|
Name |
Accession |
Description |
Interval |
E-value |
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-247 |
9.02e-132 |
|
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: 371.50 E-value: 9.02e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSFktktGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAVRRAL 80
Cdd:COG4555 1 MIEVENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 81 GVLPDARGVYKRLSARENIAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVIL 160
Cdd:COG4555 77 GVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 161 DEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADELRAATGEDNLEDAFVKAI 240
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEENLEDAFVALI 236
|
....*..
gi 1755611750 241 GSDEGLH 247
Cdd:COG4555 237 GSEEGEA 243
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-218 |
2.05e-110 |
|
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: 316.62 E-value: 2.05e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSFKTKTGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAVRRAL 80
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 81 GVLPDARGVYKRLSARENIAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVIL 160
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1755611750 161 DEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAG 218
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-244 |
9.80e-103 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 297.75 E-value: 9.80e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 2 IVVDSLHKSFKTKTglvkAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAVRRALG 81
Cdd:COG1131 1 IEVRGLTKRYGDKT----ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 82 VLPDARGVYKRLSARENIAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILD 161
Cdd:COG1131 77 YVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 162 EPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADELRAATgednLEDAFVKAIG 241
Cdd:COG1131 157 EPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL----LEDVFLELTG 232
|
...
gi 1755611750 242 SDE 244
Cdd:COG1131 233 EEA 235
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-233 |
1.11e-82 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 249.26 E-value: 1.11e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSFKTKTglvkAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDG--VDAAHdpvavRR 78
Cdd:COG4152 1 MLELKGLTKRFGDKT----AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGepLDPED-----RR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 79 ALGVLPDARGVYKRLSARENIAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNV 158
Cdd:COG4152 72 RIGYLPEERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1755611750 159 ILDEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADELRAATGEDNLE 233
Cdd:COG4152 152 ILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRNTLR 226
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-214 |
5.34e-71 |
|
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: 214.95 E-value: 5.34e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 2 IVVDSLHKSFKTKTglvkAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAVRRALG 81
Cdd:cd03230 1 IEVRNLSKRYGKKT----ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 82 VLPDARGVYKRLSARENIAYfgqlhgmsrtqiaertrllshaldmddildrqtegfSQGQRTKTAIARALVHDPRNVILD 161
Cdd:cd03230 77 YLPEEPSLYENLTVRENLKL------------------------------------SGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1755611750 162 EPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTV 214
Cdd:cd03230 121 EPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-218 |
4.97e-67 |
|
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: 206.36 E-value: 4.97e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 4 VDSLHKSFKTKTglvkAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDG--VDAAHdpvavRRALG 81
Cdd:cd03269 3 VENVTKRFGRVT----ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpLDIAA-----RNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 82 VLPDARGVYKRLSARENIAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILD 161
Cdd:cd03269 74 YLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1755611750 162 EPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAG 218
Cdd:cd03269 154 EPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
16-233 |
8.92e-64 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 201.08 E-value: 8.92e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 16 GLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAVRRALGVLPDARGVYKRLSA 95
Cdd:TIGR01188 4 GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDEDLTG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 96 RENIAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRAM 175
Cdd:TIGR01188 84 RENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAI 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1755611750 176 RGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADELRAATGEDNLE 233
Cdd:TIGR01188 164 WDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGKDTLE 221
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-224 |
2.01e-63 |
|
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: 197.59 E-value: 2.01e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 2 IVVDSLHKSFktktGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAVRRALG 81
Cdd:cd03265 1 IEVENLVKKY----GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 82 VLPDARGVYKRLSARENIAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILD 161
Cdd:cd03265 77 IVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1755611750 162 EPTNGLDVMTTRAMRGFLQQL-RAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADELR 224
Cdd:cd03265 157 EPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-218 |
1.19e-62 |
|
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: 195.13 E-value: 1.19e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 2 IVVDSLHKSFKTKTglvkAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAVRRaLG 81
Cdd:cd03268 1 LKTNDLTKTYGKKR----VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRR-IG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 82 VLPDARGVYKRLSARENIAYFGQLHGMSRTQIAErtrllshALD---MDDILDRQTEGFSQGQRTKTAIARALVHDPRNV 158
Cdd:cd03268 76 ALIEAPGFYPNLTARENLRLLARLLGIRKKRIDE-------VLDvvgLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 159 ILDEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAG 218
Cdd:cd03268 149 ILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-224 |
1.69e-62 |
|
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: 195.03 E-value: 1.69e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 2 IVVDSLHKSFKTKTglVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAVRRALG 81
Cdd:cd03263 1 LQIRNLTKTYKKGT--KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 82 VLPDARGVYKRLSARENIAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILD 161
Cdd:cd03263 79 YCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1755611750 162 EPTNGLDVMTTRAMRGFLQQLRaEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADELR 224
Cdd:cd03263 159 EPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| GldA_ABC_ATP |
TIGR03522 |
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein ... |
2-240 |
2.36e-61 |
|
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldA is an ABC transporter ATP-binding protein (pfam00005) linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae and Cytophaga hutchinsonii. Knockouts of GldA abolish the gliding phenotype. Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. Bacteroidetes with members of this protein family appear to have all of the genes associated with gliding motility.
Pssm-ID: 132561 [Multi-domain] Cd Length: 301 Bit Score: 194.99 E-value: 2.36e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 2 IVVDSLHKSFKTKtglvKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAVRRALG 81
Cdd:TIGR03522 3 IRVSSLTKLYGTQ----NALDEVSFEAQKGRIVGFLGPNGAGKSTTMKIITGYLPPDSGSVQVCGEDVLQNPKEVQRNIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 82 VLPDARGVYKRLSARENIAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILD 161
Cdd:TIGR03522 79 YLPEHNPLYLDMYVREYLQFIAGIYGMKGQLLKQRVEEMIELVGLRPEQHKKIGQLSKGYRQRVGLAQALIHDPKVLILD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1755611750 162 EPTNGLDVMTTRAMRGFLQQLrAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADELRAATGEDNLEDAFVKAI 240
Cdd:TIGR03522 159 EPTTGLDPNQLVEIRNVIKNI-GKDKTIILSTHIMQEVEAICDRVIIINKGKIVADKKLDELSAANKKQVIEVEFEEQI 236
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-218 |
1.42e-60 |
|
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: 189.71 E-value: 1.42e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 2 IVVDSLHKSFKTKtglvKAVNGVSFNAADGqITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAVRRALG 81
Cdd:cd03264 1 LQLENLTKRYGKK----RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 82 VLPDARGVYKRLSARENIAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILD 161
Cdd:cd03264 76 YLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1755611750 162 EPTNGLDVMTTRAMRGFLQQLrAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAG 218
Cdd:cd03264 156 EPTAGLDPEERIRFRNLLSEL-GEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-228 |
2.31e-59 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 190.30 E-value: 2.31e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSFKT---KTGL--------------VKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVR 63
Cdd:COG4586 1 IIEVENLSKTYRVyekEPGLkgalkglfrreyreVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 64 VDGvdaaHDPVAVRRAL----GV--------LPDargvykrLSARENIAYFGQLHGMSRTQIAERTRLLSHALDMDDILD 131
Cdd:COG4586 81 VLG----YVPFKRRKEFarriGVvfgqrsqlWWD-------LPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 132 RQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQLRAEGRC-VIFSSHIMQEVAALCDRIVIIA 210
Cdd:COG4586 150 TPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTtILLTSHDMDDIEALCDRVIVID 229
|
250
....*....|....*...
gi 1755611750 211 KGTVVAAGTADELRAATG 228
Cdd:COG4586 230 HGRIIYDGSLEELKERFG 247
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
3-218 |
1.05e-54 |
|
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: 175.60 E-value: 1.05e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 3 VVDSLHKSFKTKTGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAVRRALGV 82
Cdd:cd03267 19 LIGSLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 83 LPDARG-VYKRLSARENIAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILD 161
Cdd:cd03267 99 VFGQKTqLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1755611750 162 EPTNGLDVMTTRAMRGFLQQLRAE-GRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAG 218
Cdd:cd03267 179 EPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-218 |
6.23e-52 |
|
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: 167.70 E-value: 6.23e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 2 IVVDSLHKSFktktGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAvRRALG 81
Cdd:cd03259 1 LELKGLSKTY----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE-RRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 82 VLPDARGVYKRLSARENIAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILD 161
Cdd:cd03259 76 MVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1755611750 162 EPTNGLDVMTTRAMRGFLQQLRAE-GRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAG 218
Cdd:cd03259 156 EPLSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-223 |
1.49e-51 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 167.51 E-value: 1.49e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 2 IVVDSLHKSFKTKTglvKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVD-AAHDPVAVRRAL 80
Cdd:COG1122 1 IELENLSFSYPGGT---PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDiTKKNLRELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 81 GVL---PD----ARGVYkrlsarENIAyFGQLH-GMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALV 152
Cdd:COG1122 78 GLVfqnPDdqlfAPTVE------EDVA-FGPENlGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1755611750 153 HDPRNVILDEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:COG1122 151 MEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-223 |
6.42e-50 |
|
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: 163.10 E-value: 6.42e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 2 IVVDSLHKSFKTKtglvKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAVRRALG 81
Cdd:cd03218 1 LRAENLSKRYGKR----KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 82 V--LPDARGVYKRLSARENIAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVI 159
Cdd:cd03218 77 IgyLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1755611750 160 LDEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEI 220
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-223 |
3.64e-49 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 161.35 E-value: 3.64e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSFKTKTglvkAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAvRRA- 79
Cdd:COG1137 3 TLEAENLVKSYGKRT----VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMH-KRAr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 80 --LGVLPDARGVYKRLSARENIAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRN 157
Cdd:COG1137 78 lgIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1755611750 158 VILDEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:COG1137 158 ILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEI 223
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-223 |
5.46e-48 |
|
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: 165.46 E-value: 5.46e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSFKTK-TGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAVRRA 79
Cdd:COG1123 260 LLEVRNLSKRYPVRgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 80 LGvlPDARGVY--------KRLSARENIAYFGQLHG-MSRTQIAERTRLLSHALDMD-DILDRQTEGFSQGQRTKTAIAR 149
Cdd:COG1123 340 LR--RRVQMVFqdpysslnPRMTVGDIIAEPLRLHGlLSRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1755611750 150 ALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQLRAE-GRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEV 492
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-225 |
1.15e-47 |
|
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: 157.60 E-value: 1.15e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 4 VDSLHKSFktktGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAVRRALGVl 83
Cdd:cd03219 3 VRGLTKRF----GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGI- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 84 pdAR-----GVYKRLSARENI----------AYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIA 148
Cdd:cd03219 78 --GRtfqipRLFPELTVLENVmvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1755611750 149 RALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADELRA 225
Cdd:cd03219 156 RALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
2-223 |
4.05e-47 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 156.28 E-value: 4.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 2 IVVDSLHKSFKTKtglvKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAVRRALG 81
Cdd:TIGR04406 2 LVAENLIKSYKKR----KVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 82 V--LPDARGVYKRLSARENI-AYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNV 158
Cdd:TIGR04406 78 IgyLPQEASIFRKLTVEENImAVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1755611750 159 ILDEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:TIGR04406 158 LLDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEI 222
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
23-207 |
4.63e-47 |
|
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: 154.94 E-value: 4.63e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 23 GVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAVRRALGVLPDARGVYKRLSARENIAYF 102
Cdd:COG4133 20 GLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLGHADGLKPELTVRENLRFW 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 103 GQLHGMSRTQiAERTRLLsHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQL 182
Cdd:COG4133 100 AALYGLRADR-EAIDEAL-EAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAH 177
|
170 180
....*....|....*....|....*
gi 1755611750 183 RAEGRCVIFSSHimQEVAALCDRIV 207
Cdd:COG4133 178 LARGGAVLLTTH--QPLELAAARVL 200
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-227 |
1.07e-46 |
|
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: 155.35 E-value: 1.07e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSFKTKTGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAH-DPVAVRRA 79
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRrRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 80 LGVLP-DARG-VYKRLSARENIAYFGQLHGmsRTQIAERTRLLSHALDMD-DILDRQTEGFSQGQRTKTAIARALVHDPR 156
Cdd:COG1124 81 VQMVFqDPYAsLHPRHTVDRILAEPLRIHG--LPDREERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1755611750 157 NVILDEPTNGLDVMTTRAMRGFLQQLRAE-GRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADELRAAT 227
Cdd:COG1124 159 LLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGP 230
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-239 |
1.72e-46 |
|
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: 154.77 E-value: 1.72e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 2 IVVDSLHKSFKtktGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVD-AAHDPVAVRRAL 80
Cdd:cd03295 1 IEFENVTKRYG---GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDiREQDPVELRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 81 GVLPDARGVYKRLSARENIAYFGQLHGMSRTQIAERTRLLSHALDMDD--ILDRQTEGFSQGQRTKTAIARALVHDPRNV 158
Cdd:cd03295 78 GYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPaeFADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 159 ILDEPTNGLDVMTtramRGFLQQL-----RAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADELRAATGEDNLE 233
Cdd:cd03295 158 LMDEPFGALDPIT----RDQLQEEfkrlqQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVA 233
|
....*.
gi 1755611750 234 DaFVKA 239
Cdd:cd03295 234 E-FVGA 238
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-225 |
4.96e-46 |
|
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: 154.04 E-value: 4.96e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSFktktGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAVRRAL 80
Cdd:COG0411 4 LLEVRGLTKRF----GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 81 GVlpdAR-----GVYKRLSARENIAyFGQLHGMSRTQIAERTRLLSHA----------------LDMDDILDRQTEGFSQ 139
Cdd:COG0411 80 GI---ARtfqnpRLFPELTVLENVL-VAAHARLGRGLLAALLRLPRARreereareraeellerVGLADRADEPAGNLSY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 140 GQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQLRAE-GRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAG 218
Cdd:COG0411 156 GQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGRVIAEG 235
|
....*..
gi 1755611750 219 TADELRA 225
Cdd:COG0411 236 TPAEVRA 242
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
2-241 |
8.47e-46 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 152.55 E-value: 8.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 2 IVVDSLHKSFKTKTglvkAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVD-AAHDpvavRRAL 80
Cdd:TIGR03740 1 LETKNLSKRFGKQT----AVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPwTRKD----LHKI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 81 GVLPDARGVYKRLSARENIAYFGQLHGMSRTQIAErtrlLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVIL 160
Cdd:TIGR03740 73 GSLIESPPLYENLTARENLKVHTTLLGLPDSRIDE----VLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLIL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 161 DEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADelraatGEDNLEDAFVKAI 240
Cdd:TIGR03740 149 DEPTNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLGYQGKIN------KSENLEKLFVEVV 222
|
.
gi 1755611750 241 G 241
Cdd:TIGR03740 223 K 223
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-214 |
1.30e-45 |
|
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: 151.87 E-value: 1.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 2 IVVDSLHKSFKTKTGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVA-----V 76
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKelaafR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 77 RRALGVLPDARGVYKRLSARENIAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPR 156
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1755611750 157 NVILDEPTNGLDVMTTRAMRGFLQQL-RAEGRCVIFSSHIMqEVAALCDRIVIIAKGTV 214
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-236 |
3.12e-45 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 151.73 E-value: 3.12e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSFKTKTglvkAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVD-AAHDPVAVRRA 79
Cdd:COG1120 1 MLEAENLSVGYGGRP----VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDlASLSRRELARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 80 LGVLPDARGVYKRLSARENIA-----YFGQLHGMSRTQIAERTRLLsHALDMDDILDRQTEGFSQGQRTKTAIARALVHD 154
Cdd:COG1120 77 IAYVPQEPPAPFGLTVRELVAlgrypHLGLFGRPSAEDREAVEEAL-ERTGLEHLADRPVDELSGGERQRVLIARALAQE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 155 PRNVILDEPTNGLD------VMTTramrgfLQQL-RAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADELraAT 227
Cdd:COG1120 156 PPLLLLDEPTSHLDlahqleVLEL------LRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV--LT 227
|
....*....
gi 1755611750 228 gEDNLEDAF 236
Cdd:COG1120 228 -PELLEEVY 235
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-216 |
4.67e-45 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 150.58 E-value: 4.67e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSFKTKTGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAVRRAL 80
Cdd:COG1136 4 LLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 81 ------------GVLPdargvykRLSARENIAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIA 148
Cdd:COG1136 84 rrrhigfvfqffNLLP-------ELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1755611750 149 RALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQLRAE-GRCVIFSSHIMqEVAALCDRIVIIAKGTVVA 216
Cdd:COG1136 157 RALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDP-ELAARADRVIRLRDGRIVS 224
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
10-213 |
8.85e-45 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 149.54 E-value: 8.85e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 10 SFKTKTGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVA-VRRALG-VLPDAR 87
Cdd:cd03225 6 SFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKeLRRKVGlVFQNPD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 88 GVYKRLSARENIAyFGQLH-GMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNG 166
Cdd:cd03225 86 DQFFGPTVEEEVA-FGLENlGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAG 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1755611750 167 LDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGT 213
Cdd:cd03225 165 LDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-223 |
9.23e-44 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 150.61 E-value: 9.23e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSFktktGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPvavrral 80
Cdd:COG3839 3 SLELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLP------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 81 gvlPDARGV---------YKRLSARENIAyFG-QLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARA 150
Cdd:COG3839 72 ---PKDRNIamvfqsyalYPHMTVYENIA-FPlKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1755611750 151 LVHDPRNVILDEPTNGLDVMTTRAMRGFLQQLRAE-GRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:COG3839 148 LVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRlGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-223 |
1.26e-43 |
|
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: 146.96 E-value: 1.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSFKTKTGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVD----AAHDPVAV 76
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDltllSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 77 RRALGV------LPDARGVYkrlsarENIAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARA 150
Cdd:cd03258 81 RRRIGMifqhfnLLSSRTVF------ENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1755611750 151 LVHDPRNVILDEPTNGLDVMTTRAMRGFLQQLRAE-GRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:cd03258 155 LANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-239 |
5.53e-43 |
|
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: 145.51 E-value: 5.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSFKTKTGLvkavNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDP----VAV 76
Cdd:COG1127 5 MIEVRNLTKSFGDRVVL----DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekelYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 77 RRALGV------LPDArgvykrLSARENIAYFGQLH-GMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIAR 149
Cdd:COG1127 81 RRRIGMlfqggaLFDS------LTVFENVAFPLREHtDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 150 ALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQLRAE-GRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADELRAAtg 228
Cdd:COG1127 155 ALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLAS-- 232
|
250
....*....|.
gi 1755611750 229 ednlEDAFVKA 239
Cdd:COG1127 233 ----DDPWVRQ 239
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-223 |
9.10e-43 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 147.26 E-value: 9.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 2 IVVDSLHKSFKTKTglvkAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAVRRALG 81
Cdd:PRK13537 8 IDFRNVEKRYGDKL----VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 82 VLPDARGVYKRLSARENIAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILD 161
Cdd:PRK13537 84 VVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1755611750 162 EPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:PRK13537 164 EPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
20-218 |
4.09e-42 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 142.67 E-value: 4.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 20 AVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDpvavRRALGVLPDARGV--YKRLSARE 97
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE----RKRIGYVPQRRSIdrDFPISVRD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 98 -----NIAYFGQLHGMSRTQIAERTRLLShALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTT 172
Cdd:cd03235 90 vvlmgLYGHKGLFRRLSKADKAKVDEALE-RVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQ 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1755611750 173 RAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKgTVVAAG 218
Cdd:cd03235 169 EDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNR-TVVASG 213
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-236 |
8.02e-42 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 142.92 E-value: 8.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSFKTKTglvkAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDpvavRRAL 80
Cdd:COG1121 6 AIELENLTVSYGGRP----VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA----RRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 81 GVLPDARGVYKR--LSARENIA--YFGQLHGMSRTQIAERTRLLsHALD---MDDILDRQTEGFSQGQRTKTAIARALVH 153
Cdd:COG1121 78 GYVPQRAEVDWDfpITVRDVVLmgRYGRRGLFRRPSRADREAVD-EALErvgLEDLADRPIGELSGGQQQRVLLARALAQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 154 DPRNVILDEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGtVVAAGTADELRAatgEDNLE 233
Cdd:COG1121 157 DPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVLT---PENLS 232
|
...
gi 1755611750 234 DAF 236
Cdd:COG1121 233 RAY 235
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-223 |
8.52e-42 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 145.63 E-value: 8.52e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSFktktGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAvRRAL 80
Cdd:COG3842 5 ALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE-KRNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 81 GVL-------PDargvykrLSARENIAYFGQLHGMSRTQIAERTRllsHALDM---DDILDRQTEGFSQGQRTKTAIARA 150
Cdd:COG3842 80 GMVfqdyalfPH-------LTVAENVAFGLRMRGVPKAEIRARVA---ELLELvglEGLADRYPHQLSGGQQQRVALARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1755611750 151 LVHDPRNVILDEPTNGLDVMTTRAMRGFLQQL-RAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:COG3842 150 LAPEPRVLLLDEPLSALDAKLREEMREELRRLqRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-223 |
2.27e-41 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 144.52 E-value: 2.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 2 IVVDSLHKSFKTktglVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDpVAVRRalg 81
Cdd:COG1118 3 IEVRNISKRFGS----FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTN-LPPRE--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 82 vlpdaRGV------Y---KRLSARENIAYFGQLHGMSRTQIAER-TRLLShALDMDDILDR---QtegFSQGQRTKTAIA 148
Cdd:COG1118 75 -----RRVgfvfqhYalfPHMTVAENIAFGLRVRPPSKAEIRARvEELLE-LVQLEGLADRypsQ---LSGGQRQRVALA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1755611750 149 RALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQL-RAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:COG1118 146 RALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLhDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-227 |
2.73e-41 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 141.10 E-value: 2.73e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 2 IVVDSLHKSFKTKTGLvkavNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAH----DPVAVR 77
Cdd:cd03261 1 IELRGLTKSFGGRTVL----KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlseaELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 78 RALGVLPDARGVYKRLSARENIAYFGQLHG-MSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPR 156
Cdd:cd03261 77 RRMGMLFQSGALFDSLTVFENVAFPLREHTrLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1755611750 157 NVILDEPTNGLDVMTTRAMRGFLQQLRAE-GRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADELRAAT 227
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD 228
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
10-229 |
8.35e-41 |
|
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: 148.44 E-value: 8.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 10 SFKTKTGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAH-DPVAVRRALGVLP-DAR 87
Cdd:COG2274 480 SFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQiDPASLRRQIGVVLqDVF 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 88 ---GvykrlSARENIAYFGQLHGMSR-TQIAERTRLLSHALDMDDILDRQ-TEG---FSQGQRTKTAIARALVHDPRNVI 159
Cdd:COG2274 560 lfsG-----TIRENITLGDPDATDEEiIEAARLAGLHDFIEALPMGYDTVvGEGgsnLSGGQRQRLAIARALLRNPRILI 634
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 160 LDEPTNGLDVMTTRAMRGFLQQLRAeGRCVIFSSHIMqEVAALCDRIVIIAKGTVVAAGTADELRAATGE 229
Cdd:COG2274 635 LDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRL-STIRLADRIIVLDKGRIVEDGTHEELLARKGL 702
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-213 |
1.62e-40 |
|
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: 137.32 E-value: 1.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 2 IVVDSLHKSFKTKTglvkAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAA---HDPVAVRR 78
Cdd:cd03229 1 LELKNVSKRYGQKT----VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdleDELPPLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 79 ALGVLPDARGVYKRLSARENIAYfgqlhgmsrtqiaertrllshaldmddildrqteGFSQGQRTKTAIARALVHDPRNV 158
Cdd:cd03229 77 RIGMVFQDFALFPHLTVLENIAL----------------------------------GLSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1755611750 159 ILDEPTNGLDVMTTRAMRGFLQQLRAE-GRCVIFSSHIMQEVAALCDRIVIIAKGT 213
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-216 |
2.06e-40 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 139.45 E-value: 2.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSFKTKTGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDG--VDAAHDPVAVrr 78
Cdd:COG1116 7 ALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGkpVTGPGPDRGV-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 79 algVLPDARgVYKRLSARENIAyFG-QLHGMSRTQIAERTRllsHALDMDDIldrqtEGF--------SQGQRTKTAIAR 149
Cdd:COG1116 85 ---VFQEPA-LLPWLTVLDNVA-LGlELRGVPKAERRERAR---ELLELVGL-----AGFedayphqlSGGMRQRVAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 150 ALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQLRAEGRC-VIFSSHIMQEVAALCDRIVIIAK--GTVVA 216
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKtVLFVTHDVDEAVFLADRVVVLSArpGRIVE 221
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-218 |
2.37e-40 |
|
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: 138.16 E-value: 2.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 2 IVVDSLHKSFKTKTglvkAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPvAVRRALG 81
Cdd:cd03301 1 VELENVTKRFGNVT----ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLP-PKDRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 82 VLPDARGVYKRLSARENIAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILD 161
Cdd:cd03301 76 MVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1755611750 162 EPTNGLDVMTTRAMRGFLQQLRAE-GRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAG 218
Cdd:cd03301 156 EPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-216 |
2.78e-40 |
|
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: 137.99 E-value: 2.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 2 IVVDSLHKSFKTKTGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGvdaahDPVA-VRRAL 80
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG-----EPVTgPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 81 GVLPDARGVYKRLSARENIAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVIL 160
Cdd:cd03293 76 GYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1755611750 161 DEPTNGLDVMTTRAMRGFLQQL-RAEGRCVIFSSHIMQEVAALCDRIVIIAK--GTVVA 216
Cdd:cd03293 156 DEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVA 214
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-223 |
4.05e-40 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 141.12 E-value: 4.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 2 IVVDSLHKSFKTKTglvkAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAVRRALG 81
Cdd:PRK13536 42 IDLAGVSKSYGDKA----VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 82 VLPDARGVYKRLSARENIAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILD 161
Cdd:PRK13536 118 VVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILD 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1755611750 162 EPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:PRK13536 198 EPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
16-225 |
4.25e-40 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 137.57 E-value: 4.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 16 GLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVA--VRRALGVLPDARGVYKRL 93
Cdd:cd03224 11 GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHerARAGIGYVPEGRRIFPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 94 SARENIayfgqLHGMSRTQIAERTRLLSHALDM----DDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGL-- 167
Cdd:cd03224 91 TVEENL-----LLGAYARRRAKRKARLERVYELfprlKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLap 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1755611750 168 ----DVMTTramrgfLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADELRA 225
Cdd:cd03224 166 kiveEIFEA------IRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-213 |
4.60e-40 |
|
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: 135.45 E-value: 4.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 7 LHKSFKTKTglvkAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPvavrralgvlpda 86
Cdd:cd00267 5 LSFRYGGRT----ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLP------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 87 rgvykRLSARENIAYFGQLhgmsrtqiaertrllshaldmddildrqtegfSQGQRTKTAIARALVHDPRNVILDEPTNG 166
Cdd:cd00267 68 -----LEELRRRIGYVPQL--------------------------------SGGQRQRVALARALLLNPDLLLLDEPTSG 110
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1755611750 167 LDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGT 213
Cdd:cd00267 111 LDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-216 |
3.83e-39 |
|
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: 133.32 E-value: 3.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 2 IVVDSLHKSFktktGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAVRRALG 81
Cdd:cd03216 1 LELRGITKRF----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 82 VlpdaRGVYkrlsareniayfgQLhgmsrtqiaertrllshaldmddildrqtegfSQGQRTKTAIARALVHDPRNVILD 161
Cdd:cd03216 77 I----AMVY-------------QL--------------------------------SVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1755611750 162 EPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVA 216
Cdd:cd03216 108 EPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVG 162
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-215 |
4.49e-39 |
|
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: 135.33 E-value: 4.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSFKTKTGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAVRRAL 80
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 81 G-----VLPDARGVYK-RLSARENIAYFGQLHGMSRTQIAERTR---LLSHALDMDDILDRQTEGFSQGQRTKTAIARAL 151
Cdd:cd03257 81 RkeiqmVFQDPMSSLNpRMTIGEQIAEPLRIHGKLSKKEARKEAvllLLVGVGLPEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1755611750 152 VHDPRNVILDEPTNGLDVMTTRAMRGFLQQLRAE-GRCVIFSSHIMQEVAALCDRIVIIAKGTVV 215
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-226 |
7.90e-39 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 135.18 E-value: 7.90e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSFKTKTglvKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPV----AV 76
Cdd:COG3638 2 MLELRNLSKRYPGGT---PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGralrRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 77 RRALGVLPDARGVYKRLSARENIAyFGQLHGMS----------RTQIAERTRLLsHALDMDDILDRQTEGFSQGQRTKTA 146
Cdd:COG3638 79 RRRIGMIFQQFNLVPRLSVLTNVL-AGRLGRTStwrsllglfpPEDRERALEAL-ERVGLADKAYQRADQLSGGQQQRVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 147 IARALVHDPRnVIL-DEPTNGLDVMTTR-AMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADELR 224
Cdd:COG3638 157 IARALVQEPK-LILaDEPVASLDPKTARqVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAELT 235
|
..
