPQfdaiddlLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGC 2088
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1699326967 169 PDILIIDEVLAVGDISFQRKCLETINEFKKKGVTILFVSHNLRDIEKICDRVIWIENHKMKVMG 232
Cdd:TIGR01257 2089 PPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLG 2152
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
4-228 |
4.48e-16 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 74.55 E-value: 4.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 4 AIEFKNVTKRYPlyhhigsgikelifnprralsllsGRSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPS 83
Cdd:cd03245 2 RIEFRNVSFSYP------------------------NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPT 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 84 SGSVHVVGRVASMLEL-----GGGF---HPEL---TGRENIRLNATLLGlrrkelKQRLDKIIEFSELGEFIDEPIRVYS 152
Cdd:cd03245 58 SGSVLLDGTDIRQLDPadlrrNIGYvpqDVTLfygTLRDNITLGAPLAD------DERILRAAELAGVTDFVNKHPNGLD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 153 SgMLAKLGFSV---------ITQV---DPDILIIDEVLAVGDISFQRKCLETINEFkKKGVTILFVSHNLRdIEKICDRV 220
Cdd:cd03245 132 L-QIGERGRGLsggqrqavaLARAllnDPPILLLDEPTSAMDMNSEERLKERLRQL-LGDKTLIIITHRPS-LLDLVDRI 208
|
....*...
gi 1699326967 221 IWIENHKM 228
Cdd:cd03245 209 IVMDSGRI 216
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-220 |
4.97e-16 |
|
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: 74.58 E-value: 4.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 5 IEFKNVTKRYPlyhhigsgikelifnprralsllsgrSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSS 84
Cdd:cd03300 1 IELENVSKFYG--------------------------GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTS 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 85 GSVHVVGRvaSMLELGG------------GFHPELTGRENIRLNATLLGLRRKELKQRLDKIIEFSELGEFIDEPIRVYS 152
Cdd:cd03300 55 GEILLDGK--DITNLPPhkrpvntvfqnyALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLS 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1699326967 153 SGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKCLETINEFKKK-GVTILFVSHNLRDIEKICDRV 220
Cdd:cd03300 133 GGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRI 201
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-225 |
6.61e-16 |
|
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: 72.80 E-value: 6.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 5 IEFKNVTKRYPlyhhigsgikelifnprralsllsGRSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSS 84
Cdd:cd03228 1 IEFKNVSFSYP------------------------GRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTS 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 85 GSVHVVGRVASMLELGggfhpELtgRENI--------RLNATLlglrRKEL-----KQRLdkiiefselgefidepirvy 151
Cdd:cd03228 57 GEILIDGVDLRDLDLE-----SL--RKNIayvpqdpfLFSGTI----RENIlsggqRQRI-------------------- 105
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1699326967 152 ssgMLAK--LGfsvitqvDPDILIIDEVLAVGDISFQRKCLETINEFkKKGVTILFVSHNLRDIEKiCDRVIWIEN 225
Cdd:cd03228 106 ---AIARalLR-------DPPILILDEATSALDPETEALILEALRAL-AKGKTVIVIAHRLSTIRD-ADRIIVLDD 169
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-242 |
7.99e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 74.64 E-value: 7.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 2 SVAIEFKNVTKRYPlyhhigsgikelifnprralsllsGRSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMK 81
Cdd:PRK13632 5 SVMIKVENVSFSYP------------------------NSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLK 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 82 PSSGSVHVVGRVASMLEL-------GGGF-HPE-----LT-------GRENIRLNatllglrRKELKQRLDKIIEFSELG 141
Cdd:PRK13632 61 PQSGEIKIDGITISKENLkeirkkiGIIFqNPDnqfigATveddiafGLENKKVP-------PKKMKDIIDDLAKKVGME 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 142 EFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKCLETINEFKKKGV-TILFVSHNLRDIEKiCDRV 220
Cdd:PRK13632 134 DYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAIL-ADKV 212
|
250 260
....*....|....*....|..
gi 1699326967 221 IwienhkmkVMGEAHsVIAQYK 242
Cdd:PRK13632 213 I--------VFSEGK-LIAQGK 225
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-237 |
1.01e-15 |
|
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: 73.91 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 4 AIEFKNVTKRYPlyhhigsgikelifnprralsllsgrSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPS 83
Cdd:cd03296 2 SIEVRNVSKRFG--------------------------DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPD 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 84 SGSVHVVGRVASML---ELGGGF---H----PELTGRENIRlnatlLGLRRK---------ELKQRLDKIIEFSELGEFI 144
Cdd:cd03296 56 SGTILFGGEDATDVpvqERNVGFvfqHyalfRHMTVFDNVA-----FGLRVKprserppeaEIRAKVHELLKLVQLDWLA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 145 DEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKCLETINEFKKK-GVTILFVSHNLRDIEKICDRVIWI 223
Cdd:cd03296 131 DRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVM 210
|
250
....*....|....
gi 1699326967 224 ENHKMKVMGEAHSV 237
Cdd:cd03296 211 NKGRIEQVGTPDEV 224
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-221 |
1.06e-15 |
|
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: 73.76 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 5 IEFKNVTKRYPlyhhigsgikelifNPRRALsllsgrsylaiENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSS 84
Cdd:cd03256 1 IEVENLSKTYP--------------NGKKAL-----------KDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTS 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 85 GSVHVVG----------------RVAsMLELGGGFHPELTGRENI---RLNA-----TLLGLRRKELKQRLDKIIEFSEL 140
Cdd:cd03256 56 GSVLIDGtdinklkgkalrqlrrQIG-MIFQQFNLIERLSVLENVlsgRLGRrstwrSLFGLFPKEEKQRALAALERVGL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 141 GEFIDEPIRVYSSGMLAKLGFS-VITQvDPDILIIDEVLAVGDISFQRKCLETINEF-KKKGVTILFVSHNLRDIEKICD 218
Cdd:cd03256 135 LDKAYQRADQLSGGQQQRVAIArALMQ-QPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYAD 213
|
...
gi 1699326967 219 RVI 221
Cdd:cd03256 214 RIV 216
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-227 |
1.41e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 74.00 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 1 MSVAIEFKNVTKRYPlyhhigsgikelifnprralsllSGRSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVM 80
Cdd:PRK13650 1 MSNIIEVKNLTFKYK-----------------------EDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLL 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 81 KPSSGSVHVVGR-------------------------VASMLELGGGFhpeltGRENirlnatlLGLRRKELKQRLDKII 135
Cdd:PRK13650 58 EAESGQIIIDGDllteenvwdirhkigmvfqnpdnqfVGATVEDDVAF-----GLEN-------KGIPHEEMKERVNEAL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 136 EFSELGEFID-EPIRVySSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKCLETINEFKKK-GVTILFVSHNLRDI 213
Cdd:PRK13650 126 ELVGMQDFKErEPARL-SGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEV 204
|
250
....*....|....
gi 1699326967 214 eKICDRVIWIENHK 227
Cdd:PRK13650 205 -ALSDRVLVMKNGQ 217
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-220 |
4.15e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 74.18 E-value: 4.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 1 MSVAIEFKNVTKRYPlyhhigsGIKelifnprralsllsgrsylAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVM 80
Cdd:PRK11288 1 SSPYLSFDGIGKTFP-------GVK-------------------ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNY 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 81 KPSSGSVHVVGR------VASMLELGGG-----FH--PELTGRENI---RLNATLLGLRRKELKQRLDKIIEfsELGEFI 144
Cdd:PRK11288 55 QPDAGSILIDGQemrfasTTAALAAGVAiiyqeLHlvPEMTVAENLylgQLPHKGGIVNRRLLNYEAREQLE--HLGVDI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 145 D--EPIRVYSSG--MLAKLGFSVITqvDPDILIIDE---VLAVGDIsfqRKCLETINEFKKKGVTILFVSHNLRDIEKIC 217
Cdd:PRK11288 133 DpdTPLKYLSIGqrQMVEIAKALAR--NARVIAFDEptsSLSAREI---EQLFRVIRELRAEGRVILYVSHRMEEIFALC 207
|
...
gi 1699326967 218 DRV 220
Cdd:PRK11288 208 DAI 210
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
44-217 |
4.16e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 71.52 E-value: 4.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 44 LAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVG------RVASMLEL-----GGGFHPELTGREN 112
Cdd:PRK13540 15 PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERqsikkdLCTYQKQLcfvghRSGINPYLTLREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 113 ----IRLNATLLGlrrkelkqrLDKIIEFSELGEFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRK 188
Cdd:PRK13540 95 clydIHFSPGAVG---------ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLT 165
|
170 180 190
....*....|....*....|....*....|....
gi 1699326967 189 CLETINEFKKKGVTILFVSH-----NLRDIEKIC 217
Cdd:PRK13540 166 IITKIQEHRAKGGAVLLTSHqdlplNKADYEEYH 199
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
45-240 |
4.16e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 72.96 E-value: 4.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGR-----VASMLEL----GGGFH-PE-----LTG 109
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpidysRKGLMKLresvGMVFQdPDnqlfsASV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 110 RENIRLNATLLGLRRKELKQRLDKIIEFSELGEFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKC 189
Cdd:PRK13636 101 YQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEI 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1699326967 190 LETINEFKKK-GVTILFVSHNLRDIEKICDRVIWIENHKMKVMGEAHSVIAQ 240
Cdd:PRK13636 181 MKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
50-223 |
1.12e-14 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 70.77 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 50 SFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVG----------RVASMLELGGGFHPELTGRENI------ 113
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGqdhtttppsrRPVSMLFQENNLFSHLTVAQNIglglnp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 114 --RLNAtllglrrkELKQRLDKIIEFSELGEFIDE-PIRVySSG--MLAKLGFSVITQvDPdILIIDEVLAVGDISFQRK 188
Cdd:PRK10771 99 glKLNA--------AQREKLHAIARQMGIEDLLARlPGQL-SGGqrQRVALARCLVRE-QP-ILLLDEPFSALDPALRQE 167
|
170 180 190
....*....|....*....|....*....|....*.
gi 1699326967 189 CLETINEF-KKKGVTILFVSHNLRDIEKICDRVIWI 223
Cdd:PRK10771 168 MLTLVSQVcQERQLTLLMVSHSLEDAARIAPRSLVV 203
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
46-228 |
1.47e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 71.40 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 46 IENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVG-----------------RVASMLELGGGFHPELT 108
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnknlkklrkKVSLVFQFPEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 109 GRENIRLNATLLGLRRKELKQRLDKIIEFSELGE-FIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQR 187
Cdd:PRK13641 103 VLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRK 182
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1699326967 188 KCLETINEFKKKGVTILFVSHNLRDIEKICDRVIWIENHKM 228
Cdd:PRK13641 183 EMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
49-220 |
1.56e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 72.39 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 49 ISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRVASML------ELG-------GGFHPELTGRENIrl 115
Cdd:PRK15439 30 IDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLtpakahQLGiylvpqePLLFPNLSVKENI-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 116 natLLGL-RRKELKQRLDKIIefSELG------------EFIDEPIRVYSSGMLAklgfsvitqvDPDILIIDEVLAVGD 182
Cdd:PRK15439 108 ---LFGLpKRQASMQKMKQLL--AALGcqldldssagslEVADRQIVEILRGLMR----------DSRILILDEPTASLT 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 1699326967 183 ISFQRKCLETINEFKKKGVTILFVSHNLRDIEKICDRV 220
Cdd:PRK15439 173 PAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRI 210
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
46-225 |
2.02e-14 |
|
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: 68.78 E-value: 2.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 46 IENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRVAS---MLELGG--GFHPE----LTG--RENIr 114
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISqwdPNELGDhvGYLPQddelFSGsiAENI- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 115 lnatLLGLRRkelkQRLdkiiefselgefidepirvyssgMLAKLGFSvitqvDPDILIIDEVLAVGDISFQRKCLETIN 194
Cdd:cd03246 97 ----LSGGQR----QRL-----------------------GLARALYG-----NPRILVLDEPNSHLDVEGERALNQAIA 140
|
170 180 190
....*....|....*....|....*....|.
gi 1699326967 195 EFKKKGVTILFVSHNLRDIEkICDRVIWIEN 225
Cdd:cd03246 141 ALKAAGATRIVIAHRPETLA-SADRILVLED 170
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
45-225 |
2.48e-14 |
|
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: 69.90 E-value: 2.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKSTSLGLVAG-----VMKPSSGSVHVVGRV-----ASMLEL----GGGF-HP---E 106
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDiydldVDVLELrrrvGMVFqKPnpfP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 107 LTGRENIRLNATLLGLRRKElkqRLDKIIEFS-ELGEFIDEpirVYSSgmLAKLGFSVITQ----------VDPDILIID 175
Cdd:cd03260 95 GSIYDNVAYGLRLHGIKLKE---ELDERVEEAlRKAALWDE---VKDR--LHALGLSGGQQqrlclaralaNEPEVLLLD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1699326967 176 EVLAVGDISFQRKCLETINEFKKKgVTILFVSHNLRDIEKICDRVIWIEN 225
Cdd:cd03260 167 EPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLN 215
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
45-227 |
2.64e-14 |
|
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: 69.42 E-value: 2.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRVA-----SMLELGggfhpelTGRENIrlnatL 119
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAyvsqePWIQNG-------TIRENI-----L 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 120 LGLRRKElkQRLDKIIEFSELgefiDEPIRVYSSGMLAKLGFSVIT----Q---------V--DPDILIIDEVLA----- 179
Cdd:cd03250 88 FGKPFDE--ERYEKVIKACAL----EPDLEILPDGDLTEIGEKGINlsggQkqrislaraVysDADIYLLDDPLSavdah 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1699326967 180 VGDISFQrKCletINEFKKKGVTILFVSHNLRDIEKiCDRVIWIENHK 227
Cdd:cd03250 162 VGRHIFE-NC---ILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
42-236 |
3.10e-14 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 69.66 E-value: 3.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 42 SYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGR---------VASMLEL----GGGFH---- 104
Cdd:PRK11124 14 AHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfdfsktpsDKAIRELrrnvGMVFQqynl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 105 -PELTGREN-IRLNATLLGLRRKELKQRLDKIIEFSELGEFIDE-PIRVySSGMLAKLGFSVITQVDPDILIIDEVLAVG 181
Cdd:PRK11124 94 wPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRfPLHL-SGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1699326967 182 DISFQRKCLETINEFKKKGVTILFVSHNLRDIEKICDRVIWIENHKMKVMGEAHS 236
Cdd:PRK11124 173 DPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC 227
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
47-209 |
3.11e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 69.13 E-value: 3.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 47 ENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRVASMLELGGGFH---------PELTGRENIRLNA 117
Cdd:PRK13539 19 SGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHylghrnamkPALTVAENLEFWA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 118 TLLGLRRkelkQRLDKIIEFSELGEFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKCLETINEFK 197
Cdd:PRK13539 99 AFLGGEE----LDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAHL 174
|
170
....*....|..
