|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-244 |
2.85e-81 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 245.74 E-value: 2.85e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYKRgnqqIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEIIRGRFS 82
Cdd:COG1131 1 IEVRGLTKRYGD----KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 83 FLWEGMqNVYHYLTGEANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVVFL 162
Cdd:COG1131 77 YVPQEP-ALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 163 DEPLSGLDVLAAAELTESIKSWVKEmGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDLKNLSKEEEYILYLRNS 242
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLLEDVFLELTGEE 234
|
..
gi 2485612693 243 AK 244
Cdd:COG1131 235 AR 236
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
2-234 |
7.29e-68 |
|
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: 212.03 E-value: 7.29e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVYKrgnqQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEIIRGRF 81
Cdd:COG4555 1 MIEVENLSKKYG----KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 82 SFLWEGMqNVYHYLTGEANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVVF 161
Cdd:COG4555 77 GVLPDER-GLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2485612693 162 LDEPLSGLDVLAAAELTESIKSWvKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDLKNLSKEEE 234
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEEN 227
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3-217 |
4.67e-62 |
|
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: 194.54 E-value: 4.67e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYKRGnqqiKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEIIRGRFS 82
Cdd:cd03230 1 IEVRNLSKRYGKK----TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 83 FLWEGMqNVYHYLTGEANIlyfaylnqvpssvarrrceellrkldlyevkdqyvfTYSAGMRKKLAIATCLINDPEVVFL 162
Cdd:cd03230 77 YLPEEP-SLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2485612693 163 DEPLSGLDVLAAAELTESIKSWVKEmGKTVIIASHRMDFVEKVTNKVLWLKEGKV 217
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
3-227 |
4.12e-61 |
|
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: 193.74 E-value: 4.12e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYKrgnqQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEIIRGRFS 82
Cdd:cd03265 1 IEVENLVKKYG----DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 83 FLWEgMQNVYHYLTGEANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVVFL 162
Cdd:cd03265 77 IVFQ-DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2485612693 163 DEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDLK 227
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
10-227 |
2.04e-55 |
|
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: 181.82 E-value: 2.04e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 10 KVYkrGNqqIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEIIRGRFSFLWEgMQ 89
Cdd:TIGR01188 1 KVY--GD--FKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQ-YA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 90 NVYHYLTGEANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVVFLDEPLSGL 169
Cdd:TIGR01188 76 SVDEDLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2485612693 170 DVLAAAELTESIKSWVKEmGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDLK 227
Cdd:TIGR01188 156 DPRTRRAIWDYIRALKEE-GVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELK 212
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
2-221 |
3.95e-55 |
|
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: 178.33 E-value: 3.95e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVYKRGNQQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEIIRGRF 81
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 82 SFLWEGMqNVYHYLTGEANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVVF 161
Cdd:cd03266 81 GFVSDST-GLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 162 LDEPLSGLDVLAAAELTESIKSwVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEG 221
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRQ-LRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-249 |
3.34e-53 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 176.07 E-value: 3.34e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYkrGNQQikANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLlkKPEIIRgRFS 82
Cdd:COG4152 2 LELKGLTKRF--GDKT--AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL--DPEDRR-RIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 83 FLWE--GMqnvYHYLTGEANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVV 160
Cdd:COG4152 75 YLPEerGL---YPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 161 FLDEPLSGLDVLAAaeltESIKSWVKEM---GKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDLKNLSKEEEYIL 237
Cdd:COG4152 152 ILDEPFSGLDPVNV----ELLKDVIRELaakGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRNTLRL 227
|
250
....*....|..
gi 2485612693 238 YLRNSAKAREKL 249
Cdd:COG4152 228 EADGDAGWLRAL 239
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3-221 |
8.46e-53 |
|
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: 171.99 E-value: 8.46e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYKRGnqqiKANDNISFFVERGdVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEIIRGRFS 82
Cdd:cd03264 1 LQLENLTKRYGKK----RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 83 FLwegMQ--NVYHYLTGEANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVV 160
Cdd:cd03264 76 YL---PQefGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSIL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2485612693 161 FLDEPLSGLDVlaaaELTESIKSWVKEMG--KTVIIASHRMDFVEKVTNKVLWLKEGKVILEG 221
Cdd:cd03264 153 IVDEPTAGLDP----EERIRFRNLLSELGedRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
3-234 |
2.79e-52 |
|
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: 171.36 E-value: 2.79e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYKRGNQQIkanDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKK-PEIIRGRF 81
Cdd:COG1122 1 IELENLSFSYPGGTPAL---DDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKnLRELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 82 SFLwegMQNVYHYL---TGEANILyFAYLNQ-VPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDP 157
Cdd:COG1122 78 GLV---FQNPDDQLfapTVEEDVA-FGPENLgLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2485612693 158 EVVFLDEPLSGLDVLAAAELTESIKSWVKEmGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDLknLSKEEE 234
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV--FSDYEL 227
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
3-221 |
2.72e-51 |
|
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: 168.16 E-value: 2.72e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYKrgnqQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEIIRgRFS 82
Cdd:cd03268 1 LKTNDLTKTYG----KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALR-RIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 83 FLWEGmQNVYHYLTGEANILYFAYLNQVPSSvarrRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVVFL 162
Cdd:cd03268 76 ALIEA-PGFYPNLTARENLRLLARLLGIRKK----RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2485612693 163 DEPLSGLDVLAAAELTESIKSWVKEmGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEG 221
Cdd:cd03268 151 DEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
3-217 |
6.39e-50 |
|
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: 164.97 E-value: 6.39e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYKRGNQQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEIIRGRF- 81
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 82 ----SFLWegmQNvYH---YLTGEANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLI 154
Cdd:cd03255 81 rrhiGFVF---QS-FNllpDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2485612693 155 NDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTnKVLWLKEGKV 217
Cdd:cd03255 157 NDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYAD-RIIELRDGKI 218
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
3-227 |
8.05e-50 |
|
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: 164.99 E-value: 8.05e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYKRGNQqiKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEIIRGRFS 82
Cdd:cd03263 1 LQIRNLTKTYKKGTK--PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 83 F------LWEGmqnvyhyLTGEANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLIND 156
Cdd:cd03263 79 YcpqfdaLFDE-------LTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2485612693 157 PEVVFLDEPLSGLDVLAAAELTESIKSWVKemGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDLK 227
Cdd:cd03263 152 PSVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
4-216 |
3.58e-49 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 162.64 E-value: 3.58e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 4 EVRNLTkvYKRGNQQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKP-EIIRGRFS 82
Cdd:cd03225 1 ELKNLS--FSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSlKELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 83 FLwegMQNVYHYLTG---EANILyFAYLN-QVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPE 158
Cdd:cd03225 79 LV---FQNPDDQFFGptvEEEVA-FGLENlGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2485612693 159 VVFLDEPLSGLDVLAAAELTESIKSWvKEMGKTVIIASHRMDFVEKVTNKVLWLKEGK 216
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKL-KAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-226 |
1.25e-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: 169.70 E-value: 1.25e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVYK-RGNQQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEI---- 76
Cdd:COG1123 260 LLEVRNLSKRYPvRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRslre 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 77 IRGRFSFLwegMQNVYHYLT-----GEanILYFAYLNQ--VPSSVARRRCEELLRKLDL-YEVKDQYVFTYSAGMRKKLA 148
Cdd:COG1123 340 LRRRVQMV---FQDPYSSLNprmtvGD--IIAEPLRLHglLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVA 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2485612693 149 IATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDL 226
Cdd:COG1123 415 IARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEV 492
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-228 |
1.34e-48 |
|
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: 162.90 E-value: 1.34e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 1 MLLEVRNLTKVYKrGnqqIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKP--EIIR 78
Cdd:COG0411 3 PLLEVRGLTKRFG-G---LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPphRIAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 79 ---GRfSF----LWEGM---QNV---YHYLTGEAnilYFAYLNQVPSSV-----ARRRCEELLRKLDLYEVKDQYVFTYS 140
Cdd:COG0411 79 lgiAR-TFqnprLFPELtvlENVlvaAHARLGRG---LLAALLRLPRARreereARERAEELLERVGLADRADEPAGNLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 141 AGMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILE 220
Cdd:COG0411 155 YGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAE 234
|
....*...