gi 1755611750 225 AA 226
Cdd:COG3638 236 DA 237
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-223 |
1.11e-38 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 137.13 E-value: 1.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSFKTKTGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVD-AAHDP---VAV 76
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDlTALSErelRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 77 RRALGV------LPDARGVYkrlsarENIAYFGQLHGMSRTQIAERTRLLshaLDMDDILDRQTEGFSQ---GQRTKTAI 147
Cdd:COG1135 81 RRKIGMifqhfnLLSSRTVA------ENVALPLEIAGVPKAEIRKRVAEL---LELVGLSDKADAYPSQlsgGQKQRVGI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1755611750 148 ARALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQLRAE-GRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:COG1135 152 ARALANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDV 228
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
21-218 |
1.28e-38 |
|
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: 132.56 E-value: 1.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 21 VNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVD-AAHDPVAVRRALGVLPdargvykrlsareni 99
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDlASLSPKELARKIAYVP--------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 100 ayfgqlhgmsrtQIAERTrllshalDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRAMRGFL 179
Cdd:cd03214 80 ------------QALELL-------GLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1755611750 180 QQL-RAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAG 218
Cdd:cd03214 141 RRLaRERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-226 |
2.16e-38 |
|
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: 139.65 E-value: 2.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSFKTktGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPD---QGSVRVDGVDAAHDPVAVR 77
Cdd:COG1123 4 LLEVRDLSVRYPG--GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 78 --RALGVLPDARGVYKRLSARENIAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDP 155
Cdd:COG1123 82 grRIGMVFQDPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1755611750 156 RNVILDEPTNGLDVMTTRAMRGFLQQLRAE-GRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADELRAA 226
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-165 |
7.72e-38 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 129.69 E-value: 7.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 21 VNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAVRRA-LGVLPDARGVYKRLSARENI 99
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKeIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 100 AYFGQLHGMSRTQIAERTRLLSHALDMDDILDR----QTEGFSQGQRTKTAIARALVHDPRNVILDEPTN 165
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
24-223 |
8.84e-38 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 135.23 E-value: 8.84e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 24 VSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDG---VDAAHD---PVAvRRALG-VLPDARgVYKRLSAR 96
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSARGiflPPH-RRRIGyVFQEAR-LFPHLSVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 97 ENIAYfgqlhGMSRTQIAERTRLLSHALDMDDI---LDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTR 173
Cdd:COG4148 96 GNLLY-----GRKRAPRAERRISFDEVVELLGIghlLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1755611750 174 AMRGFLQQLRAEGRC-VIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:COG4148 171 EILPYLERLRDELDIpILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEV 221
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
19-222 |
3.07e-37 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 138.08 E-value: 3.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 19 KAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAH-DPVAVRRALGVLP-DARGVYKRLsaR 96
Cdd:TIGR03375 479 PALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQiDPADLRRNIGYVPqDPRLFYGTL--R 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 97 ENIAYFGQLHGMSRT-QIAERTRLL----SHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMT 171
Cdd:TIGR03375 557 DNIALGAPYADDEEIlRAAELAGVTefvrRHPDGLDMQIGERGRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRS 636
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1755611750 172 TRAMRGFLQQLrAEGRCVIFSSHIMQeVAALCDRIVIIAKGTVVAAGTADE 222
Cdd:TIGR03375 637 EERFKDRLKRW-LAGKTLVLVTHRTS-LLDLVDRIIVMDNGRIVADGPKDQ 685
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-223 |
4.86e-37 |
|
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: 130.05 E-value: 4.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 2 IVVDSLHKSFKTKTglvkAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAvRRALG 81
Cdd:cd03300 1 IELENVSKFYGGFV----ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH-KRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 82 VLPDARGVYKRLSARENIAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILD 161
Cdd:cd03300 76 TVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1755611750 162 EPTNGLDVMTTRAMRGFLQQLRAE-GRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
16-225 |
7.02e-37 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 129.72 E-value: 7.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 16 GLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVA--VRRALGVLPDARGVYKRL 93
Cdd:COG0410 14 GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHriARLGIGYVPEGRRIFPSL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 94 SARENIayfgQLHGMSRTQIAERTRLLSHALDM----DDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGL-- 167
Cdd:COG0410 94 TVEENL----LLGAYARRDRAEVRADLERVYELfprlKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLap 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1755611750 168 ----DVMTTramrgfLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADELRA 225
Cdd:COG0410 170 liveEIFEI------IRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-225 |
7.55e-37 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 130.01 E-value: 7.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 2 IVVDSLHKSFKTKtglvKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPV--AVRRA 79
Cdd:PRK10895 4 LTAKNLAKAYKGR----RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhaRARRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 80 LGVLPDARGVYKRLSARENIAYFGQL-HGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNV 158
Cdd:PRK10895 80 IGYLPQEASIFRRLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1755611750 159 ILDEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADELRA 225
Cdd:PRK10895 160 LLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-223 |
9.95e-37 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 135.15 E-value: 9.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSFktktGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAA-HDPVAVRRA 79
Cdd:COG1129 4 LLEMRGISKSF----GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRfRSPRDAQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 80 --------LGVLPDargvykrLSARENIaYFGQL----HGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAI 147
Cdd:COG1129 80 giaiihqeLNLVPN-------LSVAENI-FLGREprrgGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1755611750 148 ARALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:COG1129 152 ARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-222 |
1.00e-36 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 129.43 E-value: 1.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSF------------------KTKTGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSV 62
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 63 RVDGVDAAhdPVAVrrALGVLPDargvykrLSARENIAYFGQLHGMSRTQIAERtrllshaldMDDI---------LDRQ 133
Cdd:COG1134 84 EVNGRVSA--LLEL--GAGFHPE-------LTGRENIYLNGRLLGLSRKEIDEK---------FDEIvefaelgdfIDQP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 134 TEGFSQGQRTKTAIARALVHDPRNVILDEptnGLDVM----TTRAMRgFLQQLRAEGRCVIFSSHIMQEVAALCDRIVII 209
Cdd:COG1134 144 VKTYSSGMRARLAFAVATAVDPDILLVDE---VLAVGdaafQKKCLA-RIRELRESGRTVIFVSHSMGAVRRLCDRAIWL 219
|
250
....*....|...
gi 1755611750 210 AKGTVVAAGTADE 222
Cdd:COG1134 220 EKGRLVMDGDPEE 232
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-223 |
7.44e-36 |
|
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: 127.07 E-value: 7.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 2 IVVDSLHKSFktktGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAvRRALG 81
Cdd:cd03296 3 IEVRNVSKRF----GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ-ERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 82 VLPDARGVYKRLSARENIAyFG-----QLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPR 156
Cdd:cd03296 78 FVFQHYALFRHMTVFDNVA-FGlrvkpRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1755611750 157 NVILDEPTNGLDVMTTRAMRGFLQQLRAE-GRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
10-218 |
1.19e-35 |
|
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: 126.16 E-value: 1.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 10 SFKTKTGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAH-DPVAVRRALGVLP-DAR 87
Cdd:cd03245 9 SFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQlDPADLRRNIGYVPqDVT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 88 GVYKRLsaRENIAYFGQLHGMSRT-QIAERTRLLSHALDMDDILDRQT----EGFSQGQRTKTAIARALVHDPRNVILDE 162
Cdd:cd03245 89 LFYGTL--RDNITLGAPLADDERIlRAAELAGVTDFVNKHPNGLDLQIgergRGLSGGQRQAVALARALLNDPPILLLDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1755611750 163 PTNGLDVMTTRAMRGFLQQLRAeGRCVIFSSHIMQeVAALCDRIVIIAKGTVVAAG 218
Cdd:cd03245 167 PTSAMDMNSEERLKERLRQLLG-DKTLIIITHRPS-LLDLVDRIIVMDSGRIVADG 220
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-237 |
2.52e-35 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 132.94 E-value: 2.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 20 AVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDG--VDaAHDpVAVRRALGVLPDARGVYKRLSARE 97
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGqpVD-AGD-IATRRRVGYMSQAFSLYGELTVRQ 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 98 NIAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMttrAMRG 177
Cdd:NF033858 359 NLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPV---ARDM 435
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1755611750 178 F---LQQLRAEGRCVIF-SSHIMQEvAALCDRIVIIAKGTVVAAGTADELRAATGEDNLEDAFV 237
Cdd:NF033858 436 FwrlLIELSREDGVTIFiSTHFMNE-AERCDRISLMHAGRVLASDTPAALVAARGAATLEEAFI 498
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-222 |
3.27e-35 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 125.53 E-value: 3.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 2 IVVDSLHKSFKTKTglvkaVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPvAVRRALG 81
Cdd:cd03299 1 LKVENLSKDWKEFK-----LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLP-PEKRDIS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 82 VLPDARGVYKRLSARENIAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILD 161
Cdd:cd03299 75 YVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1755611750 162 EPTNGLDVMTTRAMRGFLQQLRAE-GRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADE 222
Cdd:cd03299 155 EPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEE 216
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
8-228 |
5.52e-35 |
|
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: 124.91 E-value: 5.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 8 HKSFKTKTGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVD-AAHDPVAVRRALGVLPDA 86
Cdd:cd03252 5 HVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDlALADPAWLRRQVGVVLQE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 87 RGVYKRlSARENIAYFGQlhGMSRTQIAERTRLL-SHALDM------DDILDRQTEGFSQGQRTKTAIARALVHDPRNVI 159
Cdd:cd03252 85 NVLFNR-SIRDNIALADP--GMSMERVIEAAKLAgAHDFISelpegyDTIVGEQGAGLSGGQRQRIAIARALIHNPRILI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1755611750 160 LDEPTNGLDVMTTRAMRGFLQQLRAeGRCVIFSSHIMQEVAAlCDRIVIIAKGTVVAAGTADELRAATG 228
Cdd:cd03252 162 FDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAENG 228
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-223 |
6.22e-35 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 124.99 E-value: 6.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 2 IVVDSLHKSFKtktGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPV----AVR 77
Cdd:cd03256 1 IEVENLSKTYP---NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGkalrQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 78 RALGVLPDARGVYKRLSARENI-----AYFGQLHGMSRTQIAERTRLLSHALDMDDILD---RQTEGFSQGQRTKTAIAR 149
Cdd:cd03256 78 RQIGMIFQQFNLIERLSVLENVlsgrlGRRSTWRSLFGLFPKEEKQRALAALERVGLLDkayQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1755611750 150 ALVHDPRNVILDEPTNGLDVMTTRA-MRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQvMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
20-228 |
1.14e-34 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 130.26 E-value: 1.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 20 AVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAH-DPVAVRRALGVLPdARGVYKRLSAREN 98
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDlDPASWRRQIAWVP-QNPYLFAGTIREN 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 99 IAyFGQlHGMSRTQI---AERTRLLSHALDMDDILDRQ-TE---GFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMT 171
Cdd:COG4988 431 LR-LGR-PDASDEELeaaLEAAGLDEFVAALPDGLDTPlGEggrGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAET 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1755611750 172 TRAMRGFLQQLrAEGRCVIFSSHIMqEVAALCDRIVIIAKGTVVAAGTADELRAATG 228
Cdd:COG4988 509 EAEILQALRRL-AKGRTVILITHRL-ALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-223 |
6.78e-34 |
|
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: 121.90 E-value: 6.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 2 IVVDSLHKSFKTKtglvKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTL-----MTPDQGSVRVDGVDAAH---DP 73
Cdd:cd03260 1 IELRDLNVYYGDK----HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDldvDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 74 VAVRRALGVlpdargVYKR-----LSARENIAYFGQLHGMSRTqiAERTRLLSHALDM----DDILDRQTE-GFSQGQRT 143
Cdd:cd03260 77 LELRRRVGM------VFQKpnpfpGSIYDNVAYGLRLHGIKLK--EELDERVEEALRKaalwDEVKDRLHAlGLSGGQQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 144 KTAIARALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQLRAEgRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
29-218 |
1.04e-33 |
|
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: 120.86 E-value: 1.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 29 ADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGV------DAAHDPVAvRRALGVLPDARGVYKRLSARENIAYf 102
Cdd:cd03297 21 LNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsrKKINLPPQ-QRKIGLVFQQYALFPHLNVRENLAF- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 103 gQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQL 182
Cdd:cd03297 99 -GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQI 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 1755611750 183 RAE-GRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAG 218
Cdd:cd03297 178 KKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
20-219 |
4.26e-33 |
|
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: 127.05 E-value: 4.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 20 AVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAVRRALGVLPDARGVYKRLSARENI 99
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 100 AYFGQLHGMSRtqiaERTRLLSHALDMDDIL----DRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRAM 175
Cdd:TIGR01257 1025 LFYAQLKGRSW----EEAQLEMEAMLEDTGLhhkrNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSI 1100
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1755611750 176 RGFLQQLRAeGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGT 219
Cdd:TIGR01257 1101 WDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
9-218 |
1.73e-32 |
|
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: 118.02 E-value: 1.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 9 KSFKTKTGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAhdPVAVrrALGVLPDarg 88
Cdd:cd03220 26 LGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSS--LLGL--GGGFNPE--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 89 vykrLSARENIAYFGQLHGMSRTQIAERtrllshaldMDDI---------LDRQTEGFSQGQRTKTAIARALVHDPRNVI 159
Cdd:cd03220 99 ----LTGRENIYLNGRLLGLSRKEIDEK---------IDEIiefselgdfIDLPVKTYSSGMKARLAFAIATALEPDILL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1755611750 160 LDEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAG 218
Cdd:cd03220 166 IDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-215 |
2.07e-32 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 117.85 E-value: 2.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSFKTKtglVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAA---HDPVA-V 76
Cdd:COG2884 1 MIRFENVSKRYPGG---REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSrlkRREIPyL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 77 RRALGV-------LPDaRGVYkrlsarENIAYFGQLHGMSRTQIAERTRllsHALDMDDILDRQTEgF----SQGQRTKT 145
Cdd:COG2884 78 RRRIGVvfqdfrlLPD-RTVY------ENVALPLRVTGKSRKEIRRRVR---EVLDLVGLSDKAKA-LphelSGGEQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1755611750 146 AIARALVHDPRNVILDEPTNGLD-VMTTRAMRgFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVV 215
Cdd:COG2884 147 AIARALVNRPELLLADEPTGNLDpETSWEIME-LLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
21-236 |
2.18e-32 |
|
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: 118.65 E-value: 2.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 21 VNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQG-SVRVDGVDAAHDPVA-VRRALGVL-PD-ARGVYKRLSAR 96
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWeLRKRIGLVsPAlQLRFPRDETVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 97 ENI--AYFGQLhGMSRT---QIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMT 171
Cdd:COG1119 99 DVVlsGFFDSI-GLYREptdEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGA 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1755611750 172 TRAMRGFLQQLRAEGRC-VIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADELRAatgEDNLEDAF 236
Cdd:COG1119 178 RELLLALLDKLAAEGAPtLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLT---SENLSEAF 240
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
18-194 |
3.56e-32 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 116.37 E-value: 3.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 18 VKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDP---VAVRRALGVL---PDARGVYK 91
Cdd:TIGR01166 5 PEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRkglLERRQRVGLVfqdPDDQLFAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 92 RLSarENIAyFGQLH-GMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVM 170
Cdd:TIGR01166 85 DVD--QDVA-FGPLNlGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPA 161
|
170 180
....*....|....*....|....
gi 1755611750 171 TTRAMRGFLQQLRAEGRCVIFSSH 194
Cdd:TIGR01166 162 GREQMLAILRRLRAEGMTVVISTH 185
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-222 |
7.27e-32 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 117.42 E-value: 7.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSFKTKTglvkAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAH-DPVAVRRA 79
Cdd:PRK11231 2 TLRTENLTVGYGTKR----ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMlSSRQLARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 80 LGVLPDARGVYKRLSARENIAY--------FGQLHGMSR---TQIAERTRLlshaldmDDILDRQTEGFSQGQRTKTAIA 148
Cdd:PRK11231 78 LALLPQHHLTPEGITVRELVAYgrspwlslWGRLSAEDNarvNQAMEQTRI-------NHLADRRLTDLSGGQRQRAFLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1755611750 149 RALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADE 222
Cdd:PRK11231 151 MVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEE 224
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-245 |
1.00e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 117.53 E-value: 1.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 2 IVVDSLHKSFKTKTglvKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVD-AAHDPVAVRRAL 80
Cdd:PRK13647 5 IEVEDLHFRYKDGT---KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREvNAENEKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 81 G-VLPDARGVYKRLSARENIAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVI 159
Cdd:PRK13647 82 GlVFQDPDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 160 LDEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL--RAATGEDNLEDAFV 237
Cdd:PRK13647 162 LDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLtdEDIVEQAGLRLPLV 241
|
....*...
gi 1755611750 238 KAIGSDEG 245
Cdd:PRK13647 242 AQIFEDLP 249
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-223 |
1.20e-31 |
|
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: 118.23 E-value: 1.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSFKTKTGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTP---DQGSVRVDGVDAAHDPVAVR 77
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 78 RALgvlpdaRGvyKRLSA---------------RENIAYFGQLH-GMSRTQIAERTRLLshaLDM------DDILDR--- 132
Cdd:COG0444 81 RKI------RG--REIQMifqdpmtslnpvmtvGDQIAEPLRIHgGLSKAEARERAIEL---LERvglpdpERRLDRyph 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 133 QtegFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVmTTRA--MRgFLQQLRAE-GRCVIFSSHIMQEVAALCDRIVII 209
Cdd:COG0444 150 E---LSGGMRQRVMIARALALEPKLLIADEPTTALDV-TIQAqiLN-LLKDLQRElGLAILFITHDLGVVAEIADRVAVM 224
|
250
....*....|....
gi 1755611750 210 AKGTVVAAGTADEL 223
Cdd:COG0444 225 YAGRIVEEGPVEEL 238
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
18-216 |
1.24e-30 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 118.48 E-value: 1.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 18 VKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGV--------DAAHDPVAV-RRALGVLPDarg 88
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQemrfasttAALAAGVAIiYQELHLVPE--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 89 vykrLSARENIaYFGQL---HGM-SRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPT 164
Cdd:PRK11288 94 ----MTVAENL-YLGQLphkGGIvNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1755611750 165 NGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVA 216
Cdd:PRK11288 169 SSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
20-223 |
1.53e-30 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 113.00 E-value: 1.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 20 AVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVA--VRRALGVLPDARGVYKRLSARE 97
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHerARAGIAYVPQGREIFPRLTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 98 NIayfgqLHGMSRTQIAERtRLLSHALDM----DDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTR 173
Cdd:TIGR03410 95 NL-----LTGLAALPRRSR-KIPDEIYELfpvlKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIK 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1755611750 174 AMRGFLQQLRAEGR-CVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:TIGR03410 169 DIGRVIRRLRAEGGmAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
16-238 |
1.79e-30 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 119.07 E-value: 1.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 16 GLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRV---DGVDAAHdpvavRRAlgVLPD------- 85
Cdd:NF033858 12 GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVlggDMADARH-----RRA--VCPRiaympqg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 86 -ARGVYKRLSARENIAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPT 164
Cdd:NF033858 85 lGKNLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPT 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1755611750 165 NGLDVMTTRAMRGFLQQLRAE--GRCVIFSSHIMQEvAALCDRIVIIAKGTVVAAGTADELRAATGEDNLEDAFVK 238
Cdd:NF033858 165 TGVDPLSRRQFWELIDRIRAErpGMSVLVATAYMEE-AERFDWLVAMDAGRVLATGTPAELLARTGADTLEAAFIA 239
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
6-244 |
1.89e-30 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 116.20 E-value: 1.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 6 SLHKSFKTKTglvkAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPvAVRRALGVLPD 85
Cdd:PRK09452 19 GISKSFDGKE----VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP-AENRHVNTVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 86 ARGVYKRLSARENIAYFGQLHGMSRTQIAERTRllsHALDM---DDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDE 162
Cdd:PRK09452 94 SYALFPHMTVFENVAFGLRMQKTPAAEITPRVM---EALRMvqlEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 163 PTNGLDVMTTRAMRGFLQQL-RAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADE-------LRAAT--GEDNL 232
Cdd:PRK09452 171 SLSALDYKLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREiyeepknLFVARfiGEINI 250
|
250
....*....|..
gi 1755611750 233 EDAFVKAIGSDE 244
Cdd:PRK09452 251 FDATVIERLDEQ 262
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
13-222 |
1.91e-30 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 117.82 E-value: 1.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 13 TKT-GLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVdaahdPVAVR-----RALGV---- 82
Cdd:COG3845 12 TKRfGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGK-----PVRIRsprdaIALGIgmvh 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 83 ----LPDArgvykrLSARENIAYF---GQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDP 155
Cdd:COG3845 87 qhfmLVPN------LTVAENIVLGlepTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1755611750 156 RNVILDEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADE 222
Cdd:COG3845 161 RILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAE 227
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-236 |
3.50e-30 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 112.87 E-value: 3.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSFKTKTglvkAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAVR-RA 79
Cdd:COG4604 1 MIEIKNVSKRYGGKV----VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELaKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 80 LGVLPDARGVYKRLSARENIAyFGQL-HgmSRTQI-AERTRLLSHA---LDMDDILDRQTEGFSQGQRTKTAIARALVHD 154
Cdd:COG4604 77 LAILRQENHINSRLTVRELVA-FGRFpY--SKGRLtAEDREIIDEAiayLDLEDLADRYLDELSGGQRQRAFIAMVLAQD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 155 PRNVILDEPTNGLDVMTTRAMRGFLQQLRAE-GRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADELraATgEDNLE 233
Cdd:COG4604 154 TDYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI--IT-PEVLS 230
|
...