gi 1699326967 198 KKGVTILFVSHN 209
Cdd:PRK13539 175 AQGGIVIAATHI 186
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
45-221 |
3.16e-14 |
|
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: 70.85 E-value: 3.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKP---SSGSVHVVGRvaSMLELGGG------------------- 102
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGE--DLLKLSEKelrkirgreiqmifqdpmt 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 103 -FHPELT-GR---ENIRLNatlLGLRRKELKQRLDKIIEfsELGefIDEPIRVYSS-------GM---------LAklgf 161
Cdd:COG0444 98 sLNPVMTvGDqiaEPLRIH---GGLSKAEARERAIELLE--RVG--LPDPERRLDRyphelsgGMrqrvmiaraLA---- 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1699326967 162 svitqVDPDILIIDE-VLAVgDISFQRKCLETINEFKKK-GVTILFVSHNLRDIEKICDRVI 221
Cdd:COG0444 167 -----LEPKLLIADEpTTAL-DVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVA 222
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-221 |
4.05e-14 |
|
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: 71.16 E-value: 4.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 2 SVAIEFKNVTKRYPlyhhigsgikelifnprralsllsGRSyLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMK 81
Cdd:TIGR02857 319 ASSLEFSGVSVAYP------------------------GRR-PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVD 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 82 PSSGSVHVVGRVASMLELGG--------GFHPEL---TGRENIRL---NATLLGLRRKELKQRLDKIIefSELGEFIDEP 147
Cdd:TIGR02857 374 PTEGSIAVNGVPLADADADSwrdqiawvPQHPFLfagTIAENIRLarpDASDAEIREALERAGLDEFV--AALPQGLDTP 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1699326967 148 I----RVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKCLETINEFkKKGVTILFVSHNLRDIEKiCDRVI 221
Cdd:TIGR02857 452 IgeggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALAAL-ADRIV 527
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
46-238 |
9.04e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 69.87 E-value: 9.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 46 IENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVG-------------RVASMLElGGGFHPELTGREN 112
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvealsaraasrRVASVPQ-DTSLSFEFDVRQV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 113 IRLNAT----LLGLRRKELKQRLDKIIEFSELGEFIDEPIRVYSSG-----MLAKlgfsVITQVDPdILIIDEVLAVGDI 183
Cdd:PRK09536 98 VEMGRTphrsRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGerqrvLLAR----ALAQATP-VLLLDEPTASLDI 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1699326967 184 SFQRKCLETINEFKKKGVTILFVSHNLRDIEKICDRVIWIENHKMKVMGEAHSVI 238
Cdd:PRK09536 173 NHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-244 |
1.89e-13 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 68.67 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 5 IEFKNVTKRYPLYhhigsgikelifnprralsllsGRSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSS 84
Cdd:PRK11153 2 IELKNISKVFPQG----------------------GRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTS 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 85 GSVHVVGRvaSMLELGGG------------F-HPEL----TGRENIRLNATLLGLRRKELKQRLDKIIEFSELGEFIDep 147
Cdd:PRK11153 60 GRVLVDGQ--DLTALSEKelrkarrqigmiFqHFNLlssrTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKAD-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 148 irVY----SSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKCLETINEFKKK-GVTILFVSHNLRDIEKICDRVIW 222
Cdd:PRK11153 136 --RYpaqlSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAV 213
|
250 260
....*....|....*....|..
gi 1699326967 223 IENHKMKVMGEAHSVIAQYKEA 244
Cdd:PRK11153 214 IDAGRLVEQGTVSEVFSHPKHP 235
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
45-220 |
2.04e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 69.04 E-value: 2.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRVASML------ELGGGFH-------PELTGRE 111
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLdhklaaQLGIGIIyqelsviDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 112 NI----RLNATLLGLR---RKELKQRLDKIIEFSELGEFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDIS 184
Cdd:PRK09700 100 NLyigrHLTKKVCGVNiidWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNK 179
|
170 180 190
....*....|....*....|....*....|....*.
gi 1699326967 185 FQRKCLETINEFKKKGVTILFVSHNLRDIEKICDRV 220
Cdd:PRK09700 180 EVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRY 215
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-227 |
4.10e-13 |
|
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: 66.37 E-value: 4.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 5 IEFKNVTKRyplyhhigsgikeliFNPRRALsllsgrsylaiENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSS 84
Cdd:cd03261 1 IELRGLTKS---------------FGGRTVL-----------KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDS 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 85 GSVHVVG---------------RVASMLELGGGFHPELTGRENIrlnATLLGLRRKELKQRLDKI----IEFSELGEFID 145
Cdd:cd03261 55 GEVLIDGedisglseaelyrlrRRMGMLFQSGALFDSLTVFENV---AFPLREHTRLSEEEIREIvlekLEAVGLRGAED 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 146 EPIRVYSSGMLAKLGF--SVITqvDPDILIIDEVLAVGD-ISfQRKCLETINEFKK-KGVTILFVSHNLRDIEKICDRVI 221
Cdd:cd03261 132 LYPAELSGGMKKRVALarALAL--DPELLLYDEPTAGLDpIA-SGVIDDLIRSLKKeLGLTSIMVTHDLDTAFAIADRIA 208
|
....*.
gi 1699326967 222 WIENHK 227
Cdd:cd03261 209 VLYDGK 214
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
43-240 |
4.21e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 67.02 E-value: 4.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 43 YLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRV-----ASMLELGGG------------FHP 105
Cdd:PRK13639 15 TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPikydkKSLLEVRKTvgivfqnpddqlFAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 106 elTGRENIRLNATLLGLRRKELKQRLDKIIEFSELGEFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISF 185
Cdd:PRK13639 95 --TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1699326967 186 QRKCLETINEFKKKGVTILFVSHNLRDIEKICDRVIWIENHKMKVMGEAHSVIAQ 240
Cdd:PRK13639 173 ASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSD 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
45-221 |
4.80e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 67.74 E-value: 4.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGR------VASMLELGGGFHPE------LTGREN 112
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvrirsPRDAIRAGIAYVPEdrkgegLVLDLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 113 IRLNATLLGLRRKELKQRLDKIIEFSELGEFIDE----------PIRVYSSG-----MLAKLGFSvitqvDPDILIIDE- 176
Cdd:COG1129 347 IRENITLASLDRLSRGGLLDRRRERALAEEYIKRlriktpspeqPVGNLSGGnqqkvVLAKWLAT-----DPKVLILDEp 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1699326967 177 -----VLAVGDIsfqrkcLETINEFKKKGVTILFVSHNLRDIEKICDRVI 221
Cdd:COG1129 422 trgidVGAKAEI------YRLIRELAAEGKAVIVISSELPELLGLSDRIL 465
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
45-212 |
4.80e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 66.65 E-value: 4.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHV----------------VGRV---ASMlelggGFHP 105
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIdgkdvtklpeykrakyIGRVfqdPMM-----GTAP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 106 ELTGRENIRLnATLLGLRRKeLKQRLDKiiefSELGEFIDEpirvyssgmLAKLG---------------------FSVI 164
Cdd:COG1101 96 SMTIEENLAL-AYRRGKRRG-LRRGLTK----KRRELFREL---------LATLGlglenrldtkvgllsggqrqaLSLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1699326967 165 --TQVDPDILIIDEVLAVGDISFQRKCLETINEF-KKKGVTILFVSHNLRD 212
Cdd:COG1101 161 maTLTKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHNMEQ 211
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-221 |
5.45e-13 |
|
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: 65.92 E-value: 5.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 1 MSVAIEFKNVTKRYPLyHHIGsgikelifnprralsllsGRSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVM 80
Cdd:COG4778 1 MTTLLEVENLSKTFTL-HLQG------------------GKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNY 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 81 KPSSGSVHVVGRvASMLELGggfhpELTGREnirlnatLLGLRRKEL---KQRLDKIIEFSELgEFIDEPIRvySSG--- 154
Cdd:COG4778 62 LPDSGSILVRHD-GGWVDLA-----QASPRE-------ILALRRRTIgyvSQFLRVIPRVSAL-DVVAEPLL--ERGvdr 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 155 ---------MLAKLG------------FS------------VITqvDPDILIIDEVLAVGDISFQRKCLETINEFKKKGV 201
Cdd:COG4778 126 eeararareLLARLNlperlwdlppatFSggeqqrvniargFIA--DPPLLLLDEPTASLDAANRAVVVELIEEAKARGT 203
|
250 260
....*....|....*....|
gi 1699326967 202 TILFVSHNLRDIEKICDRVI 221
Cdd:COG4778 204 AIIGIFHDEEVREAVADRVV 223
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
49-237 |
6.01e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 66.11 E-value: 6.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 49 ISFQVKKGESVALIGRNGAGKSTSLGLVAGvMKPSSGSVHVVGRVASmlelgggfhpELTGRENIRLNATL--------- 119
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQPLE----------AWSAAELARHRAYLsqqqtppfa 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 120 ------LGLRRKELKQ------RLDKIIEFSELGEFIDEPIRVYSSG-----MLAklgfSVITQVDPDI------LIIDE 176
Cdd:PRK03695 84 mpvfqyLTLHQPDKTRteavasALNEVAEALGLDDKLGRSVNQLSGGewqrvRLA----AVVLQVWPDInpagqlLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1699326967 177 VLAVGDISfQRKCLET-INEFKKKGVTILFVSHNLRDIEKICDRVIWIENHKMKVMGEAHSV 237
Cdd:PRK03695 160 PMNSLDVA-QQAALDRlLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
33-210 |
6.67e-13 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 66.29 E-value: 6.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 33 RALSLLSGRSYLaIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGR---------VASML------ 97
Cdd:COG4559 5 ENLSVRLGGRTL-LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRplaawspweLARRRavlpqh 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 98 -ELGGGFhpelTGRENIRLNATLLGLRRKELKQRLDKIIEFSELGEFIDepiRVYS--SG------MLAKlgfsVITQV- 167
Cdd:COG4559 84 sSLAFPF----TVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAG---RSYQtlSGgeqqrvQLAR----VLAQLw 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1699326967 168 -----DPDILIIDEVLAVGDISFQRKCLETINEFKKKGVTILFVSHNL 210
Cdd:COG4559 153 epvdgGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDL 200
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
45-233 |
7.53e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 67.17 E-value: 7.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVG----------RVASMLELGGGFHPELTGRENIR 114
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGvdlshvppyqRPINMMFQSYALFPHMTVEQNIA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 115 LNATLLGLRRKELKQRLDKIIEFSELGEFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQ-RKCLETI 193
Cdd:PRK11607 114 FGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRdRMQLEVV 193
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1699326967 194 NEFKKKGVTILFVSHNLRDIEKICDRVIWIENHKMKVMGE 233
Cdd:PRK11607 194 DILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGE 233
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
21-232 |
9.55e-13 |
|
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: 67.35 E-value: 9.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 21 GSGIKEL--IFNPrralsllSGRSYLAIENISFQvkKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGR-VASML 97
Cdd:TIGR01257 928 GVCVKNLvkIFEP-------SGRPAVDRLNITFY--ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKdIETNL 998
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 98 EL---GGGFHPE-------LTGRENIRLNATLLGLRRKELKQRLDKIIEFSELGEFIDEPIRVYSSGMLAKLGFSVITQV 167
Cdd:TIGR01257 999 DAvrqSLGMCPQhnilfhhLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVG 1078
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1699326967 168 DPDILIIDEVLAVGDISFQRKCLETINEFkKKGVTILFVSHNLRDIEKICDRVIWIENHKMKVMG 232
Cdd:TIGR01257 1079 DAKVVVLDEPTSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
45-225 |
1.25e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 65.29 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGR------VASMLELGGGFHPE---LTGRENIRL 115
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKditdwqTAKIMREAVAIVPEgrrVFSRMTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 116 NATLLGL--RRKELKQRLDKIIE-FSELGEFIDEPIRVYSSG---MLAkLGFSVITQvdPDILIIDE-VLAVGDISFQrK 188
Cdd:PRK11614 100 NLAMGGFfaERDQFQERIKWVYElFPRLHERRIQRAGTMSGGeqqMLA-IGRALMSQ--PRLLLLDEpSLGLAPIIIQ-Q 175
|
170 180 190
....*....|....*....|....*....|....*..
gi 1699326967 189 CLETINEFKKKGVTILFVSHNLRDIEKICDRVIWIEN 225
Cdd:PRK11614 176 IFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLEN 212
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
47-178 |
1.64e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 64.44 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 47 ENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRV---------ASMLELG--GGFHPELTGRENIRL 115
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPirrqrdeyhQDLLYLGhqPGIKTELTALENLRF 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1699326967 116 NATLLG-LRRKELKQRLDKIiefsELGEFIDEPIRVYSSGM-----LAKLGFSvitqvDPDILIIDEVL 178
Cdd:PRK13538 98 YQRLHGpGDDEALWEALAQV----GLAGFEDVPVRQLSAGQqrrvaLARLWLT-----RAPLWILDEPF 157
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
46-240 |
2.21e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 64.65 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 46 IENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRVASML---ELGG--GFHPE-LTGRENI---RLN 116
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLssrQLARrlALLPQhHLTPEGItvrELV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 117 A-------TLLGLRRKELKQRLDKIIEFSELGEFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKC 189
Cdd:PRK11231 98 AygrspwlSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVEL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1699326967 190 LETINEFKKKGVTILFVSHNLRDIEKICDRVIWIENHKMKVMGEAHSVIAQ 240
Cdd:PRK11231 178 MRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTP 228
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
5-242 |
2.85e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 65.11 E-value: 2.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 5 IEFKNVTKryplyhhigsgikelIFNPRRALSLLsgrsylAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSS 84
Cdd:PRK13651 3 IKVKNIVK---------------IFNKKLPTELK------ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDT 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 85 GSV----------HVVGRVASMLE---------------------LGGGFHP------ELTGRENIRLNATLLGLRRKEL 127
Cdd:PRK13651 62 GTIewifkdeknkKKTKEKEKVLEklviqktrfkkikkikeirrrVGVVFQFaeyqlfEQTIEKDIIFGPVSMGVSKEEA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 128 KQRLDKIIEFSELGE-FIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKCLETINEFKKKGVTILFV 206
Cdd:PRK13651 142 KKRAAKYIELVGLDEsYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILV 221
|
250 260 270
....*....|....*....|....*....|....*.
gi 1699326967 207 SHNLRDIEKICDRVIWIENHKMKVMGEAHSVIAQYK 242
Cdd:PRK13651 222 THDLDNVLEWTKRTIFFKDGKIIKDGDTYDILSDNK 257
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
8-229 |
3.50e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 64.03 E-value: 3.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 8 KNVTKRYPLYHHIGSGIKELifnprralSLLSGrsylaienISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSV 87
Cdd:PRK10584 4 ENIVEVHHLKKSVGQGEHEL--------SILTG--------VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 88 HVVGRVASMLELGG---------GFH-------PELTGRENIRLNATLLGLRRKELKQRLDKIIEFSELGEFIDEPIRVY 151
Cdd:PRK10584 68 SLVGQPLHQMDEEAraklrakhvGFVfqsfmliPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 152 SSGMLAKLGFSVITQVDPDILIIDEvlAVGDISfqRKCLETINEF-----KKKGVTILFVSHNLRdIEKICDRVIWIENH 226
Cdd:PRK10584 148 SGGEQQRVALARAFNGRPDVLFADE--PTGNLD--RQTGDKIADLlfslnREHGTTLILVTHDLQ-LAARCDRRLRLVNG 222
|
...