gi 2485612693 221 GKTEDLKN 228
Cdd:COG0411 235 GTPAEVRA 242
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-197 |
4.75e-48 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 159.95 E-value: 4.75e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 1 MLLEVRNLTKVykRGNQQIKanDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEIIRGR 80
Cdd:COG4133 1 MMLEAENLSCR--RGERLLF--SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 81 FSFLWEgmQN-VYHYLTGEANILYFAYLNQVPssVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEV 159
Cdd:COG4133 77 LAYLGH--ADgLKPELTVRENLRFWAALYGLR--ADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPL 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 2485612693 160 VFLDEPLSGLDVLAAAELTESIKSWVKEmGKTVIIASH 197
Cdd:COG4133 153 WLLDEPFTALDAAGVALLAELIAAHLAR-GGAVLLTTH 189
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
3-221 |
1.24e-47 |
|
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: 158.98 E-value: 1.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYKRgnqqIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLlkkPEIIRGRFS 82
Cdd:cd03269 1 LEVENVTKRFGR----VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL---DIAARNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 83 FLWEGmQNVYHYLTGEANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVVFL 162
Cdd:cd03269 74 YLPEE-RGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2485612693 163 DEPLSGLDVlAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEG 221
Cdd:cd03269 153 DEPFSGLDP-VNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
2-221 |
4.26e-47 |
|
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: 158.05 E-value: 4.26e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVYKRGNQQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPE----II 77
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRrlrkIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 78 RGRFSFLwegMQNVYHYLT-----GEanILYFAYLNQVPSSVA---RRRCEELLRKLDLYE-VKDQYVFTYSAGMRKKLA 148
Cdd:cd03257 81 RKEIQMV---FQDPMSSLNprmtiGE--QIAEPLRIHGKLSKKearKEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2485612693 149 IATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEG 221
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-228 |
4.58e-47 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 158.22 E-value: 4.58e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVYkrGNQQIKanDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPE----II 77
Cdd:COG1127 5 MIEVRNLTKSF--GDRVVL--DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEkelyEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 78 RGRFSF------LWEGMqNVYHyltgeaNILYfaYLNQ---VPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLA 148
Cdd:COG1127 81 RRRIGMlfqggaLFDSL-TVFE------NVAF--PLREhtdLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 149 IATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDLKN 228
Cdd:COG1127 152 LARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
3-228 |
1.13e-45 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 154.52 E-value: 1.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYKrgnqQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKP--EIIR-- 78
Cdd:cd03219 1 LEVRGLTKRFG----GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPphEIARlg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 79 -GRfSF----LWEGM---QNV---YHYLTGEAnilYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKL 147
Cdd:cd03219 77 iGR-TFqiprLFPELtvlENVmvaAQARTGSG---LLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 148 AIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSwVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDLK 227
Cdd:cd03219 153 EIARALATDPKLLLLDEPAAGLNPEETEELAELIRE-LRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVR 231
|
.
gi 2485612693 228 N 228
Cdd:cd03219 232 N 232
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-218 |
4.16e-45 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 152.89 E-value: 4.16e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVYKRGNQQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPE----II 77
Cdd:COG1136 4 LLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSErelaRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 78 RGR-FSFLWegmQNvYH---YLTGEANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCL 153
Cdd:COG1136 84 RRRhIGFVF---QF-FNllpELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2485612693 154 INDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDfVEKVTNKVLWLKEGKVI 218
Cdd:COG1136 160 VNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPE-LAARADRVIRLRDGRIV 223
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-226 |
6.72e-44 |
|
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: 156.99 E-value: 6.72e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVYKRGnqQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPD---QGDILYKGVSLLKKPEIIR 78
Cdd:COG1123 4 LLEVRDLSVRYPGG--DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 79 GRFSflweGM--QNVYHYLTGE--ANILYFAYLNQ-VPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCL 153
Cdd:COG1123 82 GRRI----GMvfQDPMTQLNPVtvGDQIAEALENLgLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2485612693 154 INDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDL 226
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
4-216 |
1.74e-43 |
|
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: 146.24 E-value: 1.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 4 EVRNLTKVYKRGnqqiKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEIIRgrfsf 83
Cdd:cd00267 1 EIENLSFRYGGR----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 84 lwegmqnvyhyltgeanilyfaylnqvpssvaRRRCeellrkldlyevkdQYVFTYSAGMRKKLAIATCLINDPEVVFLD 163
Cdd:cd00267 72 --------------------------------RRRI--------------GYVPQLSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2485612693 164 EPLSGLDVLAAAELTESIKSWVKEmGKTVIIASHRMDFVEKVTNKVLWLKEGK 216
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
3-228 |
6.23e-43 |
|
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: 147.65 E-value: 6.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKvyKRGNQQIKanDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSL--LKKPE--IIR 78
Cdd:cd03261 1 IELRGLTK--SFGGRTVL--KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsgLSEAElyRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 79 GRFSFLWegmQN--VYHYLTGEANILYFAYLN-QVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLIN 155
Cdd:cd03261 77 RRMGMLF---QSgaLFDSLTVFENVAFPLREHtRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2485612693 156 DPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDLKN 228
Cdd:cd03261 154 DPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
3-221 |
6.93e-43 |
|
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: 146.51 E-value: 6.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYkrGNQQIKanDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPeIIRGRFS 82
Cdd:cd03259 1 LELKGLSKTY--GSVRAL--DDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVP-PERRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 83 FLwegMQN--VYHYLTGEANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVV 160
Cdd:cd03259 76 MV---FQDyaLFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2485612693 161 FLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEG 221
Cdd:cd03259 153 LLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-307 |
1.66e-42 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 149.08 E-value: 1.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 4 EVRNLTKVYK-----------------RGNQQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYK 66
Cdd:COG4586 3 EVENLSKTYRvyekepglkgalkglfrREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 67 GVS-------LLKKPEIIRGRFSFLW---------EGMQNVYhyltgeanilyfaylnQVPSSVARRRCEELLRKLDLYE 130
Cdd:COG4586 83 GYVpfkrrkeFARRIGVVFGQRSQLWwdlpaidsfRLLKAIY----------------RIPDAEYKKRLDELVELLDLGE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 131 VKDQYVFTYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVL 210
Cdd:COG4586 147 LLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 211 WLKEGKVILEGKTEDLKN-LSKEEEYILYLRNSAKA--------REKLRKYELQFEILSDVTLKTTLrlgqKELFysvfs 281
Cdd:COG4586 227 VIDHGRIIYDGSLEELKErFGPYKTIVLELAEPVPPlelprggeVIEREGNRVRLEVDPRESLAEVL----ARLL----- 297
|
330 340
....*....|....*....|....*.