gi 1755611750 234 DAF 236
Cdd:COG4604 231 DIY 233
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
10-212 |
3.51e-30 |
|
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: 110.55 E-value: 3.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 10 SFKTKTGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHdpvavrralgvlpdargv 89
Cdd:cd03228 7 SFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRD------------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 90 YKRLSARENIAYFGQlhgmsrtqiaeRTRLLSHALdMDDILdrqtegfSQGQRTKTAIARALVHDPRNVILDEPTNGLDV 169
Cdd:cd03228 69 LDLESLRKNIAYVPQ-----------DPFLFSGTI-RENIL-------SGGQRQRIAIARALLRDPPILILDEATSALDP 129
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1755611750 170 MTTRAMRGFLQQLRaEGRCVIFSSHIMQEVaALCDRIVIIAKG 212
Cdd:cd03228 130 ETEALILEALRALA-KGKTVIVIAHRLSTI-RDADRIIVLDDG 170
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
19-228 |
3.61e-30 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 117.57 E-value: 3.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 19 KAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVD-AAHDPVAVRRALGVLP-DArGVYKRlSAR 96
Cdd:COG1132 354 PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDiRDLTLESLRRQIGVVPqDT-FLFSG-TIR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 97 ENIAYfGQLhGMSRTQIAErtrllshALDM---DDILDRQTEGF-----------SQGQRTKTAIARALVHDPRNVILDE 162
Cdd:COG1132 432 ENIRY-GRP-DATDEEVEE-------AAKAaqaHEFIEALPDGYdtvvgergvnlSGGQRQRIAIARALLKDPPILILDE 502
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 163 PTNGLDVMTTRAMRGFLQQLRAeGRCVIFSSH----IMQevaalCDRIVIIAKGTVVAAGTADELRAATG 228
Cdd:COG1132 503 ATSALDTETEALIQEALERLMK-GRTTIVIAHrlstIRN-----ADRILVLDDGRIVEQGTHEELLARGG 566
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-223 |
8.75e-30 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 111.24 E-value: 8.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSFktktGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPV---AVR 77
Cdd:COG1126 1 MIEIENLHKSF----GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKdinKLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 78 RALGVlpdargV------YKRLSARENIAYfGQLH--GMSRTQIAERTRllsHALDMDDILDRQTEGFSQ---GQRTKTA 146
Cdd:COG1126 77 RKVGM------VfqqfnlFPHLTVLENVTL-APIKvkKMSKAEAEERAM---ELLERVGLADKADAYPAQlsgGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 147 IARALVHDPRnVIL-DEPTNGLD---------VMttramrgflQQLRAEGRCVIFSSHIMQ---EVAalcDRIVIIAKGT 213
Cdd:COG1126 147 IARALAMEPK-VMLfDEPTSALDpelvgevldVM---------RDLAKEGMTMVVVTHEMGfarEVA---DRVVFMDGGR 213
|
250
....*....|
gi 1755611750 214 VVAAGTADEL 223
Cdd:COG1126 214 IVEEGPPEEF 223
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-223 |
1.39e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 111.71 E-value: 1.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSFKTKTglvKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDP---VAVR 77
Cdd:PRK13639 1 ILETRDLKYSYPDGT---EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKkslLEVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 78 RALGVL---PDARGVYKRLsaRENIAyFGQLH-GMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVH 153
Cdd:PRK13639 78 KTVGIVfqnPDDQLFAPTV--EEDVA-FGPLNlGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 154 DPRNVILDEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
12-214 |
1.81e-29 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 109.80 E-value: 1.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 12 KTKTGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDP----VAVRRALG-VLPDA 86
Cdd:cd03292 8 KTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraiPYLRRKIGvVFQDF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 87 RGVYKRlSARENIAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNG 166
Cdd:cd03292 88 RLLPDR-NVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGN 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1755611750 167 LDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTV 214
Cdd:cd03292 167 LDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
20-228 |
2.02e-29 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 115.63 E-value: 2.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 20 AVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAH-DPVAVRRALGVLP------DArgvykr 92
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDlDEDDLRRRIAVVPqrphlfDT------ 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 93 lSARENI------AYFGQLHgmsrtQIAERTRL--LSHALD--MDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDE 162
Cdd:COG4987 424 -TLRENLrlarpdATDEELW-----AALERVGLgdWLAALPdgLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDE 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1755611750 163 PTNGLDVMTTRA-MRGFLQQLRaeGRCVIFSSHIMQEVAAlCDRIVIIAKGTVVAAGTADELRAATG 228
Cdd:COG4987 498 PTEGLDAATEQAlLADLLEALA--GRTVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEELLAQNG 561
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
17-229 |
2.28e-29 |
|
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: 116.27 E-value: 2.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 17 LVKAVNGVSFNAAD--------GQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAVRRALGVLPDARG 88
Cdd:TIGR01257 1943 LTKVYSGTSSPAVDrlcvgvrpGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDA 2022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 89 VYKRLSARENIAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLD 168
Cdd:TIGR01257 2023 IDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMD 2102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1755611750 169 VMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADELRAATGE 229
Cdd:TIGR01257 2103 PQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGD 2163
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
26-226 |
7.46e-29 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 108.78 E-value: 7.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 26 FNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGvdaaHDPVAVRRALGVLP-----------DARGVYkrLS 94
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAG----ASPGKGWRHIGYVPqrhefawdfpiSVAHTV--MS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 95 AREniayfGQLHGMSRTQIAERtRLLSHALD---MDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMT 171
Cdd:TIGR03771 75 GRT-----GHIGWLRRPCVADF-AAVRDALRrvgLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPT 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1755611750 172 TRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIaKGTVVAAGTADELRAA 226
Cdd:TIGR03771 149 QELLTELFIELAGAGTAILMTTHDLAQAMATCDRVVLL-NGRVIADGTPQQLQDP 202
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-219 |
7.49e-29 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 111.43 E-value: 7.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSFKTKTGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVD----AAHDPVAV 76
Cdd:PRK11153 1 MIELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDltalSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 77 RRALGV------LPDARGVYkrlsarENIAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARA 150
Cdd:PRK11153 81 RRQIGMifqhfnLLSSRTVF------DNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 151 LVHDPRNVILDEPTNGLDVMTTRAMRGFLQQLRAE-GRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGT 219
Cdd:PRK11153 155 LASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGT 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
13-240 |
1.23e-28 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 109.27 E-value: 1.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 13 TKTGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVD----AAHDPVAVRR--------AL 80
Cdd:cd03294 32 KKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDiaamSRKELRELRRkkismvfqSF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 81 GVLPdargvykRLSARENIAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVIL 160
Cdd:cd03294 112 ALLP-------HRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLM 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 161 DEPTNGLDVMTTRAMRGFLQQLRAE-GRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADELRAATGEDNLEDaFVKA 239
Cdd:cd03294 185 DEAFSALDPLIRREMQDELLRLQAElQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVRE-FFRG 263
|
.
gi 1755611750 240 I 240
Cdd:cd03294 264 V 264
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-214 |
1.92e-28 |
|
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: 106.36 E-value: 1.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 19 KAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAVRRALGV--LPDAR---GVYKRL 93
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIayVPEDRkreGLVLDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 94 SARENIAYfgqlhgmsrtqiaerTRLLShaldmddildrqteGfsqGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTR 173
Cdd:cd03215 94 SVAENIAL---------------SSLLS--------------G---GNQQKVVLARWLARDPRVLILDEPTRGVDVGAKA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1755611750 174 AMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTV 214
Cdd:cd03215 142 EIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
21-222 |
3.41e-28 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 112.15 E-value: 3.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 21 VNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAH-DPVAVRRALGVLP------DArgvykrl 93
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQwDREELGRHIGYLPqdvelfDG------- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 94 SARENIAYFGQ--------------LHGM-SR------TQIAERTRLLShaldmddildrqteGfsqGQRTKTAIARALV 152
Cdd:COG4618 421 TIAENIARFGDadpekvvaaaklagVHEMiLRlpdgydTRIGEGGARLS--------------G---GQRQRIGLARALY 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 153 HDPRNVILDEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQeVAALCDRIVIIAKGTVVAAGTADE 222
Cdd:COG4618 484 GDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDE 552
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-229 |
5.00e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 111.26 E-value: 5.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 19 KAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDG--VDAAHDPVAVRRALGVLPDAR---GVYKRL 93
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRSPRDAIRAGIAYVPEDRkgeGLVLDL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 94 SARENI-----AYFGQLHGMSRTQIAERTRLLSHALD--MDDIlDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNG 166
Cdd:COG1129 346 SIRENItlaslDRLSRGGLLDRRRERALAEEYIKRLRikTPSP-EQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRG 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1755611750 167 LDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVA---AGTADE---LRAATGE 229
Cdd:COG1129 425 IDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGeldREEATEeaiMAAATGG 493
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-213 |
1.03e-27 |
|
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: 105.59 E-value: 1.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSF-------KTktglVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVD----GVD- 68
Cdd:COG4778 4 LLEVENLSKTFtlhlqggKR----LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 69 ---AAHDPVAVRRA--------LGVLPdargvykRLSARENIAYFGQLHGMSRTQIAERTRLLSHALDMDDILDR---QT 134
Cdd:COG4778 80 aqaSPREILALRRRtigyvsqfLRVIP-------RVSALDVVAEPLLERGVDREEARARARELLARLNLPERLWDlppAT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1755611750 135 egFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGT 213
Cdd:COG4778 153 --FSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-223 |
1.43e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 106.23 E-value: 1.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLhkSFKTKTGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVA-VRRA 79
Cdd:PRK13632 7 MIKVENV--SFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKeIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 80 LGVL---PDARGVykRLSARENIAyFGQLHGM-SRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDP 155
Cdd:PRK13632 85 IGIIfqnPDNQFI--GATVEDDIA-FGLENKKvPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1755611750 156 RNVILDEPTNGLDVMTTRAMRGFLQQLRAEG-RCVIFSSHIMQEvAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHDMDE-AILADKVIVFSEGKLIAQGKPKEI 229
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
8-223 |
3.57e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 105.48 E-value: 3.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 8 HKSFKTKTGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPV-AVRRALGVL--- 83
Cdd:PRK13635 10 HISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVwDVRRQVGMVfqn 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 84 PDARGVYKrlSARENIAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEP 163
Cdd:PRK13635 90 PDNQFVGA--TVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1755611750 164 TNGLDVMTTRAMRGFLQQLRAEGRCVIFS-SHIMQEvAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:PRK13635 168 TSMLDPRGRREVLETVRQLKEQKGITVLSiTHDLDE-AAQADRVIVMNKGEILEEGTPEEI 227
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
21-218 |
5.80e-27 |
|
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: 102.63 E-value: 5.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 21 VNGVSFNAADGQITGLLGPNGAGKTTTLRML--YTLMTPDQGSVRVDGVDAahDPVAVRRALGVLPDARGVYKRLSAREN 98
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPL--DKRSFRKIIGYVPQDDILHPTLTVRET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 99 IAYFGQLHGMSrtqiaertrllshaldmddildrqteGfsqGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRAMRGF 178
Cdd:cd03213 103 LMFAAKLRGLS--------------------------G---GERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1755611750 179 LQQLRAEGRCVIFSSHimQ---EVAALCDRIVIIAKGTVVAAG 218
Cdd:cd03213 154 LRRLADTGRTIICSIH--QpssEIFELFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
19-222 |
9.38e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 104.74 E-value: 9.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 19 KAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVA---VRRALGVL---PDAR----G 88
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlsdIRKKVGLVfqyPEYQlfeeT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 89 VYKrlsareNIAYFGQLHGMSRTQIAERTRLLSHA--LDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNG 166
Cdd:PRK13637 101 IEK------DIAFGPINLGLSEEEIENRVKRAMNIvgLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1755611750 167 LDVMTTRAMRGFLQQLRAE-GRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADE 222
Cdd:PRK13637 175 LDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPRE 231
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-236 |
1.29e-26 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 103.70 E-value: 1.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSFKTKTGLvkavNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAH-DPVAVRRA 79
Cdd:PRK13548 2 MLEARNLSVRLGGRTLL----DDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwSPAELARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 80 LGVLPDARGVYKRLSARENIAYFGQLHGMSRtqiAERTRLLSHAL---DMDDILDRQTEGFSQGQRTKTAIARALV---- 152
Cdd:PRK13548 78 RAVLPQHSSLSFPFTVEEVVAMGRAPHGLSR---AEDDALVAAALaqvDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwe 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 153 --HDPRNVILDEPTNGLD------VMTTramrgfLQQL-RAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADE- 222
Cdd:PRK13548 155 pdGPPRWLLLDEPTSALDlahqhhVLRL------ARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEv 228
|
250
....*....|....
gi 1755611750 223 LRAatgeDNLEDAF 236
Cdd:PRK13548 229 LTP----ETLRRVY 238
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
25-223 |
1.39e-26 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 102.91 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 25 SFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPvavrralgvlPDARGV---------YKRLSA 95
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP----------PAERPVsmlfqennlFPHLTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 96 RENIAyFGqLH-GMSRTQiAERTRlLSHALD---MDDILDRQTEGFSQGQRTKTAIARALVhDPRNV-ILDEPTNGLDVM 170
Cdd:COG3840 89 AQNIG-LG-LRpGLKLTA-EQRAQ-VEQALErvgLAGLLDRLPGQLSGGQRQRVALARCLV-RKRPIlLLDEPFSALDPA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1755611750 171 TTRAMRGFLQQLRAE-GRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:COG3840 164 LRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAAL 217
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-224 |
1.65e-26 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 107.06 E-value: 1.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSFktktGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAVRRAL 80
Cdd:PRK15439 11 LLCARSISKQY----SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 81 GV--LPDARGVYKRLSARENIayfgqLHGMSRTQIAERT-----RLLSHALDMD------DILDRQTegfsqgqrtkTAI 147
Cdd:PRK15439 87 GIylVPQEPLLFPNLSVKENI-----LFGLPKRQASMQKmkqllAALGCQLDLDssagslEVADRQI----------VEI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1755611750 148 ARALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADELR 224
Cdd:PRK15439 152 LRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLS 228
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
21-214 |
1.65e-26 |
|
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: 101.14 E-value: 1.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 21 VNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAH-DPVAVRRALGVLPdargvykrlsareni 99
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwDPNELGDHVGYLP--------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 100 ayfgqlhgmsrtqiaERTRLLSHALdMDDILdrqtegfSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRAMRGFL 179
Cdd:cd03246 83 ---------------QDDELFSGSI-AENIL-------SGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAI 139
|
170 180 190
....*....|....*....|....*....|....*
gi 1755611750 180 QQLRAEGRCVIFSSHIMqEVAALCDRIVIIAKGTV 214
Cdd:cd03246 140 AALKAAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-228 |
1.80e-26 |
|
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: 102.69 E-value: 1.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 2 IVVDSLHKSFKTKtglVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAH-DPVAVRRAL 80
Cdd:cd03253 1 IEFENVTFAYDPG---RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvTLDSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 81 GVLP-DArgVYKRLSARENIAYfGQLhGMSRTQIAERTRllshALDMDDILDRQTEGF-----------SQGQRTKTAIA 148
Cdd:cd03253 78 GVVPqDT--VLFNDTIGYNIRY-GRP-DATDEEVIEAAK----AAQIHDKIMRFPDGYdtivgerglklSGGEKQRVAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 149 RALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQLrAEGRCVIFSSHIMQEVAAlCDRIVIIAKGTVVAAGTADELRAATG 228
Cdd:cd03253 150 RAILKNPPILLLDEATSALDTHTEREIQAALRDV-SKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLAKGG 227
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-223 |
1.81e-26 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 105.69 E-value: 1.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 4 VDSLHKSFKTKtglvKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPvAVRRALGVL 83
Cdd:PRK11607 22 IRNLTKSFDGQ----HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP-PYQRPINMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 84 PDARGVYKRLSARENIAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEP 163
Cdd:PRK11607 97 FQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEP 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1755611750 164 TNGLDvmttRAMRGFLQQ-----LRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:PRK11607 177 MGALD----KKLRDRMQLevvdiLERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
13-223 |
2.84e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 102.96 E-value: 2.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 13 TKTGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPV-AVRRALGVL---PDARg 88
Cdd:PRK13652 12 SYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIrEVRKFVGLVfqnPDDQ- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 89 VYKRlSARENIAyFGQLH-GMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGL 167
Cdd:PRK13652 91 IFSP-TVEQDIA-FGPINlGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1755611750 168 DVMTTRAMRGFLQQLRAE-GRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:PRK13652 169 DPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
19-228 |
7.64e-26 |
|
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: 100.77 E-value: 7.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 19 KAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVA-VRRALGVLPDARGVYKRlSARE 97
Cdd:cd03251 16 PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLAsLRRQIGLVSQDVFLFND-TVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 98 NIAYfgQLHGMSRTQIAERTRlLSHAldmDDILDRQTEGF-----------SQGQRTKTAIARALVHDPRNVILDEPTNG 166
Cdd:cd03251 95 NIAY--GRPGATREEVEEAAR-AANA---HEFIMELPEGYdtvigergvklSGGQRQRIAIARALLKDPPILILDEATSA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1755611750 167 LDVMTTRAMRGFLQQLrAEGRCVIFSSHIMQEVAAlCDRIVIIAKGTVVAAGTADELRAATG 228
Cdd:cd03251 169 LDTESERLVQAALERL-MKNRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLAQGG 228
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-223 |
9.98e-26 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 103.24 E-value: 9.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 2 IVVDSLHKSFktktGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHdpVAVR-RAL 80
Cdd:PRK10851 3 IEIANIKKSF----GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSR--LHARdRKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 81 GVLPDARGVYKRLSARENIAyFG--QLHGMSRTQIAERTRLLSHALDM---DDILDRQTEGFSQGQRTKTAIARALVHDP 155
Cdd:PRK10851 77 GFVFQHYALFRHMTVFDNIA-FGltVLPRRERPNAAAIKAKVTQLLEMvqlAHLADRYPAQLSGGQKQRVALARALAVEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1755611750 156 RNVILDEPTNGLDVMTTRAMRGFLQQLRAEGRCV-IFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:PRK10851 156 QILLLDEPFGALDAQVRKELRRWLRQLHEELKFTsVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
23-210 |
1.61e-25 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 99.11 E-value: 1.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 23 GVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAVRRALGVLPDARGVYKRLSARENIAYF 102
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLGHQPGIKTELTALENLRFY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 103 GQLHGMSRTQIAErtrllsHALDM------DDILDRQtegFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRAMR 176
Cdd:PRK13538 99 QRLHGPGDDEALW------EALAQvglagfEDVPVRQ---LSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLE 169
|
170 180 190
....*....|....*....|....*....|....
gi 1755611750 177 GFLQQLRAEGRCVIFSSHimQEVAALCDRIVIIA 210
Cdd:PRK13538 170 ALLAQHAEQGGMVILTTH--QDLPVASDKVRKLR 201
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-223 |
1.75e-25 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 102.49 E-value: 1.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 2 IVVDSLHKSFKTKTglvkAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAVRRALG 81
Cdd:PRK11432 7 VVLKNITKRFGSNT----VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 82 VLpDARGVYKRLSARENIAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILD 161
Cdd:PRK11432 83 VF-QSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1755611750 162 EPTNGLDVMTTRAMRGFLQQLRAE-GRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:PRK11432 162 EPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-214 |
1.81e-25 |
|
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: 99.53 E-value: 1.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 2 IVVDSLHKSFKTKtglvKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVA---VRR 78
Cdd:cd03262 1 IEIKNLHKSFGDF----HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNineLRQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 79 ALGVLPDARGVYKRLSARENIAyFG--QLHGMSRTQIAERTRllsHALDMDDILDRQTEGFSQ---GQRTKTAIARALVH 153
Cdd:cd03262 77 KVGMVFQQFNLFPHLTVLENIT-LApiKVKGMSKAEAEERAL---ELLEKVGLADKADAYPAQlsgGQQQRVAIARALAM 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1755611750 154 DPRNVILDEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIM---QEVAalcDRIVIIAKGTV 214
Cdd:cd03262 153 NPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMgfaREVA---DRVIFMDDGRI 213
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
20-228 |
2.32e-25 |
|
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: 99.61 E-value: 2.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 20 AVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVA-VRRALGVLPDARGVYKRlSAREN 98
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKsLRSMIGVVLQDTFLFSG-TIMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 99 IAYFGQLHGMSRTQIAERtrllshALDMDDILDRQTEG-----------FSQGQRTKTAIARALVHDPRNVILDEPTNGL 167
Cdd:cd03254 97 IRLGRPNATDEEVIEAAK------EAGAHDFIMKLPNGydtvlgenggnLSQGERQLLAIARAMLRDPKILILDEATSNI 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1755611750 168 DVMTTRAMRGFLQQLRaEGRCVIFSSH---IMQEVaalcDRIVIIAKGTVVAAGTADELRAATG 228
Cdd:cd03254 171 DTETEKLIQEALEKLM-KGRTSIIIAHrlsTIKNA----DKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
29-218 |
2.78e-25 |
|
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: 98.72 E-value: 2.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 29 ADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAvRRALGVLPDARGVYKRLSARENIAyFGQLHGM 108
Cdd:cd03298 22 AQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA-DRPVSMLFQENNLFAHLTVEQNVG-LGLSPGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 109 SRTQIaERTRLLSHALDM--DDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQLRAE- 185
Cdd:cd03298 100 KLTAE-DRQAIEVALARVglAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAEt 178
|
170 180 190
....*....|....*....|....*....|...
gi 1755611750 186 GRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAG 218
Cdd:cd03298 179 KMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-212 |
2.87e-25 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 99.94 E-value: 2.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSFKTKTGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVdAAHDPVAVRral 80
Cdd:COG4525 3 MLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGV-PVTGPGADR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 81 GVLPDARGVYKRLSARENIAyFG-QLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVI 159
Cdd:COG4525 79 GVVFQKDALLPWLNVLDNVA-FGlRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1755611750 160 LDEPTNGLDVMTTRAMRGFLQQL-RAEGRCVIFSSHIMQEVAALCDRIVIIAKG 212
Cdd:COG4525 158 MDEPFGALDALTREQMQELLLDVwQRTGKGVFLITHSVEEALFLATRLVVMSPG 211
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-228 |
3.39e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 102.23 E-value: 3.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSFktktGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVD-AAHDPVAVRRA 79
Cdd:PRK09536 3 MIDVSDLSVEF----GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDvEALSARAASRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 80 LGVLPDARGVYKRLSARENI-----AYFGQLHGMSRTQIAERTRLLSHAlDMDDILDRQTEGFSQGQRTKTAIARALVHD 154
Cdd:PRK09536 79 VASVPQDTSLSFEFDVRQVVemgrtPHRSRFDTWTETDRAAVERAMERT-GVAQFADRPVTSLSGGERQRVLLARALAQA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 155 PRNVILDEPTNGLDVmtTRAMRGF--LQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAG------TADELRAA 226
Cdd:PRK09536 158 TPVLLLDEPTASLDI--NHQVRTLelVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGppadvlTADTLRAA 235
|
..
gi 1755611750 227 TG 228
Cdd:PRK09536 236 FD 237
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
23-228 |
3.42e-25 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 103.65 E-value: 3.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 23 GVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVD-AAHDPVAVRRALGVLPDARGVYKRlSARENIAY 101
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPlVQYDHHYLHRQVALVGQEPVLFSG-SVRENIAY 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 102 fgqlhGMSRTQIAErTRLLSHALDMDDILDRQTEGF-----------SQGQRTKTAIARALVHDPRNVILDEPTNGLDVM 170
Cdd:TIGR00958 578 -----GLTDTPDEE-IMAAAKAANAHDFIMEFPNGYdtevgekgsqlSGGQKQRIAIARALVRKPRVLILDEATSALDAE 651
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1755611750 171 TTRAmrgfLQQLR-AEGRCVIFSSHIMQEVAAlCDRIVIIAKGTVVAAGTADELRAATG 228
Cdd:TIGR00958 652 CEQL----LQESRsRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQG 705
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
19-209 |
4.15e-25 |
|
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: 103.14 E-value: 4.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 19 KAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAH-DPVAVRRALGVLPDARGVYKRlSARE 97
Cdd:TIGR02857 336 PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADaDADSWRDQIAWVPQHPFLFAG-TIAE 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 98 NIAyFGQLhGMSRTQIAERTRL-----LSHAL--DMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVM 170
Cdd:TIGR02857 415 NIR-LARP-DASDAEIREALERagldeFVAALpqGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAE 492
|
170 180 190
....*....|....*....|....*....|....*....
gi 1755611750 171 TTRAMRGFLQQLrAEGRCVIFSSHiMQEVAALCDRIVII 209
Cdd:TIGR02857 493 TEAEVLEALRAL-AQGRTVLLVTH-RLALAALADRIVVL 529
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-218 |
4.92e-25 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 102.94 E-value: 4.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSFktktGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAH-DP-VAVRR 78
Cdd:PRK09700 5 YISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKlDHkLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 79 ALGVLPDARGVYKRLSARENIaYFGQL--------HGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARA 150
Cdd:PRK09700 81 GIGIIYQELSVIDELTVLENL-YIGRHltkkvcgvNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1755611750 151 LVHDPRNVILDEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAG 218
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-236 |
5.50e-25 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 99.03 E-value: 5.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSFKTKTglvkAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVD-AAHDPVAVRRA 79
Cdd:COG4559 1 MLEAENLSVRLGGRT----LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPlAAWSPWELARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 80 LGVLPDARGVYKRLSARENIAyFGQL-HGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARAL--VHDPR 156
Cdd:COG4559 77 RAVLPQHSSLAFPFTVEEVVA-LGRApHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqLWEPV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 157 N-----VILDEPTNGLD------VMTTramrgfLQQLRAEGRCVIFsshIMQEV--AAL-CDRIVIIAKGTVVAAGTADE 222
Cdd:COG4559 156 DggprwLFLDEPTSALDlahqhaVLRL------ARQLARRGGGVVA---VLHDLnlAAQyADRILLLHQGRLVAQGTPEE 226
|
250
....*....|....*
gi 1755611750 223 -LRAAtgedNLEDAF 236
Cdd:COG4559 227 vLTDE----LLERVY 237
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-223 |
7.69e-25 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 100.19 E-value: 7.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 2 IVVDSLHKSFKTKTGL-------VKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPV 74
Cdd:COG4608 8 LEVRDLKKHFPVRGGLfgrtvgvVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 75 AVRRAL------------GVL-PdargvykRLSARENIAYFGQLHGM-SRTQIAERTRLLshaLDM----DDILDRQTEG 136
Cdd:COG4608 88 RELRPLrrrmqmvfqdpyASLnP-------RMTVGDIIAEPLRIHGLaSKAERRERVAEL---LELvglrPEHADRYPHE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 137 FSQGQRTKTAIARALVHDPRNVILDEPTNGLDVmTTRA----MrgfLQQLRAE-GRCVIFSSHIMQEVAALCDRIVIIAK 211
Cdd:COG4608 158 FSGGQRQRIGIARALALNPKLIVCDEPVSALDV-SIQAqvlnL---LEDLQDElGLTYLFISHDLSVVRHISDRVAVMYL 233
|
250
....*....|..