gi 1699326967 227 KMK 229
Cdd:PRK10584 223 QLQ 225
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
45-240 |
3.70e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 64.44 E-value: 3.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGR------VASMLELGG---------GFHPelTG 109
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenIREVRKFVGlvfqnpddqIFSP--TV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 110 RENIRLNATLLGLRRKELKQRLDKIIEFSELGEFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKC 189
Cdd:PRK13652 97 EQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKEL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1699326967 190 LETINEFKKK-GVTILFVSHNLRDIEKICDRVIWIENHKMKVMGEAHSVIAQ 240
Cdd:PRK13652 177 IDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
45-221 |
4.89e-12 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 62.45 E-value: 4.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGR------VASMLELGGGFHPE------LTGREN 112
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKpvtrrsPRDAIRAGIAYVPEdrkregLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 113 IRLNATLlglrrkelkqrldkiiefselgefidepiRVYSSG------MLAKlgfsVITQvDPDILIIDEVlAVG-DISF 185
Cdd:cd03215 95 VAENIAL-----------------------------SSLLSGgnqqkvVLAR----WLAR-DPRVLILDEP-TRGvDVGA 139
|
170 180 190
....*....|....*....|....*....|....*.
gi 1699326967 186 QRKCLETINEFKKKGVTILFVSHNLRDIEKICDRVI 221
Cdd:cd03215 140 KAEIYRLIRELADAGKAVLLISSELDELLGLCDRIL 175
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
49-237 |
5.99e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 63.32 E-value: 5.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 49 ISFQVKKGESVALIGRNGAGKSTSLGLVAGvMKPSSGSVHVVGRVASmlelgggfhpELTGRENIRLNATL--------- 119
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGRPLS----------DWSAAELARHRAYLsqqqsppfa 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 120 ------------LGLRRKELKQRLDKIIEFSELGEFIDEPIRVYSSG-----MLAKlgfsVITQVDPDI------LIIDE 176
Cdd:COG4138 84 mpvfqylalhqpAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGewqrvRLAA----VLLQVWPTInpegqlLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1699326967 177 VLAVGDISFQRKCLETINEFKKKGVTILFVSHNLRDIEKICDRVIWIENHKMKVMGEAHSV 237
Cdd:COG4138 160 PMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEV 220
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
45-224 |
6.21e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 63.98 E-value: 6.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRVASMLELGGGFHP-----------------EL 107
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPvrkkvgvvfqfpesqlfEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 108 TGRENIRLNATLLGLRRKELKQRLDKIIEFSELG-EFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQ 186
Cdd:PRK13643 101 TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKAR 180
|
170 180 190
....*....|....*....|....*....|....*...
gi 1699326967 187 RKCLETINEFKKKGVTILFVSHNLRDIEKICDRVIWIE 224
Cdd:PRK13643 181 IEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLE 218
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
46-221 |
8.88e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 63.19 E-value: 8.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 46 IENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRVASM-------LELGGGF-HPE-----LTGREN 112
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAenvwnlrRKIGMVFqNPDnqfvgATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 113 IRLNATLLGLRRKELKQRLDKIIEFSELGEF-IDEPIRVySSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKCLE 191
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDEALLAVNMLDFkTREPARL-SGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMR 181
|
170 180 190
....*....|....*....|....*....|.
gi 1699326967 192 TINEFKKK-GVTILFVSHNLrDIEKICDRVI 221
Cdd:PRK13642 182 VIHEIKEKyQLTVLSITHDL-DEAASSDRIL 211
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
4-232 |
1.27e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 63.83 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 4 AIEFKNVTKRYPlyhhigsgikelifNPRRAlsllsgrsylaIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPS 83
Cdd:PRK13657 334 AVEFDDVSFSYD--------------NSRQG-----------VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQ 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 84 SGSVHV-------VGRVASMLELGGGFHPEL----TGRENIRL---NATLLGLRRK-ELKQRLDkIIEFSELG--EFIDE 146
Cdd:PRK13657 389 SGRILIdgtdirtVTRASLRRNIAVVFQDAGlfnrSIEDNIRVgrpDATDEEMRAAaERAQAHD-FIERKPDGydTVVGE 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 147 PIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKCLETINEFkKKGVTILFVSHNLRDIEKiCDRVIWIENH 226
Cdd:PRK13657 468 RGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDEL-MKGRTTFIIAHRLSTVRN-ADRILVFDNG 545
|
....*.
gi 1699326967 227 KMKVMG 232
Cdd:PRK13657 546 RVVESG 551
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-224 |
1.37e-11 |
|
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: 61.78 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 5 IEFKNVTKRYplyhhigsGIKElifnprralsllsgrsylAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSS 84
Cdd:cd03262 1 IEIKNLHKSF--------GDFH------------------VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDS 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 85 GSVHVVGRV-----ASMLEL----GGGFH-----PELTGRENIRLN-ATLLGLRRKELKQRLDKIIEFSELGEFIDEPIR 149
Cdd:cd03262 55 GTIIIDGLKltddkKNINELrqkvGMVFQqfnlfPHLTVLENITLApIKVKGMSKAEAEERALELLEKVGLADKADAYPA 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1699326967 150 VYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKCLETINEFKKKGVTILFVSHNLRDIEKICDRVIWIE 224
Cdd:cd03262 135 QLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMD 209
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
5-240 |
2.09e-11 |
|
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: 61.86 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 5 IEFKNVTKRYPlyhhigsgikelifnprralsllsGRSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSS 84
Cdd:cd03251 1 VEFKNVTFRYP------------------------GDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDS 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 85 GSVHVVGRVASMLELgggfhPEL----------------TGRENI---RLNATLLGLRRK-ELKQRLDKIIEFSE-LGEF 143
Cdd:cd03251 57 GRILIDGHDVRDYTL-----ASLrrqiglvsqdvflfndTVAENIaygRPGATREEVEEAaRAANAHEFIMELPEgYDTV 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 144 IDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKCLETINEFkKKGVTILFVSHNLRDIEKIcDRVIWI 223
Cdd:cd03251 132 IGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERL-MKNRTTFVIAHRLSTIENA-DRIVVL 209
|
250
....*....|....*..
gi 1699326967 224 ENHKMKVMGEAHSVIAQ 240
Cdd:cd03251 210 EDGKIVERGTHEELLAQ 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
45-240 |
3.38e-11 |
|
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: 62.51 E-value: 3.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVvgRVAS----MLELGggfhPELTGRENirlnaTLL 120
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNV--RVGDewvdMTKPG----PDGRGRAK-----RYI 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 121 GLRRKEL-----KQRLDKIIEFSELgEFIDEPIRVYSSGMLAKLGFS-----------------------VITQV---DP 169
Cdd:TIGR03269 368 GILHQEYdlyphRTVLDNLTEAIGL-ELPDELARMKAVITLKMVGFDeekaeeildkypdelsegerhrvALAQVlikEP 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1699326967 170 DILIIDEVLAVGDISFQRKCLETINEFKKK-GVTILFVSHNLRDIEKICDRVIWIENHKMKVMGEAHSVIAQ 240
Cdd:TIGR03269 447 RIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
38-228 |
5.09e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 60.66 E-value: 5.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 38 LSGRSylAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRVASML----------ELGGGF--HP 105
Cdd:PRK10908 12 LGGRQ--ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLknrevpflrrQIGMIFqdHH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 106 ELTGR---ENIRLNATLLGLRRKELKQR----LDKIIEFSELGEFidePIRVySSGMLAKLGFSVITQVDPDILIIDEVL 178
Cdd:PRK10908 90 LLMDRtvyDNVAIPLIIAGASGDDIRRRvsaaLDKVGLLDKAKNF---PIQL-SGGEQQRVGIARAVVNKPAVLLADEPT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1699326967 179 AVGDISFQRKCLETINEFKKKGVTILFVSHNLRDIEKICDRVIWIENHKM 228
Cdd:PRK10908 166 GNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
44-232 |
6.13e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 60.77 E-value: 6.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 44 LAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSV-----HVVGRVASMLELGG---GFH-----PELTGR 110
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIllrgqHIEGLPGHQIARMGvvrTFQhvrlfREMTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 111 ENI------RLNATLL-GL------RRKElKQRLDKIIEFSE---LGEFIDEPIRVYSSGMLAKLGFS--VITQvdPDIL 172
Cdd:PRK11300 99 ENLlvaqhqQLKTGLFsGLlktpafRRAE-SEALDRAATWLErvgLLEHANRQAGNLAYGQQRRLEIArcMVTQ--PEIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1699326967 173 IIDEVLAVGDISFQRKCLETINEFKKK-GVTILFVSHNLRDIEKICDRVIWIENHKMKVMG 232
Cdd:PRK11300 176 MLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANG 236
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-240 |
6.69e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 61.76 E-value: 6.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 2 SVAIEFKNVTKRYPlyhhigsgikelifnprralsllsGRSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMK 81
Cdd:PRK11160 336 QVSLTLNNVSFTYP------------------------DQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 82 PSSGSVHVVGRVASMLelgggfhPELTGRENI-----R---LNATLlglrRKELK---------------QR--LDKIIE 136
Cdd:PRK11160 392 PQQGEILLNGQPIADY-------SEAALRQAIsvvsqRvhlFSATL----RDNLLlaapnasdealievlQQvgLEKLLE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 137 FSE-LGEFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKCLETINEFkKKGVTILFVSHNLRDIEK 215
Cdd:PRK11160 461 DDKgLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEH-AQNKTVLMITHRLTGLEQ 539
|
250 260
....*....|....*....|....*
gi 1699326967 216 IcDRVIWIENHKMKVMGEAHSVIAQ 240
Cdd:PRK11160 540 F-DRICVMDNGQIIEQGTHQELLAQ 563
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1-238 |
7.92e-11 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 61.20 E-value: 7.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 1 MSVAIEFKNVTKRY-----PLYHHIGSGI-KELIFNpRRALSLlsgrsylAIENISFQVKKGESVALIGRNGAGKSTSLG 74
Cdd:PRK10070 1 MAIKLEIKNLYKIFgehpqRAFKYIEQGLsKEQILE-KTGLSL-------GVKDASLAIEEGEIFVIMGLSGSGKSTMVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 75 LVAGVMKPSSGSVHVVG----------------RVASMLELGGGFHPELTGRENIRLNATLLGLRRKELKQRLDKIIEFS 138
Cdd:PRK10070 73 LLNRLIEPTRGQVLIDGvdiakisdaelrevrrKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 139 ELGEFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKCLETINEFK-KKGVTILFVSHNLRDIEKIC 217
Cdd:PRK10070 153 GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQaKHQRTIVFISHDLDEAMRIG 232
|
250 260
....*....|....*....|.
gi 1699326967 218 DRVIWIENHKMKVMGEAHSVI 238
Cdd:PRK10070 233 DRIAIMQNGEVVQVGTPDEIL 253
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
45-239 |
8.39e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 60.57 E-value: 8.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRvasMLELGGGFHPELTGRENIRLNATLLGLRR 124
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDH---PLHFGDYSYRSQRIRMIFQDPSTSLNPRQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 125 K-----ELKQRLDKIIEFSELGEFIDEPIR---------VYSSGMLA-----KLGFSVITQVDPDILIIDEVLAVGDISF 185
Cdd:PRK15112 105 RisqilDFPLRLNTDLEPEQREKQIIETLRqvgllpdhaSYYPHMLApgqkqRLGLARALILRPKVIIADEALASLDMSM 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1699326967 186 QRKCLETINEFK-KKGVTILFVSHNLRDIEKICDRVIWIENHKMKVMGEAHSVIA 239
Cdd:PRK15112 185 RSQLINLMLELQeKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLA 239
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
33-221 |
9.18e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 61.20 E-value: 9.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 33 RALSLLSGRSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGR------VASMLELGGGFHPE 106
Cdd:COG3845 261 ENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEditglsPRERRRLGVAYIPE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 107 ----------LTGRENIRLN-------ATLLGLRRKELKQRLDKIIEfselgEF------IDEPIRVYSSGMLAKLgfsV 163
Cdd:COG3845 341 drlgrglvpdMSVAENLILGryrrppfSRGGFLDRKAIRAFAEELIE-----EFdvrtpgPDTPARSLSGGNQQKV---I 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1699326967 164 ----ITQvDPDILIIDEV---LAVGDISFQRKcleTINEFKKKGVTILFVSHNLRDIEKICDRVI 221
Cdd:COG3845 413 lareLSR-DPKLLIAAQPtrgLDVGAIEFIHQ---RLLELRDAGAAVLLISEDLDEILALSDRIA 473
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
44-239 |
1.28e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 60.03 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 44 LAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHV--------------------VGRVASMLElgggf 103
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitagkknkklkplrkkVGIVFQFPE----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 104 HP--ELTGRENIRLNATLLGLRRKELKQRLDKIIEFSELGEFIDE--PI--------RVYSSGMLAklgfsvitqVDPDI 171
Cdd:PRK13634 96 HQlfEETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELLArsPFelsggqmrRVAIAGVLA---------MEPEV 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1699326967 172 LIIDEVLAVGDISFQRKCLETINEF-KKKGVTILFVSHNLRDIEKICDRVIWIENHKMKVMGEAHSVIA 239
Cdd:PRK13634 167 LVLDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFA 235
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
45-229 |
1.30e-10 |
|
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: 58.96 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRVASMLELGggfhpelTGRENIRLNATLLGLRR 124
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLE-------DLRSSLTIIPQDPTLFS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 125 KELKQRLDKIIEFSElgEFIDEPIRVYSSGM--------LAKLGFSVITQvdPDILIIDEVLAVGDISFQRKCLETINEf 196
Cdd:cd03369 96 GTIRSNLDPFDEYSD--EEIYGALRVSEGGLnlsqgqrqLLCLARALLKR--PRVLVLDEATASIDYATDALIQKTIRE- 170
|
170 180 190
....*....|....*....|....*....|...
gi 1699326967 197 KKKGVTILFVSHNLRDIEKiCDRVIWIENHKMK 229
Cdd:cd03369 171 EFTNSTILTIAHRLRTIID-YDKILVMDAGEVK 202
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-87 |
1.69e-10 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 60.56 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 4 AIEFKNVTKRYPlyhhigsgikelifnprralsllSGRsyLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPS 83
Cdd:COG1132 339 EIEFENVSFSYP-----------------------GDR--PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPT 393
|
....
gi 1699326967 84 SGSV 87
Cdd:COG1132 394 SGRI 397
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
46-239 |
2.08e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 59.14 E-value: 2.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 46 IENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRVASMLEL------GGGFHPE---LTGRENIRLN 116
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhararrGIGYLPQeasIFRRLSVYDN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 117 ATLLGLRRKEL--KQRLDKIIEFSElgEFIDEPIR-----VYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKC 189
Cdd:PRK10895 99 LMAVLQIRDDLsaEQREDRANELME--EFHIEHLRdsmgqSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1699326967 190 LETINEFKKKGVTILFVSHNLRDIEKICDRVIWIENHKMKVMGEAHSVIA 239
Cdd:PRK10895 177 KRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
5-240 |
2.58e-10 |
|
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: 58.78 E-value: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 5 IEFKNVTKRYplyhhigsgikelifNPRRalsllsgrsyLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSS 84
Cdd:cd03253 1 IEFENVTFAY---------------DPGR----------PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSS 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 85 GSVHVVGRVASMLELGG-----GFHPE------LTGRENI---RLNATLLGLRRKELKQRL-DKIIEFSE-----LGEfi 144
Cdd:cd03253 56 GSILIDGQDIREVTLDSlrraiGVVPQdtvlfnDTIGYNIrygRPDATDEEVIEAAKAAQIhDKIMRFPDgydtiVGE-- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 145 depiR--VYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKCLETINEFkKKGVTILFVSHNLRDIEKiCDRVIW 222
Cdd:cd03253 134 ----RglKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDV-SKGRTTIVIAHRLSTIVN-ADKIIV 207
|
250
....*....|....*...