gi 2485612693 282 dPDFEVLNLEKKSPDFEAIFRRLYGE 307
Cdd:COG4586 298 -ARYPVRDLTIEEPPIEEVIRRIYKE 322
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
3-221 |
1.26e-41 |
|
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: 144.01 E-value: 1.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVY-----------------KRGNQQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILY 65
Cdd:cd03267 1 IEVSNLSKSYrvyskepgligslkslfKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 66 KGVSLLKKPEIIRGRFSFLWEGMQNVYHYLTGEANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRK 145
Cdd:cd03267 81 AGLVPWKRRKKFLRRIGVVFGQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2485612693 146 KLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEG 221
Cdd:cd03267 161 RAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
4-221 |
6.84e-41 |
|
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: 140.26 E-value: 6.84e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 4 EVRNLTkvYKRGNQQIKanDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEIIRGRfsf 83
Cdd:cd03214 1 EVENLS--VGYGGRTVL--DDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELAR--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 84 lwegmqnvyhyltgeanilYFAYLNQVpssvarrrceelLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVVFLD 163
Cdd:cd03214 74 -------------------KIAYVPQA------------LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2485612693 164 EPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEG 221
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
4-218 |
1.25e-40 |
|
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: 140.47 E-value: 1.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 4 EVRNLTKVYKRGNqqiKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPeiirgRFSF 83
Cdd:cd03226 1 RIENISFSYKKGT---EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE-----RRKS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 84 LWEGMQNVYHYLTGE--ANILYfayLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVVF 161
Cdd:cd03226 73 IGYVMQDVDYQLFTDsvREELL---LGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2485612693 162 LDEPLSGLDVLAAAELTESIKSwVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVI 218
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRE-LAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
2-226 |
2.69e-40 |
|
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: 140.41 E-value: 2.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVYKRGNQQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEI----I 77
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKelrkA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 78 RGR-------FSFLWEgmQNVYHyltgeaNILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIA 150
Cdd:cd03258 81 RRRigmifqhFNLLSS--RTVFE------NVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 151 TCLINDPEVVFLDEPLSGLDvlaaAELTESI----KSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDL 226
Cdd:cd03258 153 RALANNPKVLLCDEATSALD----PETTQSIlallRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
3-225 |
3.19e-39 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 138.29 E-value: 3.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYKRGNQQ------------------IKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDIl 64
Cdd:COG1134 5 IEVENVSKSYRLYHEPsrslkelllrrrrtrreeFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 65 ykgvsllkkpeIIRGRFSFLWE---GMQNvyhYLTGEANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSA 141
Cdd:COG1134 84 -----------EVNGRVSALLElgaGFHP---ELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 142 GMRKKL--AIATCLinDPEVVFLDEPLSGLDVL----AAAELTESIKSwvkemGKTVIIASHRMDFVEKVTNKVLWLKEG 215
Cdd:COG1134 150 GMRARLafAVATAV--DPDILLVDEVLAVGDAAfqkkCLARIRELRES-----GRTVIFVSHSMGAVRRLCDRAIWLEKG 222
|
250
....*....|
gi 2485612693 216 KVILEGKTED 225
Cdd:COG1134 223 RLVMDGDPEE 232
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
3-226 |
5.34e-39 |
|
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: 137.31 E-value: 5.34e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYKRGNQQIKandNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSL--LKKPEI--IR 78
Cdd:cd03256 1 IEVENLSKTYPNGKKALK---DVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInkLKGKALrqLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 79 GRFSFLWEG---------MQNVYHYLTGEANILYfAYLNQVPSSvARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAI 149
Cdd:cd03256 78 RQIGMIFQQfnlierlsvLENVLSGRLGRRSTWR-SLFGLFPKE-EKQRALAALERVGLLDKAYQRADQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2485612693 150 ATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDL 226
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
3-216 |
9.13e-39 |
|
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: 135.01 E-value: 9.13e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYKrgnqQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEIIRgrfs 82
Cdd:cd03229 1 LELKNVSKRYG----QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELP---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 83 flwegmqnvyhyltgeanilyfaylnqvpssVARRRCEELLRKLDLY---EVKDQYVFTYSAGMRKKLAIATCLINDPEV 159
Cdd:cd03229 73 -------------------------------PLRRRIGMVFQDFALFphlTVLENIALGLSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2485612693 160 VFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGK 216
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-231 |
1.32e-38 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 136.37 E-value: 1.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 1 MLLEVRNLTkvYKRGNQQIKanDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEIIrG- 79
Cdd:COG1121 5 PAIELENLT--VSYGGRPVL--EDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRI-Gy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 80 ---RFSFLWE----GMQNVYHYLTGEANILYFaylnqvPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATC 152
Cdd:COG1121 80 vpqRAEVDWDfpitVRDVVLMGRYGRRGLFRR------PSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 153 LINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEmGKTVIIASHRMDFVEKVTNKVLWLKEGkVILEGKTEDL---KNL 229
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVltpENL 231
|
..
gi 2485612693 230 SK 231
Cdd:COG1121 232 SR 233
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
3-228 |
1.35e-36 |
|
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: 130.74 E-value: 1.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYKRGnqqiKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEIIRGRFs 82
Cdd:cd03218 1 LRAENLSKRYGKR----KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARL- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 83 flweGM------QNVYHYLTGEANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLIND 156
Cdd:cd03218 76 ----GIgylpqeASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATN 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2485612693 157 PEVVFLDEPLSGLDVLAAAELTESIKSwVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDLKN 228
Cdd:cd03218 152 PKFLLLDEPFAGVDPIAVQDIQKIIKI-LKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
4-221 |
2.22e-36 |
|
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: 129.58 E-value: 2.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 4 EVRNLTkvYKRGNQQIKanDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEIIrG---- 79
Cdd:cd03235 1 EVEDLT--VSYGGHPVL--EDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRI-Gyvpq 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 80 RFSFLWEGMQNVYHY-LTGeanILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPE 158
Cdd:cd03235 76 RRSIDRDFPISVRDVvLMG---LYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2485612693 159 VVFLDEPLSGLDVLAAAELTESIKSWvKEMGKTVIIASHRMDFVEKVTNKVLWLKeGKVILEG 221
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLREL-RREGMTILVVTHDLGLVLEYFDRVLLLN-RTVVASG 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
2-226 |
2.41e-36 |
|
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: 130.93 E-value: 2.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTkvYKRGNQQIkaNDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSL--LKKPEIIRg 79
Cdd:COG1120 1 MLEAENLS--VGYGGRPV--LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLasLSRRELAR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 80 RFSFLWEGMQNVYHyLTGEANILY--FAYLN--QVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLIN 155
Cdd:COG1120 76 RIAYVPQEPPAPFG-LTVRELVALgrYPHLGlfGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2485612693 156 DPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDL 226
Cdd:COG1120 155 EPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-197 |
4.65e-36 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 130.21 E-value: 4.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 1 MLLEVRNLTKVYKRGNQQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKK-PEIirg 79
Cdd:COG1116 6 PALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPgPDR--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 80 rfsflweGM--QN--VYHYLTGEANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLIN 155
Cdd:COG1116 83 -------GVvfQEpaLLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2485612693 156 DPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASH 197
Cdd:COG1116 156 DPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTH 197
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-226 |
6.09e-36 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 129.38 E-value: 6.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 1 MLLEVRNLTKVYKRgnqqIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEIIRGR 80
Cdd:COG1137 2 MTLEAENLVKSYGK----RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 81 FsflweGM----QN--VYHYLTGEANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLI 154
Cdd:COG1137 78 L-----GIgylpQEasIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2485612693 155 NDPEVVFLDEPLSGLDVLAAAELTESIKSwVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDL 226
Cdd:COG1137 153 TNPKFILLDEPFAGVDPIAVADIQKIIRH-LKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEI 223
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
3-200 |
7.92e-36 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 128.36 E-value: 7.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYKRGNQQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLlKKPEIIRG--- 79
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV-TGPGPDRGyvf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 80 -RFSFL-WegmqnvyhyLTGEANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDP 157
Cdd:cd03293 80 qQDALLpW---------LTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDP 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2485612693 158 EVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMD 200
Cdd:cd03293 151 DVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDID 193
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-226 |
4.54e-35 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 129.81 E-value: 4.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYKRGNQQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSL--LKKPEIIRGR 80
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLtaLSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 81 ---------FSFLWEgmQNVYhyltgeANIlyfAY---LNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLA 148
Cdd:COG1135 82 rkigmifqhFNLLSS--RTVA------ENV---ALpleIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 149 IATCLINDPEVVFLDEPLSGLDvlaaAELTESI----KSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTE 224
Cdd:COG1135 151 IARALANNPKVLLCDEATSALD----PETTRSIldllKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVL 226
|
..