gi 1755611750 212 GTVVAAGTADEL 223
Cdd:COG4608 234 GKIVEIAPRDEL 245
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
16-223 |
8.66e-25 |
|
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: 102.19 E-value: 8.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 16 GLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRV----DGVDAAHDPVAVR----RALGVLPDAR 87
Cdd:TIGR03269 295 GVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPDGRgrakRYIGILHQEY 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 88 GVYKRLSARENIAYFGQLH-----GMSRTQIAertrLLSHALDMD---DILDRQTEGFSQGQRTKTAIARALVHDPRNVI 159
Cdd:TIGR03269 375 DLYPHRTVLDNLTEAIGLElpdelARMKAVIT----LKMVGFDEEkaeEILDKYPDELSEGERHRVALAQVLIKEPRIVI 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1755611750 160 LDEPTNGLDVMTTRAMRGFLQQLRAE-GRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:TIGR03269 451 LDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-223 |
9.90e-25 |
|
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: 102.07 E-value: 9.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 4 VDSLHKSFKTKTGL-------VKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMtPDQGSVRVDGVD-AAHDPVA 75
Cdd:COG4172 278 ARDLKVWFPIKRGLfrrtvghVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDlDGLSRRA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 76 ---VRRALGVlpdargVYK--------RLSARENIAYFGQLH--GMSRTQIAERTRLLSHALDMD-DILDRQTEGFSQGQ 141
Cdd:COG4172 357 lrpLRRRMQV------VFQdpfgslspRMTVGQIIAEGLRVHgpGLSAAERRARVAEALEEVGLDpAARHRYPHEFSGGQ 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 142 RTKTAIARALVHDPRNVILDEPTNGLDvMTTRA-MRGFLQQLRAE-GRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGT 219
Cdd:COG4172 431 RQRIAIARALILEPKLLVLDEPTSALD-VSVQAqILDLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGP 509
|
....
gi 1755611750 220 ADEL 223
Cdd:COG4172 510 TEQV 513
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
21-226 |
1.04e-24 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 102.04 E-value: 1.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 21 VNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAH-DPVAVRRALGVLPDARGVYKRlSARENI 99
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQwDRETFGKHIGYLPQDVELFPG-TVAENI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 100 AYFGQlhGMSRTQIAERTRL-------LSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTT 172
Cdd:TIGR01842 413 ARFGE--NADPEKIIEAAKLagvheliLRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGE 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1755611750 173 RAMRGFLQQLRAEGRCVIFSSHiMQEVAALCDRIVIIAKGTVVAAGTADELRAA 226
Cdd:TIGR01842 491 QALANAIKALKARGITVVVITH-RPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
20-225 |
1.15e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 99.15 E-value: 1.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 20 AVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDG--VD-AAHDPVAVRRALGVL---PD----ARGV 89
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDySRKGLMKLRESVGMVfqdPDnqlfSASV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 90 YKRLSareniayFGQLH-GMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLD 168
Cdd:PRK13636 101 YQDVS-------FGAVNlKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1755611750 169 VMTTRAMRGFLQQLRAE-GRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADELRA 225
Cdd:PRK13636 174 PMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFA 231
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
20-228 |
1.21e-24 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 101.96 E-value: 1.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 20 AVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVA-VRRALGVLPDARGVYKRlSAREN 98
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAsLRRNIAVVFQDAGLFNR-SIEDN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 99 IAYfgqlhGMSRTQIAERTRLLSHALDMDDILdRQTEGF-----------SQGQRTKTAIARALVHDPRNVILDEPTNGL 167
Cdd:PRK13657 429 IRV-----GRPDATDEEMRAAAERAQAHDFIE-RKPDGYdtvvgergrqlSGGERQRLAIARALLKDPPILILDEATSAL 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1755611750 168 DVMTTRAMRGFLQQLRaEGRCVIFSSHIMQEVAAlCDRIVIIAKGTVVAAGTADELRAATG 228
Cdd:PRK13657 503 DVETEAKVKAALDELM-KGRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFDELVARGG 561
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
16-219 |
1.37e-24 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 97.18 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 16 GLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAH-DPVAVRRALGVLP-DA---RGvy 90
Cdd:cd03244 15 NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiGLHDLRSRISIIPqDPvlfSG-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 91 krlSARENIAYFGQLHGMSRTQIAERTRLLSHALDMDDILD-RQTEG---FSQGQRTKTAIARALVHDPRNVILDEPTNG 166
Cdd:cd03244 93 ---TIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDtVVEEGgenLSVGQRQLLCLARALLRKSKILVLDEATAS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1755611750 167 LDVMTTRAMRgflQQLRAE--GRCVIFSSH----IMQevaalCDRIVIIAKGTVVAAGT 219
Cdd:cd03244 170 VDPETDALIQ---KTIREAfkDCTVLTIAHrldtIID-----SDRILVLDKGRVVEFDS 220
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
23-236 |
1.55e-24 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 97.60 E-value: 1.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 23 GVSFNAADGQITGLLGPNGAGKTTTLRMLYTLmTPDQGSVRVDGVDAAHDPV---AVRRA-LG---VLPDARGVYKRLsa 95
Cdd:COG4138 14 PISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAaelARHRAyLSqqqSPPFAMPVFQYL-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 96 reniayfgQLHGMSRTQIAERTRLLSH---ALDMDDILDRQTEGFSQG--QRTKtaIARAL--VH-----DPRNVILDEP 163
Cdd:COG4138 91 --------ALHQPAGASSEAVEQLLAQlaeALGLEDKLSRPLTQLSGGewQRVR--LAAVLlqVWptinpEGQLLLLDEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1755611750 164 TNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADELRAatgEDNLEDAF 236
Cdd:COG4138 161 MNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMT---PENLSEVF 230
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
23-195 |
2.92e-24 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 96.10 E-value: 2.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 23 GVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGvDAAHDPvAVRRALGVLPDARGVYKRLSARENIAYF 102
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG-GDIDDP-DVAEACHYLGHRNAMKPALTVAENLEFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 103 GQLHGMSRTQIAERTRllshALDMDDILDRQTEGFSQGQRTKTAIARALVHdPRNV-ILDEPTNGLDVMTTRAMRGFLQQ 181
Cdd:PRK13539 98 AAFLGGEELDIAAALE----AVGLAPLAHLPFGYLSAGQKRRVALARLLVS-NRPIwILDEPTAALDAAAVALFAELIRA 172
|
170
....*....|....
gi 1755611750 182 LRAEGRCVIFSSHI 195
Cdd:PRK13539 173 HLAQGGIVIAATHI 186
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-223 |
4.71e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 98.00 E-value: 4.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 4 VDSLHKSFKTKT-GLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAVRRALGV 82
Cdd:PRK13631 24 VKNLYCVFDEKQeNELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELITNP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 83 LPDARGVYKRLSARENIAY-----------------FGQLH-GMSRTQIAERTR--LLSHALDmDDILDRQTEGFSQGQR 142
Cdd:PRK13631 104 YSKKIKNFKELRRRVSMVFqfpeyqlfkdtiekdimFGPVAlGVKKSEAKKLAKfyLNKMGLD-DSYLERSPFGLSGGQK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 143 TKTAIARALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADE 222
Cdd:PRK13631 183 RRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYE 262
|
.
gi 1755611750 223 L 223
Cdd:PRK13631 263 I 263
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
16-225 |
5.46e-24 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 96.10 E-value: 5.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 16 GLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVA--VRRALGVLPDARGVYKRL 93
Cdd:PRK11614 16 GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAkiMREAVAIVPEGRRVFSRM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 94 SARENIAYFGQLhgMSRTQIAERTRLLSHALDMddILDRQTE---GFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVM 170
Cdd:PRK11614 96 TVEENLAMGGFF--AERDQFQERIKWVYELFPR--LHERRIQragTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPI 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1755611750 171 TTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADELRA 225
Cdd:PRK11614 172 IIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLA 226
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
25-214 |
6.59e-24 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 95.31 E-value: 6.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 25 SFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPvAVRRALGVLPDARGVYKRLSARENIAyFGQ 104
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLA-PYQRPVSMLFQENNLFAHLTVRQNIG-LGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 105 LHGMSRTQI-AERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQLR 183
Cdd:TIGR01277 96 HPGLKLNAEqQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLC 175
|
170 180 190
....*....|....*....|....*....|..
gi 1755611750 184 AE-GRCVIFSSHIMQEVAALCDRIVIIAKGTV 214
Cdd:TIGR01277 176 SErQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
20-212 |
7.26e-24 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 96.31 E-value: 7.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 20 AVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVdAAHDPVAVRralGVLPDARGVYKRLSARENI 99
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK-PVEGPGAER---GVVFQNEGLLPWRNVQDNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 100 AYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRAMRGFL 179
Cdd:PRK11248 92 AFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLL 171
|
170 180 190
....*....|....*....|....*....|....
gi 1755611750 180 QQLRAE-GRCVIFSSHIMQEVAALCDRIVIIAKG 212
Cdd:PRK11248 172 LKLWQEtGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
16-224 |
3.72e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 94.29 E-value: 3.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 16 GLVkAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAVRRALGVLPDARGV--YKRL 93
Cdd:PRK11300 17 GLL-AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRTFQHVrlFREM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 94 SAREN--IAYFGQ-----LHGMSRT---QIAERTRL--LSHALDMDDILD---RQTEGFSQGQRTKTAIARALVHDPRNV 158
Cdd:PRK11300 96 TVIENllVAQHQQlktglFSGLLKTpafRRAESEALdrAATWLERVGLLEhanRQAGNLAYGQQRRLEIARCMVTQPEIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1755611750 159 ILDEPTNGLDVMTTRAMRGFLQQLRAE-GRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADELR 224
Cdd:PRK11300 176 MLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIR 242
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
19-223 |
4.17e-23 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 94.33 E-value: 4.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 19 KAVNGVSFNAADGQITGLLGPNGAGKTTTLRmlyTL-----MTPDQ---GSVRVDGVDAAH---DPVAVRRALGVlpdar 87
Cdd:COG1117 25 QALKDINLDIPENKVTALIGPSGCGKSTLLR---CLnrmndLIPGArveGEILLDGEDIYDpdvDVVELRRRVGM----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 88 gVYKR-----LSARENIAYFGQLHGM-SRTQIAERTR--LLSHAL--DMDDILDRQTEGFSQGQRTKTAIARALVHDPRn 157
Cdd:COG1117 97 -VFQKpnpfpKSIYDNVAYGLRLHGIkSKSELDEIVEesLRKAALwdEVKDRLKKSALGLSGGQQQRLCIARALAVEPE- 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1755611750 158 VIL-DEPTNGLDVMTTRAMRGFLQQLRAEgRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:COG1117 175 VLLmDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQI 240
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-230 |
1.24e-22 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 92.89 E-value: 1.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSFKTKTGLvkavNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGV--DAAHdPV---- 74
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVL----HGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDItiDTAR-SLsqqk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 75 ----AVRRALGVLPDARGVYKRLSARENIAYfG--QLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIA 148
Cdd:PRK11264 78 glirQLRQHVGFVFQNFNLFPHRTVLENIIE-GpvIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 149 RALVHDPRNVILDEPTNGLD------VMTTramrgfLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADE 222
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDpelvgeVLNT------IRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKA 230
|
....*...
gi 1755611750 223 LRAATGED 230
Cdd:PRK11264 231 LFADPQQP 238
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-227 |
1.29e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 93.15 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 21 VNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDP---VAVRRALGVL---PDARGVYKRLS 94
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKrglLALRQQVATVfqdPEQQIFYTDID 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 95 AreNIAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRA 174
Cdd:PRK13638 97 S--DIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1755611750 175 MRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADELRAAT 227
Cdd:PRK13638 175 MIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACT 227
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
23-195 |
1.76e-22 |
|
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: 91.40 E-value: 1.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 23 GVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAVRRALGVLPDARGVYKRLSARENIAYF 102
Cdd:cd03231 18 GLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 103 GQLHgmSRTQIAErtrllshALDMDDIL---DRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRAMRGFL 179
Cdd:cd03231 98 HADH--SDEQVEE-------ALARVGLNgfeDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAM 168
|
170
....*....|....*.
gi 1755611750 180 QQLRAEGRCVIFSSHI 195
Cdd:cd03231 169 AGHCARGGMVVLTTHQ 184
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
18-228 |
1.96e-22 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 95.55 E-value: 1.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 18 VKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAVRRALGVLPDARGVYKRLSARE 97
Cdd:TIGR02203 345 RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIAN 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 98 NIAYfGQLHGMSRTQIAERTRllshALDMDDILDRQTEGF-----------SQGQRTKTAIARALVHDPRNVILDEPTNG 166
Cdd:TIGR02203 425 NIAY-GRTEQADRAEIERALA----AAYAQDFVDKLPLGLdtpigengvllSGGQRQRLAIARALLKDAPILILDEATSA 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1755611750 167 LDVMTTRAMRGFLQQLRaEGRCVIFSSHIMQEVAAlCDRIVIIAKGTVVAAGTADELRAATG 228
Cdd:TIGR02203 500 LDNESERLVQAALERLM-QGRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNELLARNG 559
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
4-215 |
2.76e-22 |
|
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: 90.78 E-value: 2.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 4 VDSLHKSFKTKTglvKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDaAHDPVAVRRALGVL 83
Cdd:cd03226 2 IENISFSYKKGT---EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP-IKAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 84 PDARGVYKRLSARENIAYFGQLHGMSRTQIAERTRLlshaLDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEP 163
Cdd:cd03226 78 QDVDYQLFTDSVREELLLGLKELDAGNEQAETVLKD----LDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1755611750 164 TNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVV 215
Cdd:cd03226 154 TSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
16-233 |
3.23e-22 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 93.65 E-value: 3.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 16 GLVKAVNGVSFNAADGQITGLLGPNGAGKTTTlRMLYTLMTPDQGSVRVDGVDAAHDPVAVRRALGV-LPDARGVYKRLS 94
Cdd:NF000106 24 GEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGRRPWRF*TWCANRRALRRTIG*hRPVR*GRRESFS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 95 ARENIAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRA 174
Cdd:NF000106 103 GRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1755611750 175 MRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADELRAATGEDNLE 233
Cdd:NF000106 183 VWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGGRTLQ 241
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-214 |
4.45e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 94.36 E-value: 4.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 4 VDSLHKSFKTKTGLvkavNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVD-GVDAAH---DPVA---- 75
Cdd:COG0488 1 LENLSKSFGGRPLL----DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPkGLRIGYlpqEPPLdddl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 76 -----VRRALGVLPDARGVYKRLSAR-----ENIAYFGQLHgmsrTQIAE--------RTRLLSHALDM-DDILDRQTEG 136
Cdd:COG0488 77 tvldtVLDGDAELRALEAELEELEAKlaepdEDLERLAELQ----EEFEAlggweaeaRAEEILSGLGFpEEDLDRPVSE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 137 FSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQLRAegrCVIFSSH---IMQEVaalCDRIVIIAKGT 213
Cdd:COG0488 153 LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPG---TVLVVSHdryFLDRV---ATRILELDRGK 226
|
.
gi 1755611750 214 V 214
Cdd:COG0488 227 L 227
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
11-218 |
4.51e-22 |
|
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: 90.79 E-value: 4.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 11 FKTKTGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTL-----RMLYTLMTpdQGSVRVDGVdaAHDPVAVRRALGVLPD 85
Cdd:cd03234 13 AKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLdaisgRVEGGGTT--SGQILFNGQ--PRKPDQFQKCVAYVRQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 86 ARGVYKRLSARENIAYFGQLHGMS------RTQIAERTRLLSHALDMddILDRQTEGFSQGQRTKTAIARALVHDPRNVI 159
Cdd:cd03234 89 DDILLPGLTVRETLTYTAILRLPRkssdaiRKKRVEDVLLRDLALTR--IGGNLVKGISGGERRRVSIAVQLLWDPKVLI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1755611750 160 LDEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHimQ---EVAALCDRIVIIAKGTVVAAG 218
Cdd:cd03234 167 LDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIH--QprsDLFRLFDRILLLSSGEIVYSG 226
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
12-242 |
4.56e-22 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 92.98 E-value: 4.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 12 KTKTGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGvdaahdpvavRRALGVLPDARGV-- 89
Cdd:PRK11650 11 KSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGG----------RVVNELEPADRDIam 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 90 -------YKRLSARENIAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDE 162
Cdd:PRK11650 81 vfqnyalYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 163 PTNGLDVMTTRAMRGFLQQL-RAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL--RAATgednledAFVKA 239
Cdd:PRK11650 161 PLSNLDAKLRVQMRLEIQRLhRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVyeKPAS-------TFVAS 233
|
....
gi 1755611750 240 -IGS 242
Cdd:PRK11650 234 fIGS 237
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-223 |
5.84e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 91.26 E-value: 5.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 24 VSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDG-----------VDAahdpVAVRRALGVLPDARGVYKR 92
Cdd:PRK14246 29 ITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGkvlyfgkdifqIDA----IKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 93 LSARENIAYFGQLHGMSRTQ-----IAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGL 167
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIKEKReikkiVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1755611750 168 DVMTTRAMRGFLQQLRAEgRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:PRK14246 185 DIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
23-195 |
7.66e-22 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 89.34 E-value: 7.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 23 GVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAVRRALGVLPDARGVYKRLSARENIAYF 102
Cdd:TIGR01189 18 GLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSALENLHFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 103 GQLHGMSRTQIAERTRllshALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQL 182
Cdd:TIGR01189 98 AAIHGGAQRTIEDALA----AVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAH 173
|
170
....*....|...
gi 1755611750 183 RAEGRCVIFSSHI 195
Cdd:TIGR01189 174 LARGGIVLLTTHQ 186
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-225 |
8.35e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 90.56 E-value: 8.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 4 VDSLHKSFktktGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAVRRALGVl 83
Cdd:COG4674 13 VEDLTVSF----DGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIARLGI- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 84 pdAR-----GVYKRLSAREN--IAY------FGQL-HGMSRTQ------IAERTRLLSHAldmddilDRQTEGFSQGQRT 143
Cdd:COG4674 88 --GRkfqkpTVFEELTVFENleLALkgdrgvFASLfARLTAEErdrieeVLETIGLTDKA-------DRLAGLLSHGQKQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 144 KTAIARALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQLrAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:COG4674 159 WLEIGMLLAQDPKLLLLDEPVAGMTDAETERTAELLKSL-AGKHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGSLDEV 237
|
..
gi 1755611750 224 RA 225
Cdd:COG4674 238 QA 239
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
18-223 |
1.05e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 93.17 E-value: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 18 VKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAVRRALGV--LPD---ARGVYKR 92
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVayIPEdrlGRGLVPD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 93 LSARENIA-------YFGQLHGMSRTQIAERTRllsHALDMDDI----LDRQTEGFSQGQRTKTAIARALVHDPRNVILD 161
Cdd:COG3845 351 MSVAENLIlgryrrpPFSRGGFLDRKAIRAFAE---ELIEEFDVrtpgPDTPARSLSGGNQQKVILARELSRDPKLLIAA 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1755611750 162 EPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:COG3845 428 QPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
10-218 |
1.13e-21 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 88.52 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 10 SFKTKTGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAVRRALGVLPDARGV 89
Cdd:cd03247 7 SFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVLNQRPYL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 90 YKRlSARENIAyfgqlhgmsrtqiaertrllshaldmddildrqtEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDV 169
Cdd:cd03247 87 FDT-TLRNNLG----------------------------------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1755611750 170 MTTRA-MRGFLQQLraEGRCVIFSSHIMQEVAALcDRIVIIAKGTVVAAG 218
Cdd:cd03247 132 ITERQlLSLIFEVL--KDKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
14-236 |
1.21e-21 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 92.40 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 14 KTGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAV-----RRALGVLPDARG 88
Cdd:PRK10070 37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevrRKKIAMVFQSFA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 89 VYKRLSARENIAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLD 168
Cdd:PRK10070 117 LMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1755611750 169 VMTTRAMRGFLQQLRAE-GRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADELRAATGEDNLEDAF 236
Cdd:PRK10070 197 PLIRTEMQDELVKLQAKhQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFF 265
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-230 |
1.35e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 93.23 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSFKTKTGLVK-------AVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMtPDQGSVRVDGVDAAH-- 71
Cdd:PRK15134 275 LLDVEQLQVAFPIRKGILKrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNln 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 72 --DPVAVRRALGVL---PDArGVYKRLSARENIAYFGQLH--GMSRTQIAERTRLLSHALDMD-DILDRQTEGFSQGQRT 143
Cdd:PRK15134 354 rrQLLPVRHRIQVVfqdPNS-SLNPRLNVLQIIEEGLRVHqpTLSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQ 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 144 KTAIARALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQLRAEGRCV-IFSSHIMQEVAALCDRIVIIAKGTVVAAGTADE 222
Cdd:PRK15134 433 RIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAyLFISHDLHVVRALCHQVIVLRQGEVVEQGDCER 512
|
....*...
gi 1755611750 223 LRAATGED 230
Cdd:PRK15134 513 VFAAPQQE 520
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-223 |
1.76e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 90.56 E-value: 1.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSFKTKTGLV-KAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGV-----DAAHDPV 74
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFAsRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIvvsstSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 75 AVRRALGVL---PDARgVYKRlSARENIAYFGQLHGMSRTqiaERTRLLSHALDM----DDILDRQTEGFSQGQRTKTAI 147
Cdd:PRK13643 81 PVRKKVGVVfqfPESQ-LFEE-TVLKDVAFGPQNFGIPKE---KAEKIAAEKLEMvglaDEFWEKSPFELSGGQMRRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1755611750 148 ARALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDV 231
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
8-215 |
2.36e-21 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 89.75 E-value: 2.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 8 HKSFKTKTGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAVRRALG-----V 82
Cdd:PRK10419 15 HGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRrdiqmV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 83 LPDARG-VYKRLSARENIAY-FGQLHGMSRTQIAERTRLLSHALDMDD-ILDRQTEGFSQGQRTKTAIARALVHDPRNVI 159
Cdd:PRK10419 95 FQDSISaVNPRKTVREIIREpLRHLLSLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1755611750 160 LDEPTNGLDVMTTRAMRGFLQQLRAE-GRCVIFSSHIMQEVAALCDRIVIIAKGTVV 215
Cdd:PRK10419 175 LDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-222 |
2.73e-21 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 88.64 E-value: 2.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSFKTKTGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAH---DPVAVR 77
Cdd:COG4181 8 IIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAldeDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 78 RALGV---------LPDargvykrLSARENIAYFGQLHGMSRTQiaERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIA 148
Cdd:COG4181 88 RARHVgfvfqsfqlLPT-------LTALENVMLPLELAGRRDAR--ARARALLERVGLGHRLDHYPAQLSGGEQQRVALA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1755611750 149 RALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQLRAE-GRCVIFSSHiMQEVAALCDRIVIIAKGTVVAAGTADE 222
Cdd:COG4181 159 RAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRErGTTLVLVTH-DPALAARCDRVLRLRAGRLVEDTAATA 232
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-223 |
3.13e-21 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 89.00 E-value: 3.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSFktktGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGV---DAAHDPVAVR 77
Cdd:PRK09493 1 MIEFKNVSKHF----GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLkvnDPKVDERLIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 78 RALGVLPDARGVYKRLSARENIAyFGQLH--GMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDP 155
Cdd:PRK09493 77 QEAGMVFQQFYLFPHLTALENVM-FGPLRvrGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1755611750 156 RNVILDEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVL 223
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-223 |
3.51e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 88.82 E-value: 3.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 9 KSFKTKTGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTL--MTPD---QGSVRVDGVDA-AHDPVAVRRALGV 82
Cdd:PRK14247 7 RDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEarvSGEVYLDGQDIfKMDVIELRRRVQM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 83 LPDARGVYKRLSARENIAYFGQLHGM--SRTQIAERTR-LLSHALDMDDILDR---QTEGFSQGQRTKTAIARALVHDPR 156
Cdd:PRK14247 87 VFQIPNPIPNLSIFENVALGLKLNRLvkSKKELQERVRwALEKAQLWDEVKDRldaPAGKLSGGQQQRLCIARALAFQPE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1755611750 157 NVILDEPTNGLDVMTTRAMRGFLQQLRAEgRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:PRK14247 167 VLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
21-233 |
4.05e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 89.41 E-value: 4.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 21 VNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPV-AVRRALGVL---PDARGVykRLSAR 96
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVwDIRHKIGMVfqnPDNQFV--GATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 97 ENIAYFGQLHGMSRTQIAERtrlLSHALD---MDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTR 173
Cdd:PRK13650 101 DDVAFGLENKGIPHEEMKER---VNEALElvgMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1755611750 174 AMRGFLQQLRAE-GRCVIFSSHIMQEVaALCDRIVIIAKGTVVAAGTADELrAATGEDNLE 233
Cdd:PRK13650 178 ELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPREL-FSRGNDLLQ 236
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
22-228 |
4.51e-21 |
|
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: 91.81 E-value: 4.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 22 NGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAH-DPVAVRRALGVLP-------Dargvykrl 93
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDvTQASLRAAIGIVPqdtvlfnD-------- 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 94 SARENIAYfGQLhGMSRTQIAERTRlLSHaldMDDILDRQTEGF-----------SQGQRTKTAIARALVHDPRNVILDE 162
Cdd:COG5265 447 TIAYNIAY-GRP-DASEEEVEAAAR-AAQ---IHDFIESLPDGYdtrvgerglklSGGEKQRVAIARTLLKNPPILIFDE 520
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1755611750 163 PTNGLDVMTTRAMRGFLQQLrAEGRCVIFSSHIMQEVAAlCDRIVIIAKGTVVAAGTADELRAATG 228
Cdd:COG5265 521 ATSALDSRTERAIQAALREV-ARGRTTLVIAHRLSTIVD-ADEILVLEAGRIVERGTHAELLAQGG 584
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-221 |
6.07e-21 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 88.15 E-value: 6.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 2 IVVDSLHKSFktktGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDG--VDAAHDP-----V 74
Cdd:COG4161 3 IQLKNINCFY----GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqFDFSQKPsekaiR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 75 AVRRALGVLPDARGVYKRLSAREN-IAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVH 153
Cdd:COG4161 79 LLRQKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1755611750 154 DPRNVILDEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSH---IMQEVAAlcdRIVIIAKGTVVAAGTAD 221
Cdd:COG4161 159 EPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHeveFARKVAS---QVVYMEKGRIIEQGDAS 226
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
20-209 |
8.68e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 86.52 E-value: 8.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 20 AVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDG------------VDAAHdPVAVRR--ALGVLPD 85
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgarvayvpqrseVPDSL-PLTVRDlvAMGRWAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 86 aRGVYKRLSAREniayfgqlhgmsrtqiaerTRLLSHALD---MDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDE 162
Cdd:NF040873 86 -RGLWRRLTRDD-------------------RAAVDDALErvgLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1755611750 163 PTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMqEVAALCDRIVII 209
Cdd:NF040873 146 PTTGLDAESRERIIALLAEEHARGATVVVVTHDL-ELVRRADPCVLL 191
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
24-229 |
8.74e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 90.67 E-value: 8.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 24 VSFNAADGQITGLLGPNGAGKTTTLRMLYTLMtPDQGSVRVDGVD-AAHDPVAVRRALG------VLPDArgvykrlSAR 96
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIElRELDPESWRKHLSwvgqnpQLPHG-------TLR 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 97 ENIAyFGQ--------LHGMSRTQIAERTRLLSHALDMDdILDrQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLD 168
Cdd:PRK11174 441 DNVL-LGNpdasdeqlQQALENAWVSEFLPLLPQGLDTP-IGD-QAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1755611750 169 VMTTRAMRGFLQQLrAEGRCVIFSSHIMQEVAAlCDRIVIIAKGTVVAAGTADELRAATGE 229
Cdd:PRK11174 518 AHSEQLVMQALNAA-SRRQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQGDYAELSQAGGL 576
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-219 |
1.12e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 88.26 E-value: 1.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 19 KAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPV-----AVRRALGVL---PDARgVY 90
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdikQIRKKVGLVfqfPESQ-LF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 91 KRlSARENIAYFGQLHGMSRTQiAERTRLLSHALD--MDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLD 168
Cdd:PRK13649 100 EE-TVLKDVAFGPQNFGVSQEE-AEALAREKLALVgiSESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1755611750 169 VMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGT 219
Cdd:PRK13649 178 PKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGK 228
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
5-223 |
1.16e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 88.87 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 5 DSLHKSFKTKTGL------VKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAVRR 78
Cdd:PRK11308 9 IDLKKHYPVKRGLfkperlVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 79 ALgvlpdARGV-------YKRLSARENIayfGQLHG--------MSRTQIAERTRLL--------SHAldmddilDRQTE 135
Cdd:PRK11308 89 LL-----RQKIqivfqnpYGSLNPRKKV---GQILEepllintsLSAAERREKALAMmakvglrpEHY-------DRYPH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 136 GFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQLRAE-GRCVIFSSHIMQEVAALCDRIVIIAKGTV 214
Cdd:PRK11308 154 MFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGRC 233
|
....*....