gi 1699326967 223 IENHKMKVMGEAHSVIAQ 240
Cdd:cd03253 208 LKDGRIVERGTHEELLAK 225
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
45-214 |
4.41e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 58.17 E-value: 4.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRVAS--MLELGGGFH-----PELTGRENIRLNA 117
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEgpGAERGVVFQnegllPWRNVQDNVAFGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 118 TLLGLRRKELKQRLDKIIEFSELGEFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDiSFQRKCLET--INE 195
Cdd:PRK11248 96 QLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD-AFTREQMQTllLKL 174
|
170
....*....|....*....
gi 1699326967 196 FKKKGVTILFVSHnlrDIE 214
Cdd:PRK11248 175 WQETGKQVLLITH---DIE 190
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-92 |
5.84e-10 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 57.79 E-value: 5.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 5 IEFKNVTKRYplyhhigsgikelifnprralsllsgRSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSS 84
Cdd:COG4604 2 IEIKNVSKRY--------------------------GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDS 55
|
....*...
gi 1699326967 85 GSVHVVGR 92
Cdd:COG4604 56 GEVLVDGL 63
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
43-221 |
6.11e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 58.25 E-value: 6.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 43 YLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSV-----------------HVVGRVASMLELGGGFHP 105
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVtvdditithktkdkyirPVRKRIGMVFQFPESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 106 ELTGRENIRLNATLLGLRRKELKQR-LDKIIEFSELGEFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDIS 184
Cdd:PRK13646 100 EDTVEREIIFGPKNFKMNLDEVKNYaHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQ 179
|
170 180 190
....*....|....*....|....*....|....*...
gi 1699326967 185 FQRKCLETINEFK-KKGVTILFVSHNLRDIEKICDRVI 221
Cdd:PRK13646 180 SKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVI 217
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
45-176 |
7.35e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 58.60 E-value: 7.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVG------------RVASMLElggGF--HPELTGR 110
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGqpvdagdiatrrRVGYMSQ---AFslYGELTVR 357
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1699326967 111 ENIRLNATLLGLRRKELKQRLDKIIEFSELGEFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDE 176
Cdd:NF033858 358 QNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDE 423
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
31-246 |
7.50e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.52 E-value: 7.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 31 PRRALSLLSGRSYLaieNISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGR------VASMLELGGGFH 104
Cdd:PRK15439 267 PVLTVEDLTGEGFR---NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKeinalsTAQRLARGLVYL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 105 PELTGRENIRLNATL-------------LGLRRKELKQRLDKI-----IEFSElgefIDEPIRVYSSGMLAKLGFSVITQ 166
Cdd:PRK15439 344 PEDRQSSGLYLDAPLawnvcalthnrrgFWIKPARENAVLERYrralnIKFNH----AEQAARTLSGGNQQKVLIAKCLE 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 167 VDPDILIIDEVLAVGDISFQRKCLETINEFKKKGVTILFVSHNLRDIEKICDRVIwienhkmkVMGEAHSVIAQYKEAMS 246
Cdd:PRK15439 420 ASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVL--------VMHQGEISGALTGAAIN 491
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
45-246 |
9.08e-10 |
|
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: 58.28 E-value: 9.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKSTSLGLVAGV--MKPSSGSV--HV--------------VG--------------- 91
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyHValcekcgyverpskVGepcpvcggtlepeev 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 92 ---------------RVASMLELGGGFHPELTGRENIRLNATLLGLRRKELKQRLDKIIEFSELGEFIDEPIRVYSSGML 156
Cdd:TIGR03269 95 dfwnlsdklrrrirkRIAIMLQRTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRITHIARDLSGGEK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 157 AKLGFSVITQVDPDILIIDEVLAVGDISFQRKCLETINE-FKKKGVTILFVSHNLRDIEKICDRVIWIENHKMKVMGEAH 235
Cdd:TIGR03269 175 QRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEaVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIKEEGTPD 254
|
250
....*....|.
gi 1699326967 236 SVIAQYKEAMS 246
Cdd:TIGR03269 255 EVVAVFMEGVS 265
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
33-210 |
9.42e-10 |
|
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: 58.14 E-value: 9.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 33 RALSLLSGRSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRVASMLELGG-----GFHPE- 106
Cdd:TIGR02868 338 RDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEvrrrvSVCAQd 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 107 -----LTGRENIRL---NAT----LLGLRRKELKQRLDKIIEfsELGEFIDEPIRVYSSGMLAKLGFSVITQVDPDILII 174
Cdd:TIGR02868 418 ahlfdTTVRENLRLarpDATdeelWAALERVGLADWLRALPD--GLDTVLGEGGARLSGGERQRLALARALLADAPILLL 495
|
170 180 190
....*....|....*....|....*....|....*.
gi 1699326967 175 DEVLAVGDISFQRKCLETINEfKKKGVTILFVSHNL 210
Cdd:TIGR02868 496 DEPTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
48-227 |
9.54e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 57.38 E-value: 9.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 48 NISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGsvhvvgrvasmlELGGGFHPELTGRENIRL---NATL----- 119
Cdd:PRK11247 30 QLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG------------ELLAGTAPLAEAREDTRLmfqDARLlpwkk 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 120 ------LGLR---RKELKQRLDKIiefsELGEFIDEPIRVYSSGM-----LAKlgfSVITQvdPDILIIDEVLAVGD--- 182
Cdd:PRK11247 98 vidnvgLGLKgqwRDAALQALAAV----GLADRANEWPAALSGGQkqrvaLAR---ALIHR--PGLLLLDEPLGALDalt 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1699326967 183 -ISFQrKCLETIneFKKKGVTILFVSHNLRDIEKICDRVIWIENHK 227
Cdd:PRK11247 169 rIEMQ-DLIESL--WQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
41-193 |
1.63e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 56.76 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 41 RSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPS--SGSVHVVGRVAsmlelgggfhpeLTGRENIRLNAT 118
Cdd:PRK13547 12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaPRGARVTGDVT------------LNGEPLAAIDAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 119 LLGLRRKELKQRLDKIIEFSE-----LGEF-----------------------------IDEPIRVYSSGMLAKLGFSVI 164
Cdd:PRK13547 80 RLARLRAVLPQAAQPAFAFSAreivlLGRYpharragalthrdgeiawqalalagatalVGRDVTTLSGGELARVQFARV 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 1699326967 165 ---------TQVDPDILIIDEVLAVGDISFQRKCLETI 193
Cdd:PRK13547 160 laqlwpphdAAQPPRYLLLDEPTAALDLAHQHRLLDTV 197
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
45-220 |
1.77e-09 |
|
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: 57.39 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKSTS----LGLVAGVMKPSSGSVHVVGR------VASMLELGGG-----F------ 103
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGQdllglsERELRRIRGNriamiFqepmts 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 104 -HPELT-GR---ENIRLNatlLGLRRKELKQRldkIIE-FSELGefIDEP---IRVY----SSGM---------LAklgf 161
Cdd:COG4172 105 lNPLHTiGKqiaEVLRLH---RGLSGAAARAR---ALElLERVG--IPDPerrLDAYphqlSGGQrqrvmiamaLA---- 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1699326967 162 svitqVDPDILIIDE---VLavgDISFQRKCLETINEFKKK-GVTILFVSHNLRDIEKICDRV 220
Cdd:COG4172 173 -----NEPDLLIADEpttAL---DVTVQAQILDLLKDLQRElGMALLLITHDLGVVRRFADRV 227
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
45-220 |
1.94e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 57.25 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMkPS---SGSVHVVGR--VASML-------------ELggGFHPE 106
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEelQASNIrdteragiaiihqEL--ALVKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 107 LTGRENIRLNATLLGLRR---KELKQRLDKIIEfsELGEFIDEPIRVYSSGM----LAKLGFSVITQVdpDILIIDEVLA 179
Cdd:PRK13549 97 LSVLENIFLGNEITPGGImdyDAMYLRAQKLLA--QLKLDINPATPVGNLGLgqqqLVEIAKALNKQA--RLLILDEPTA 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1699326967 180 VGDISFQRKCLETINEFKKKGVTILFVSHNLRDIEKICDRV 220
Cdd:PRK13549 173 SLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTI 213
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
48-221 |
2.13e-09 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 57.02 E-value: 2.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 48 NISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRVASML---ELGGGF---HPEL----TGRENIRLNA 117
Cdd:PRK10851 20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLharDRKVGFvfqHYALfrhmTVFDNIAFGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 118 TLLGLRRK----ELKQRLDKIIEFSELGEFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQ---RKCL 190
Cdd:PRK10851 100 TVLPRRERpnaaAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRkelRRWL 179
|
170 180 190
....*....|....*....|....*....|..
gi 1699326967 191 ETI-NEFKKKGVtilFVSHNLRDIEKICDRVI 221
Cdd:PRK10851 180 RQLhEELKFTSV---FVTHDQEEAMEVADRVV 208
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
45-228 |
2.31e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 56.35 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVgrVASMLELGGGFHPELTGR--------ENIRLN 116
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKI--TVDGITLTAKTVWDIREKvgivfqnpDNQFVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 117 ATL-----LGLR-----RKELKQRLDKIIEFSELGEFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQ 186
Cdd:PRK13640 100 ATVgddvaFGLEnravpRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1699326967 187 RKCLETINEF-KKKGVTILFVSHNLRDIEkICDRVIWIENHKM 228
Cdd:PRK13640 180 EQILKLIRKLkKKNNLTVISITHDIDEAN-MADQVLVLDDGKL 221
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
44-240 |
2.62e-09 |
|
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: 55.96 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 44 LAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVG-------------RVASMLELGGGFHPELtgR 110
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawlrrQVGVVLQENVLFNRSI--R 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 111 ENIRLNATLLGLRRKELKQRLDKIIEF-SELGE----FIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISF 185
Cdd:cd03252 94 DNIALADPGMSMERVIEAAKLAGAHDFiSELPEgydtIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYES 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1699326967 186 QRKCLETINEFkKKGVTILFVSHNLRDIeKICDRVIWIENHKMKVMGEAHSVIAQ 240
Cdd:cd03252 174 EHAIMRNMHDI-CAGRTVIIIAHRLSTV-KNADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
30-234 |
3.29e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 55.49 E-value: 3.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 30 NPRRALSLLSGRSYLA-----IENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRVASMLElgggfh 104
Cdd:PRK10247 2 QENSPLLQLQNVGYLAgdakiLNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLK------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 105 PElTGRENIRLNA---TLLG------------LRRK--ELKQRLDKIIEFSELGEFIDEPIRVYSSGmlAKLGFSVI--T 165
Cdd:PRK10247 76 PE-IYRQQVSYCAqtpTLFGdtvydnlifpwqIRNQqpDPAIFLDDLERFALPDTILTKNIAELSGG--EKQRISLIrnL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 166 QVDPDILIIDEVLAVGDISFQRKCLETINEF-KKKGVTILFVSHNLRDIeKICDRVIWIENHKMKvMGEA 234
Cdd:PRK10247 153 QFMPKVLLLDEITSALDESNKHNVNEIIHRYvREQNIAVLWVTHDKDEI-NHADKVITLQPHAGE-MQEA 220
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
46-244 |
3.40e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 55.75 E-value: 3.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 46 IENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRVASMLELGGGfHPELTGRENIRLNAT------- 118
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDG-QLKVADKNQLRLLRTrltmvfq 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 119 --------------------LLGLRRKELKQR----LDKI-IEFSELGEFidePIRVySSGMLAKLGFSVITQVDPDILI 173
Cdd:PRK10619 100 hfnlwshmtvlenvmeapiqVLGLSKQEARERavkyLAKVgIDERAQGKY---PVHL-SGGQQQRVSIARALAMEPEVLL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1699326967 174 IDEVLAVGDISFQRKCLETINEFKKKGVTILFVSHNLRDIEKICDRVIWIENHKMKVMGEAHSVIAQYKEA 244
Cdd:PRK10619 176 FDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSP 246
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
39-232 |
3.82e-09 |
|
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: 54.86 E-value: 3.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 39 SGRSYLAI-ENISFQVKKGESVALIGRNGAGKSTSLGLVAG--VMKPSSGSVHVVGRVASMLELGG--GF-------HPE 106
Cdd:cd03213 17 PSKSGKQLlKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDKRSFRKiiGYvpqddilHPT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 107 LTGRENIRLNATLLGLRRKELKqrldkiiefselgefidepiRVyssgmlaKLGFSVITqvDPDILIIDEVLAVGDISFQ 186
Cdd:cd03213 97 LTVRETLMFAAKLRGLSGGERK--------------------RV-------SIALELVS--NPSLLFLDEPTSGLDSSSA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1699326967 187 RKCLETINEFKKKGVTILFVSHNLR-DIEKICDRVIWIENHKMKVMG 232
Cdd:cd03213 148 LQVMSLLRRLADTGRTIICSIHQPSsEIFELFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
45-237 |
4.07e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 56.01 E-value: 4.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHV----------------------------VGRVASM 96
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknnhelitnpyskkiknfkeLRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 97 LelgggFH-PEL-----TGRENIRLNATLLGLRRKELKQRLDKIIEFSELGE-FIDEPIRVYSSGMLAKLGFSVITQVDP 169
Cdd:PRK13631 121 V-----FQfPEYqlfkdTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDsYLERSPFGLSGGQKRRVAIAGILAIQP 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1699326967 170 DILIIDEVLAVGDISFQRKCLETINEFKKKGVTILFVSHNLRDIEKICDRVIWIENHKMKVMGEAHSV 237
Cdd:PRK13631 196 EILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEI 263
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
45-221 |
4.33e-09 |
|
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: 56.23 E-value: 4.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKSTsLGLvaGVMK--PSSGSVHVVGRvasmlelgggfhpeltgrenirlnaTLLGL 122
Cdd:COG4172 301 AVDGVSLTLRRGETLGLVGESGSGKST-LGL--ALLRliPSEGEIRFDGQ-------------------------DLDGL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 123 RRKELKQ-RLD-KII---EFSEL------GEFIDEPIRVYSSGM------------LAKLG------------FS----- 162
Cdd:COG4172 353 SRRALRPlRRRmQVVfqdPFGSLsprmtvGQIIAEGLRVHGPGLsaaerrarvaeaLEEVGldpaarhrypheFSggqrq 432
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1699326967 163 -------VITQvdPDILIIDEVLAVGDISFQRKCLETINEFKKK-GVTILFVSHNLRDIEKICDRVI 221
Cdd:COG4172 433 riaiaraLILE--PKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVM 497
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
45-220 |
4.47e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.17 E-value: 4.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRVASM------LELG-GGFH------PELTGRE 111
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFngpkssQEAGiGIIHqelnliPQLTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 112 NIrlnatLLGlrrKELKQRLDKIiefsELGEFIDEpirvySSGMLAKLGFSvitqVDPDILIIDevLAVGD--------- 182
Cdd:PRK10762 99 NI-----FLG---REFVNRFGRI----DWKKMYAE-----ADKLLARLNLR----FSSDKLVGE--LSIGEqqmveiakv 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1699326967 183 ISFQRKCL------------ET------INEFKKKGVTILFVSHNLRDIEKICDRV 220
Cdd:PRK10762 156 LSFESKVIimdeptdaltdtETeslfrvIRELKSQGRGIVYISHRLKEIFEICDDV 211
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
44-209 |
5.18e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.95 E-value: 5.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 44 LAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHvvgrVASMLELGGGFHPELtgrENIRLNAT----L 119
Cdd:PRK10636 326 IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIG----LAKGIKLGYFAQHQL---EFLRADESplqhL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 120 LGLRRKELKQRL-DKIIEFSELGEFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKCLETINEFKK 198
Cdd:PRK10636 399 ARLAPQELEQKLrDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEG 478
|
170
....*....|.