gi 2485612693 225 DL 226
Cdd:COG1135 227 DV 228
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
2-226 |
2.89e-34 |
|
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: 127.09 E-value: 2.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVYKRGNQQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIP---DQGDILYKGVSLLKKPE--- 75
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEkel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 76 -IIRGR-----FsflwegmQNVYHYLT---------GEAnilyFAYLNQVPSSVARRRCEELLRKLDL---YEVKDQYVF 137
Cdd:COG0444 81 rKIRGReiqmiF-------QDPMTSLNpvmtvgdqiAEP----LRIHGGLSKAEARERAIELLERVGLpdpERRLDRYPH 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 138 TYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKV 217
Cdd:COG0444 150 ELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRI 229
|
....*....
gi 2485612693 218 ILEGKTEDL 226
Cdd:COG0444 230 VEEGPVEEL 238
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
3-234 |
8.53e-34 |
|
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: 123.60 E-value: 8.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYKrgNQQIKandNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEIIRGrFS 82
Cdd:cd03299 1 LKVENLSKDWK--EFKLK---NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRD-IS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 83 FLWegmQN--VYHYLTGEANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVV 160
Cdd:cd03299 75 YVP---QNyaLFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKIL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2485612693 161 FLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHrmDFVEKVT--NKVLWLKEGKVILEGKTEDLKNLSKEEE 234
Cdd:cd03299 152 LLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTH--DFEEAWAlaDKVAIMLNGKLIQVGKPEEVFKKPKNEF 225
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
3-228 |
1.33e-33 |
|
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: 122.54 E-value: 1.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYKRgnqqIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKP--EIIRGR 80
Cdd:cd03224 1 LEVENLNAGYGK----SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPphERARAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 81 FSFLWEGmQNVYHYLTGEANILYFAYLNqvPSSVARRRCEELLRKL-DLYEVKDQYVFTYSAGMRKKLAIATCLINDPEV 159
Cdd:cd03224 77 IGYVPEG-RRIFPELTVEENLLLGAYAR--RRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2485612693 160 VFLDEPLSGLDVLAAAELTESIKsWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDLKN 228
Cdd:cd03224 154 LLLDEPSEGLAPKIVEEIFEAIR-ELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-226 |
6.16e-33 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 123.38 E-value: 6.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYkrGNQQIKanDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEIIRGRFS 82
Cdd:PRK13537 8 IDFRNVEKRY--GDKLVV--DGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 83 FLWEgMQNVYHYLTGEANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVVFL 162
Cdd:PRK13537 84 VVPQ-FDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2485612693 163 DEPLSGLDVLAAAELTESIKSWVKEmGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDL 226
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
3-221 |
9.34e-33 |
|
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: 120.72 E-value: 9.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYKRGNQQ------------------IKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDIl 64
Cdd:cd03220 1 IELENVSKSYPTYKGGssslkklgilgrkgevgeFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 65 ykgvsllkkpeIIRGRFSFLWE---GMQNVyhyLTGEANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSA 141
Cdd:cd03220 80 -----------TVRGRVSSLLGlggGFNPE---LTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 142 GMRKKL--AIATCLinDPEVVFLDEPLSGLDVLAAAELTESIKSWvKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVIL 219
Cdd:cd03220 146 GMKARLafAIATAL--EPDILLIDEVLAVGDAAFQEKCQRRLREL-LKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRF 222
|
..
gi 2485612693 220 EG 221
Cdd:cd03220 223 DG 224
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
23-167 |
9.85e-33 |
|
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: 118.13 E-value: 9.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 23 DNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKP-EIIRGRFSFLWEGMQNVYHyLTGEANI 101
Cdd:pfam00005 2 KNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDErKSLRKEIGYVFQDPQLFPR-LTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 102 LYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQ----YVFTYSAGMRKKLAIATCLINDPEVVFLDEPLS 167
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
3-226 |
3.22e-32 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 119.71 E-value: 3.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYKRGNqqiKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEI-IRGRF 81
Cdd:cd03295 1 IEFENVTKRYGGGK---KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVeLRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 82 SFLwegMQNV--YHYLTGEANILYFAYLNQVPSSVARRRCEELLRKLDL--YEVKDQYVFTYSAGMRKKLAIATCLINDP 157
Cdd:cd03295 78 GYV---IQQIglFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2485612693 158 EVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDL 226
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-231 |
4.30e-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: 119.42 E-value: 4.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 1 MLLEVRNLTkvYKRGNQQIKanDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDilykGVSLLKKPeiiRGR 80
Cdd:COG1119 2 PLLELRNVT--VRRGGKTIL--DDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGN----DVRLFGER---RGG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 81 FSfLWE-----G------MQNVYHYLTGEANIL--YFAY--LNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRK 145
Cdd:COG1119 71 ED-VWElrkriGlvspalQLRFPRDETVLDVVLsgFFDSigLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 146 KLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTED 225
Cdd:COG1119 150 RVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEE 229
|
....*....
gi 2485612693 226 L---KNLSK 231
Cdd:COG1119 230 VltsENLSE 238
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
3-217 |
6.53e-32 |
|
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: 118.02 E-value: 6.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYkrGNQQIKanDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLK-KPEI--IRG 79
Cdd:cd03262 1 IEIKNLHKSF--GDFHVL--KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdKKNIneLRQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 80 RFsflweGM--Q--NVYHYLTGEANI-LYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLI 154
Cdd:cd03262 77 KV-----GMvfQqfNLFPHLTVLENItLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2485612693 155 NDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEmGKTVIIASHRMDFVEKVTNKVLWLKEGKV 217
Cdd:cd03262 152 MNPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-228 |
9.63e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 119.46 E-value: 9.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYKRGNqqiKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEI-IRGRF 81
Cdd:PRK13647 5 IEVEDLHFRYKDGT---KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 82 SFLWEGMQNVYHYLTGEANILyFAYLNQ-VPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVV 160
Cdd:PRK13647 82 GLVFQDPDDQVFSSTVWDDVA-FGPVNMgLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2485612693 161 FLDEPLSGLDVLAAAELTEsIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDLKN 228
Cdd:PRK13647 161 VLDEPMAYLDPRGQETLME-ILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTD 227
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-218 |
1.71e-31 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 117.08 E-value: 1.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYKRGNqqiKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSL--LKKPEIIRGR 80
Cdd:COG2884 2 IRFENVSKRYPGGR---EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLsrLKRREIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 81 FSFlweGM----------QNVYhyltgeANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIA 150
Cdd:COG2884 79 RRI---GVvfqdfrllpdRTVY------ENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2485612693 151 TCLINDPEVVFLDEPLSGLDVLAAAELTESIKSwVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVI 218
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETSWEIMELLEE-INRRGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
3-228 |
2.26e-31 |
|
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: 117.38 E-value: 2.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYKRGnqqiKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEIIRGR-- 80
Cdd:TIGR04406 2 LVAENLIKSYKKR----KVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARlg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 81 FSFLWEGmQNVYHYLTGEANILyfAYLN---QVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDP 157
Cdd:TIGR04406 78 IGYLPQE-ASIFRKLTVEENIM--AVLEirkDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2485612693 158 EVVFLDEPLSGLDVLAAAELTESIKSwVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDLKN 228
Cdd:TIGR04406 155 KFILLDEPFAGVDPIAVGDIKKIIKH-LKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVA 224
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
3-221 |
1.12e-30 |
|
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: 114.99 E-value: 1.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYKrgNQQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLK-KPEIIRGRF 81
Cdd:cd03245 3 IEFRNVSFSYP--NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQlDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 82 SFLwegMQNVY-HYLTGEANILYFAylnqvPSSVArrrcEELLRKLDLYEVkDQYV---------------FTYSAGMRK 145
Cdd:cd03245 81 GYV---PQDVTlFYGTLRDNITLGA-----PLADD----ERILRAAELAGV-TDFVnkhpngldlqigergRGLSGGQRQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2485612693 146 KLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKemGKTVIIASHRMDFVEKVtNKVLWLKEGKVILEG 221
Cdd:cd03245 148 AVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLLDLV-DRIIVMDSGRIVADG 220
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-233 |
2.96e-30 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 119.36 E-value: 2.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 1 MLLEVRNLTKVYkrGNqqIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSL-LKKPE---- 75
Cdd:COG3845 4 PALELRGITKRF--GG--VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVrIRSPRdaia 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 76 --IirgrfsflweGMqnVY-HY-----LTGEANILyfayLNQVPS-------SVARRRCEELLRKLDLyEVK-DQYVFTY 139
Cdd:COG3845 80 lgI----------GM--VHqHFmlvpnLTVAENIV----LGLEPTkggrldrKAARARIRELSERYGL-DVDpDAKVEDL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 140 SAGMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSwVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVIL 219
Cdd:COG3845 143 SVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRR-LAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVG 221
|
250
....*....|....