gi 1755611750 215 VAAGTADEL 223
Cdd:PRK11308 234 VEKGTKEQI 242
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
22-225 |
1.19e-20 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 87.43 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 22 NGVSFNAADGQITGLLGPNGAGKTTtlrMLYTLM-----TPDQGSVRVDGVD----------------AAHDPVAV---- 76
Cdd:COG0396 17 KGVNLTIKPGEVHAIMGPNGSGKST---LAKVLMghpkyEVTSGSILLDGEDilelspderaragiflAFQYPVEIpgvs 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 77 -----RRALGVLPDargvyKRLSAREniayfgqlhgmSRTQIAERTRLLshalDMD-DILDRQ-TEGFSQGQRTKTAIAR 149
Cdd:COG0396 94 vsnflRTALNARRG-----EELSARE-----------FLKLLKEKMKEL----GLDeDFLDRYvNEGFSGGEKKRNEILQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 150 ALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSH---IMQEVAAlcDRIVIIAKGTVVAAGT---ADEL 223
Cdd:COG0396 154 MLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHyqrILDYIKP--DFVHVLVDGRIVKSGGkelALEL 231
|
..
gi 1755611750 224 RA 225
Cdd:COG0396 232 EE 233
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
20-236 |
1.21e-20 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 88.02 E-value: 1.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 20 AVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVdaahdpvAVRRAL-----GVLPDARGV-YKRL 93
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQ-------PTRQALqknlvAYVPQSEEVdWSFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 94 SARENIAYFGQL--HGMSRTQIAERTRLLSHAL---DMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLD 168
Cdd:PRK15056 95 VLVEDVVMMGRYghMGWLRRAKKRDRQIVTAALarvDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1755611750 169 VMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIaKGTVVAAGTADELRAAtgeDNLEDAF 236
Cdd:PRK15056 175 VKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMV-KGTVLASGPTETTFTA---ENLELAF 238
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
30-223 |
1.67e-20 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 88.93 E-value: 1.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 30 DGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAvRRALGVLPDARGVYKRLSARENIAYFGQLHGMS 109
Cdd:PRK11000 28 EGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA-ERGVGMVFQSYALYPHLSVAENMSFGLKLAGAK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 110 RTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQL-RAEGRC 188
Cdd:PRK11000 107 KEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLhKRLGRT 186
|
170 180 190
....*....|....*....|....*....|....*
gi 1755611750 189 VIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:PRK11000 187 MIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
18-233 |
1.70e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 87.84 E-value: 1.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 18 VKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPV-AVRRALGVL---PDARgvYKRL 93
Cdd:PRK13642 20 VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVwNLRRKIGMVfqnPDNQ--FVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 94 SARENIAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTR 173
Cdd:PRK13642 98 TVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQ 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1755611750 174 AMRGFLQQLRAEGRCVIFS-SHIMQEvAALCDRIVIIAKGTVVAAGTADELrAATGEDNLE 233
Cdd:PRK13642 178 EIMRVIHEIKEKYQLTVLSiTHDLDE-AASSDRILVMKAGEIIKEAAPSEL-FATSEDMVE 236
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-228 |
2.01e-20 |
|
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: 86.44 E-value: 2.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 18 VKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAH-DPVAVRRALGVLPDARGVYKRlSAR 96
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlNLRWLRSQIGLVSQEPVLFDG-TIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 97 ENIAYfgQLHGMSRTQIAERTRLLSHaldmDDILDRQTEGF-----------SQGQRTKTAIARALVHDPRNVILDEPTN 165
Cdd:cd03249 95 ENIRY--GKPDATDEEVEEAAKKANI----HDFIMSLPDGYdtlvgergsqlSGGQKQRIAIARALLRNPKILLLDEATS 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1755611750 166 GLDVMTTRAMRGFLQQLRaEGRCVIFSSHIMQEVAAlCDRIVIIAKGTVVAAGTADELRAATG 228
Cdd:cd03249 169 ALDAESEKLVQEALDRAM-KGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDELMAQKG 229
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
8-223 |
4.88e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 86.39 E-value: 4.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 8 HKSFKTKTGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPD---QGSVRVDGVDAAHDPV-AVRRALGVL 83
Cdd:PRK13640 10 HVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDdnpNSKITVDGITLTAKTVwDIREKVGIV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 84 ---PDARGVYKRLSarENIAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVIL 160
Cdd:PRK13640 90 fqnPDNQFVGATVG--DDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1755611750 161 DEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFS-SHIMQEvAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:PRK13640 168 DESTSMLDPAGKEQILKLIRKLKKKNNLTVISiTHDIDE-ANMADQVLVLDDGKLLAQGSPVEI 230
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
20-204 |
5.57e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 85.99 E-value: 5.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 20 AVNGVSFNAADGQITGLLGPNGAGKTTTLRmLYTLMTPDQGSVRVDGVDAAH---------DPVAVRRALGVL-----PD 85
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILR-CFNRLNDLIPGFRVEGKVTFHgknlyapdvDPVEVRRRIGMVfqkpnPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 86 ARGVYkrlsarENIAYFGQLHGM--SRTQIAERTrlLSHALDMDDILDRQTE---GFSQGQRTKTAIARALVHDPRNVIL 160
Cdd:PRK14243 104 PKSIY------DNIAYGARINGYkgDMDELVERS--LRQAALWDEVKDKLKQsglSLSGGQQQRLCIARAIAVQPEVILM 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1755611750 161 DEPTNGLDVMTTRAMRGFLQQLRaEGRCVIFSSHIMQEVAALCD 204
Cdd:PRK14243 176 DEPCSALDPISTLRIEELMHELK-EQYTIIIVTHNMQQAARVSD 218
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-213 |
1.13e-19 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 82.11 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 2 IVVDSLHKSFKTKTGLvkavNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDgvdaahdpvavrralg 81
Cdd:cd03221 1 IELENLSKTYGGKLLL----KDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG---------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 82 vlpdargvykrlsARENIAYFGQLhgmsrtqiaertrllshaldmddildrqtegfSQGQRTKTAIARALVHDPRNVILD 161
Cdd:cd03221 61 -------------STVKIGYFEQL--------------------------------SGGEKMRLALAKLLLENPNLLLLD 95
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1755611750 162 EPTNGLDVMTTRAMRGFLQQLRaegRCVIFSSHIMQEVAALCDRIVIIAKGT 213
Cdd:cd03221 96 EPTNHLDLESIEALEEALKEYP---GTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-223 |
1.43e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 85.22 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 19 KAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAH---DPV--AVRRALGVL---PDARgVY 90
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkDKYirPVRKRIGMVfqfPESQ-LF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 91 KRLSARENIayFGQLH-GMSRTQIAERtrllSHALDMD-----DILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPT 164
Cdd:PRK13646 100 EDTVEREII--FGPKNfKMNLDEVKNY----AHRLLMDlgfsrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 165 NGLDVMTTRAMRGFLQQLRAE-GRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLQTDeNKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
20-223 |
3.46e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 83.98 E-value: 3.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 20 AVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDA--AHDPVAVRRALGVL---PDARGVYKRLs 94
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTsdEENLWDIRNKAGMVfqnPDNQIVATIV- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 95 aRENIAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRA 174
Cdd:PRK13633 104 -EEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRRE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1755611750 175 MRGFLQQL-RAEGRCVIFSSHIMQEvAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:PRK13633 183 VVNTIKELnKKYGITIILITHYMEE-AVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-223 |
5.50e-19 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 82.71 E-value: 5.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 25 SFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAvRRALGVLPDARGVYKRLSARENIAyFGq 104
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS-RRPVSMLFQENNLFSHLTVAQNIG-LG- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 105 LHGMSRTQIAERTRLLSHALDM--DDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQL 182
Cdd:PRK10771 96 LNPGLKLNAAQREKLHAIARQMgiEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQV 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1755611750 183 RAEGR-CVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:PRK10771 176 CQERQlTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-223 |
5.54e-19 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 84.39 E-value: 5.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSFKTKTGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPD---QGSVRVDGvdaahdpvavR 77
Cdd:PRK09473 12 LLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNG----------R 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 78 RALGvLPDARgvYKRLSArENIAYFGQ---------------------LH-GMSRTQ-IAERTRLLShALDMDDILDRQT 134
Cdd:PRK09473 82 EILN-LPEKE--LNKLRA-EQISMIFQdpmtslnpymrvgeqlmevlmLHkGMSKAEaFEESVRMLD-AVKMPEARKRMK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 135 ---EGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQLRAE-GRCVIFSSHIMQEVAALCDRIVIIA 210
Cdd:PRK09473 157 mypHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMY 236
|
250
....*....|...
gi 1755611750 211 KGTVVAAGTADEL 223
Cdd:PRK09473 237 AGRTMEYGNARDV 249
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
19-223 |
5.59e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 83.53 E-value: 5.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 19 KAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRV-DGVDAAH----DPVAVRRALGVL---PDAR--- 87
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgERVITAGkknkKLKPLRKKVGIVfqfPEHQlfe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 88 -GVYKrlsareNIAYFGQLHGMSRtqiAERTRLLSHALDM----DDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDE 162
Cdd:PRK13634 101 eTVEK------DICFGPMNFGVSE---EDAKQKAREMIELvglpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1755611750 163 PTNGLDVMTTRAMRGFLQQLRAE-GRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:PRK13634 172 PTAGLDPKGRKEMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-215 |
5.99e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 85.12 E-value: 5.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSFKTKTgLVKavnGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVdgvdaahdpvavrral 80
Cdd:COG0488 315 VLELEGLSKSYGDKT-LLD---DLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL---------------- 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 81 gvlpdARGVykrlsareNIAYFGQlhgmSRTQIAERTRLLSHaldMDDILDRQTE----------GFSQ----------- 139
Cdd:COG0488 375 -----GETV--------KIGYFDQ----HQEELDPDKTVLDE---LRDGAPGGTEqevrgylgrfLFSGddafkpvgvls 434
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1755611750 140 -GQRTKTAIARALVHDPrNV-ILDEPTNGLDVMTTRAMRGFLQQLraEGrCVIFSSHIMQEVAALCDRIVIIAKGTVV 215
Cdd:COG0488 435 gGEKARLALAKLLLSPP-NVlLLDEPTNHLDIETLEALEEALDDF--PG-TVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-235 |
6.28e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 85.06 E-value: 6.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 21 VNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGvdaahDPVAVRRALGVLpdARG-VY-----KR-- 92
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDG-----HEVVTRSPQDGL--ANGiVYisedrKRdg 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 93 ----LSAREN-----IAYFGQLHGmsRTQIAERTRLLSHALDMDDI----LDRQTEGFSQGQRTKTAIARALVHDPRNVI 159
Cdd:PRK10762 341 lvlgMSVKENmsltaLRYFSRAGG--SLKHADEQQAVSDFIRLFNIktpsMEQAIGLLSGGNQQKVAIARGLMTRPKVLI 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 160 LDEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADE------LRAATGEDNLE 233
Cdd:PRK10762 419 LDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTREQatqeklMAAAVGKLNRV 498
|
..
gi 1755611750 234 DA 235
Cdd:PRK10762 499 NQ 500
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-221 |
7.79e-19 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 82.37 E-value: 7.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 2 IVVDSLHKSFktktGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDG--VDAAHDP-----V 74
Cdd:PRK11124 3 IQLNGINCFY----GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhFDFSKTPsdkaiR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 75 AVRRALGVLPDARGVYKRLSAREN-IAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVH 153
Cdd:PRK11124 79 ELRRNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1755611750 154 DPRNVILDEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSH---IMQEVAAlcdRIVIIAKGTVVAAGTAD 221
Cdd:PRK11124 159 EPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHeveVARKTAS---RVVYMENGHIVEQGDAS 226
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
12-178 |
7.93e-19 |
|
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: 82.46 E-value: 7.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 12 KTKTGLVKAVNGVSFNaaDGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAVRralgvlPDARG-VY 90
Cdd:cd03237 8 KTLGEFTLEVEGGSIS--ESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIK------ADYEGtVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 91 KRLSARENIAYfgqLHGMSRTQIAErtrllshALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDV- 169
Cdd:cd03237 80 DLLSSITKDFY---THPYFKTEIAK-------PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVe 149
|
170
....*....|..
gi 1755611750 170 ---MTTRAMRGF 178
Cdd:cd03237 150 qrlMASKVIRRF 161
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
23-214 |
8.83e-19 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 82.13 E-value: 8.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 23 GVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVD-AAHDPVAVRRALGVLPDARGVYKRlSARENIAY 101
Cdd:cd03248 32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPiSQYEHKYLHSKVSLVGQEPVLFAR-SLQDNIAY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 102 -FGQLHGMSRTQIAERTR------LLSHALDMDdiLDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRA 174
Cdd:cd03248 111 gLQSCSFECVKEAAQKAHahsfisELASGYDTE--VGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQ 188
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1755611750 175 MRGFLQQlRAEGRCVIFSSHIMQEVAAlCDRIVIIAKGTV 214
Cdd:cd03248 189 VQQALYD-WPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
20-194 |
1.99e-18 |
|
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: 83.95 E-value: 1.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 20 AVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPV-AVRRALGVLPDARGVYKRlSAREN 98
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQdEVRRRVSVCAQDAHLFDT-TVREN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 99 IAYF-GQLHGMSRTQIAERTRLLSHALDMDDILD-RQTEG---FSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTR 173
Cdd:TIGR02868 429 LRLArPDATDEELWAALERVGLADWLRALPDGLDtVLGEGgarLSGGERQRLALARALLADAPILLLDEPTEHLDAETAD 508
|
170 180
....*....|....*....|...
gi 1755611750 174 AMrgfLQQLRA--EGRCVIFSSH 194
Cdd:TIGR02868 509 EL---LEDLLAalSGRTVVLITH 528
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-223 |
3.46e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 81.04 E-value: 3.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 21 VNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQ-----GSVRVDGVDAAH---DPVAVRRALGVLPDARGVYKR 92
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIYSpdvDPIEVRREVGMVFQYPNPFPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 93 LSARENIAYFGQLHGM--SRTQIAERTR-LLSHALDMDDILDRQTE---GFSQGQRTKTAIARALVHDPRNVILDEPTNG 166
Cdd:PRK14267 100 LTIYDNVAIGVKLNGLvkSKKELDERVEwALKKAALWDEVKDRLNDypsNLSGGQRQRLVIARALAMKPKILLMDEPTAN 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1755611750 167 LDVMTTRAMRGFLQQLRAEgRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:PRK14267 180 IDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKV 235
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
24-236 |
3.51e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 80.75 E-value: 3.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 24 VSFNAADGQITGLLGPNGAGKTTTLRMLYTLmTPDQGSVRVDGVDAAHDP---VAVRRAlgvlpdargvYkrLSARENIA 100
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSaaeLARHRA----------Y--LSQQQTPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 101 Y------FGQLHGMSRTQIAERTRLLS---HALDMDDILDRQTEGFSQG--QRTKTA-----IARALVHDPRNVILDEPT 164
Cdd:PRK03695 82 FampvfqYLTLHQPDKTRTEAVASALNevaEALGLDDKLGRSVNQLSGGewQRVRLAavvlqVWPDINPAGQLLLLDEPM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1755611750 165 NGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADELRAatgEDNLEDAF 236
Cdd:PRK03695 162 NSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLT---PENLAQVF 230
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
11-223 |
3.79e-18 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 82.06 E-value: 3.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 11 FKTKTGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVD----AAHDPVAVRRALGVL--- 83
Cdd:PRK15079 27 FWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDllgmKDDEWRAVRSDIQMIfqd 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 84 PDArGVYKRLSARENIA-----YFGQlhgMSRTQIAERTR--LLSHALdMDDILDRQTEGFSQGQRTKTAIARALVHDPR 156
Cdd:PRK15079 107 PLA-SLNPRMTIGEIIAeplrtYHPK---LSRQEVKDRVKamMLKVGL-LPNLINRYPHEFSGGQCQRIGIARALILEPK 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1755611750 157 NVILDEPTNGLDVMTTRAMRGFLQQLRAE-GRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:PRK15079 182 LIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 249
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-218 |
4.76e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 81.29 E-value: 4.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 2 IVVDSLHKSFKTKTGLV-KAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAVRRAL 80
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTElKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 81 GV------------LPDARGVYKRL--------------SARENIAyFGQL-HGMSRTQIAERTRLLSHALDMD-DILDR 132
Cdd:PRK13651 83 VLeklviqktrfkkIKKIKEIRRRVgvvfqfaeyqlfeqTIEKDII-FGPVsMGVSKEEAKKRAAKYIELVGLDeSYLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 133 QTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKG 212
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDG 241
|
....*.
gi 1755611750 213 TVVAAG 218
Cdd:PRK13651 242 KIIKDG 247
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
6-228 |
5.30e-18 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 82.85 E-value: 5.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 6 SLHKSFKTKTGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAA---HDPVAV--RRAL 80
Cdd:PRK10535 9 DIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVAtldADALAQlrREHF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 81 GVLPDARGVYKRLSARENIAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVIL 160
Cdd:PRK10535 89 GFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1755611750 161 DEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQeVAALCDRIVIIAKGTVVAAGTADELRAATG 228
Cdd:PRK10535 169 DEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQ-VAAQAERVIEIRDGEIVRNPPAQEKVNVAG 235
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
21-224 |
6.11e-18 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 79.11 E-value: 6.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 21 VNGVSFNAADGQITGLLGPNGAGKTTtlrMLYTLM-----TPDQGSVRVDGVDAAHDPVAVRRALGVLpdargvykrLSA 95
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKST---LAKTIMghpkyEVTEGEILFKGEDITDLPPEERARLGIF---------LAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 96 RENIAYFGqlhgmsrtqiaertrllshaLDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRAM 175
Cdd:cd03217 84 QYPPEIPG--------------------VKNADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLV 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1755611750 176 RGFLQQLRAEGRCVIFSSHiMQEVAALC--DRIVIIAKGTVVAAGTADELR 224
Cdd:cd03217 144 AEVINKLREEGKSVLIITH-YQRLLDYIkpDRVHVLYDGRIVKSGDKELAL 193
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
19-228 |
8.55e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 82.18 E-value: 8.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 19 KAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVD-AAHDPVAVRRALGVLPdargvyKR---LS 94
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPiADYSEAALRQAISVVS------QRvhlFS 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 95 A--REN--IAyfgqLHGMSRTQIAERTRL--LSHALDMDDILD-------RQTEGfsqGQRTKTAIARALVHDPRNVILD 161
Cdd:PRK11160 428 AtlRDNllLA----APNASDEALIEVLQQvgLEKLLEDDKGLNawlgeggRQLSG---GEQRRLGIARALLHDAPLLLLD 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1755611750 162 EPTNGLDVMTTRAMrgfLQQLR--AEGRCVIFSSHIMQEVAALcDRIVIIAKGTVVAAGTADELRAATG 228
Cdd:PRK11160 501 EPTEGLDAETERQI---LELLAehAQNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQELLAQQG 565
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-221 |
9.87e-18 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 79.58 E-value: 9.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSFktktGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDG-----VDAAHDPVA 75
Cdd:PRK11701 6 LLSVRGLTKLY----GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALSEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 76 VRRALG------VLPDAR-GVYKRLSARENIA---------YFGQL-----HGMSRTQIAErtrllshaldmdDILDRQT 134
Cdd:PRK11701 82 ERRRLLrtewgfVHQHPRdGLRMQVSAGGNIGerlmavgarHYGDIratagDWLERVEIDA------------ARIDDLP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 135 EGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQLRAE-GRCVIFSSHIMQEVAALCDRIVIIAKGT 213
Cdd:PRK11701 150 TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
....*...
gi 1755611750 214 VVAAGTAD 221
Cdd:PRK11701 230 VVESGLTD 237
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
24-225 |
1.15e-17 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 79.81 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 24 VSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVD----AAHDPVAVRRALGVLPDARGVYKRLSARENI 99
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENipamSRSRLYTVRKRMSMLFQSGALFTDMNVFDNV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 100 AYFGQLHGMSRTQIAERTRLLS-HALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRAMRGF 178
Cdd:PRK11831 106 AYPLREHTQLPAPLLHSTVMMKlEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1755611750 179 LQQL-RAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADELRA 225
Cdd:PRK11831 186 ISELnSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQA 233
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
17-219 |
1.19e-17 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 78.61 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 17 LVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDP-VAVRRALGVLPDARGVYKRlSA 95
Cdd:cd03369 20 LPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPlEDLRSSLTIIPQDPTLFSG-TI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 96 RENIAYFGQlhgMSRTQIAERTRLLSHALDmddildrqtegFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRAM 175
Cdd:cd03369 99 RSNLDPFDE---YSDEEIYGALRVSEGGLN-----------LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1755611750 176 RGFLQQLRAeGRCVIFSSHIMQEVAAlCDRIVIIAKGTVVAAGT 219
Cdd:cd03369 165 QKTIREEFT-NSTILTIAHRLRTIID-YDKILVMDAGEVKEYDH 206
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-212 |
1.31e-17 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 79.05 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 21 VNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDG---VDAAHDPVAVRRALGVLPdargvykRLSARE 97
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGkqiTEPGPDRMVVFQNYSLLP-------WLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 98 NIAYFGQ--LHGMSRTqiaERTRLLSHALDMDDI---LDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTT 172
Cdd:TIGR01184 74 NIALAVDrvLPDLSKS---ERRAIVEEHIALVGLteaADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1755611750 173 RAMRGFLQQLRAEGRC-VIFSSHIMQEVAALCDRIVIIAKG 212
Cdd:TIGR01184 151 GNLQEELMQIWEEHRVtVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-222 |
1.52e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 81.37 E-value: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 19 KAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVD-AAHDPV-AVRRALGVLPDAR---GVYKRL 93
Cdd:PRK09700 277 KKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDiSPRSPLdAVKKGMAYITESRrdnGFFPNF 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 94 SARENIAY------------FGQLHGMSRTQIAERTRLLShALDMDDILDRQTEgFSQGQRTKTAIARALVHDPRNVILD 161
Cdd:PRK09700 357 SIAQNMAIsrslkdggykgaMGLFHEVDEQRTAENQRELL-ALKCHSVNQNITE-LSGGNQQKVLISKWLCCCPEVIIFD 434
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1755611750 162 EPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADE 222
Cdd:PRK09700 435 EPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRD 495
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
33-218 |
2.56e-17 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 79.92 E-value: 2.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 33 ITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDG---VDAAHD---PVAVRRALGVLPDARgVYKRLSARENIAYfgqlh 106
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAEKGiclPPEKRRIGYVFQDAR-LFPHYKVRGNLRY----- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 107 GMSRTQIAERTRLLShALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQLRAEG 186
Cdd:PRK11144 100 GMAKSMVAQFDKIVA-LLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREI 178
|
170 180 190
....*....|....*....|....*....|...