gi 1699326967 199 kgvTILFVSHN 209
Cdd:PRK10636 479 ---ALVVVSHD 486
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
46-89 |
8.40e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 55.34 E-value: 8.40e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1699326967 46 IENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHV 89
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC 378
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
42-238 |
9.35e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 54.61 E-value: 9.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 42 SYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHV------------VGRVASMLELGGGFHPELTG 109
Cdd:PRK10253 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLdgehiqhyaskeVARRIGLLAQNATTPGDITV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 110 RENI---RLNATLLGLR-RKELKQRLDKIIEFSELGEFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISF 185
Cdd:PRK10253 99 QELVargRYPHQPLFTRwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISH 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1699326967 186 QRKCLETINEF-KKKGVTILFVSHNLRDIEKICDRVIWIENHKMKVMGEAHSVI 238
Cdd:PRK10253 179 QIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
45-243 |
9.94e-09 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 54.71 E-value: 9.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRvasmlelgggfhpELTGRENIRLNATllglrR 124
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGK-------------DLLGMKDDEWRAV-----R 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 125 KE-----------LKQRLDkiiefseLGEFIDEPIRVYS------------SGMLAKLGF--SVITQ------------- 166
Cdd:PRK15079 98 SDiqmifqdplasLNPRMT-------IGEIIAEPLRTYHpklsrqevkdrvKAMMLKVGLlpNLINRyphefsggqcqri 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 167 -------VDPDILIIDEVLAVGDISFQRKCLETINEFKKK-GVTILFVSHNLRDIEKICDRVIwienhkmkVMGEAHSV- 237
Cdd:PRK15079 171 giaraliLEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVL--------VMYLGHAVe 242
|
....*.
gi 1699326967 238 IAQYKE 243
Cdd:PRK15079 243 LGTYDE 248
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
34-225 |
1.38e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 54.73 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 34 ALSLLSG--RSYLA-------IENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRVASMLELGG--- 101
Cdd:PRK10535 3 ALLELKDirRSYPSgeeqvevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAlaq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 102 ------GF-----H--PELTGRENIRLNATLLGLRRKELKQRLDKIIEFSELGEFIDEPIRVYSSGMLAKLGFSVITQVD 168
Cdd:PRK10535 83 lrrehfGFifqryHllSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1699326967 169 PDILIIDEVLAVGDISFQRKCLETINEFKKKGVTILFVSHNlRDIEKICDRVIWIEN 225
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRD 218
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
44-242 |
1.79e-08 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 53.14 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 44 LAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVhvVGRVASMLELGGG--FHPELTGRENIRLNATLLG 121
Cdd:PRK15177 1 VVLDKTDFVMGYHEHIGILAAPGSGKTTLTRLLCGLDAPDEGDF--IGLRGDALPLGANsfILPGLTGEENARMMASLYG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 122 LRRKELKQRldkIIEFSELGEFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKCLETIN-EFKKKG 200
Cdd:PRK15177 79 LDGDEFSHF---CYQLTQLEQCYTDRVSEYSVTMKTHLAFAINLLLPCRLYIADGKLYTGDNATQLRMQAALAcQLQQKG 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1699326967 201 VTILfvSHNLRDIEKICDRVIWIENHKMKV---MGEAHSVIAQYK 242
Cdd:PRK15177 156 LIVL--THNPRLIKEHCHAFGVLLHGKITMcedLAQATALFEQYQ 198
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
29-226 |
1.92e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 53.58 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 29 FNPRRALSllsgrsylaieNISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVH-----VVGRVASMLELGGGF 103
Cdd:PRK09544 14 FGQRRVLS-----------DVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKrngklRIGYVPQKLYLDTTL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 104 hpELTGRENIRLNAtllGLRRKELKQRLDKIiefsELGEFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDI 183
Cdd:PRK09544 83 --PLTVNRFLRLRP---GTKKEDILPALKRV----QAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1699326967 184 SFQRKCLETINEFKKK-GVTILFVSHNLRDIEKICDRVIWIENH 226
Cdd:PRK09544 154 NGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNHH 197
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
45-240 |
2.01e-08 |
|
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: 53.00 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGR------VASMLELGGGFHPEL-----TGRENI 113
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIdirdisRKSLRSMIGVVLQDTflfsgTIMENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 114 RLNAtlLGLRRKELKQ-----RLDKIIEFSELG--EFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQ 186
Cdd:cd03254 98 RLGR--PNATDEEVIEaakeaGAHDFIMKLPNGydTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1699326967 187 RKCLETINEFkKKGVTILFVSHNLRDIEKiCDRVIWIENHKMKVMGEAHSVIAQ 240
Cdd:cd03254 176 KLIQEALEKL-MKGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLAK 227
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
26-246 |
2.55e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 53.13 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 26 ELIFNPRRALSLLSGRSYLaiENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRVASM--------- 96
Cdd:PRK14246 8 EDVFNISRLYLYINDKAIL--KDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFgkdifqida 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 97 ----LELGGGFH-----PELTGRENIRLNATLLGLRRKE-----LKQRLDKIIEFSELGEFIDEPIRVYSSGMLAKLGFS 162
Cdd:PRK14246 86 iklrKEVGMVFQqpnpfPHLSIYDNIAYPLKSHGIKEKReikkiVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 163 VITQVDPDILIIDEVLAVGDISFQRKCLETINEFKKKgVTILFVSHNLRDIEKICDRVIWIENHKMKVMGEAHSVIAQYK 242
Cdd:PRK14246 166 RALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPK 244
|
....
gi 1699326967 243 EAMS 246
Cdd:PRK14246 245 NELT 248
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
45-225 |
4.35e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 53.29 E-value: 4.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSS--GSVHVVGR--VASML---ELGG--------GFHPELTG 109
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSplKASNIrdtERAGiviihqelTLVPELSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 110 RENI-----------RLNATLLGLRRKELKQ--RLDKIIEFSELGEfidepirvYSSG--MLAKLGFSVITQVdpDILII 174
Cdd:TIGR02633 96 AENIflgneitlpggRMAYNAMYLRAKNLLRelQLDADNVTRPVGD--------YGGGqqQLVEIAKALNKQA--RLLIL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1699326967 175 DEVLAVGDISFQRKCLETINEFKKKGVTILFVSHNLRDIEKICDRVIWIEN 225
Cdd:TIGR02633 166 DEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRD 216
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
48-223 |
4.81e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 52.92 E-value: 4.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 48 NISFQVKKGESVALIGRNGAGKSTSLGLVAGVMkPSSGSVHVVGRVASMLELGG--------GFHPEL---TGRENIRL- 115
Cdd:PRK11174 368 PLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESwrkhlswvGQNPQLphgTLRDNVLLg 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 116 --NATllglrrkelKQRLDKIIEFSELGEFI-------DEPIRVYSSGM---------LAK-LGfsvitqVDPDILIIDE 176
Cdd:PRK11174 447 npDAS---------DEQLQQALENAWVSEFLpllpqglDTPIGDQAAGLsvgqaqrlaLARaLL------QPCQLLLLDE 511
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1699326967 177 VLAVGDISFQRKCLETINEfKKKGVTILFVSHNLRDIEKiCDRvIWI 223
Cdd:PRK11174 512 PTASLDAHSEQLVMQALNA-ASRRQTTLMVTHQLEDLAQ-WDQ-IWV 555
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
5-240 |
4.88e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 53.10 E-value: 4.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 5 IEFKNVTKRYPlyhhigsgikelifnprralsllsGRSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSS 84
Cdd:PRK11176 342 IEFRNVTFTYP------------------------GKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 85 GSVHVVG------RVASMlelgggfhpeltgRENIRL--------NATL---LGLRRKELKQRlDKIIEFSELG---EFI 144
Cdd:PRK11176 398 GEILLDGhdlrdyTLASL-------------RNQVALvsqnvhlfNDTIannIAYARTEQYSR-EQIEEAARMAyamDFI 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 145 D-----------EPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKCLETINEFKKKGvTILFVSHNLRDI 213
Cdd:PRK11176 464 NkmdngldtvigENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR-TSLVIAHRLSTI 542
|
250 260
....*....|....*....|....*..
gi 1699326967 214 EKiCDRVIWIENHKMKVMGEAHSVIAQ 240
Cdd:PRK11176 543 EK-ADEILVVEDGEIVERGTHAELLAQ 568
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
46-130 |
5.28e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 52.13 E-value: 5.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 46 IENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRVASML-----------ELG--GGFH---PELTG 109
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaakaelrnqKLGfiYQFHhllPDFTA 104
|
90 100
....*....|....*....|.
gi 1699326967 110 RENIRLNATLLGLRRKELKQR 130
Cdd:PRK11629 105 LENVAMPLLIGKKKPAEINSR 125
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
33-99 |
7.63e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 51.85 E-value: 7.63e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1699326967 33 RALSLLSGRsYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRVASMLEL 99
Cdd:PRK11701 10 RGLTKLYGP-RKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDL 75
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
5-232 |
8.68e-08 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 52.42 E-value: 8.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 5 IEFKNVTKRYPlyhhigsgikelifnprralsllsGRSYLAI-ENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPS 83
Cdd:TIGR00958 479 IEFQDVSFSYP------------------------NRPDVPVlKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPT 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 84 SGSVHVVG-------------RVASMlelggGFHPELTG---RENIrlnatLLGLRRKELKQRL---------DKIIEFS 138
Cdd:TIGR00958 535 GGQVLLDGvplvqydhhylhrQVALV-----GQEPVLFSgsvRENI-----AYGLTDTPDEEIMaaakaanahDFIMEFP 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 139 E-LGEFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDIsfqrKCLETINEFKK-KGVTILFVSHNLRDIEKi 216
Cdd:TIGR00958 605 NgYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDA----ECEQLLQESRSrASRTVLLIAHRLSTVER- 679
|
250
....*....|....*.
gi 1699326967 217 CDRVIWIENHKMKVMG 232
Cdd:TIGR00958 680 ADQILVLKKGSVVEMG 695
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
45-224 |
8.95e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 51.81 E-value: 8.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGR-------------VASMLELGGGFhPELTgrE 111
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlvayVPQSEEVDWSF-PVLV--E 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 112 NIRL-----NATLLGLRRKELKQRLDKIIEFSELGEFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQ 186
Cdd:PRK15056 99 DVVMmgrygHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTE 178
|
170 180 190
....*....|....*....|....*....|....*...
gi 1699326967 187 RKCLETINEFKKKGVTILFVSHNLRDIEKICDRVIWIE 224
Cdd:PRK15056 179 ARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVK 216
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
46-239 |
9.81e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 51.24 E-value: 9.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 46 IENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKP----SSGSVHVVGRVASMLELGG------------GFHPELTG 109
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALRGrkiatimqnprsAFNPLHTM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 110 RENIRlnATLLGLRRKELKQRLDKIIEfsELGefIDEPIRV-------YSSGMLAKLGFSVITQVDPDILIIDEVLAVGD 182
Cdd:PRK10418 99 HTHAR--ETCLALGKPADDATLTAALE--AVG--LENAARVlklypfeMSGGMLQRMMIALALLCEAPFIIADEPTTDLD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1699326967 183 ISFQRKCLETINEF-KKKGVTILFVSHNLRDIEKICDRVIWIENHKMKVMGEAHSVIA 239
Cdd:PRK10418 173 VVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFN 230
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
45-233 |
1.02e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 51.66 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKSTSlGLVAGVMKPSSGS------VHVVGRVASMLELGG------GFHPELTGREN 112
Cdd:NF000106 28 AVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGRrpwrf*TWCANRRALRRTIG*hrpvr*GRRESFSGREN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 113 IRLNATLLGLRRKELKQRLDKIIEFSELGEFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKCLET 192
Cdd:NF000106 107 LYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDE 186
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1699326967 193 INEFKKKGVTILFVSHNLRDIEKICDRVIWIENHKMKVMGE 233
Cdd:NF000106 187 VRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGK 227
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-229 |
1.22e-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: 51.75 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 1 MSVAIEFKNVTKRYPlyHHIGSGIKEL-------IFNPRRAlsllsgrsylAIENISFQVKKGESVALIGRNGAGKSTSL 73
Cdd:TIGR02633 236 MMVGREITSLYPHEP--HEIGDVILEArnltcwdVINPHRK----------RVDDVSFSLRRGEILGVAGLVGAGRTELV 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 74 GLVAGVMKPS-SGSVHVVGR------VASMLELGGGFHPELTGRENI------RLNATLLGLRRKELKQRLDKIIEFSEL 140
Cdd:TIGR02633 304 QALFGAYPGKfEGNVFINGKpvdirnPAQAIRAGIAMVPEDRKRHGIvpilgvGKNITLSVLKSFCFKMRIDAAAELQII 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 141 GEFI----------DEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKCLETINEFKKKGVTILFVSHNL 210
Cdd:TIGR02633 384 GSAIqrlkvktaspFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSEL 463
|
250
....*....|....*....
gi 1699326967 211 RDIEKICDRVIWIENHKMK 229
Cdd:TIGR02633 464 AEVLGLSDRVLVIGEGKLK 482
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
45-237 |
1.22e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 51.28 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHV--------------------VGRVASMLElGGGFh 104
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVddtlitstsknkdikqirkkVGLVFQFPE-SQLF- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 105 pELTGRENIRLNATLLGLRRKELKQRLDKIIEFSELGE--FIDEPIRVySSGMLAKLGFSVITQVDPDILIIDEVLAVGD 182
Cdd:PRK13649 100 -EETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISEslFEKNPFEL-SGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1699326967 183 ISFQRKCLETINEFKKKGVTILFVSHNLRDIEKICDRVIWIENHKMKVMGEAHSV 237
Cdd:PRK13649 178 PKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
5-225 |
1.24e-07 |
|
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: 50.57 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 5 IEFKNVTKRYplyhhigsgikelifnpRRALSLlsgrsylAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSS 84
Cdd:cd03244 3 IEFKNVSLRY-----------------RPNLPP-------VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSS 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 85 GSVHVVGRVASMLELgggfhpeLTGRENI--------------RLNATLLGLRRKElkqRLDKIIEFSELGEFIDEPI-- 148
Cdd:cd03244 59 GSILIDGVDISKIGL-------HDLRSRIsiipqdpvlfsgtiRSNLDPFGEYSDE---ELWQALERVGLKEFVESLPgg 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 149 ---RVYSSGmlakLGFSV-ITQV---------DPDILIIDEVLAVGDISFQRKCLETI-NEFkkKGVTILFVSHNLRDIE 214
Cdd:cd03244 129 ldtVVEEGG----ENLSVgQRQLlclarallrKSKILVLDEATASVDPETDALIQKTIrEAF--KDCTVLTIAHRLDTII 202
|
250
....*....|.