gi 2485612693 220 EGKTEDlknLSKEE 233
Cdd:COG3845 222 TVDTAE---TSEEE 232
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-220 |
4.13e-30 |
|
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: 111.75 E-value: 4.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYkrGNqqIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILykgvsllkkpeiIRGR-F 81
Cdd:cd03216 1 LELRGITKRF--GG--VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEIL------------VDGKeV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 82 SFLwegmqNVYHyltgeanilyfaylnqvpssvARRRceellrkldlyevKDQYVFTYSAGMRKKLAIATCLINDPEVVF 161
Cdd:cd03216 65 SFA-----SPRD---------------------ARRA-------------GIAMVYQLSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2485612693 162 LDEPLSGLDVLAAAELTESIKSwVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILE 220
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRR-LRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-228 |
4.50e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 114.06 E-value: 4.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 1 MLLEVRNLTKVYKrGnqqIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPE--IIR 78
Cdd:COG4674 9 PILYVEDLTVSFD-G---FKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEheIAR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 79 ---GR-FsflwegmQN--VYHYLTGEANIL--------YFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMR 144
Cdd:COG4674 85 lgiGRkF-------QKptVFEELTVFENLElalkgdrgVFASLFARLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 145 KKLAIATCLINDPEVVFLDEPLSGLDV---LAAAELTESIKSwvkemGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEG 221
Cdd:COG4674 158 QWLEIGMLLAQDPKLLLLDEPVAGMTDaetERTAELLKSLAG-----KHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEG 232
|
....*..
gi 2485612693 222 KTEDLKN 228
Cdd:COG4674 233 SLDEVQA 239
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2-221 |
5.22e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 114.94 E-value: 5.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVYKRGNQQIKandNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGvsllkKPeiIRGRF 81
Cdd:PRK13636 5 ILKVEELNYNYSDGTHALK---GININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDG-----KP--IDYSR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 82 SFLWEGMQNVYHYLTGEANILY---------FAYLN-QVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIAT 151
Cdd:PRK13636 75 KGLMKLRESVGMVFQDPDNQLFsasvyqdvsFGAVNlKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 152 CLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEG 221
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQG 224
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
3-216 |
6.35e-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: 111.71 E-value: 6.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYKRGNQQIKanDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLK-KPEIIRGRF 81
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVL--KDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 82 S------FLWEGmqnvyhylTGEANILyfaylnqvpssvarrrceellrkldlyevkdqyvftySAGMRKKLAIATCLIN 155
Cdd:cd03228 79 AyvpqdpFLFSG--------TIRENIL-------------------------------------SGGQRQRIAIARALLR 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2485612693 156 DPEVVFLDEPLSGLDVLAAAELTESIKSWVKemGKTVIIASHRMDFVEKVtNKVLWLKEGK 216
Cdd:cd03228 114 DPPILILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIRDA-DRIIVLDDGR 171
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-235 |
1.03e-29 |
|
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: 118.78 E-value: 1.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTkvYKRGNQQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLK-KPEIIRGRF 81
Cdd:COG2274 474 IELENVS--FRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQiDPASLRRQI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 82 SFLwegMQNVYhyL---TGEANILYFAYlnQVPSSVARRRCE-----ELLRKLDL-YE--VKDQYVfTYSAGMRKKLAIA 150
Cdd:COG2274 552 GVV---LQDVF--LfsgTIRENITLGDP--DATDEEIIEAARlaglhDFIEALPMgYDtvVGEGGS-NLSGGQRQRLAIA 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 151 TCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKemGKTVIIASHRMDFVEKVtNKVLWLKEGKVILEGKTEDLknLS 230
Cdd:COG2274 624 RALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRLA-DRIIVLDKGRIVEDGTHEEL--LA 698
|
....*
gi 2485612693 231 KEEEY 235
Cdd:COG2274 699 RKGLY 703
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
2-197 |
1.30e-29 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 115.20 E-value: 1.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVYkrGNQQikANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKP----EIi 77
Cdd:COG3842 5 ALELENVSKRY--GDVT--ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPpekrNV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 78 rgrfsflweGM--QNvY----HyLTGEANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIAT 151
Cdd:COG3842 80 ---------GMvfQD-YalfpH-LTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALAR 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2485612693 152 CLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASH 197
Cdd:COG3842 149 ALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTH 194
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-225 |
1.44e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 114.41 E-value: 1.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 1 MLLEVRNLTKVYKRGNQ-QIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDI--LYKGVSLLKKPEI- 76
Cdd:PRK13651 1 MQIKVKNIVKIFNKKLPtELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewIFKDEKNKKKTKEk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 77 ----------------------IRGR----FSF----LWEGmqnvyhylTGEANILYFAYLNQVPSSVARRRCEELLRKL 126
Cdd:PRK13651 81 ekvleklviqktrfkkikkikeIRRRvgvvFQFaeyqLFEQ--------TIEKDIIFGPVSMGVSKEEAKKRAAKYIELV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 127 DLYEvkdQYV----FTYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSwVKEMGKTVIIASHRMDFV 202
Cdd:PRK13651 153 GLDE---SYLqrspFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDN-LNKQGKTIILVTHDLDNV 228
|
250 260
....*....|....*....|...