gi 1755611750 187 RC-VIFSSHIMQEVAALCDRIVIIAKGTVVAAG 218
Cdd:PRK11144 179 NIpILYVSHSLDEILRLADRVVVLEQGKVKAFG 211
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
31-223 |
2.80e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 78.68 E-value: 2.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 31 GQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDG-VDAAHDPVAVRRALGVLPDARGVYKRLSARENIAyFGQL--HG 107
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAqPLESWSSKAFARKVAYLPQQLPAAEGMTVRELVA-IGRYpwHG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 108 -MSRTQIAERTRlLSHALDMDDI---LDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQL- 182
Cdd:PRK10575 116 aLGRFGAADREK-VEEAISLVGLkplAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLs 194
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1755611750 183 RAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:PRK10575 195 QERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-223 |
3.30e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 78.47 E-value: 3.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 2 IVVDSLHKSFktktGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDG--------------V 67
Cdd:PRK10619 6 LNVIDLHKRY----GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdgqlkV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 68 DAAHDPVAVRRALGVLPDARGVYKRLSARENIAYFG-QLHGMSRTQIAERTRLLshaLDMDDILDRQTEGF----SQGQR 142
Cdd:PRK10619 82 ADKNQLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPiQVLGLSKQEARERAVKY---LAKVGIDERAQGKYpvhlSGGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 143 TKTAIARALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADE 222
Cdd:PRK10619 159 QRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQ 238
|
.
gi 1755611750 223 L 223
Cdd:PRK10619 239 L 239
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-214 |
3.40e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 78.18 E-value: 3.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 2 IVVDSLHKSFKTKTGLvkavNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRvdgvdAAHDPVAVRRAlg 81
Cdd:PRK11247 13 LLLNAVSKRYGERTVL----NQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL-----AGTAPLAEARE-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 82 vlpDARGVYK--RL----SARENIAyFGqLHGMSRTQIAErtrllshALDMDDILDRQTE---GFSQGQRTKTAIARALV 152
Cdd:PRK11247 82 ---DTRLMFQdaRLlpwkKVIDNVG-LG-LKGQWRDAALQ-------ALAAVGLADRANEwpaALSGGQKQRVALARALI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1755611750 153 HDPRNVILDEPTNGLDVMTTRAMRGFLQQL-RAEGRCVIFSSHIMQEVAALCDRIVIIAKGTV 214
Cdd:PRK11247 150 HRPGLLLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
19-223 |
4.56e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 77.89 E-value: 4.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 19 KAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTL--MTPD---QGSVRVDGVD---AAHDPVAVRRALGVlpdargVY 90
Cdd:PRK14239 19 KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNiysPRTDTVDLRKEIGM------VF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 91 KR-----LSARENIAYFGQLHGMSRTQIAERT--RLLSHALDMDDILDRQTE---GFSQGQRTKTAIARALVHDPRNVIL 160
Cdd:PRK14239 93 QQpnpfpMSIYENVVYGLRLKGIKDKQVLDEAveKSLKGASIWDEVKDRLHDsalGLSGGQQQRVCIARVLATSPKIILL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1755611750 161 DEPTNGLDVMTTRAMRGFLQQLRaEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:PRK14239 173 DEPTSALDPISAGKIEETLLGLK-DDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
7-232 |
5.49e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 79.66 E-value: 5.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 7 LHKSFKTktglVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHD-PVAVRRA-LGVLP 84
Cdd:PRK10762 10 IDKAFPG----VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNgPKSSQEAgIGIIH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 85 DARGVYKRLSARENIaYFGQ--LHGMSRTQ----IAERTRLLSHaLDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNV 158
Cdd:PRK10762 86 QELNLIPQLTIAENI-FLGRefVNRFGRIDwkkmYAEADKLLAR-LNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1755611750 159 ILDEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADELRaatgEDNL 232
Cdd:PRK10762 164 IMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLT----EDSL 233
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
11-242 |
6.35e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 80.02 E-value: 6.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 11 FKTKTGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVA-VRRALGVLPDARGV 89
Cdd:PLN03232 1242 LRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTdLRRVLSIIPQSPVL 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 90 YKRlSARENIAYFGQ------LHGMSRTQIAERTRLLSHALDMDdiLDRQTEGFSQGQRTKTAIARALVHDPRNVILDEP 163
Cdd:PLN03232 1322 FSG-TVRFNIDPFSEhndadlWEALERAHIKDVIDRNPFGLDAE--VSEGGENFSVGQRQLLSLARALLRRSKILVLDEA 1398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 164 TNGLDVMTTRAMRgflQQLRAEGR-C-VIFSSHIMQEVAAlCDRIVIIAKGTVVAAGTADELRAATGEdnledAFVKAIG 241
Cdd:PLN03232 1399 TASVDVRTDSLIQ---RTIREEFKsCtMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTS-----AFFRMVH 1469
|
.
gi 1755611750 242 S 242
Cdd:PLN03232 1470 S 1470
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
13-216 |
6.94e-17 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 79.48 E-value: 6.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 13 TKT-GLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRML---YTLMTPDqGSVRVDG--VDAAHDPVAVRRALGVLPDA 86
Cdd:TIGR02633 8 VKTfGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILsgvYPHGTWD-GEIYWSGspLKASNIRDTERAGIVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 87 RGVYKRLSARENIAYFGQL-HGMSRTQIAE---RTRLLSHALDMDDILD-RQTEGFSQGQRTKTAIARALVHDPRNVILD 161
Cdd:TIGR02633 87 LTLVPELSVAENIFLGNEItLPGGRMAYNAmylRAKNLLRELQLDADNVtRPVGDYGGGQQQLVEIAKALNKQARLLILD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1755611750 162 EPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVA 216
Cdd:TIGR02633 167 EPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVA 221
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-226 |
7.99e-17 |
|
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: 78.96 E-value: 7.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 4 VDSLHKSFKTKTGLVKAVNGVSFNAADGQITGLLGPNGAGKTTT----LRMLYTLMTPDQGSVRVDGVDAAHDPVAVRRA 79
Cdd:COG4172 9 VEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGQDLLGLSERELRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 80 LgvlpdaRG-------------------VYKRLSarENIayfgQLH-GMSRTQIAERTRLLshaLDMDDI------LDRQ 133
Cdd:COG4172 89 I------RGnriamifqepmtslnplhtIGKQIA--EVL----RLHrGLSGAAARARALEL---LERVGIpdperrLDAY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 134 TEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVmTTRA-MRGFLQQLRAE-GRCVIFSSHIMQEVAALCDRIVIIAK 211
Cdd:COG4172 154 PHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDV-TVQAqILDLLKDLQRElGMALLLITHDLGVVRRFADRVAVMRQ 232
|
250
....*....|....*
gi 1755611750 212 GTVVAAGTADELRAA 226
Cdd:COG4172 233 GEIVEQGPTAELFAA 247
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
13-223 |
9.27e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 78.82 E-value: 9.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 13 TKT-GLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRML---YTLMTPDqGSVRVDG--VDAAHDPVAVRRALGVLPDA 86
Cdd:PRK13549 12 TKTfGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLsgvYPHGTYE-GEIIFEGeeLQASNIRDTERAGIAIIHQE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 87 RGVYKRLSARENI------AYFGQLHGMSRTQIAERtrLLSH-ALDMDdiLDRQTEGFSQGQRTKTAIARALVHDPRNVI 159
Cdd:PRK13549 91 LALVKELSVLENIflgneiTPGGIMDYDAMYLRAQK--LLAQlKLDIN--PATPVGNLGLGQQQLVEIAKALNKQARLLI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1755611750 160 LDEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:PRK13549 167 LDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGM 230
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-194 |
9.75e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 75.76 E-value: 9.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 21 VNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAVRRALGVLPDARGVYKRLSARENIA 100
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLRENCL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 101 YfgQLHGMSRT-QIAERTRLLShaldMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRAMRGFL 179
Cdd:PRK13540 97 Y--DIHFSPGAvGITELCRLFS----LEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKI 170
|
170
....*....|....*
gi 1755611750 180 QQLRAEGRCVIFSSH 194
Cdd:PRK13540 171 QEHRAKGGAVLLTSH 185
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
20-223 |
1.11e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 77.33 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 20 AVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAhDPV---AVRRALGVL---PDARGVYKrl 93
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTG-DFSklqGIRKLVGIVfqnPETQFVGR-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 94 SARENIAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTR 173
Cdd:PRK13644 94 TVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1755611750 174 AMRGFLQQLRAEGRCVIFSSHIMQEVAAlCDRIVIIAKGTVVAAGTADEL 223
Cdd:PRK13644 174 AVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENV 222
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-223 |
2.21e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 76.59 E-value: 2.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 2 IVVDSLHKSFKTKTGL-VKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVD------GVDAAHDPV 74
Cdd:PRK13645 7 IILDNVSYTYAKKTPFeFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGdyaipaNLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 75 AVRRALGVL---PDARGVYKRLsaRENIAyFGQLH-GMSRTQIAERTRLLSHALDM-DDILDRQTEGFSQGQRTKTAIAR 149
Cdd:PRK13645 87 RLRKEIGLVfqfPEYQLFQETI--EKDIA-FGPVNlGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAG 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1755611750 150 ALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQLRAE-GRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:PRK13645 164 IIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEI 238
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
5-197 |
3.61e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 74.85 E-value: 3.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 5 DSLHKSFKTKTGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDG-----VDAAHDPVAVRRA 79
Cdd:PRK11629 9 DNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpmskLSSAAKAELRNQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 80 LG-------VLPDargvykrLSARENIAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALV 152
Cdd:PRK11629 89 LGfiyqfhhLLPD-------FTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALV 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1755611750 153 HDPRNVILDEPTNGLDVMTTRAMRGFLQQL-RAEGRCVIFSSHIMQ 197
Cdd:PRK11629 162 NNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQ 207
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
24-226 |
3.61e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 75.41 E-value: 3.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 24 VSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAH-DPVAVRRALGVLPDARGVYKRLSARENIA-- 100
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyASKEVARRIGLLAQNATTPGDITVQELVArg 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 101 -YFGQ-LHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRAMRGF 178
Cdd:PRK10253 106 rYPHQpLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLEL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1755611750 179 LQQL-RAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADELRAA 226
Cdd:PRK10253 186 LSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTA 234
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
20-228 |
3.72e-16 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 77.37 E-value: 3.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 20 AVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDaahdpvavrralgvLPDargvYKRLSARE-- 97
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHD--------------LRD----YTLASLRNqv 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 98 ----------------NIAYFGQLHgMSRTQIaERTRLLSHALD----MDDILD----RQTEGFSQGQRTKTAIARALVH 153
Cdd:PRK11176 420 alvsqnvhlfndtianNIAYARTEQ-YSREQI-EEAARMAYAMDfinkMDNGLDtvigENGVLLSGGQRQRIAIARALLR 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1755611750 154 DPRNVILDEPTNGLDVMTTRAMRGFLQQLRAEgRCVIFSSHIMQEVAAlCDRIVIIAKGTVVAAGTADELRAATG 228
Cdd:PRK11176 498 DSPILILDEATSALDTESERAIQAALDELQKN-RTSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAELLAQNG 570
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
22-218 |
6.25e-16 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 74.60 E-value: 6.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 22 NGVSFNAADGQITGLLGPNGAGKTTtlrMLYTLM-TPD----QGSVRVDGVDAAHDPVAVRRALGVL------PDARGVY 90
Cdd:TIGR01978 17 KGVNLTVKKGEIHAIMGPNGSGKST---LSKTIAgHPSyevtSGTILFKGQDLLELEPDERARAGLFlafqypEEIPGVS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 91 KRL---SARENIAYFGQLHGMSRTQIAERTRLLSHALDMD-DILDRQ-TEGFSQGQRTKTAIARALVHDPRNVILDEPTN 165
Cdd:TIGR01978 94 NLEflrSALNARRSARGEEPLDLLDFEKLLKEKLALLDMDeEFLNRSvNEGFSGGEKKRNEILQMALLEPKLAILDEIDS 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1755611750 166 GLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALC-DRIVIIAKGTVVAAG 218
Cdd:TIGR01978 174 GLDIDALKIVAEGINRLREPDRSFLIITHYQRLLNYIKpDYVHVLLDGRIVKSG 227
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-223 |
7.02e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 74.66 E-value: 7.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSFKTKtglvKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQG----------SVRVDGvDAA 70
Cdd:PRK09984 4 IIRVEKLAKTFNQH----QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSagshiellgrTVQREG-RLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 71 HDPVAVRRALGVLPDARGVYKRLSAREN--IAYFGQ-------LHGMSRTQIAERTRLLSHaLDMDDILDRQTEGFSQGQ 141
Cdd:PRK09984 79 RDIRKSRANTGYIFQQFNLVNRLSVLENvlIGALGStpfwrtcFSWFTREQKQRALQALTR-VGMVHFAHQRVSTLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 142 RTKTAIARALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQL-RAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTA 220
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSS 237
|
...
gi 1755611750 221 DEL 223
Cdd:PRK09984 238 QQF 240
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
8-223 |
7.24e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 74.79 E-value: 7.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 8 HKSFKTKTGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSV-----RVDgvdaAHDPVAVRRALGV 82
Cdd:PRK13648 12 NVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqAIT----DDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 83 L---PDARGVYKrlSARENIAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVI 159
Cdd:PRK13648 88 VfqnPDNQFVGS--IVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVII 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1755611750 160 LDEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFS-SHIMQEvAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:PRK13648 166 LDEATSMLDPDARQNLLDLVRKVKSEHNITIISiTHDLSE-AMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
18-235 |
1.73e-15 |
|
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: 75.25 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 18 VKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMtPDQ--GSVRVDG--VDAAHDPVAVRRALGVLPDAR---GVY 90
Cdd:TIGR02633 273 RKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAY-PGKfeGNVFINGkpVDIRNPAQAIRAGIAMVPEDRkrhGIV 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 91 KRLSARENI--AYFGQLHGMSRTQIAERTRLLSHALDMDDIL----DRQTEGFSQGQRTKTAIARALVHDPRNVILDEPT 164
Cdd:TIGR02633 352 PILGVGKNItlSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKtaspFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPT 431
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1755611750 165 NGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADELraaTGEDNLEDA 235
Cdd:TIGR02633 432 RGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDFVNHAL---TQEQVLAAA 499
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
19-207 |
2.34e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.22 E-value: 2.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 19 KAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDG------------VDAAHdPVAVRRALGVLPDA 86
Cdd:PRK09544 18 RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGklrigyvpqklyLDTTL-PLTVNRFLRLRPGT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 87 RgvykrlsaRENIayfgqLHGMSRTQIAErtrllshaldmddILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNG 166
Cdd:PRK09544 97 K--------KEDI-----LPALKRVQAGH-------------LIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQG 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1755611750 167 LDVMTTRAMRGFLQQLRAEGRC-VIFSSHIMQEVAALCDRIV 207
Cdd:PRK09544 151 VDVNGQVALYDLIDQLRRELDCaVLMVSHDLHLVMAKTDEVL 192
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
24-216 |
4.40e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 74.18 E-value: 4.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 24 VSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDG--VDAAHDPVAVRRALGVLPDAR---GVYKRLSAREN 98
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRSPRDAIRAGIMLCPEDRkaeGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 99 IA--------YFGQLhgMSRTQIAERTRLLSHALDMDDILDRQTEGF-SQGQRTKTAIARALVHDPRNVILDEPTNGLDV 169
Cdd:PRK11288 352 INisarrhhlRAGCL--INNRWEAENADRFIRSLNIKTPSREQLIMNlSGGNQQKAILGRWLSEDMKVILLDEPTRGIDV 429
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1755611750 170 MTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVA 216
Cdd:PRK11288 430 GAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAG 476
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
24-246 |
5.74e-15 |
|
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: 72.19 E-value: 5.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 24 VSFNAADGQITGLLGPNGAGKTTT----LRMLYTlmtpdQGSVRVDGVDAAHDPVAV-RRALGVLPDARGVYKRlSAREN 98
Cdd:cd03289 23 ISFSISPGQRVGLLGRTGSGKSTLlsafLRLLNT-----EGDIQIDGVSWNSVPLQKwRKAFGVIPQKVFIFSG-TFRKN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 99 IAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEG----FSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRA 174
Cdd:cd03289 97 LDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDggcvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQV 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1755611750 175 MRGFLQQLRAEgrC-VIFSSHIMqEVAALCDRIVIIAKGTVvaaGTADELRAATGEDNLedaFVKAIGSDEGL 246
Cdd:cd03289 177 IRKTLKQAFAD--CtVILSEHRI-EAMLECQRFLVIEENKV---RQYDSIQKLLNEKSH---FKQAISPSDRL 240
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
21-201 |
8.77e-15 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 70.59 E-value: 8.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 21 VNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPD---QGSVRVDGVDAAHDPVAvRRALGVLPDARGVYKRLSARE 97
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAE-QRRIGILFQDDLLFPHLSVGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 98 NIAyFGQLHGMSRtqiAERTRLLSHALD---MDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRA 174
Cdd:COG4136 96 NLA-FALPPTIGR---AQRRARVEQALEeagLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQ 171
|
170 180
....*....|....*....|....*...
gi 1755611750 175 MRGF-LQQLRAEGRCVIFSSHIMQEVAA 201
Cdd:COG4136 172 FREFvFEQIRQRGIPALLVTHDEEDAPA 199
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
24-212 |
2.14e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 72.01 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 24 VSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAVRRALGV--LPDAR---GVYKRLSAREN 98
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLvyLPEDRqssGLYLDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 99 IAYFGQ------LHGMSRTQIAERTRL-----LSHAldmddilDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGL 167
Cdd:PRK15439 362 VCALTHnrrgfwIKPARENAVLERYRRalnikFNHA-------EQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1755611750 168 DVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKG 212
Cdd:PRK15439 435 DVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQG 479
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
22-223 |
2.26e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 72.00 E-value: 2.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 22 NGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPD---QGSVRVDGVDAAHDPVAVRRALgVLPDARGVyKRLSAREN 98
Cdd:TIGR00955 42 KNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRAISAY-VQQDDLFI-PTLTVREH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 99 IAYFGQLHgMSRT-----------QIAERTRLLSHALDMDDILDRqTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGL 167
Cdd:TIGR00955 120 LMFQAHLR-MPRRvtkkekrervdEVLQALGLRKCANTRIGVPGR-VKGLSGGERKRLAFASELLTDPPLLFCDEPTSGL 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1755611750 168 DVMTTRAMRGFLQQLRAEGRCVIFSSHimQ---EVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:TIGR00955 198 DSFMAYSVVQVLKGLAQKGKTIICTIH--QpssELFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
11-229 |
4.17e-14 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 71.07 E-value: 4.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 11 FKTKTGLVK-AVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAhdpVAVrralgvlpdARGV 89
Cdd:PRK13545 29 FRSKDGEYHyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAAL---IAI---------SSGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 90 YKRLSARENIAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDV 169
Cdd:PRK13545 97 NGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQ 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 170 MTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADELRAATGE 229
Cdd:PRK13545 177 TFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYDE 236
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-204 |
4.25e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 69.68 E-value: 4.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 2 IVVDSLHKSFKTKtglvKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLyTLMTPDQGSVRVDG-VDAAHDPV------ 74
Cdd:PRK14258 8 IKVNNLSFYYDTQ----KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGrVEFFNQNIyerrvn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 75 --AVRRALGVLPDARGVYKrLSARENIAYFGQLHGMsRTQIaERTRLLSHALDMDDILD-------RQTEGFSQGQRTKT 145
Cdd:PRK14258 83 lnRLRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGW-RPKL-EIDDIVESALKDADLWDeikhkihKSALDLSGGQQQRL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1755611750 146 AIARALVHDPRNVILDEPTNGLDVMTTRAMRGFLQ--QLRAEGRCVIFsSHIMQEVAALCD 204
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIV-SHNLHQVSRLSD 219
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
20-228 |
6.00e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 70.90 E-value: 6.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 20 AVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPV-AVRRALGVLPDARGVYKRLSAReN 98
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLdSWRSRLAVVSQTPFLFSDTVAN-N 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 99 IAyFGQlHGMSRTQIAERTRLLS-HaldmDDILdRQTEGF-----------SQGQRTKTAIARALVHDPRNVILDEPTNG 166
Cdd:PRK10789 409 IA-LGR-PDATQQEIEHVARLASvH----DDIL-RLPQGYdtevgergvmlSGGQKQRISIARALLLNAEILILDDALSA 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1755611750 167 LDVMTTRAMrgfLQQLR--AEGRCVIFSSHimqEVAAL--CDRIVIIAKGTVVAAGTADELRAATG 228
Cdd:PRK10789 482 VDGRTEHQI---LHNLRqwGEGRTVIISAH---RLSALteASEILVMQHGHIAQRGNHDQLAQQSG 541
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
20-223 |
6.19e-14 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 69.46 E-value: 6.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 20 AVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGvdaahdpvavrrALGVLPDARGVYKRLSARENI 99
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG------------EVSVIAISAGLSGQLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 100 AYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRAMRGFL 179
Cdd:PRK13546 107 EFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKI 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1755611750 180 QQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:PRK13546 187 YEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV 230
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
18-223 |
6.73e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 70.53 E-value: 6.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 18 VKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDG--VDAAHDPVAVRRALGVLPDARGVYKRLSA 95
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkeIDFKSSKEALENGISMVHQELNLVLQRSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 96 RENIaYFGQ--LHGM--SRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMT 171
Cdd:PRK10982 91 MDNM-WLGRypTKGMfvDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1755611750 172 TRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:PRK10982 170 VNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGL 221
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
18-235 |
7.15e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 70.34 E-value: 7.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 18 VKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLY-TLMTPDQGSVRVDG--VDAAHDPVAVRRALGVLPDAR---GVYK 91
Cdd:PRK13549 275 IKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFgAYPGRWEGEIFIDGkpVKIRNPQQAIAQGIAMVPEDRkrdGIVP 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 92 RLSARENI--AYFGQLHGMSRtqiaertrlLSHALDMDDILDRQTE-------------GFSQGQRTKTAIARALVHDPR 156
Cdd:PRK13549 355 VMGVGKNItlAALDRFTGGSR---------IDDAAELKTILESIQRlkvktaspelaiaRLSGGNQQKAVLAKCLLLNPK 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1755611750 157 NVILDEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADELraaTGEDNLEDA 235
Cdd:PRK13549 426 ILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLKGDLINHNL---TQEQVMEAA 501
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-218 |
1.05e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 70.27 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 18 VKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDG--VDAAHDPV--AVRRALGVLpdARGVYKRL 93
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqrIDTLSPGKlqALRRDIQFI--FQDPYASL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 94 SARENIAY--------FGQLHG-MSRTQIA---ERTRLL-SHALdmddildRQTEGFSQGQRTKTAIARALVHDPRNVIL 160
Cdd:PRK10261 415 DPRQTVGDsimeplrvHGLLPGkAAAARVAwllERVGLLpEHAW-------RYPHEFSGGQRQRICIARALALNPKVIIA 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1755611750 161 DEPTNGLDVMTTRAMRGFLQQLRAE-GRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAG 218
Cdd:PRK10261 488 DEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
15-176 |
1.75e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 69.45 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 15 TGLVKAVNGVSFNAADGQI-----TGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDgVDAAHDPVAVRralgvlPDARG- 88
Cdd:PRK13409 344 PDLTKKLGDFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKISYKPQYIK------PDYDGt 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 89 VYKRL-SARENIA--YFgqlhgmsRTQIAERtrllshaLDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTN 165
Cdd:PRK13409 417 VEDLLrSITDDLGssYY-------KSEIIKP-------LQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSA 482
|
170
....*....|....*
gi 1755611750 166 GLDV----MTTRAMR 176
Cdd:PRK13409 483 HLDVeqrlAVAKAIR 497
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
23-242 |
1.85e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 69.77 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 23 GVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVA-VRRALGVLPDARGVYKRlSARENIAY 101
Cdd:PLN03130 1257 GLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMdLRKVLGIIPQAPVLFSG-TVRFNLDP 1335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 102 FGQLHGMSRTQIAERTRLLS----HALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTramrG 177
Cdd:PLN03130 1336 FNEHNDADLWESLERAHLKDvirrNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTD----A 1411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1755611750 178 FLQQ-LRAEgrcviFSSHIMQEVAAL------CDRIVIIAKGTVVAAGTADELRAatgedNLEDAFVKAIGS 242
Cdd:PLN03130 1412 LIQKtIREE-----FKSCTMLIIAHRlntiidCDRILVLDAGRVVEFDTPENLLS-----NEGSAFSKMVQS 1473
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
24-214 |
2.98e-13 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 69.17 E-value: 2.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 24 VSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDqGSVRVDGVdaAHDPVAV---RRALGVLPDARGVYKRlSARENIA 100
Cdd:TIGR01271 1238 LSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGV--SWNSVTLqtwRKAFGVIPQKVFIFSG-TFRKNLD 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 101 YFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEG----FSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRAMR 176
Cdd:TIGR01271 1314 PYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDggyvLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIR 1393
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1755611750 177 GFLQQLRAEgrC-VIFSSHimqEVAAL--CDRIVIIAKGTV 214
Cdd:TIGR01271 1394 KTLKQSFSN--CtVILSEH---RVEALleCQQFLVIEGSSV 1429
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-223 |
7.31e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 66.39 E-value: 7.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 19 KAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVD-----AAHDPVAVRRALG------------ 81
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHitpetGNKNLKKLRKKVSlvfqfpeaqlfe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 82 --VLPDARGVYKRLSARENIAYFGQLHGMSRTQIAErtrllshaldmdDILDRQTEGFSQGQRTKTAIARALVHDPRNVI 159
Cdd:PRK13641 101 ntVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSE------------DLISKSPFELSGGQMRRVAIAGVMAYEPEILC 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1755611750 160 LDEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:PRK13641 169 LDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
11-223 |
8.07e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 66.85 E-value: 8.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 11 FKTKTGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLmTPDQGSVRVD-----GVDAAHDPVAVRRAL----- 80
Cdd:COG4170 13 IDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGI-TKDNWHVTADrfrwnGIDLLKLSPRERRKIigrei 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 81 --------GVLPDARGVYKRLSarENI------AYFGQLHGMSRTQIAErtrlLSHAL---DMDDILDRQTEGFSQGQRT 143
Cdd:COG4170 92 amifqepsSCLDPSAKIGDQLI--EAIpswtfkGKWWQRFKWRKKRAIE----LLHRVgikDHKDIMNSYPHELTEGECQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 144 KTAIARALVHDPRNVILDEPTNGLDVmTTRA--MRGF--LQQLRaeGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGT 219
Cdd:COG4170 166 KVMIAMAIANQPRLLIADEPTNAMES-TTQAqiFRLLarLNQLQ--GTSILLISHDLESISQWADTITVLYCGQTVESGP 242
|
....