gi 1699326967 215 KiCDRVIWIEN 225
Cdd:cd03244 203 D-SDRILVLDK 212
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
34-182 |
1.26e-07 |
|
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: 50.57 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 34 ALSLLSGRSYLAI-ENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGR---------VASMLELG--G 101
Cdd:cd03231 3 ADELTCERDGRALfSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGpldfqrdsiARGLLYLGhaP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 102 GFHPELTGRENIRLNATLLGlrRKELKQRLDKIiefsELGEFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVG 181
Cdd:cd03231 83 GIKTTLSVLENLRFWHADHS--DEQVEEALARV----GLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
.
gi 1699326967 182 D 182
Cdd:cd03231 157 D 157
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
46-235 |
1.32e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.54 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 46 IENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGR--------------VASMLE--LGGGFHPELTG 109
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHevvtrspqdglangIVYISEdrKRDGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 110 RENIRLNA------TLLGLRRKELKQRLDKIIE-FSELGEFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGD 182
Cdd:PRK10762 348 KENMSLTAlryfsrAGGSLKHADEQQAVSDFIRlFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1699326967 183 ISFQRKCLETINEFKKKGVTILFVSHNLRDIEKICDRVIwienhkmkVMGEAH 235
Cdd:PRK10762 428 VGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRIL--------VMHEGR 472
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-89 |
1.37e-07 |
|
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: 51.86 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 5 IEFKNVTKRYplyhhigsGIKELifnprralsllsgrsylaIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSS 84
Cdd:TIGR03719 323 IEAENLTKAF--------GDKLL------------------IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDS 376
|
....*
gi 1699326967 85 GSVHV 89
Cdd:TIGR03719 377 GTIEI 381
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-221 |
1.40e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 51.71 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 1 MSVAIEFKNvtkRYP-LYHHIGSGIKELIFNPRRalslLSGRSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGV 79
Cdd:PRK09700 240 LMVGRELQN---RFNaMKENVSNLAHETVFEVRN----VTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGV 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 80 MKPSSGSVHVVGRVAS------MLELG----------GGFHPELTGRENIRLNATL--------LGL--RRKELK----Q 129
Cdd:PRK09700 313 DKRAGGEIRLNGKDISprspldAVKKGmayitesrrdNGFFPNFSIAQNMAISRSLkdggykgaMGLfhEVDEQRtaenQ 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 130 RLDKIIEFSELGEFIDEpirvYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKCLETINEFKKKGVTILFVSHN 209
Cdd:PRK09700 393 RELLALKCHSVNQNITE----LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSE 468
|
250
....*....|..
gi 1699326967 210 LRDIEKICDRVI 221
Cdd:PRK09700 469 LPEIITVCDRIA 480
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
60-232 |
1.57e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 51.41 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 60 ALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRVASMLELGGGFHPEltgRENI-------RL--NATLLG-LR---RKE 126
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLPPE---KRRIgyvfqdaRLfpHYKVRGnLRygmAKS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 127 LKQRLDKIIEFSELGEFID---------EPIRVyssgmlaKLGFSVITqvDPDILIIDEVLAVGDISFQRKCL------- 190
Cdd:PRK11144 105 MVAQFDKIVALLGIEPLLDrypgslsggEKQRV-------AIGRALLT--APELLLMDEPLASLDLPRKRELLpylerla 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1699326967 191 ETINefkkkgVTILFVSHNLRDIEKICDRVIWIENHKMKVMG 232
Cdd:PRK11144 176 REIN------IPILYVSHSLDEILRLADRVVVLEQGKVKAFG 211
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-221 |
1.62e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 51.12 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 1 MSVAIEFKNVTKRYPlyhhigsgIKELIFNPRRALSLLSGrsylaienISFQVKKGESVALIGRNGAGKSTSLGLVAGVM 80
Cdd:PRK11308 2 QQPLLQAIDLKKHYP--------VKRGLFKPERLVKALDG--------VSFTLERGKTLAVVGESGCGKSTLARLLTMIE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 81 KPSSGSVHVVGRvasmlelgggfhpeltgrenirlnaTLLGLRRKELKQRLDKI-IEFS----------ELGEFIDEPIR 149
Cdd:PRK11308 66 TPTGGELYYQGQ-------------------------DLLKADPEAQKLLRQKIqIVFQnpygslnprkKVGQILEEPLL 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 150 VYSS-----------GMLAKLG------------FS-------VITQ---VDPDILIIDEVLAVGDISFQRKCLETINEF 196
Cdd:PRK11308 121 INTSlsaaerrekalAMMAKVGlrpehydryphmFSggqrqriAIARalmLDPDVVVADEPVSALDVSVQAQVLNLMMDL 200
|
250 260
....*....|....*....|....*.
gi 1699326967 197 KKK-GVTILFVSHNLRDIEKICDRVI 221
Cdd:PRK11308 201 QQElGLSYVFISHDLSVVEHIADEVM 226
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
5-237 |
1.74e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 50.91 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 5 IEFKNVTKRYplyhhigsgikelifnprralsllSGRSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSS 84
Cdd:PRK13648 8 IVFKNVSFQY------------------------QSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKS 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 85 GSVHVVGRVAS---MLELGGGFHPELTGRENIRLNATL-----LGLRR-----KELKQRLDKIIEFSELGEFIDEPIRVY 151
Cdd:PRK13648 64 GEIFYNNQAITddnFEKLRKHIGIVFQNPDNQFVGSIVkydvaFGLENhavpyDEMHRRVSEALKQVDMLERADYEPNAL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 152 SSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKCLETINEFK-KKGVTILFVSHNLRDIEKiCDRVIWIENHKMKV 230
Cdd:PRK13648 144 SGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKsEHNITIISITHDLSEAME-ADHVIVMNKGTVYK 222
|
....*..
gi 1699326967 231 MGEAHSV 237
Cdd:PRK13648 223 EGTPTEI 229
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-89 |
2.52e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.89 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 2 SVAIEFKNVTKRYplyhhigsGIKELifnprralsllsgrsylaIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMK 81
Cdd:PRK11819 322 DKVIEAENLSKSF--------GDRLL------------------IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQ 375
|
....*...
gi 1699326967 82 PSSGSVHV 89
Cdd:PRK11819 376 PDSGTIKI 383
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
44-221 |
2.70e-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: 49.96 E-value: 2.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 44 LAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVM---KPSSGSVHVVGR---------VASMLELGGGFHPELTGRE 111
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQprkpdqfqkCVAYVRQDDILLPGLTVRE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 112 NIRLNATLLGLRRKELKQRlDKIIEFSELGEFIDEPIRVY-----SSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQ 186
Cdd:cd03234 101 TLTYTAILRLPRKSSDAIR-KKRVEDVLLRDLALTRIGGNlvkgiSGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTA 179
|
170 180 190
....*....|....*....|....*....|....*.
gi 1699326967 187 RKCLETINEFKKKGVTILFVSHNLR-DIEKICDRVI 221
Cdd:cd03234 180 LNLVSTLSQLARRNRIVILTIHQPRsDLFRLFDRIL 215
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
45-220 |
2.84e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.88 E-value: 2.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRVASM------LELGGGF-HPEL------TGRE 111
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFksskeaLENGISMvHQELnlvlqrSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 112 NIRLNA-TLLGLRRKELKQRLDKIIEFSELGEFIDEPIRVyssgmlAKLGFSVITQV--------DPDILIIDEVLAvgd 182
Cdd:PRK10982 93 NMWLGRyPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKV------ATLSVSQMQMIeiakafsyNAKIVIMDEPTS--- 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1699326967 183 iSFQRKCLE----TINEFKKKGVTILFVSHNLRDIEKICDRV 220
Cdd:PRK10982 164 -SLTEKEVNhlftIIRKLKERGCGIVYISHKMEEIFQLCDEI 204
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
54-210 |
3.52e-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: 50.55 E-value: 3.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 54 KKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRVASMLElgggfhpELTGREnirLNATLLGLRRKELK----- 128
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPSWDEVLK-------RFRGTE---LQDYFKKLANGEIKvahkp 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 129 Q------------------------RLDKIIEFSELGEFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDIs 184
Cdd:COG1245 167 QyvdlipkvfkgtvrellekvdergKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI- 245
|
170 180
....*....|....*....|....*..
gi 1699326967 185 FQR-KCLETINEFKKKGVTILFVSHNL 210
Cdd:COG1245 246 YQRlNVARLIRELAEEGKYVLVVEHDL 272
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
45-221 |
5.35e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 50.09 E-value: 5.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKSTSlGLVAGVMKPSSGSV-------HVVGRvASMLEL-----------GGGFHPE 106
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTT-GLALLRLINSQGEIwfdgqplHNLNR-RQLLPVrhriqvvfqdpNSSLNPR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 107 LTGRENIrlnATLLGLRRKEL--KQRLDKIIE-FSELGefIDEPIR-----VYSSGMLAKLGFSVITQVDPDILIIDEVL 178
Cdd:PRK15134 379 LNVLQII---EEGLRVHQPTLsaAQREQQVIAvMEEVG--LDPETRhrypaEFSGGQRQRIAIARALILKPSLIILDEPT 453
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1699326967 179 AVGDISFQRKCLETINEFKKK-GVTILFVSHNLRDIEKICDRVI 221
Cdd:PRK15134 454 SSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVI 497
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
45-221 |
7.70e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 48.86 E-value: 7.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKSTSL----GLVAGVMKPSS------GSVHVVGRVA-----SMLELGGGFHP---- 105
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsGLITGDKSAGShiellgRTVQREGRLArdirkSRANTGYIFQQfnlv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 106 -ELTGRENIRLNA--------TLLGLRRKELKQRLDKIIEFSELGEFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDE 176
Cdd:PRK09984 99 nRLSVLENVLIGAlgstpfwrTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1699326967 177 VLAVGDISFQRKCLETINEFKKK-GVTILFVSHNLRDIEKICDRVI 221
Cdd:PRK09984 179 PIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIV 224
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
5-224 |
8.20e-07 |
|
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: 48.62 E-value: 8.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 5 IEFKNVTKRYPlyhhigsgikelifnpRRALSLLsgrsylaIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSS 84
Cdd:cd03248 12 VKFQNVTFAYP----------------TRPDTLV-------LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 85 GSVHVVGRVASMLE--------LGGGFHPELTGR---ENIRLNATLLGLRR-KELKQRL---DKIIEF-SELGEFIDEPI 148
Cdd:cd03248 69 GQVLLDGKPISQYEhkylhskvSLVGQEPVLFARslqDNIAYGLQSCSFECvKEAAQKAhahSFISELaSGYDTEVGEKG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1699326967 149 RVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKCLETINEFKKKgVTILFVSHNLRDIEKiCDRVIWIE 224
Cdd:cd03248 149 SQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPER-RTVLVIAHRLSTVER-ADQILVLD 222
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
40-225 |
1.13e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 48.93 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 40 GRSYLAIENISFQVKKGESVALIGRNGAGKS-TSLGlvagVMK--PSSGSVHVVGRV----ASMLELGggfHPELTG-RE 111
Cdd:PRK15134 19 QTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALS----ILRllPSPPVVYPSGDIrfhgESLLHAS---EQTLRGvRG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 112 N----------IRLN---------ATLL----GLRRK----ELKQRLDKIIEFSELGEFIDEPIRVySSG-----MLAkl 159
Cdd:PRK15134 92 NkiamifqepmVSLNplhtlekqlYEVLslhrGMRREaargEILNCLDRVGIRQAAKRLTDYPHQL-SGGerqrvMIA-- 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1699326967 160 gFSVITQvdPDILIIDEVLAVGDISFQRKCLETINEFKKK-GVTILFVSHNLRDIEKICDRVIWIEN 225
Cdd:PRK15134 169 -MALLTR--PELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQN 232
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
52-221 |
1.24e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 48.65 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 52 QVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRVAsmlelgggFHP-------ELTGRENIRLNATLLG--L 122
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKIS--------YKPqyikpdyDGTVEDLLRSITDDLGssY 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 123 RRKELKQRLDkiiefseLGEFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKCLETINEF-KKKGV 201
Cdd:PRK13409 433 YKSEIIKPLQ-------LERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIaEEREA 505
|
170 180
....*....|....*....|
gi 1699326967 202 TILFVSHNLRDIEKICDRVI 221
Cdd:PRK13409 506 TALVVDHDIYMIDYISDRLM 525
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
43-231 |
1.27e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 48.47 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 43 YLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVhVVG--RVASML-----------ELGGGFH-PEL- 107
Cdd:PRK13645 24 FKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQT-IVGdyAIPANLkkikevkrlrkEIGLVFQfPEYq 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 108 ----TGRENIRLNATLLGLRRKELKQRLDKIIEFSELG-EFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLA--- 179
Cdd:PRK13645 103 lfqeTIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPeDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGgld 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1699326967 180 -VGDISFQRKCLETINEFKKKgvtILFVSHNLRDIEKICDRVIWIenHKMKVM 231
Cdd:PRK13645 183 pKGEEDFINLFERLNKEYKKR---IIMVTHNMDQVLRIADEVIVM--HEGKVI 230
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
5-232 |
1.42e-06 |
|
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: 47.92 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 5 IEFKNVTKRYPlyhhigsgikelifnprralsllSGRSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSS 84
Cdd:cd03249 1 IEFKNVSFRYP-----------------------SRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTS 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 85 GSVHVVGRVASMLELGG-----GF---HPEL---TGRENIRlnatlLGLRRKELKQRlDKIIEFSELGEFIDE-PIRVYS 152
Cdd:cd03249 58 GEILLDGVDIRDLNLRWlrsqiGLvsqEPVLfdgTIAENIR-----YGKPDATDEEV-EEAAKKANIHDFIMSlPDGYDT 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 153 sgMLAKLGFS---------VITQV---DPDILIIDEVLAVGDISFQRKCLETINEFkKKGVTILFVSHNLRDIEKiCDRV 220
Cdd:cd03249 132 --LVGERGSQlsggqkqriAIARAllrNPKILLLDEATSALDAESEKLVQEALDRA-MKGRTTIVIAHRLSTIRN-ADLI 207
|
250
....*....|..