gi 2485612693 203 EKVTNKVLWLKEGKVILEGKTED 225
Cdd:PRK13651 229 LEWTKRTIFFKDGKIIKDGDTYD 251
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
3-226 |
2.37e-29 |
|
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: 111.89 E-value: 2.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYKrgnqQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLL-----IPDQGDILYKGVSLLKK---P 74
Cdd:cd03260 1 IELRDLNVYYG----DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLdvdV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 75 EIIRGRFsflweGM--Q--NVYHyLTGEANILYFAYLNQV-PSSVARRRCEELLRKLDLY-EVKDQYVFTY-SAGMRKKL 147
Cdd:cd03260 77 LELRRRV-----GMvfQkpNPFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWdEVKDRLHALGlSGGQQQRL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2485612693 148 AIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMgkTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDL 226
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-234 |
7.22e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 112.06 E-value: 7.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 1 MLLEVRNLTKVYKRGNQ-QIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKpeiiRG 79
Cdd:PRK13637 1 MSIKIENLTHIYMEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDK----KV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 80 RFSFLWEGMQNVYHYL-------TGEANILY-FAYLNQVPSSVARRRCEEL-LRKLDLYEVKDQYVFTYSAGMRKKLAIA 150
Cdd:PRK13637 77 KLSDIRKKVGLVFQYPeyqlfeeTIEKDIAFgPINLGLSEEEIENRVKRAMnIVGLDYEDYKDKSPFELSGGQKRRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 151 TCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDL-KNL 229
Cdd:PRK13637 157 GVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVfKEV 236
|
....*
gi 2485612693 230 SKEEE 234
Cdd:PRK13637 237 ETLES 241
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
2-226 |
1.15e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 111.05 E-value: 1.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVYKrgnQQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKP-EIIRGR 80
Cdd:PRK13652 3 LIETRDLCYSYS---GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENiREVRKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 81 FSFLWEGMQNVYHYLTGEANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVV 160
Cdd:PRK13652 80 VGLVFQNPDDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2485612693 161 FLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDL 226
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
3-217 |
1.57e-28 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 109.27 E-value: 1.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYkrGNQqiKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEIIRGRfs 82
Cdd:cd03301 1 VELENVTKRF--GNV--TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDI-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 83 flweGM--QN--VYHYLTGEANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPE 158
Cdd:cd03301 75 ----AMvfQNyaLYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2485612693 159 VVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHrmDFVEKVT--NKVLWLKEGKV 217
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTH--DQVEAMTmaDRIAVMNDGQI 209
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-226 |
1.79e-28 |
|
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: 114.51 E-value: 1.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVY---KRGnqQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYK----GVSLLKKP 74
Cdd:TIGR03269 279 IIKVRNVSKRYisvDRG--VVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgdeWVDMTKPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 75 EIIRGR----FSFLWEGMqNVYHYLTGEANiLYFAYLNQVPSSVARRRCEELLRKLDLYEVK-----DQYVFTYSAGMRK 145
Cdd:TIGR03269 357 PDGRGRakryIGILHQEY-DLYPHRTVLDN-LTEAIGLELPDELARMKAVITLKMVGFDEEKaeeilDKYPDELSEGERH 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 146 KLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTED 225
Cdd:TIGR03269 435 RVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEE 514
|
.
gi 2485612693 226 L 226
Cdd:TIGR03269 515 I 515
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
3-228 |
2.01e-28 |
|
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: 109.25 E-value: 2.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYkrGNQQikANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEIIRGrfs 82
Cdd:cd03300 1 IELENVSKFY--GGFV--ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRP--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 83 flwegMQNVY-HY-----LTGEANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLIND 156
Cdd:cd03300 74 -----VNTVFqNYalfphLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNE 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2485612693 157 PEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDLKN 228
Cdd:cd03300 149 PKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYE 220
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-228 |
3.15e-28 |
|
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: 108.92 E-value: 3.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 1 MLLEVRNLTKVYKrgnqQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKP--EIIR 78
Cdd:COG0410 2 PMLEVENLHAGYG----GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPphRIAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 79 GRFSFLWEGmQNVYHYLTGEANILYFAYLNQVPSSVARRRcEELLRKL-DLYEVKDQYVFTYSAGMRKKLAIATCLINDP 157
Cdd:COG0410 78 LGIGYVPEG-RRIFPSLTVEENLLLGAYARRDRAEVRADL-ERVYELFpRLKERRRQRAGTLSGGEQQMLAIGRALMSRP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2485612693 158 EVVFLDEPLSGLDVLAAAELTESIKSwVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDLKN 228
Cdd:COG0410 156 KLLLLDEPSLGLAPLIVEEIFEIIRR-LNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
3-217 |
5.01e-28 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 107.88 E-value: 5.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYKRGnqqIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSL--LKKPEI--IR 78
Cdd:cd03292 1 IEFINVTKTYPNG---TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdLRGRAIpyLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 79 GRFSFLWEGMQNVYHyLTGEANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPE 158
Cdd:cd03292 78 RKIGVVFQDFRLLPD-RNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2485612693 159 VVFLDEPLSGLDVLAAAELTESIKSwVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKV 217
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKK-INKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-226 |
6.45e-28 |
|
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: 113.32 E-value: 6.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTkvYKRGNQQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPE-IIRGRF 81
Cdd:COG4987 334 LELEDVS--FRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEdDLRRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 82 SFLwegMQNVYhyL---TGEANILyfaylnqvpssVARRRC--EEL---LRKLDLYEVKDQYVFTY-----------SAG 142
Cdd:COG4987 412 AVV---PQRPH--LfdtTLRENLR-----------LARPDAtdEELwaaLERVGLGDWLAALPDGLdtwlgeggrrlSGG 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 143 MRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKemGKTVIIASHRMDFVEKVtNKVLWLKEGKVILEGK 222
Cdd:COG4987 476 ERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLERM-DRILVLEDGRIVEQGT 552
|
....
gi 2485612693 223 TEDL 226
Cdd:COG4987 553 HEEL 556
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-306 |
7.58e-28 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 110.31 E-value: 7.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 1 MLLEVRNLTKVYkrGNQQIKanDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEIIRGR 80
Cdd:PRK13536 40 VAIDLAGVSKSY--GDKAVV--NGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARAR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 81 FSFLWEgMQNVYHYLTGEANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVV 160
Cdd:PRK13536 116 IGVVPQ-FDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 161 FLDEPLSGLDVLAAAELTESIKSWVKEmGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDLKnlskeEEYI---- 236
Cdd:PRK13536 195 ILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALI-----DEHIgcqv 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 237 --LYLRNSAKAREKLRKYELQFEIlsdvtlkttlrlgQKELFYSVFSDPDfEV---------LNLEKKSPDFEAIFRRLY 305
Cdd:PRK13536 269 ieIYGGDPHELSSLVKPYARRIEV-------------SGETLFCYAPDPE-QVrvqlrgragLRLLQRPPNLEDVFLRLT 334
|
.
gi 2485612693 306 G 306
Cdd:PRK13536 335 G 335
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
2-223 |
7.89e-28 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 108.47 E-value: 7.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVYKRGnqqiKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKG-----VSLLKKPE- 75
Cdd:PRK11701 6 LLSVRGLTKLYGPR----KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALSEa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 76 ----IIRGRFSFLWEG------MQ-----NV---------YHYltgeANILYFA--YLNQVpsSVARRRCEELLRkldly 129
Cdd:PRK11701 82 errrLLRTEWGFVHQHprdglrMQvsaggNIgerlmavgaRHY----GDIRATAgdWLERV--EIDAARIDDLPT----- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 130 evkdqyvfTYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKV 209
Cdd:PRK11701 151 --------TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRL 222
|
250
....*....|....
gi 2485612693 210 LWLKEGKVILEGKT 223
Cdd:PRK11701 223 LVMKQGRVVESGLT 236
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
3-239 |
1.33e-27 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 107.15 E-value: 1.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYkrgNQQIKandNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEIIRGrFS 82
Cdd:COG3840 2 LRLDDLTYRY---GDFPL---RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERP-VS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 83 FLWegmQ--NVYHYLTGEANIlyfaYLNQVP----SSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLIND 156
Cdd:COG3840 75 MLF---QenNLFPHLTVAQNI----GLGLRPglklTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 157 PEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDLKNLSKEEEYI 236
Cdd:COG3840 148 RPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALA 227
|
...