gi 1755611750 220 ADEL 223
Cdd:COG4170 243 TEQI 246
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-223 |
8.59e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.57 E-value: 8.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSFKTKTGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDgvdaahdPVAVRR-- 78
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCD-------KMLLRRrs 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 79 ----ALGVLPDARGVYKR------------------LSARENIAYFGQLH-GMSRTQ-IAERTRLLSHAL--DMDDILDR 132
Cdd:PRK10261 85 rqviELSEQSAAQMRHVRgadmamifqepmtslnpvFTVGEQIAESIRLHqGASREEaMVEAKRMLDQVRipEAQTILSR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 133 QTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVmTTRA----MRGFLQQLRAEGrcVIFSSHIMQEVAALCDRIVI 208
Cdd:PRK10261 165 YPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDV-TIQAqilqLIKVLQKEMSMG--VIFITHDMGVVAEIADRVLV 241
|
250
....*....|....*
gi 1755611750 209 IAKGTVVAAGTADEL 223
Cdd:PRK10261 242 MYQGEAVETGSVEQI 256
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-194 |
1.05e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 66.88 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 2 IVVDSLHKSFKTKTglvkAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRV-DGVDAAHdpvaVRRAL 80
Cdd:TIGR03719 323 IEAENLTKAFGDKL----LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETVKLAY----VDQSR 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 81 GVLPDARGVYKRLSARENIAYFGQLHGMSRTQI-------AERTRLLSHaldmddildrqtegFSQGQRTKTAIARALvH 153
Cdd:TIGR03719 395 DALDPNKTVWEEISGGLDIIKLGKREIPSRAYVgrfnfkgSDQQKKVGQ--------------LSGGERNRVHLAKTL-K 459
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1755611750 154 DPRNVI-LDEPTNGLDVMTTRAMRgflQQLRAEGRCVIFSSH 194
Cdd:TIGR03719 460 SGGNVLlLDEPTNDLDVETLRALE---EALLNFAGCAVVISH 498
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
33-223 |
1.45e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 65.50 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 33 ITGLLGPNGAGKTTTLRMLyTLMTPDQGSVRVDG--------VDAAHDPVAVRRALGVLPDARGVYKrLSARENIAYFGQ 104
Cdd:PRK14271 49 VTSLMGPTGSGKTTFLRTL-NRMNDKVSGYRYSGdvllggrsIFNYRDVLEFRRRVGMLFQRPNPFP-MSIMDNVLAGVR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 105 LHGM-SRTQI--AERTRLLSHALdMDDILDRQTEG---FSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRAMRGF 178
Cdd:PRK14271 127 AHKLvPRKEFrgVAQARLTEVGL-WDAVKDRLSDSpfrLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEF 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1755611750 179 LQQLrAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:PRK14271 206 IRSL-ADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
38-168 |
3.64e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 63.71 E-value: 3.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 38 GPNGAGKTTTLRMLYTLMTPDQGSVRVDGvdaAHDPVAVR-RALGVLPDARGVYKRLSARENIAYFGQLHGMSRTQIAER 116
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQIDG---KTATRGDRsRFMAYLGHLPGLKADLSTLENLHFLCGLHGRRAKQMPGS 120
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1755611750 117 TRLLSHALDMDDILDRQtegFSQGQRTKTAIARALVHDPRNVILDEPTNGLD 168
Cdd:PRK13543 121 ALAIVGLAGYEDTLVRQ---LSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-212 |
6.29e-12 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 62.97 E-value: 6.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSFktkTGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAH----DPVAV 76
Cdd:PRK10908 1 MIRFEHVSKAY---LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRlknrEVPFL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 77 RRALGVLPDARGVYKRLSARENIAYFGQLHGMSRTQIAERTrllSHALDMDDILDRQTE---GFSQGQRTKTAIARALVH 153
Cdd:PRK10908 78 RRQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRV---SAALDKVGLLDKAKNfpiQLSGGEQQRVGIARAVVN 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1755611750 154 DPRNVILDEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKG 212
Cdd:PRK10908 155 KPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-208 |
8.14e-12 |
|
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: 64.42 E-value: 8.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 31 GQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDgVDAAHDPVAVRralgvlPDARG-VYKRLSARENIAYFGQLHgms 109
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-LKISYKPQYIS------PDYDGtVEEFLRSANTDDFGSSYY--- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 110 RTQIAERtrllshaLDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDV----MTTRAMRGFlqqLRAE 185
Cdd:COG1245 436 KTEIIKP-------LGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrlAVAKAIRRF---AENR 505
|
170 180
....*....|....*....|...
gi 1755611750 186 GRCVIFSSHIMQEVAALCDRIVI 208
Cdd:COG1245 506 GKTAMVVDHDIYLIDYISDRLMV 528
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
11-226 |
1.02e-11 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 63.67 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 11 FKTKTGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLmTPDQGSV-----RVDGVDAAH-DPVAVRRALG--- 81
Cdd:PRK15093 13 FKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDNWRVtadrmRFDDIDLLRlSPRERRKLVGhnv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 82 ----------VLPDARGVYKRLSARENIAYFGQ----LHGMSRTQIAertrlLSHAL---DMDDILDRQTEGFSQGQRTK 144
Cdd:PRK15093 92 smifqepqscLDPSERVGRQLMQNIPGWTYKGRwwqrFGWRKRRAIE-----LLHRVgikDHKDAMRSFPYELTEGECQK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 145 TAIARALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQL-RAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:PRK15093 167 VMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKEL 246
|
...
gi 1755611750 224 RAA 226
Cdd:PRK15093 247 VTT 249
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-209 |
1.83e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 63.29 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 30 DGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDgvdaahdpvavrralgvlPDARGVYKRLSARENIAYFGQLH--- 106
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEE------------------PSWDEVLKRFRGTELQNYFKKLYnge 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 107 ------------------GMSR---TQIAERTRL--LSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEP 163
Cdd:PRK13409 160 ikvvhkpqyvdlipkvfkGKVRellKKVDERGKLdeVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1755611750 164 TNGLDV---MTT-RAMRGFlqqlrAEGRCVIFSSHIMQEVAALCDRIVII 209
Cdd:PRK13409 240 TSYLDIrqrLNVaRLIREL-----AEGKYVLVVEHDLAVLDYLADNVHIA 284
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-174 |
2.19e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.21 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 2 IVVDSLHKSFKTKTgLVKavnGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRV-DGVDAAHdpvaVRRAL 80
Cdd:PRK11819 325 IEAENLSKSFGDRL-LID---DLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIgETVKLAY----VDQSR 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 81 GVLPDARGVYKRLSARENIAYFGQLHGMSRTQIA----------ERTRLLShaldmddildrqteGfsqGQRTKTAIARA 150
Cdd:PRK11819 397 DALDPNKTVWEEISGGLDIIKVGNREIPSRAYVGrfnfkggdqqKKVGVLS--------------G---GERNRLHLAKT 459
|
170 180
....*....|....*....|....*
gi 1755611750 151 LvHDPRNVI-LDEPTNGLDVMTTRA 174
Cdd:PRK11819 460 L-KQGGNVLlLDEPTNDLDVETLRA 483
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
21-226 |
4.05e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 61.38 E-value: 4.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 21 VNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTpdqGSVRVDGVD------------AAHDPVAVRRALGVLPDARG 88
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLT---GGGAPRGARvtgdvtlngeplAAIDAPRLARLRAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 89 VYKRLSARENIAYFGQLHGMSRTQIAERTR-LLSHAL---DMDDILDRQTEGFSQGQRTKTAIARALVH---------DP 155
Cdd:PRK13547 94 PAFAFSAREIVLLGRYPHARRAGALTHRDGeIAWQALalaGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaqPP 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1755611750 156 RNVILDEPTNGLDVMTTRAMRGFLQQLRAEGRC-VIFSSHIMQEVAALCDRIVIIAKGTVVAAGT-ADELRAA 226
Cdd:PRK13547 174 RYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHDPNLAARHADRIAMLADGAIVAHGApADVLTPA 246
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
4-225 |
4.48e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 61.34 E-value: 4.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 4 VDSLHKSFKTKTGL-----VKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAVR- 77
Cdd:PRK15112 7 VRNLSKTFRYRTGWfrrqtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRs 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 78 -RALGVLPDARgvyKRLSARENIAYFGQLHGMSRTQIA--ERTRLLSHALDMDDILDRQT----EGFSQGQRTKTAIARA 150
Cdd:PRK15112 87 qRIRMIFQDPS---TSLNPRQRISQILDFPLRLNTDLEpeQREKQIIETLRQVGLLPDHAsyypHMLAPGQKQRLGLARA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1755611750 151 LVHDPRNVILDEPTNGLDV-MTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAG-TADELRA 225
Cdd:PRK15112 164 LILRPKVIIADEALASLDMsMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGsTADVLAS 240
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-229 |
4.88e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 62.11 E-value: 4.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 19 KAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLY--TLMTPDQGSVRVDG--VDAAHDPVAVRRALGVLPDARGVY---- 90
Cdd:NF040905 274 KVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFgrSYGRNISGTVFKDGkeVDVSTVSDAIDAGLAYVTEDRKGYglnl 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 91 ----KR---LSARENIAYFGQLHGMSRTQIAE--RTRLLSHALDmddiLDRQTEGFSQGQRTKTAIARALVHDPRNVILD 161
Cdd:NF040905 354 iddiKRnitLANLGKVSRRGVIDENEEIKVAEeyRKKMNIKTPS----VFQKVGNLSGGNQQKVVLSKWLFTDPDVLILD 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1755611750 162 EPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADElraATGE 229
Cdd:NF040905 430 EPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRITGELPREE---ASQE 494
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
36-228 |
6.16e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 61.66 E-value: 6.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 36 LLGPNGAGKTTTLRMLYTLMTPDQGSVRVDG---VDAAH------------DPVavrralgVLPDArgVYKRLSARENIA 100
Cdd:PRK10790 372 LVGHTGSGKSTLASLLMGYYPLTEGEIRLDGrplSSLSHsvlrqgvamvqqDPV-------VLADT--FLANVTLGRDIS 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 101 YFGQLHGMSRTQIAERTRLLSHALDmdDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRAMRGFLQ 180
Cdd:PRK10790 443 EEQVWQALETVQLAELARSLPDGLY--TPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALA 520
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1755611750 181 QLRAEGRCVIFSSHIMQEVAAlcDRIVIIAKGTVVAAGTADELRAATG 228
Cdd:PRK10790 521 AVREHTTLVVIAHRLSTIVEA--DTILVLHRGQAVEQGTHQQLLAAQG 566
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
4-226 |
6.29e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 61.64 E-value: 6.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 4 VDSLHKSFKTKTGLVKAVNGVSFNAADGQITGLLGPNGAGKT-TTLRMLYTLMTPD----QGSVRVDGVDAAHDPVAVRR 78
Cdd:PRK15134 8 IENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQTLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 79 ALgvlpdaRGVYKRLSARENIAYFGQLH--------------GMSRTqiAERTRLLShALDMDDIldRQTEG-------- 136
Cdd:PRK15134 88 GV------RGNKIAMIFQEPMVSLNPLHtlekqlyevlslhrGMRRE--AARGEILN-CLDRVGI--RQAAKrltdyphq 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 137 FSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQLRAE-GRCVIFSSHIMQEVAALCDRIVIIAKGTVV 215
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCV 236
|
250
....*....|.
gi 1755611750 216 AAGTADELRAA 226
Cdd:PRK15134 237 EQNRAATLFSA 247
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-194 |
1.34e-10 |
|
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: 59.69 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 29 ADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGS-------------------------VRVDGVDAAHDPVAVRRalgvL 83
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKfddppdwdeildefrgselqnyftkLLEGDVKVIVKPQYVDL----I 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 84 PDA-RGvykrlSARENIayfgqlhgmSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDE 162
Cdd:cd03236 100 PKAvKG-----KVGELL---------KKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDE 165
|
170 180 190
....*....|....*....|....*....|..
gi 1755611750 163 PTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSH 194
Cdd:cd03236 166 PSSYLDIKQRLNAARLIRELAEDDNYVLVVEH 197
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
31-212 |
1.40e-10 |
|
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: 58.79 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 31 GQITGLLGPNGAGKTTTLRMLytlmtpdqgsvrvdgvdaahdpvAVRRALGV-----LPDARGVYKRLSARenIAYFGQL 105
Cdd:cd03232 33 GTLTALMGESGAGKTTLLDVL-----------------------AGRKTAGVitgeiLINGRPLDKNFQRS--TGYVEQQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 106 HGMSRTQIAERTRLLSHALdmddildrqtEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQLRAE 185
Cdd:cd03232 88 DVHSPNLTVREALRFSALL----------RGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADS 157
|
170 180 190
....*....|....*....|....*....|
gi 1755611750 186 GRCVIFSSHimQEVAALC---DRIVIIAKG 212
Cdd:cd03232 158 GQAILCTIH--QPSASIFekfDRLLLLKRG 185
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
10-228 |
1.88e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 60.73 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 10 SFKTKTGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAA----HDpvaVRRALGVLPD 85
Cdd:TIGR00957 1291 CLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAkiglHD---LRFKITIIPQ 1367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 86 ARGVYKRlSARENIAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQT----EGFSQGQRTKTAIARALVHDPRNVILD 161
Cdd:TIGR00957 1368 DPVLFSG-SLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECaeggENLSVGQRQLVCLARALLRKTKILVLD 1446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1755611750 162 EPTNGLDVMTTRAMRGFLQQLRAEgrCVIFSshIMQEVAALCD--RIVIIAKGTVVAAGTADELRAATG 228
Cdd:TIGR00957 1447 EATAAVDLETDNLIQSTIRTQFED--CTVLT--IAHRLNTIMDytRVIVLDKGEVAEFGAPSNLLQQRG 1511
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
22-215 |
2.88e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 58.43 E-value: 2.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 22 NGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLM--TPDQGSVRVDGVDaahdpvavrralgvlpdargVYKRLSARENI 99
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQ--------------------FGREASLIDAI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 100 AyfgqlhgmSRTQIAERTRLLSHALDMDDILDRQT-EGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRAM-RG 177
Cdd:COG2401 107 G--------RKGDFKDAVELLNAVGLSDAVLWLRRfKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVaRN 178
|
170 180 190
....*....|....*....|....*....|....*....
gi 1755611750 178 FLQQLRAEGRCVIFSSHIMQEVAALC-DRIVIIAKGTVV 215
Cdd:COG2401 179 LQKLARRAGITLVVATHHYDVIDDLQpDLLIFVGYGGVP 217
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-225 |
6.77e-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: 58.66 E-value: 6.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 2 IVVDSLHKSFKTKtglvKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTL--MTPDQGSV----------------- 62
Cdd:TIGR03269 1 IEVKNLTKKFDGK----EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 63 ----------------RVDGVDAAhDPVAVR----------RALGVLPDARGVYKRLSARENIAYFGQLHGMSRTQIAER 116
Cdd:TIGR03269 77 kvgepcpvcggtlepeEVDFWNLS-DKLRRRirkriaimlqRTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 117 TRLlSHALDMddiLDRQTEGfsqGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQL-RAEGRCVIFSSHI 195
Cdd:TIGR03269 156 VQL-SHRITH---IARDLSG---GEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHW 228
|
250 260 270
....*....|....*....|....*....|
gi 1755611750 196 MQEVAALCDRIVIIAKGTVVAAGTADELRA 225
Cdd:TIGR03269 229 PEVIEDLSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
22-213 |
7.85e-10 |
|
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: 56.71 E-value: 7.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 22 NGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGvdaahdPVA-------VRRAlgvlpdargvykrlS 94
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG------SIAyvsqepwIQNG--------------T 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 95 ARENIAyFGQLHGMSRTQIAertrLLSHALDMD-DILDR--QTE----GF--SQGQRTKTAIARALVHDPRNVILDEPTN 165
Cdd:cd03250 82 IRENIL-FGKPFDEERYEKV----IKACALEPDlEILPDgdLTEigekGInlSGGQKQRISLARAVYSDADIYLLDDPLS 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1755611750 166 GLDVMTTRA-MRGFLQQLRAEGRCVIFSSHIMQeVAALCDRIVIIAKGT 213
Cdd:cd03250 157 AVDAHVGRHiFENCILGLLLNNKTRILVTHQLQ-LLPHADQIVVLDNGR 204
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-190 |
9.41e-10 |
|
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: 58.26 E-value: 9.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 31 GQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDgvdaahdpvavrralgvlPDARGVYKRLSARENIAYFGQLH---- 106
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGELKPNLGDYDEE------------------PSWDEVLKRFRGTELQDYFKKLAngei 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 107 -----------------GMSRT---QIAERTRL--LSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPT 164
Cdd:COG1245 161 kvahkpqyvdlipkvfkGTVRElleKVDERGKLdeLAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPS 240
|
170 180
....*....|....*....|....*.
gi 1755611750 165 NGLDVMTTRAMRGFLQQLRAEGRCVI 190
Cdd:COG1245 241 SYLDIYQRLNVARLIRELAEEGKYVL 266
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-214 |
1.09e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.82 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 20 AVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAA-HDPV-AVRRALGVLPDAR---GVYKRLS 94
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINnHNANeAINHGFALVTEERrstGIYAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 95 AREN--IA----YFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEG-FSQGQRTKTAIARALVHDPRNVILDEPTNGL 167
Cdd:PRK10982 343 IGFNslISnirnYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIGsLSGGNQQKVIIGRWLLTQPEILMLDEPTRGI 422
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1755611750 168 DVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTV 214
Cdd:PRK10982 423 DVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
14-224 |
1.27e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 56.65 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 14 KTGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVD-AAHDPVAVRRALGVLPDARGVYKR 92
Cdd:PRK10247 16 LAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDiSTLKPEIYRQQVSYCAQTPTLFGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 93 lSARENIAYFGQLhgmsRTQIAERTRLLS----HALDmDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLD 168
Cdd:PRK10247 96 -TVYDNLIFPWQI----RNQQPDPAIFLDdlerFALP-DTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1755611750 169 VMTTRAMRGFLQQL-RAEGRCVIFSSHIMQEVAAlCDRIVIIAKgtvvAAGTADELR 224
Cdd:PRK10247 170 ESNKHNVNEIIHRYvREQNIAVLWVTHDKDEINH-ADKVITLQP----HAGEMQEAR 221
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
36-215 |
1.78e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 57.65 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 36 LLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGvdaahdPVAVRRaLGVLP--DARG-VYKRLSA--RENIAYFGQLHGMSR 110
Cdd:PRK11147 34 LVGRNGAGKSTLMKILNGEVLLDDGRIIYEQ------DLIVAR-LQQDPprNVEGtVYDFVAEgiEEQAEYLKRYHDISH 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 111 -----------TQIAERTRLLSHA----LD--MDDIL-------DRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNG 166
Cdd:PRK11147 107 lvetdpseknlNELAKLQEQLDHHnlwqLEnrINEVLaqlgldpDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNH 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1755611750 167 LDVMTTRAMRGFLQQLRAegrCVIFSSHIMQEVAALCDRIVIIAKGTVV 215
Cdd:PRK11147 187 LDIETIEWLEGFLKTFQG---SIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1-215 |
1.89e-09 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 55.73 E-value: 1.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSFKTKTGLVKA--VNGVSFNAADGQITGLLGPNGAGKTTTLRMLyTLMTPD----QGSVRVDGVDAAhdpv 74
Cdd:cd03233 1 ASTLSWRNISFTTGKGRSKIpiLKDFSGVVKPGEMVLVLGRPGSGCSTLLKAL-ANRTEGnvsvEGDIHYNGIPYK---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 75 avrralgvlpDARGVYKRlsareNIAYFGQ--LHgmsrtqIAERT--RLLSHALDM--DDILdrqtEGFSQGQRTKTAIA 148
Cdd:cd03233 76 ----------EFAEKYPG-----EIIYVSEedVH------FPTLTvrETLDFALRCkgNEFV----RGISGGERKRVSIA 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 149 RALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSShIMQ---EVAALCDRIVIIAKGTVV 215
Cdd:cd03233 131 EALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVS-LYQasdEIYDLFDKVLVLYEGRQI 199
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-169 |
7.80e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.56 E-value: 7.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSFKTKTGLVKAVNGVSfnaaDGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDA-----AHDPVA 75
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATIN----PGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQlawvnQETPAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 76 VRRALGVLPDARGVYKRLSARENIA-----------YFGQLHGMSRTQIAERTRLLSHALDM-DDILDRQTEGFSQGQRT 143
Cdd:PRK10636 77 PQPALEYVIDGDREYRQLEAQLHDAnerndghaiatIHGKLDAIDAWTIRSRAASLLHGLGFsNEQLERPVSDFSGGWRM 156
|
170 180
....*....|....*....|....*.
gi 1755611750 144 KTAIARALVHDPRNVILDEPTNGLDV 169
Cdd:PRK10636 157 RLNLAQALICRSDLLLLDEPTNHLDL 182
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
36-194 |
1.25e-08 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 52.93 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 36 LLGPNGAGKTTTLRMLYTLMTPDQGSVrvdgvdaahdpvavrralgVLPDARGVYkRLSAReniAYFGQlhGMSRTQIAe 115
Cdd:cd03223 32 ITGPSGTGKSSLFRALAGLWPWGSGRI-------------------GMPEGEDLL-FLPQR---PYLPL--GTLREQLI- 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1755611750 116 rtrllshaLDMDDILdrqtegfSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRAMrgfLQQLRAEGRCVIFSSH 194
Cdd:cd03223 86 --------YPWDDVL-------SGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRL---YQLLKELGITVISVGH 146
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
21-212 |
2.31e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 54.12 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 21 VNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPD--QGSVRVDGVDAAHDpvaVRRALGVLPDARGVYKRLSAREN 98
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQ---ILKRTGFVTQDDILYPHLTVRET 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 99 IAYFGQLHGMSRTQIAERTRLLSHAL--------DMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVM 170
Cdd:PLN03211 161 LVFCSLLRLPKSLTKQEKILVAESVIselgltkcENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDAT 240
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1755611750 171 TTRAMRGFLQQLRAEGRCVIFSSH-IMQEVAALCDRIVIIAKG 212
Cdd:PLN03211 241 AAYRLVLTLGSLAQKGKTIVTSMHqPSSRVYQMFDSVLVLSEG 283
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
23-214 |
2.40e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 52.86 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 23 GVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAVRRAL-----GVLPDARGVYKRLSARE 97
Cdd:PRK10584 28 GVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLrakhvGFVFQSFMLIPTLNALE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 98 NIAYFGQLHGMSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRAMRG 177
Cdd:PRK10584 108 NVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIAD 187
|
170 180 190
....*....|....*....|....*....|....*...
gi 1755611750 178 FLQQL-RAEGRCVIFSSHIMQeVAALCDRIVIIAKGTV 214
Cdd:PRK10584 188 LLFSLnREHGTTLILVTHDLQ-LAARCDRRLRLVNGQL 224
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
13-230 |
3.00e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 53.64 E-value: 3.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 13 TKT-GLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRML---YTLMTPDqGSVRVDGVDA---------AHDPVAVRRA 79
Cdd:NF040905 8 TKTfPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLsgvYPHGSYE-GEILFDGEVCrfkdirdseALGIVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 80 LGVLPDargvykrLSARENIaYFGQLHG----MSRTQIAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDP 155
Cdd:NF040905 87 LALIPY-------LSIAENI-FLGNERAkrgvIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1755611750 156 RNVILDEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAagTADELRAATGED 230
Cdd:NF040905 159 KLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIE--TLDCRADEVTED 231
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
31-213 |
3.22e-08 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 52.33 E-value: 3.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 31 GQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAVRRALGVLPDARGVYK----RLSARENIAyFGQLH 106
Cdd:cd03290 27 GQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKpwllNATVEENIT-FGSPF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 107 GMSRTQIAERTRLLSHALDMDDILDrQTE------GFSQGQRTKTAIARALVHDPRNVILDEPTNGLDV-MTTRAMR-GF 178
Cdd:cd03290 106 NKQRYKAVTDACSLQPDIDLLPFGD-QTEigergiNLSGGQRQRICVARALYQNTNIVFLDDPFSALDIhLSDHLMQeGI 184
|
170 180 190
....*....|....*....|....*....|....*
gi 1755611750 179 LQQLRAEGRCVIFSSHIMQEVAAlCDRIVIIAKGT 213
Cdd:cd03290 185 LKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDGS 218
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
21-185 |
3.35e-08 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 53.66 E-value: 3.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 21 VNGVSFNAADGQitGLL--GPNGAGKTTTLRMLYTLMTPDQGSVRV-DGVDAAHDPvavRRA---LGVLpdargvykrls 94
Cdd:COG4178 379 LEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLFLP---QRPylpLGTL----------- 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 95 aRENIAYFGQLHGMSRTQIAE---RTRL--LSHALDMDDILDRQtegFSQGQRTKTAIARALVHDPRNVILDEPTNGLDV 169
Cdd:COG4178 443 -REALLYPATAEAFSDAELREaleAVGLghLAERLDEEADWDQV---LSLGEQQRLAFARLLLHKPDWLFLDEATSALDE 518
|
170
....*....|....*.