gi 1699326967 221 IWIENHKMKVMG 232
Cdd:cd03249 208 AVLQNGQVVEQG 219
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
52-221 |
1.44e-06 |
|
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: 48.63 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 52 QVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRVAsmlelgggFHP-------ELTGRENIrlnatllglrR 124
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKIS--------YKPqyispdyDGTVEEFL----------R 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 125 KELKQRLDKIIEFSE------LGEFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISfQR----KCLETIN 194
Cdd:COG1245 424 SANTDDFGSSYYKTEiikplgLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE-QRlavaKAIRRFA 502
|
170 180
....*....|....*....|....*..
gi 1699326967 195 EfkKKGVTILFVSHNLRDIEKICDRVI 221
Cdd:COG1245 503 E--NRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
6-220 |
1.47e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 48.63 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 6 EFKNVTKRYPlyhhigsGIKelifnprralsllsgrsylAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSS- 84
Cdd:NF040905 3 EMRGITKTFP-------GVK-------------------ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSy 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 85 -GSVHVVGRVASmlelgggFH--------------------PELTGRENIRL------------NATLlgLRRKELkqrL 131
Cdd:NF040905 57 eGEILFDGEVCR-------FKdirdsealgiviihqelaliPYLSIAENIFLgnerakrgvidwNETN--RRAREL---L 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 132 DKIiefsELGEFIDEPIRVYSSGM---------LAKlgfsvitqvDPDILIIDEVLAVGDISFQRKCLETINEFKKKGVT 202
Cdd:NF040905 125 AKV----GLDESPDTLVTDIGVGKqqlveiakaLSK---------DVKLLILDEPTAALNEEDSAALLDLLLELKAQGIT 191
|
250
....*....|....*...
gi 1699326967 203 ILFVSHNLRDIEKICDRV 220
Cdd:NF040905 192 SIIISHKLNEIRRVADSI 209
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
45-221 |
1.57e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 48.70 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKS-TSLGLVAgVMKPSSGSVHVVGRV----------------ASMLELGGG----- 102
Cdd:PRK10261 31 AVRNLSFSLQRGETLAIVGESGSGKSvTALALMR-LLEQAGGLVQCDKMLlrrrsrqvielseqsaAQMRHVRGAdmami 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 103 FHPELTG-----------RENIRLNAtllGLRRK----ELKQRLDKiIEFSELGEFIDEPIRVYSSGMLAKLGFSVITQV 167
Cdd:PRK10261 110 FQEPMTSlnpvftvgeqiAESIRLHQ---GASREeamvEAKRMLDQ-VRIPEAQTILSRYPHQLSGGMRQRVMIAMALSC 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1699326967 168 DPDILIIDEVLAVGDISFQRKCLETINEFKKK-GVTILFVSHNLRDIEKICDRVI 221
Cdd:PRK10261 186 RPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVL 240
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
46-87 |
1.93e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 48.35 E-value: 1.93e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1699326967 46 IENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSV 87
Cdd:PRK15064 335 FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
49-208 |
1.97e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 48.04 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 49 ISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRVASMLELGG----------GFHP--ELTGRENIRLN 116
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDyrklfsavftDFHLfdQLLGPEGKPAN 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 117 ATLLG--LRRKELKQRLdkiiEFSElGEFIDepIRVySSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKC-LETI 193
Cdd:PRK10522 422 PALVEkwLERLKMAHKL----ELED-GRISN--LKL-SKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFyQVLL 493
|
170
....*....|....*
gi 1699326967 194 NEFKKKGVTILFVSH 208
Cdd:PRK10522 494 PLLQEMGKTIFAISH 508
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
47-237 |
2.20e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 47.45 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 47 ENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVG---------------RVASMLELGGGFHPELTG-- 109
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGenipamsrsrlytvrKRMSMLFQSGALFTDMNVfd 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 110 ------RENIRLNATLLglrRKELKQRLDKI-------IEFSELgefidepirvySSGMLAKLGFSVITQVDPDILIIDE 176
Cdd:PRK11831 104 nvayplREHTQLPAPLL---HSTVMMKLEAVglrgaakLMPSEL-----------SGGMARRAALARAIALEPDLIMFDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1699326967 177 VLAVGDISFQRKCLETINEFKKK-GVTILFVSHNLRDIEKICDRVIWIENHKMKVMGEAHSV 237
Cdd:PRK11831 170 PFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
48-209 |
2.37e-06 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 47.72 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 48 NISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVG----------RVASMLELGGGFHPELTGRENIRLNA 117
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEkrmndvppaeRGVGMVFQSYALYPHLSVAENMSFGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 118 TLLGLRRKELKQRLDKIIEFSELGEFIDEPIRVYSSGMLAK--LGFSVITQvdPDILIIDEVLAVGDISFQRKCLETINE 195
Cdd:PRK11000 101 KLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRvaIGRTLVAE--PSVFLLDEPLSNLDAALRVQMRIEISR 178
|
170
....*....|....*
gi 1699326967 196 FKKK-GVTILFVSHN 209
Cdd:PRK11000 179 LHKRlGRTMIYVTHD 193
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
45-221 |
2.48e-06 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 47.63 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRVASML-----ELGGGFH-----PELTGRENIR 114
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVpaenrHVNTVFQsyalfPHMTVFENVA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 115 lnatlLGLR-----RKELKQRLDKIIEFSELGEFIDEPIRVYSSGM-----LAKlgfSVITQvdPDILIIDEVLAVGDIS 184
Cdd:PRK09452 109 -----FGLRmqktpAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQqqrvaIAR---AVVNK--PKVLLLDESLSALDYK 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1699326967 185 FqRKCLEtiNEFK----KKGVTILFVSHNLRDIEKICDRVI 221
Cdd:PRK09452 179 L-RKQMQ--NELKalqrKLGITFVFVTHDQEEALTMSDRIV 216
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
47-221 |
2.97e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 47.60 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 47 ENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRVASM------LELGGGFHPE----------LTGR 110
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIrsprdaIRAGIMLCPEdrkaegiipvHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 111 ENIRLNAtllglRRKELKQR--LDKIIEFSELGEFI----------DEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVL 178
Cdd:PRK11288 350 DNINISA-----RRHHLRAGclINNRWEAENADRFIrslniktpsrEQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPT 424
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1699326967 179 AVGDISFQRKCLETINEFKKKGVTILFVSHNLRDIEKICDRVI 221
Cdd:PRK11288 425 RGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIV 467
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
46-192 |
3.61e-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: 47.60 E-value: 3.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 46 IENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRVAsmlelgggFHPEL------TGRENIrlnatL 119
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRIS--------FSPQTswimpgTIKDNI-----I 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 120 LGLRRKELKQRldKIIEFSELGEFID-----------EPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRK 188
Cdd:TIGR01271 509 FGLSYDEYRYT--SVIKACQLEEDIAlfpekdktvlgEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKE 586
|
....
gi 1699326967 189 CLET 192
Cdd:TIGR01271 587 IFES 590
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
49-179 |
4.05e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 46.38 E-value: 4.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 49 ISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRVAS-------MLELG--GGFHPELTGRENIRLNATL 119
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATrgdrsrfMAYLGhlPGLKADLSTLENLHFLCGL 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 120 LGLRRKELKQRLDKIIefsELGEFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLA 179
Cdd:PRK13543 110 HGRRAKQMPGSALAIV---GLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYA 166
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
45-219 |
4.25e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 46.69 E-value: 4.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKSTSLGLV--AGVMKPS---SGSVHVVGR---------VASMLELGGGFH-PE--- 106
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHniysprtdtVDLRKEIGMVFQqPNpfp 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 107 LTGRENIrlnatLLGLRRKEL--KQRLDKIIEFSELGEFIDEPI--RVYSS------GMLAKLGFSVITQVDPDILIIDE 176
Cdd:PRK14239 100 MSIYENV-----VYGLRLKGIkdKQVLDEAVEKSLKGASIWDEVkdRLHDSalglsgGQQQRVCIARVLATSPKIILLDE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1699326967 177 VLAVGDISFQRKCLETINEFKKKgVTILFVSHNLRDIEKICDR 219
Cdd:PRK14239 175 PTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDR 216
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
46-94 |
6.02e-06 |
|
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: 46.39 E-value: 6.02e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1699326967 46 IENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRVA 94
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRIS 101
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
46-216 |
6.42e-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: 45.60 E-value: 6.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 46 IENISFQVKKGESVALIGRNGAGKSTSLGLVAGVM--KPSSGSVHVVGRVASMLE--------LGGGFH--PELTGREN- 112
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPpeerarlgIFLAFQypPEIPGVKNa 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 113 --IR-LNATLLGLRRK--ELKQrldkiiefselgefidepirvyssgMLAklgfsvitqVDPDILIIDEVLAVGDISFQR 187
Cdd:cd03217 96 dfLRyVNEGFSGGEKKrnEILQ-------------------------LLL---------LEPDLAILDEPDSGLDIDALR 141
|
170 180
....*....|....*....|....*....
gi 1699326967 188 KCLETINEFKKKGVTILFVSHNLRDIEKI 216
Cdd:cd03217 142 LVAEVINKLREEGKSVLIITHYQRLLDYI 170
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
46-233 |
7.14e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 46.46 E-value: 7.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 46 IENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMK-PSSGSVHVVGRVASM------LELGGGFHPELTGRENIRL--- 115
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIrnpqqaIAQGIAMVPEDRKRDGIVPvmg 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 116 ---NATLLGLRRKELKQRLDKIIEFSELGEFIDEpIRV-YSSGMLAKLGFS-------VITQ---VDPDILIIDEVLAVG 181
Cdd:PRK13549 358 vgkNITLAALDRFTGGSRIDDAAELKTILESIQR-LKVkTASPELAIARLSggnqqkaVLAKcllLNPKILILDEPTRGI 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1699326967 182 DISFQRKCLETINEFKKKGVTILFVSHNLRDIEKICDRVIwienhkmkVMGE 233
Cdd:PRK13549 437 DVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVL--------VMHE 480
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
44-176 |
7.90e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.39 E-value: 7.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 44 LAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSV----HVVGRVASMLELGGgfhPELTGRENIRLNATL 119
Cdd:PLN03073 523 LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVfrsaKVRMAVFSQHHVDG---LDLSSNPLLYMMRCF 599
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1699326967 120 LGLRRKELKQRLDkiiEFSELGEFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDE 176
Cdd:PLN03073 600 PGVPEQKLRAHLG---SFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDE 653
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
46-218 |
7.93e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 45.80 E-value: 7.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 46 IENISFQVKKGESVALIGRNGAGKSTSLGLVaGVMKPSSGSVHVVGRV--------------------ASMLELGGGFHP 105
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGRVeffnqniyerrvnlnrlrrqVSMVHPKPNLFP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 106 eLTGRENIRLNATLLGLRRK-ELKQRLDKIIEFSELGEFIDEPIRV----YSSGMLAKLGFSVITQVDPDILIIDEVLAV 180
Cdd:PRK14258 102 -MSVYDNVAYGVKIVGWRPKlEIDDIVESALKDADLWDEIKHKIHKsaldLSGGQQQRLCIARALAVKPKVLLMDEPCFG 180
|
170 180 190
....*....|....*....|....*....|....*....
gi 1699326967 181 GDISFQRKCLETINEFK-KKGVTILFVSHNLRDIEKICD 218
Cdd:PRK14258 181 LDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSD 219
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
41-220 |
1.01e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 46.00 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 41 RSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRVASMLELG-----------------GGF 103
Cdd:PRK10261 335 REVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGklqalrrdiqfifqdpyASL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 104 HPELTG----RENIRLNATLLGlrrKELKQRLDKIIEfsELGEFIDEPIRV---YSSGMLAKLGFSVITQVDPDILIIDE 176
Cdd:PRK10261 415 DPRQTVgdsiMEPLRVHGLLPG---KAAAARVAWLLE--RVGLLPEHAWRYpheFSGGQRQRICIARALALNPKVIIADE 489
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1699326967 177 VLAVGDISFQRKCLETINEFKKK-GVTILFVSHNLRDIEKICDRV 220
Cdd:PRK10261 490 AVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRV 534
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
46-237 |
1.08e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 45.22 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 46 IENISFQVKKGESVALIGRNGAGKSTSL------------GLVAG--------VMKPSSGSVHVVGRVASMLELGGGFhP 105
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLrtfnrllelneeARVEGevrlfgrnIYSPDVDPIEVRREVGMVFQYPNPF-P 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 106 ELTGRENIRLNATLLGL--RRKELKQRLDKIIEFSELGEFIDEPIRVY----SSGMLAKLGFSVITQVDPDILIIDEVLA 179
Cdd:PRK14267 99 HLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALWDEVKDRLNDYpsnlSGGQRQRLVIARALAMKPKILLMDEPTA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1699326967 180 VGDISFQRKCLETINEFKKKgVTILFVSHNLRDIEKICDRVIWIENHKMKVMGEAHSV 237
Cdd:PRK14267 179 NIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKV 235
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
55-225 |
1.12e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 44.29 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 55 KGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVhvvgrvasmlelgggfhpeltgrenIRLNATllglrrkelkqRLDKI 134
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV-------------------------IYIDGE-----------DILEE 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 135 IEFSELGEFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGD------ISFQRKCLETINEFKKKGVTILFVSH 208
Cdd:smart00382 45 VLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDaeqealLLLLEELRLLLLLKSEKNLTVILTTN 124
|
170 180
....*....|....*....|..