gi 2485612693 237 LYL 239
Cdd:COG3840 228 AYL 230
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-226 |
5.37e-27 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 108.31 E-value: 5.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 1 MLLEVRNLTKVYKrgnqQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKG-VSLLKKPeiIRG 79
Cdd:COG1118 1 MSIEVRNISKRFG----SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGrDLFTNLP--PRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 80 R---FSFlwegmQnvyHY-----LTGEANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIAT 151
Cdd:COG1118 75 RrvgFVF-----Q---HYalfphMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALAR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2485612693 152 CLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDL 226
Cdd:COG1118 147 ALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-226 |
6.54e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 109.72 E-value: 6.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 1 MLLEVRNLTKVYkrGNqqIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGvsllkKPEIIRGR 80
Cdd:COG1129 3 PLLEMRGISKSF--GG--VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDG-----EPVRFRSP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 81 FSFLWEGMQNVYH------YLTGEANIlyfaYLNQVPSS-------VARRRCEELLRKLDLyEVK-DQYVFTYSAGMRKK 146
Cdd:COG1129 74 RDAQAAGIAIIHQelnlvpNLSVAENI----FLGREPRRgglidwrAMRRRARELLARLGL-DIDpDTPVGDLSVAQQQL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 147 LAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSwVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDL 226
Cdd:COG1129 149 VEIARALSRDARVLILDEPTASLTEREVERLFRIIRR-LKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
2-226 |
7.91e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 106.32 E-value: 7.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVYKRGNQQIKandNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGV-------SLLKkp 74
Cdd:PRK13639 1 ILETRDLKYSYPDGTEALK---GINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpikydkkSLLE-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 75 eiIRGRFSFLWEGMQNVYHYLTGEANILyFAYLN-QVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCL 153
Cdd:PRK13639 76 --VRKTVGIVFQNPDDQLFAPTVEEDVA-FGPLNlGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGIL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2485612693 154 INDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEmGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDL 226
Cdd:PRK13639 153 AMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
3-226 |
1.82e-26 |
|
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: 105.03 E-value: 1.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVY-KRGNQQIK-------------------ANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGD 62
Cdd:cd03294 1 IKIKGLYKIFgKNPQKAFKllakgkskeeilkktgqtvGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 63 ILYKGVSLLKKP-----EIIRGRFSFLWEGMQNVYHyLTGEANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVF 137
Cdd:cd03294 81 VLIDGQDIAAMSrkelrELRRKKISMVFQSFALLPH-RTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 138 TYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKV 217
Cdd:cd03294 160 ELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
....*....
gi 2485612693 218 ILEGKTEDL 226
Cdd:cd03294 240 VQVGTPEEI 248
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
3-240 |
4.18e-26 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 103.68 E-value: 4.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYKrGNQQIKAndnISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDI------LYKGVSLLKKPEI 76
Cdd:PRK11264 4 IEVKNLVKKFH-GQTVLHG---IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgditIDTARSLSQQKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 77 IRG---RFSFLWEGMqNVYHYLTGEANILYF-AYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATC 152
Cdd:PRK11264 80 IRQlrqHVGFVFQNF-NLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 153 LINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMgKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDLKNLSKE 232
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQ 237
|
....*...
gi 2485612693 233 EEYILYLR 240
Cdd:PRK11264 238 PRTRQFLE 245
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
3-221 |
6.14e-26 |
|
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: 101.24 E-value: 6.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYKRGNQQIKanDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEIIRGRFS 82
Cdd:cd03247 1 LSINNVSFSYPEQEQQVL--KNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 83 FLwegMQNVYHYLTgeanilyfaylnQVPSSVARRrceellrkldlyevkdqyvftYSAGMRKKLAIATCLINDPEVVFL 162
Cdd:cd03247 79 VL---NQRPYLFDT------------TLRNNLGRR---------------------FSGGERQRLALARILLQDAPIVLL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2485612693 163 DEPLSGLDVLAAAELTESIKSWVKEmgKTVIIASHRMDFVEKVtNKVLWLKEGKVILEG 221
Cdd:cd03247 123 DEPTVGLDPITERQLLSLIFEVLKD--KTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
24-218 |
7.26e-26 |
|
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: 101.99 E-value: 7.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 24 NISFFVErGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEII-----RGRFSFLWEGMQNVYHyLTGE 98
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKInlppqQRKIGLVFQQYALFPH-LNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 99 ANILYfaYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELT 178
Cdd:cd03297 94 ENLAF--GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2485612693 179 ESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVI 218
Cdd:cd03297 172 PELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
2-221 |
1.17e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 103.24 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVYKRGNQQIK--ANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEI--I 77
Cdd:PRK13633 4 MIKCKNVSYKYESNEESTEklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwdI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 78 RGRFSFLWEGMQNVYHYLTGEANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDP 157
Cdd:PRK13633 84 RNKAGMVFQNPDNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2485612693 158 EVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKvTNKVLWLKEGKVILEG 221
Cdd:PRK13633 164 ECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEG 226
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
20-200 |
1.17e-25 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 100.96 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 20 KANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSL-LKKPEIIRGRfsflwegmQNVYHYLTGE 98
Cdd:TIGR01166 6 EVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLdYSRKGLLERR--------QRVGLVFQDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 99 ANILYFAYLNQ----------VPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVVFLDEPLSG 168
Cdd:TIGR01166 78 DDQLFAADVDQdvafgplnlgLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAG 157
|
170 180 190
....*....|....*....|....*....|..
gi 2485612693 169 LDVLAAAELTESIKSwVKEMGKTVIIASHRMD 200
Cdd:TIGR01166 158 LDPAGREQMLAILRR-LRAEGMTVVISTHDVD 188
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-226 |
1.42e-25 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 102.08 E-value: 1.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 4 EVRNLTKVYkrGNQQIKanDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGvsllkkpeiirgrfsf 83
Cdd:COG4604 3 EIKNVSKRY--GGKVVL--DDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDG---------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 84 lwegmQNVYHYLTGE-ANILyfAYLNQVPSSVARRRCEEL------------------------LRKLDLYEVKDQYVFT 138
Cdd:COG4604 63 -----LDVATTPSRElAKRL--AILRQENHINSRLTVRELvafgrfpyskgrltaedreiideaIAYLDLEDLADRYLDE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 139 YSAGMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVI 218
Cdd:COG4604 136 LSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVV 215
|
....*...
gi 2485612693 219 LEGKTEDL 226
Cdd:COG4604 216 AQGTPEEI 223
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
24-221 |
1.67e-25 |
|
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: 101.58 E-value: 1.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 24 NISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPD---QGDILYKGVSLlkKPEIIRGRFSFLWEGMQNVyHYLTGEAN 100
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPR--KPDQFQKCVAYVRQDDILL-PGLTVRET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 101 ILYFAYL-NQVPSSVARRRCE---ELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAE 176
Cdd:cd03234 102 LTYTAILrLPRKSSDAIRKKRvedVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALN 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2485612693 177 LTESIKSWVKEmGKTVIIASH--RMDfVEKVTNKVLWLKEGKVILEG 221
Cdd:cd03234 182 LVSTLSQLARR-NRIVILTIHqpRSD-LFRLFDRILLLSSGEIVYSG 226
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
3-226 |
1.97e-25 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 104.00 E-value: 1.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYkrGNQQikANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKG--VSLL--KKPEIir 78
Cdd:COG3839 4 LELENVSKSY--GGVE--ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGrdVTDLppKDRNI-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 79 grfsflweGM--QN--VYHYLTGEANIlyfAY---LNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIAT 151
Cdd:COG3839 78 --------AMvfQSyaLYPHMTVYENI---AFplkLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2485612693 152 CLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHrmDFVEKVT--NKVLWLKEGKVILEGKTEDL 226
Cdd:COG3839 147 ALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTH--DQVEAMTlaDRIAVMNDGRIQQVGTPEEL 221
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-226 |
2.66e-25 |
|
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: 101.26 E-value: 2.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 1 MLLEVRNLTKVYKRgnqqIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPeiIRGR 80
Cdd:cd03296 1 MSIEVRNVSKRFGD----FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP--VQER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 81 ---FSFlwegmQN--VYHYLTGEANI---LYFAYLNQVPSSVA-RRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIAT 151
Cdd:cd03296 75 nvgFVF-----QHyaLFRHMTVFDNVafgLRVKPRSERPPEAEiRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2485612693 152 CLINDPEVVFLDEPLSGLDvlaaAELTESIKSWVK----EMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDL 226
Cdd:cd03296 150 ALAVEPKVLLLDEPFGALD----AKVRKELRRWLRrlhdELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
3-221 |
3.89e-25 |
|
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: 99.55 E-value: 3.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYKRGNQQIKAN--DNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIP--DQGDILYKGVSLlkKPEIIR 78
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSGKQllKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPL--DKRSFR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 79 GRFSFLwegMQN--VYHYLTGEANILYFAylnqvpssvarrrceeLLRKLdlyevkdqyvftySAGMRKKLAIATCLIND 156
Cdd:cd03213 82 KIIGYV---PQDdiLHPTLTVRETLMFAA----------------KLRGL-------------SGGERKRVSIALELVSN 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2485612693 157 PEVVFLDEPLSGLDVLAAAELTESIKSWVKeMGKTVIIASHR-MDFVEKVTNKVLWLKEGKVILEG 221
Cdd:cd03213 130 PSLLFLDEPTSGLDSSSALQVMSLLRRLAD-TGRTIICSIHQpSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-228 |
3.96e-25 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 100.86 E-value: 3.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 1 MLLEVRNLTKVYkrGNQQikANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQG--DILYKGVSLLKKPEIIR 78
Cdd:PRK11124 1 MSIQLNGINCFY--GAHQ--ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGtlNIAGNHFDFSKTPSDKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 79 GRfsflwEGMQNV------YH---YLTGEANilyfayLNQVPSSV-------ARRRCEELLRKLDLYEVKDQYVFTYSAG 142
Cdd:PRK11124 77 IR-----ELRRNVgmvfqqYNlwpHLTVQQN------LIEAPCRVlglskdqALARAEKLLERLRLKPYADRFPLHLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 143 MRKKLAIATCLINDPEVVFLDEPLSGLDvlaaAELTESIKSWVKEM---GKTVIIASHRMDFVEKVTNKVLWLKEGKVIL 219
Cdd:PRK11124 146 QQQRVAIARALMMEPQVLLFDEPTAALD----PEITAQIVSIIRELaetGITQVIVTHEVEVARKTASRVVYMENGHIVE 221
|
250
....*....|....*..