gi 1755611750 170 MTTRAMrgfLQQLRAE 185
Cdd:COG4178 519 ENEAAL---YQLLREE 531
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
21-226 |
3.65e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 52.78 E-value: 3.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 21 VNGVSFNAADGQITGLLGPNGAGKTTT----LRMLYTLMTPDQGSVRVDGVDAAHDPVAVRRALGVLPDARGVYK----- 91
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTcaaaLGILPAGVRQTAGRVLLDGKPVAPCALRGRKIATIMQNPRSAFNplhtm 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 92 RLSARENIAYFGQ-------LHGMSRTQIAERTRLL-SHALDMddildrqtegfSQGQRTKTAIARALVHDPRNVILDEP 163
Cdd:PRK10418 99 HTHARETCLALGKpaddatlTAALEAVGLENAARVLkLYPFEM-----------SGGMLQRMMIALALLCEAPFIIADEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1755611750 164 TNGLDVMTTRAMRGFLQQL-RAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADELRAA 226
Cdd:PRK10418 168 TTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNA 231
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
31-212 |
6.29e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.19 E-value: 6.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 31 GQITGLLGPNGAGKTTTLRMLYTLMTP---DQGSVRVDG--VDAAhdpvaVRRALGVLPDARGVYKRLSARENIAYFGQL 105
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGrpLDSS-----FQRSIGYVQQQDLHLPTSTVRESLRFSAYL 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 106 HGMSRTQIAERTRLLSHALDM-------DDILDRQTEGFSQGQRTKTAIARALVHDPRNVI-LDEPTNGLDVMTTRAMRG 177
Cdd:TIGR00956 864 RQPKSVSKSEKMEYVEEVIKLlemesyaDAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICK 943
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1755611750 178 FLQQLRAEGRCVIFSSH-----IMQEVaalcDRIVIIAKG 212
Cdd:TIGR00956 944 LMRKLADHGQAILCTIHqpsaiLFEEF----DRLLLLQKG 979
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
114-223 |
7.53e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.32 E-value: 7.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 114 AERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSS 193
Cdd:PRK10938 113 PARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVL 192
|
90 100 110
....*....|....*....|....*....|
gi 1755611750 194 HIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:PRK10938 193 NRFDEIPDFVQFAGVLADCTLAETGEREEI 222
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-222 |
9.89e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.20 E-value: 9.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 2 IVVDSLHKSFKTKTglvkAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVrvdgvdaahdpvavrralg 81
Cdd:PRK15064 320 LEVENLTKGFDNGP----LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV------------------- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 82 vlpdargvykRLSARENIAYFGQLH------GMSRTQIAERTRLLSHaldmDDILDRQTEG---FSQ------------G 140
Cdd:PRK15064 377 ----------KWSENANIGYYAQDHaydfenDLTLFDWMSQWRQEGD----DEQAVRGTLGrllFSQddikksvkvlsgG 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 141 QRTKTAIARALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQLraEGrCVIFSSHIMQEVAALCDRIV-IIAKGTVVAAGT 219
Cdd:PRK15064 443 EKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKY--EG-TLIFVSHDREFVSSLATRIIeITPDGVVDFSGT 519
|
...
gi 1755611750 220 ADE 222
Cdd:PRK15064 520 YEE 522
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
22-194 |
1.24e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.94 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 22 NGVSFNAADGQITGLLGPNGAGKTTtlrmLYTLMTPDQ-----------GSVRVDGvDAAHDpvaVRRALGVLPDARGVY 90
Cdd:PRK10938 277 HNLSWQVNPGEHWQIVGPNGAGKST----LLSLITGDHpqgysndltlfGRRRGSG-ETIWD---IKKHIGYVSSSLHLD 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 91 KRLS--ARENI--AYFGQLhGMSRtQIAERTRLLS----HALDMDDIL-DRQTEGFSQGQRTKTAIARALVHDPRNVILD 161
Cdd:PRK10938 349 YRVStsVRNVIlsGFFDSI-GIYQ-AVSDRQQKLAqqwlDILGIDKRTaDAPFHSLSWGQQRLALIVRALVKHPTLLILD 426
|
170 180 190
....*....|....*....|....*....|....
gi 1755611750 162 EPTNGLDVMTTRAMRGFLQQLRAEGRC-VIFSSH 194
Cdd:PRK10938 427 EPLQGLDPLNRQLVRRFVDVLISEGETqLLFVSH 460
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
31-239 |
2.10e-07 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 50.68 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 31 GQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPV-AVRRALGVL----------------PDARGVYKRL 93
Cdd:cd03288 47 GQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLhTLRSRLSIIlqdpilfsgsirfnldPECKCTDDRL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 94 SARENIAyfgQLHGMSRTqiaertrlLSHALDMddILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTR 173
Cdd:cd03288 127 WEALEIA---QLKNMVKS--------LPGGLDA--VVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATEN 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1755611750 174 AMRGFLQQLRAEgRCVIFSSHIMQEVAAlCDRIVIIAKGTVVAAGTADELRAAtgEDNLEDAFVKA 239
Cdd:cd03288 194 ILQKVVMTAFAD-RTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQ--EDGVFASLVRT 255
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
21-171 |
3.51e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.72 E-value: 3.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 21 VNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRV---------DGVDAAHDP--------------VAV- 76
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCgtklevayfDQHRAELDPektvmdnlaegkqeVMVn 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 77 ---RRALGVLPD-------ARGVYKRLSAreniayfgqlhgmsrtqiAERTRLLshaldmddildrqtegfsqgqrtkta 146
Cdd:PRK11147 415 grpRHVLGYLQDflfhpkrAMTPVKALSG------------------GERNRLL-------------------------- 450
|
170 180
....*....|....*....|....*.
gi 1755611750 147 IARALVHdPRN-VILDEPTNGLDVMT 171
Cdd:PRK11147 451 LARLFLK-PSNlLILDEPTNDLDVET 475
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
10-228 |
9.68e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 49.56 E-value: 9.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 10 SFKTKTGLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGvdaahdpvavrrALGVLPDARGV 89
Cdd:TIGR00957 643 TFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG------------SVAYVPQQAWI 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 90 yKRLSARENIAYFGQLHGMSRTQIAERTRLLSHaLDMDDILDRQTEG-----FSQGQRTKTAIARALVHDPRNVILDEPT 164
Cdd:TIGR00957 711 -QNDSLRENILFGKALNEKYYQQVLEACALLPD-LEILPSGDRTEIGekgvnLSGGQKQRVSLARAVYSNADIYLFDDPL 788
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1755611750 165 NGLDVMTTRAM-------RGFLQqlraeGRCVIFSSHIMQEVAALcDRIVIIAKGTVVAAGTADELRAATG 228
Cdd:TIGR00957 789 SAVDAHVGKHIfehvigpEGVLK-----NKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQRDG 853
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
4-223 |
1.10e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 48.58 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 4 VDSLHKSFKTKTGLVKAVNGVSFNAADGQITGLLGPNGAGKT-TTLRMLYTLMTPDQ---GSVRVDGVDAAHDPVAVRRA 79
Cdd:PRK11022 6 VDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPGRvmaEKLEFNGQDLQRISEKERRN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 80 LgVLPDARGVYKRLSARENIAY---FGQLHGMSRTQIAERTRLLSHALDMDDI---------LDRQTEGFSQGQRTKTAI 147
Cdd:PRK11022 86 L-VGAEVAMIFQDPMTSLNPCYtvgFQIMEAIKVHQGGNKKTRRQRAIDLLNQvgipdpasrLDVYPHQLSGGMSQRVMI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1755611750 148 ARALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQL-RAEGRCVIFSSHIMQEVAALCDRIVIIAKGTVVAAGTADEL 223
Cdd:PRK11022 165 AMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-194 |
1.31e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 48.25 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSFKTKTGLvkavNGVSFNAADGQITGLLGPNGAGKTT---TL--RMLYTLmtpDQGSVRVDGVDAAHDPVA 75
Cdd:PRK09580 1 MLSIKDLHVSVEDKAIL----RGLNLEVRPGEVHAIMGPNGSGKSTlsaTLagREDYEV---TGGTVEFKGKDLLELSPE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 76 VRRALGVL------PDARGVYKRL---SARENIAYFGQLHGMSRTQIAERTRLLSHALDM-DDILDRQ-TEGFSQGQRTK 144
Cdd:PRK09580 74 DRAGEGIFmafqypVEIPGVSNQFflqTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMpEDLLTRSvNVGFSGGEKKR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1755611750 145 TAIARALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSH 194
Cdd:PRK09580 154 NDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-247 |
1.43e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.01 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 16 GLVKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVD-AAHDPVAVRRALGVLPDARGVYKRlS 94
Cdd:PTZ00243 1321 GLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREiGAYGLRELRRQFSMIPQDPVLFDG-T 1399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 95 ARENIAYFGQ-----------LHGMsrtqiaeRTRLLSHALDMDdilDRQTEG---FSQGQRTKTAIARALVHDPRNVIL 160
Cdd:PTZ00243 1400 VRQNVDPFLEassaevwaaleLVGL-------RERVASESEGID---SRVLEGgsnYSVGQRQLMCMARALLKKGSGFIL 1469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 161 -DEPTNGLDVMTTR-----AMRGFlqqlraEGRCVIFSSHIMQEVAAlCDRIVIIAKGTVVAAGTADELraATGEDNLED 234
Cdd:PTZ00243 1470 mDEATANIDPALDRqiqatVMSAF------SAYTVITIAHRLHTVAQ-YDKIIVMDHGAVAEMGSPREL--VMNRQSIFH 1540
|
250
....*....|...
gi 1755611750 235 AFVKAIGSDEGLH 247
Cdd:PTZ00243 1541 SMVEALGRSEAKR 1553
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
12-194 |
1.47e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.07 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 12 KTKTGLVKAVNGVsFNAadGQITGLLGPNGAGKTTTLRMLYTLMTPD--QGSVRVDGVDAAHDPVAvrRALGVLPDARGV 89
Cdd:PLN03140 890 EDRLQLLREVTGA-FRP--GVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFPKKQETFA--RISGYCEQNDIH 964
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 90 YKRLSARENIAYFGQLHGMSRTQIAERTRLLS---HALDMDDILDR-----QTEGFSQGQRTKTAIARALVHDPRNVILD 161
Cdd:PLN03140 965 SPQVTVRESLIYSAFLRLPKEVSKEEKMMFVDevmELVELDNLKDAivglpGVTGLSTEQRKRLTIAVELVANPSIIFMD 1044
|
170 180 190
....*....|....*....|....*....|....*....
gi 1755611750 162 EPTNGLD------VMttRAMRGFLQQlraeGRCVIFSSH 194
Cdd:PLN03140 1045 EPTSGLDaraaaiVM--RTVRNTVDT----GRTVVCTIH 1077
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
35-181 |
1.61e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 48.39 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 35 GLLGPNGAGKTTTLRMLYTLMTPDQGSVRV-DGVDAAH-------DPVA-----VRRALGVLPDARGVYKRLSAR--ENI 99
Cdd:TIGR03719 35 GVLGLNGAGKSTLLRIMAGVDKDFNGEARPqPGIKVGYlpqepqlDPTKtvrenVEEGVAEIKDALDRFNEISAKyaEPD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 100 AYFGQLhgmsrtqIAERTRL-----------LSHALDMD-DIL-----DRQTEGFSQGQRTKTAIARALVHDPRNVILDE 162
Cdd:TIGR03719 115 ADFDKL-------AAEQAELqeiidaadawdLDSQLEIAmDALrcppwDADVTKLSGGERRRVALCRLLLSKPDMLLLDE 187
|
170
....*....|....*....
gi 1755611750 163 PTNGLDVMTTRAMRGFLQQ 181
Cdd:TIGR03719 188 PTNHLDAESVAWLERHLQE 206
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
24-223 |
1.80e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.82 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 24 VSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVrvdgvdaahdpVAVRRALGVLPDARGVYKRlSARENIaYFG 103
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSS-----------VVIRGSVAYVPQVSWIFNA-TVRENI-LFG 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 104 QLHGMSRTQIAERTRLLSHALDMDDILDRQTEG-----FSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRAM--R 176
Cdd:PLN03232 703 SDFESERYWRAIDVTALQHDLDLLPGRDLTEIGergvnISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVfdS 782
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1755611750 177 GFLQQLRAEGRCVIFSS-HIMqevaALCDRIVIIAKGTVVAAGTADEL 223
Cdd:PLN03232 783 CMKDELKGKTRVLVTNQlHFL----PLMDRIILVSEGMIKEEGTFAEL 826
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
33-194 |
3.06e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 46.40 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 33 ITGLLGPNGAGKTTTLRMLYTLMTPDQGSV--RVDGVDAAHDPVavrraLGVLPDARGVYKRLSARENIAYFGQLHGMSR 110
Cdd:PRK13541 28 ITYIKGANGCGKSSLLRMIAGIMQPSSGNIyyKNCNINNIAKPY-----CTYIGHNLGLKLEMTVFENLKFWSEIYNSAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 111 TQIAErtrllSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDvMTTRAMRGFLQQLRA-EGRCV 189
Cdd:PRK13541 103 TLYAA-----IHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS-KENRDLLNNLIVMKAnSGGIV 176
|
....*
gi 1755611750 190 IFSSH 194
Cdd:PRK13541 177 LLSSH 181
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
130-218 |
3.44e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.90 E-value: 3.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 130 LDRQTEGFSQGQRTKTAIARALVHDPRNV--ILDEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVaALCDRIV 207
Cdd:PRK00635 470 PERALATLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMI-SLADRII 548
|
90
....*....|.
gi 1755611750 208 IIAKGTVVAAG 218
Cdd:PRK00635 549 DIGPGAGIFGG 559
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
31-206 |
3.98e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 45.44 E-value: 3.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 31 GQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGvdaahdpvavrralgvlpdargvykrlsareniayfgqlhgmsr 110
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYID-------------------------------------------- 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 111 tqiAERTRLLSHALDMDDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRA------MRGFLQQLRA 184
Cdd:smart00382 38 ---GEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALlllleeLRLLLLLKSE 114
|
170 180
....*....|....*....|..
gi 1755611750 185 EGRCVIFSSHIMQEVAALCDRI 206
Cdd:smart00382 115 KNLTVILTTNDEKDLGPALLRR 136
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
135-238 |
6.07e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.95 E-value: 6.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 135 EGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSshIMQEVAAL--CDRIVIIAK- 211
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIIT--IAHRIASIkrSDKIVVFNNp 1434
|
90 100 110
....*....|....*....|....*....|.
gi 1755611750 212 ---GTVVAA-GTADELRAAtgEDNLEDAFVK 238
Cdd:PTZ00265 1435 drtGSFVQAhGTHEELLSV--QDGVYKKYVK 1463
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
24-225 |
7.92e-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: 46.83 E-value: 7.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 24 VSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAvrralGVLPDargvykrlSARENIayfg 103
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTS-----WIMPG--------TIKDNI---- 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 104 qLHGMSRTQIAERTRLLSHALDMDDIL----DRQTEG-----FSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRA 174
Cdd:TIGR01271 508 -IFGLSYDEYRYTSVIKACQLEEDIALfpekDKTVLGeggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKE 586
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1755611750 175 M--RGFLQQLRAEGRCVIFS--SHIMQevaalCDRIVIIAKGTVVAAGTADELRA 225
Cdd:TIGR01271 587 IfeSCLCKLMSNKTRILVTSklEHLKK-----ADKILLLHEGVCYFYGTFSELQA 636
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-221 |
8.70e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 45.79 E-value: 8.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 1 MIVVDSLHKSFKTKTgLVKAVNgVSFNAadGQITGLLGPNGAGKTTTLRML-----YTL--------------MTPDQGS 61
Cdd:CHL00131 7 ILEIKNLHASVNENE-ILKGLN-LSINK--GEIHAIMGPNGSGKSTLSKVIaghpaYKIlegdilfkgesildLEPEERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 62 -----------VRVDGVDAAHdpvAVRRALgvlpDARGVYKRLSARENIAYFgqlhgmsrTQIAERTRLLshalDMDDI- 129
Cdd:CHL00131 83 hlgiflafqypIEIPGVSNAD---FLRLAY----NSKRKFQGLPELDPLEFL--------EIINEKLKLV----GMDPSf 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 130 LDRQ-TEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQevaaLCDRIV- 207
Cdd:CHL00131 144 LSRNvNEGFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQR----LLDYIKp 219
|
250
....*....|....*...
gi 1755611750 208 ----IIAKGTVVAAGTAD 221
Cdd:CHL00131 220 dyvhVMQNGKIIKTGDAE 237
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
24-224 |
9.83e-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: 45.62 E-value: 9.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 24 VSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAvrralGVLPDargvykrlSARENIAY-- 101
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFS-----WIMPG--------TIKENIIFgv 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 102 -FGQLHGMSRTQIAERTRLLSHALDMDDILdrQTEG---FSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRAM-R 176
Cdd:cd03291 123 sYDEYRYKSVVKACQLEEDITKFPEKDNTV--LGEGgitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIfE 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1755611750 177 GFLQQLRAEGRCVIFSSHIMQEVAAlcDRIVIIAKGTVVAAGTADELR 224
Cdd:cd03291 201 SCVCKLMANKTRILVTSKMEHLKKA--DKILILHEGSSYFYGTFSELQ 246
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
20-194 |
1.43e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 45.73 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 20 AVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDG--VDAAhDPVAVRralgvlpdargvyKRLSAR- 96
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGkpVTAE-QPEDYR-------------KLFSAVf 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 97 ENIAYFGQLHGMSRTQIAER------TRL-LSHALDMDD--ILDRQtegFSQGQRTKTAIARALVHDPRNVILDEPTNGL 167
Cdd:PRK10522 404 TDFHLFDQLLGPEGKPANPAlvekwlERLkMAHKLELEDgrISNLK---LSKGQKKRLALLLALAEERDILLLDEWAADQ 480
|
170 180
....*....|....*....|....*...
gi 1755611750 168 DVMTTRAM-RGFLQQLRAEGRCVIFSSH 194
Cdd:PRK10522 481 DPHFRREFyQVLLPLLQEMGKTIFAISH 508
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
30-83 |
2.11e-05 |
|
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: 43.71 E-value: 2.11e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1755611750 30 DGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAVRRALGVL 83
Cdd:cd03222 24 EGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQYIDLSGGEL 77
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
24-225 |
3.65e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 44.73 E-value: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 24 VSFNAADGQITGLLGPNGAGKTTTLR-MLYTLMTPDQGSVrvdgvdaahdpvAVRRALGVLPDARGVYKRlSARENIaYF 102
Cdd:PLN03130 636 INLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASV------------VIRGTVAYVPQVSWIFNA-TVRDNI-LF 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 103 GQLHGMSRTQIAERTRLLSHAL------DMDDILDRQTEgFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRAM- 175
Cdd:PLN03130 702 GSPFDPERYERAIDVTALQHDLdllpggDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVf 780
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1755611750 176 -RGFLQQLRAEGRCVIFSS-HIMQEVaalcDRIVIIAKGTVVAAGTADELRA 225
Cdd:PLN03130 781 dKCIKDELRGKTRVLVTNQlHFLSQV----DRIILVHEGMIKEEGTYEELSN 828
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
18-194 |
4.64e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 44.25 E-value: 4.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 18 VKAVNGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVD-----------------GVdAAHDPVA----- 75
Cdd:PTZ00265 398 VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdshnlkdinlkwwrskiGV-VSQDPLLfsnsi 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 76 ---VRRALGVLPDARGVYKRLSARENIAYFGQLHGMS-RTQIAERTRLLSHALDMDDILDRQTE---------------- 135
Cdd:PTZ00265 477 knnIKYSLYSLKDLEALSNYYNEDGNDSQENKNKRNScRAKCAGDLNDMSNTTDSNELIEMRKNyqtikdsevvdvskkv 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 136 ----------------------GFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRAMRGFLQQLRA-EGRCVIFS 192
Cdd:PTZ00265 557 lihdfvsalpdkyetlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGnENRITIII 636
|
..
gi 1755611750 193 SH 194
Cdd:PTZ00265 637 AH 638
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
128-169 |
1.05e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.92 E-value: 1.05e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1755611750 128 DILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDV 169
Cdd:PLN03073 336 EMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
92-229 |
2.17e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 42.32 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 92 RLSARENIAYFGQLH-GMSRTQIAE------RTRL----------LShaldmddiLDRQTEGFSQG--QRTK--TAIARA 150
Cdd:COG0178 432 ALSIDEALEFFENLElTEREAEIAErilkeiRSRLgflvdvgldyLT--------LDRSAGTLSGGeaQRIRlaTQIGSG 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 151 LVhdprNV--ILDEPTNGL---DvmtTRAMRGFLQQLRAEGRCVIFSSH---IMQEvaalCDRIVII------AKGTVVA 216
Cdd:COG0178 504 LV----GVlyVLDEPSIGLhqrD---NDRLIETLKRLRDLGNTVIVVEHdedTIRA----ADYIIDIgpgageHGGEVVA 572
|
170
....*....|....*..
gi 1755611750 217 AGTADELRAA----TGE 229
Cdd:COG0178 573 QGTPEEILKNpdslTGQ 589
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
24-218 |
8.14e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 40.53 E-value: 8.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 24 VSFNAADGQITGLLGPNGAGKTTtlrMLYTLMTPdqgsvrvdgVDAAHDPVAVRRALGVLPDARGVYKRlSARENIAYF- 102
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKST---LLQSLLSQ---------FEISEGRVWAERSIAYVPQQAWIMNA-TVRGNILFFd 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 103 ----GQLHGMSR-TQIAERTRLLSHALDMDdiLDRQTEGFSQGQRTKTAIARAlVHDPRNV-ILDEPTNGLDV-MTTRAM 175
Cdd:PTZ00243 746 eedaARLADAVRvSQLEADLAQLGGGLETE--IGEKGVNLSGGQKARVSLARA-VYANRDVyLLDDPLSALDAhVGERVV 822
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1755611750 176 RG-FLQQLRAEGRcvIFSSHIMQeVAALCDRIVIIAKGTVVAAG 218
Cdd:PTZ00243 823 EEcFLGALAGKTR--VLATHQVH-VVPRADYVVALGDGRVEFSG 863
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
24-63 |
8.66e-04 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 39.60 E-value: 8.66e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1755611750 24 VSFNAADGqITGLLGPNGAGKTTTLRMLYTLMTPDQGSVR 63
Cdd:COG3950 19 IDFDNPPR-LTVLVGENGSGKTTLLEAIALALSGLLSRLD 57
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
92-225 |
1.27e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.61 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 92 RLSARENIAYFGQLH-GMSRTQIAE------RTR---LLSHALDMDDiLDRQTEGFSQGQRTKTAIARALVHDPRNV--I 159
Cdd:TIGR00630 435 ELSIREAHEFFNQLTlTPEEKKIAEevlkeiRERlgfLIDVGLDYLS-LSRAAGTLSGGEAQRIRLATQIGSGLTGVlyV 513
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1755611750 160 LDEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMQEVAAlCDRIVIIAKGT------VVAAGTADELRA 225
Cdd:TIGR00630 514 LDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRA-ADYVIDIGPGAgehggeVVASGTPEEILA 584
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
158-219 |
2.38e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 38.36 E-value: 2.38e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1755611750 158 VILDEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHIMqEVAALCDRIVII------AKGTVVAAGT 219
Cdd:cd03271 194 YILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNL-DVIKCADWIIDLgpeggdGGGQVVASGT 260
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
30-63 |
3.07e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 38.78 E-value: 3.07e-03
10 20 30
....*....|....*....|....*....|....
gi 1755611750 30 DGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVR 63
Cdd:PRK04863 26 DELVTTLSGGNGAGKSTTMAAFVTALIPDLTLLH 59
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
21-211 |
3.32e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 37.34 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 21 VNGVSFnaADGQITGLLGPNGAGKTTTLRmlytlmtpdqgsvrvdgvdaahdpvAVRRALGVLPDARGVYKRLSARENIA 100
Cdd:cd03227 13 PNDVTF--GEGSLTIITGPNGSGKSTILD-------------------------AIGLALGGAQSATRRRSGVKAGCIVA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 101 YfgqlhgmsrtQIAERTRLLShaldmddildrqteGFSQGQRTKTAIARALVH---DPRN-VILDEPTNGLDVMTTRAMR 176
Cdd:cd03227 66 A----------VSAELIFTRL--------------QLSGGEKELSALALILALaslKPRPlYILDEIDRGLDPRDGQALA 121
|
170 180 190
....*....|....*....|....*....|....*
gi 1755611750 177 GFLQQLRAEGRCVIFSSHiMQEVAALCDRIVIIAK 211
Cdd:cd03227 122 EAILEHLVKGAQVIVITH-LPELAELADKLIHIKK 155
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
130-213 |
6.43e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 36.53 E-value: 6.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 130 LDRQTEGFSQGQRTKTAIARALVHDPRNV--ILDEPTNGLDVMTTRAMRGFLQQLRAEGRCVIFSSHimqEVAALC--DR 205
Cdd:cd03238 81 LGQKLSTLSGGELQRVKLASELFSEPPGTlfILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEH---NLDVLSsaDW 157
|
....*...
gi 1755611750 206 IVIIAKGT 213
Cdd:cd03238 158 IIDFGPGS 165
|
|
| PRK05335 |
PRK05335 |
tRNA (uracil-5-)-methyltransferase Gid; Reviewed |
195-240 |
6.86e-03 |
|
tRNA (uracil-5-)-methyltransferase Gid; Reviewed
Pssm-ID: 235416 Cd Length: 436 Bit Score: 37.43 E-value: 6.86e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1755611750 195 IMQEVAALCDRIVIIAKGTVVAAGTADELRAATGEDNLedAFVKAI 240
Cdd:PRK05335 118 IREEVTEIPEDITIIATGPLTSDALAEAIKALTGEDYL--YFFDAA 161
|
|
| ABC_MSH6_euk |
cd03286 |
ATP-binding cassette domain of eukaryotic MutS6 homolog; The MutS protein initiates DNA ... |
22-153 |
9.78e-03 |
|
ATP-binding cassette domain of eukaryotic MutS6 homolog; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213253 [Multi-domain] Cd Length: 218 Bit Score: 36.25 E-value: 9.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755611750 22 NGVSFNAADGQITGLLGPNGAGKTTTLRMLYTLMTPDQGSVRVDGVDAAHDPVAvrralgvlpdarGVYKRLSARENIay 101
Cdd:cd03286 21 NDVDLGATSPRILVLTGPNMGGKSTLLRTVCLAVIMAQMGMDVPAKSMRLSLVD------------RIFTRIGARDDI-- 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1755611750 102 fgqLHGMSR--TQIAERTRLLSHA----LDMDDILDRQTEGFSqgqrtKTAIARALVH 153
Cdd:cd03286 87 ---MKGESTfmVELSETANILRHAtpdsLVILDELGRGTSTHD-----GYAIAHAVLE 136
|
|
| |