gi 1699326967 209 NLRDIEKIC-----DRVIWIEN 225
Cdd:smart00382 125 DEKDLGPALlrrrfDRRIVLLL 146
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
46-216 |
1.67e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 44.63 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 46 IENISFQVKKGESVALIGRNGAGKSTSLGLVAGvmKPS----SGSVHVVGRvaSMLELgggfHPELTGRENIRL------ 115
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGE--SILDL----EPEERAHLGIFLafqypi 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 116 ------NATLLGL----RRKELKQRLDKIIEFSELgefIDEPIRVYssGMLAKL-------GFS-------VITQ---VD 168
Cdd:CHL00131 95 eipgvsNADFLRLaynsKRKFQGLPELDPLEFLEI---INEKLKLV--GMDPSFlsrnvneGFSggekkrnEILQmalLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1699326967 169 PDILIIDEVLAVGDISFQRKCLETINEFKKKGVTILFVSHNLRDIEKI 216
Cdd:CHL00131 170 SELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDYI 217
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
44-236 |
1.94e-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: 44.71 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 44 LAIENISFqvKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRVASmlelgggFHP-ELTGRENIRLNATLLGL 122
Cdd:cd03237 15 LEVEGGSI--SESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-------YKPqYIKADYEGTVRDLLSSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 123 RRK--ELKQRLDKIIEFSELGEFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDiSFQR----KCLETINEF 196
Cdd:cd03237 86 TKDfyTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD-VEQRlmasKVIRRFAEN 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1699326967 197 KKKgvTILFVSHNLRDIEKICDRVIWIENhKMKVMGEAHS 236
Cdd:cd03237 165 NEK--TAFVVEHDIIMIDYLADRLIVFEG-EPSVNGVANP 201
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
33-218 |
2.14e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 44.39 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 33 RALSLLSGrSYLAIENISFQVKKGESVALIGRNGAGKSTSL-------GLVAG-------------VMKPSSGSVHVVGR 92
Cdd:PRK14243 14 ENLNVYYG-SFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlnDLIPGfrvegkvtfhgknLYAPDVDPVEVRRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 93 VASMLELGGGFHPELtgRENIRLNATLLGlrrkeLKQRLDKIIEFS--------ELGEFIDEPIRVYSSGMLAKLGFSVI 164
Cdd:PRK14243 93 IGMVFQKPNPFPKSI--YDNIAYGARING-----YKGDMDELVERSlrqaalwdEVKDKLKQSGLSLSGGQQQRLCIARA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1699326967 165 TQVDPDILIIDEVLAVGDISFQRKCLETINEFKKKgVTILFVSHNLRDIEKICD 218
Cdd:PRK14243 166 IAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSD 218
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
58-177 |
2.52e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 43.71 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 58 SVALI-GRNGAGKSTSLGLVAGVMKPSSGSVHV------------VGRVASMLelggGFHPELTGRENIRLNATLLglrr 124
Cdd:PRK13541 27 AITYIkGANGCGKSSLLRMIAGIMQPSSGNIYYkncninniakpyCTYIGHNL----GLKLEMTVFENLKFWSEIY---- 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1699326967 125 kELKQRLDKIIEFSELGEFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEV 177
Cdd:PRK13541 99 -NSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEV 150
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
45-221 |
2.73e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 44.33 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKSTS----LGLVA--GVMkpsSGSVHVVGRvaSMLELgggfhPEltgRENIRLNA- 117
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTafalMGLLAanGRI---GGSATFNGR--EILNL-----PE---KELNKLRAe 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 118 ----------TLLG--LRRKE-------LKQRLDKIIEFSELGEFID--------EPIRVY----SSGMLAKLGFSVITQ 166
Cdd:PRK09473 98 qismifqdpmTSLNpyMRVGEqlmevlmLHKGMSKAEAFEESVRMLDavkmpearKRMKMYphefSGGMRQRVMIAMALL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1699326967 167 VDPDILIIDEVLAVGDISFQRKCLETINEFKKK-GVTILFVSHNLRDIEKICDRVI 221
Cdd:PRK09473 178 CRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVL 233
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
46-164 |
3.15e-05 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 43.39 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 46 IENISFQVKKGESVALIGRNGAGKSTSLGLVA-----GVMKpssGSVHVVG--------RVASMLELGGGFHPELTGREN 112
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAgrktaGVIT---GEILINGrpldknfqRSTGYVEQQDVHSPNLTVREA 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1699326967 113 IRLNATLLGLRRKElKQRLDKIIEFSELGE--FIDEPirvySSGMLAKLGFSVI 164
Cdd:cd03232 100 LRFSALLRGLSVEQ-RKRLTIGVELAAKPSilFLDEP----TSGLDSQAAYNIV 148
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
49-243 |
3.49e-05 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 43.97 E-value: 3.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 49 ISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHV------------------------VGRVASMLELgggfH 104
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidtarslsqqkglirqlrqhVGFVFQNFNL----F 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 105 PELTGRENIRLNATLL-GLRRKELKQRLDKIIEFSELGEFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDI 183
Cdd:PRK11264 98 PHRTVLENIIEGPVIVkGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDP 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 184 SFQRKCLETINEFKKKGVTILFVSHNLRDIEKICDRVIWIENHKMKVMGEAHSVIAQYKE 243
Cdd:PRK11264 178 ELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQ 237
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
4-145 |
3.92e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 44.06 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 4 AIEFKNVTKRYPlyhhigSGIKelifnprralsllsgrsylAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPS 83
Cdd:PRK11650 3 GLKLQAVRKSYD------GKTQ-------------------VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERIT 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 84 SGSVHVVGRVASMLE--------------LgggfHPELTGREN------IRlnatllGLRRKELKQRLDKIIEFSELGEF 143
Cdd:PRK11650 58 SGEIWIGGRVVNELEpadrdiamvfqnyaL----YPHMSVRENmayglkIR------GMPKAEIEERVAEAARILELEPL 127
|
..
gi 1699326967 144 ID 145
Cdd:PRK11650 128 LD 129
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
47-89 |
4.76e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.11 E-value: 4.76e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1699326967 47 ENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHV 89
Cdd:PRK15064 18 ENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSL 60
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
53-210 |
7.02e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 43.64 E-value: 7.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 53 VKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVH-------VVGRVASMlELGGGFHpELTGREnIR----------L 115
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEeepswdeVLKRFRGT-ELQNYFK-KLYNGE-IKvvhkpqyvdlI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 116 NATLLGLRRKELKQ-----RLDKIIEFSELGEFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDIsFQR-KC 189
Cdd:PRK13409 173 PKVFKGKVRELLKKvdergKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDI-RQRlNV 251
|
170 180
....*....|....*....|.
gi 1699326967 190 LETINEFkKKGVTILFVSHNL 210
Cdd:PRK13409 252 ARLIREL-AEGKYVLVVEHDL 271
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
25-176 |
7.35e-05 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 43.50 E-value: 7.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 25 KELIFNPRRALSLLSGRSYLaIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPS---SGSVHVVGRV--ASMLEL 99
Cdd:TIGR00955 21 KQLVSRLRGCFCRERPRKHL-LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPidAKEMRA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 100 GGG-------FHPELTGRENIRLNATLLGLRR---KELKQRLDKIIEFSELGE----FIDEPIRVY--SSGMLAKLGFSV 163
Cdd:TIGR00955 100 ISAyvqqddlFIPTLTVREHLMFQAHLRMPRRvtkKEKRERVDEVLQALGLRKcantRIGVPGRVKglSGGERKRLAFAS 179
|
170
....*....|...
gi 1699326967 164 ITQVDPDILIIDE 176
Cdd:TIGR00955 180 ELLTDPPLLFCDE 192
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
53-210 |
8.33e-05 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 42.74 E-value: 8.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 53 VKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRVASMLEL--GGGFHPELTGRENIRLNA------------- 117
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDEILDEfrGSELQNYFTKLLEGDVKVivkpqyvdlipka 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 118 ----TLLGLRRKELKQRLDKIIEFSELGEFIDEPIRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKCLETI 193
Cdd:cd03236 103 vkgkVGELLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLI 182
|
170
....*....|....*..
gi 1699326967 194 NEFKKKGVTILFVSHNL 210
Cdd:cd03236 183 RELAEDDNYVLVVEHDL 199
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
35-88 |
1.12e-04 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 41.37 E-value: 1.12e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1699326967 35 LSLLSGRSYLAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVH 88
Cdd:cd03223 6 LSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG 59
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
46-147 |
2.71e-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: 41.84 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 46 IENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVV-GRVASMLELGGGFHPELTGRENIrlnatLLGLRr 124
Cdd:TIGR03719 21 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQpGIKVGYLPQEPQLDPTKTVRENV-----EEGVA- 94
|
90 100
....*....|....*....|...
gi 1699326967 125 kELKQRLDkiiEFSELGEFIDEP 147
Cdd:TIGR03719 95 -EIKDALD---RFNEISAKYAEP 113
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
40-73 |
3.39e-04 |
|
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: 41.82 E-value: 3.39e-04
10 20 30
....*....|....*....|....*....|....
gi 1699326967 40 GRSYLaiENISFQVKKGESVALIGRNGAGKSTSL 73
Cdd:TIGR01271 1231 GRAVL--QDLSFSVEGGQRVGLLGRTGSGKSTLL 1262
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
46-240 |
5.67e-04 |
|
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: 41.08 E-value: 5.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 46 IENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGRVAsmlelgggFHPELTGRENIRLNATLL---GL 122
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVA--------YVPQQAWIQNDSLRENILfgkAL 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 123 RRKELKQRLD--------KIIEFSELGEFIDEPIRVySSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKCLETI- 193
Cdd:TIGR00957 726 NEKYYQQVLEacallpdlEILPSGDRTEIGEKGVNL-SGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVi 804
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1699326967 194 -NEFKKKGVTILFVSHNLRDIEKIcDRVIWIENHKMKVMGEAHSVIAQ 240
Cdd:TIGR00957 805 gPEGVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQR 851
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
31-208 |
6.30e-04 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 39.94 E-value: 6.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 31 PRRALSLLS--GRSYLAIE-----NISFQVKKGESVALIGRNGAGKSTSLGLVAGVMK--PSSGSVHV----VGRVASML 97
Cdd:COG2401 24 SERVAIVLEafGVELRVVEryvlrDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVpdnqFGREASLI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 98 ELGGGFHPELTGREniRLNATLLG----LRRKelkqrldkiieFSELgefidepirvySSGMLAKLGFSVITQVDPDILI 173
Cdd:COG2401 104 DAIGRKGDFKDAVE--LLNAVGLSdavlWLRR-----------FKEL-----------STGQKFRFRLALLLAERPKLLV 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 1699326967 174 IDEVLAVGDISFQRKCLETINEF-KKKGVTILFVSH 208
Cdd:COG2401 160 IDEFCSHLDRQTAKRVARNLQKLaRRAGITLVVATH 195
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
21-97 |
6.62e-04 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 40.47 E-value: 6.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 21 GSGIKELIFNPR-------RALSllSGRsyLAIENISFQVKKGESV--------------ALIGRNGAGKSTSLGLVAGV 79
Cdd:PRK10790 315 GERVFELMDGPRqqygnddRPLQ--SGR--IDIDNVSFAYRDDNLVlqninlsvpsrgfvALVGHTGSGKSTLASLLMGY 390
|
90
....*....|....*...
gi 1699326967 80 MKPSSGSVHVVGRVASML 97
Cdd:PRK10790 391 YPLTEGEIRLDGRPLSSL 408
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
46-78 |
8.04e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 40.32 E-value: 8.04e-04
10 20 30
....*....|....*....|....*....|...
gi 1699326967 46 IENISFQVKKGESVALIGRNGAGKSTSLGLVAG 78
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNG 51
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
45-221 |
1.10e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 39.72 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKSTS----LGLV---AGVMK-------------PSSGSVHVVGRVASMLelgggFH 104
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSVSslaiMGLIdypGRVMAeklefngqdlqriSEKERRNLVGAEVAMI-----FQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 105 PELT--------GRENIRLNATLLGLRRKELKQRldkIIEFSELGEFIDEPIR--VY----SSGMLAKLGFSVITQVDPD 170
Cdd:PRK11022 97 DPMTslnpcytvGFQIMEAIKVHQGGNKKTRRQR---AIDLLNQVGIPDPASRldVYphqlSGGMSQRVMIAMAIACRPK 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1699326967 171 ILIIDEVLAVGDISFQRKCLETINEF-KKKGVTILFVSHNLRDIEKICDRVI 221
Cdd:PRK11022 174 LLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKII 225
|
|
| RadA_SMS_N |
cd01121 |
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a ... |
58-208 |
1.11e-03 |
|
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a role in recombination and recombinational repair of DNA damaged by UV radiation, X-rays, and chemical agent and is responsible for the stabilization or processing of branched DNA molecules.
Pssm-ID: 410866 [Multi-domain] Cd Length: 268 Bit Score: 39.44 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 58 SVALIGRN-GAGKSTSLGLVAGVMKPSSGSVHVVgrvasmlelgggfhpelTGREN---IRLNATLLGLRRKELK----Q 129
Cdd:cd01121 83 SVVLIGGDpGIGKSTLLLQVAARLAQRGGKVLYV-----------------SGEESlsqIKLRAERLGLGSDNLYllaeT 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 130 RLDKIIefselgefidepirvyssgmlaklgfSVITQVDPDILIIDEVLAV---------GDISFQRKCLETINEF-KKK 199
Cdd:cd01121 146 NLEAIL--------------------------AEIEELKPSLVVIDSIQTVyspeltsspGSVSQVRECAAELLRLaKET 199
|
....*....
gi 1699326967 200 GVTILFVSH 208
Cdd:cd01121 200 GIPVFLVGH 208
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
46-78 |
1.23e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 39.61 E-value: 1.23e-03
10 20 30
....*....|....*....|....*....|...
gi 1699326967 46 IENISFQVKKGESVALIGRNGAGKSTSLGLVAG 78
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG 308
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
4-71 |
1.43e-03 |
|
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: 39.42 E-value: 1.43e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1699326967 4 AIEFKNVTKRYplyhhigsgikelifNPRRALsllsgrsylaIENISFQVKKGESVALIGRNGAGKST 71
Cdd:COG5265 357 EVRFENVSFGY---------------DPERPI----------LKGVSFEVPAGKTVAIVGPSGAGKST 399
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
56-208 |
1.72e-03 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 39.48 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 56 GESVALIGRNGAGKSTSLGLVAGVMKPSS--GSVHVVGR-VASMLELGGGF-------HPELTGRENIrLNATLLGLRRK 125
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRkPTKQILKRTGFvtqddilYPHLTVRETL-VFCSLLRLPKS 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 126 ELKQRLDKIIE--FSELGEFIDEP-------IRVYSSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKCLETINEF 196
Cdd:PLN03211 173 LTKQEKILVAEsvISELGLTKCENtiignsfIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSL 252
|
170
....*....|..
gi 1699326967 197 KKKGVTILFVSH 208
Cdd:PLN03211 253 AQKGKTIVTSMH 264
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
46-146 |
1.91e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 38.95 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 46 IENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHV-----VGrvasMLELGGGFHPELTGRENIRlnatlL 120
Cdd:PRK11819 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPapgikVG----YLPQEPQLDPEKTVRENVE-----E 93
|
90 100
....*....|....*....|....*...
gi 1699326967 121 GLR-RKELKQRLDKI-IEFSELGEFIDE 146
Cdd:PRK11819 94 GVAeVKAALDRFNEIyAAYAEPDADFDA 121
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
46-87 |
2.09e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 39.00 E-value: 2.09e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1699326967 46 IENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSV 87
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSY 58
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
53-85 |
2.36e-03 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 37.94 E-value: 2.36e-03
10 20 30
....*....|....*....|....*....|...
gi 1699326967 53 VKKGESVALIGRNGAGKSTSLGLVAGVMKPSSG 85
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGD 54
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
46-73 |
3.99e-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: 37.53 E-value: 3.99e-03
10 20
....*....|....*....|....*...
gi 1699326967 46 IENISFQVKKGESVALIGRNGAGKSTSL 73
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLL 47
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
145-244 |
4.17e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 37.77 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699326967 145 DEPIRVySSGMLAKLGFSVITQVDPDILIIDEVLAVGDISFQRKCLETINEFKKKgVTILFVSHNLRDIEKICDRVIWIE 224
Cdd:PRK14271 159 DSPFRL-SGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFF 236
|
90 100
....*....|....*....|
gi 1699326967 225 NHKMKVMGEAHSVIAQYKEA 244
Cdd:PRK14271 237 DGRLVEEGPTEQLFSSPKHA 256
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
44-92 |
6.68e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 37.45 E-value: 6.68e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1699326967 44 LAIENISFQVKKGESVALIGRNGAGKSTSLGLVAGVMKPSSGSVHVVGR 92
Cdd:PTZ00243 1324 LVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGR 1372
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
45-71 |
7.05e-03 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 36.94 E-value: 7.05e-03
10 20
....*....|....*....|....*..
gi 1699326967 45 AIENISFQVKKGESVALIGRNGAGKST 71
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKST 52
|
|
| |