gi 2485612693 220 EG--------KTEDLKN 228
Cdd:PRK11124 222 QGdascftqpQTEAFKN 238
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
2-221 |
5.99e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 102.24 E-value: 5.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVY-KRGNQQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEIIRGR 80
Cdd:PRK13631 21 ILRVKNLYCVFdEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 81 FSFLWEGMQN----------VYHYL-------TGEANILYFAYLNQVPSSVARRRCEELLRKLDL-YEVKDQYVFTYSAG 142
Cdd:PRK13631 101 TNPYSKKIKNfkelrrrvsmVFQFPeyqlfkdTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGG 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2485612693 143 MRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSwVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEG 221
Cdd:PRK13631 181 QKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTG 258
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-225 |
6.07e-25 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 102.57 E-value: 6.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 4 EVRNLTKVYKRGNQQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSL--LKKPEIIRGRF 81
Cdd:PRK11153 3 ELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtaLSEKELRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 82 SFlweGM----------QNVYhyltgeANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIAT 151
Cdd:PRK11153 83 QI---GMifqhfnllssRTVF------DNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2485612693 152 CLINDPEVVFLDEPLSGLDvlaaAELTESI----KSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTED 225
Cdd:PRK11153 154 ALASNPKVLLCDEATSALD----PATTRSIlellKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSE 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-246 |
2.37e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 102.84 E-value: 2.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 5 VRNLTKVYkrGNQQIKanDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDI----------------LYKGV 68
Cdd:COG0488 1 LENLSKSF--GGRPLL--DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVsipkglrigylpqeppLDDDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 69 SLLkkpEIIRGRFSFLWEGMQNvYHYL-----TGEANILYFAYLNQVPSSV----ARRRCEELLRKLDLYEVK-DQYVFT 138
Cdd:COG0488 77 TVL---DTVLDGDAELRALEAE-LEELeaklaEPDEDLERLAELQEEFEALggweAEARAEEILSGLGFPEEDlDRPVSE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 139 YSAGMRKKLAIATCLINDPEVVFLDEPLSGLDVlaaaeltESIK---SWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEG 215
Cdd:COG0488 153 LSGGWRRRVALARALLSEPDLLLLDEPTNHLDL-------ESIEwleEFLKNYPGTVLVVSHDRYFLDRVATRILELDRG 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2485612693 216 KVI---------LEGKTEDLKN-----------LSKEEEYIlyLRNSAKAR 246
Cdd:COG0488 226 KLTlypgnysayLEQRAERLEQeaaayakqqkkIAKEEEFI--RRFRAKAR 274
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
29-221 |
4.94e-24 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 97.18 E-value: 4.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 29 VERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEIIRGRFSFLWEgmQNVYHYLTGEANIlyfaYLN 108
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQE--NNLFAHLTVEQNV----GLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 109 QVPS----SVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSW 184
Cdd:cd03298 95 LSPGlkltAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDL 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 2485612693 185 VKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEG 221
Cdd:cd03298 175 HAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
2-197 |
9.27e-24 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 96.03 E-value: 9.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVykRGNQQIkaNDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGvsllkkPEIIRGRF 81
Cdd:PRK13538 1 MLEARNLACE--RDERIL--FSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQG------EPIRRQRD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 82 SF----LWEGMQN-VYHYLTGEANILYFAYLNQVPSsvaRRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLIND 156
Cdd:PRK13538 71 EYhqdlLYLGHQPgIKTELTALENLRFYQRLHGPGD---DEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTR 147
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2485612693 157 PEVVFLDEPLSGLDVLAAAELTESIKSWVkEMGKTVIIASH 197
Cdd:PRK13538 148 APLWILDEPFTAIDKQGVARLEALLAQHA-EQGGMVILTTH 187
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
3-217 |
9.33e-24 |
|
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: 95.36 E-value: 9.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYKRGNQQIKanDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLK-KPEIIRGRF 81
Cdd:cd03246 1 LEVENVSFRYPGAEPPVL--RNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwDPNELGDHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 82 SFLwegMQNVyhyltgeanILYfaylnqvPSSVArrrcEELLrkldlyevkdqyvftySAGMRKKLAIATCLINDPEVVF 161
Cdd:cd03246 79 GYL---PQDD---------ELF-------SGSIA----ENIL----------------SGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2485612693 162 LDEPLSGLDVLAAAELTESIKSwVKEMGKTVIIASHRMDFVEKVtNKVLWLKEGKV 217
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAA-LKAAGATRIVIAHRPETLASA-DRILVLEDGRV 173
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
3-227 |
1.70e-23 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 98.65 E-value: 1.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYKrgnqQIKANDNISFFVERGDVLGILGPNGAG--KTTLIKQIATlliPDQGDILYKGVSLLKKPEIIRGR 80
Cdd:NF000106 14 VEVRGLVKHFG----EVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPWRF*TWCANRRALRRT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 81 FSFLWEGMQNVYHYLTGEANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVV 160
Cdd:NF000106 87 IG*HRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2485612693 161 FLDEPLSGLDVLAAAELTESIKSWVKEmGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDLK 227
Cdd:NF000106 167 YLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELK 232
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-240 |
3.78e-23 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 100.09 E-value: 3.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 5 VRNLTKVYKRGNQQIKANDNISFFveRGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEIIRGRFsfl 84
Cdd:TIGR01257 931 VKNLVKIFEPSGRPAVDRLNITFY--ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSL--- 1005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 85 weGM---QNV-YHYLTGEANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVV 160
Cdd:TIGR01257 1006 --GMcpqHNIlFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVV 1083
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 161 FLDEPLSGLDVLAAAELTESIKSWvkEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDLKNLSKEEEYILYLR 240
Cdd:TIGR01257 1084 VLDEPTSGVDPYSRRSIWDLLLKY--RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVR 1161
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
3-216 |
3.84e-23 |
|
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: 92.90 E-value: 3.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYkrGNQQIKanDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVsllkkpeiirgrfs 82
Cdd:cd03221 1 IELENLSKTY--GGKLLL--KDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST-------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 83 flwegmqnvyhyltgeaniLYFAYLNQvpssvarrrceellrkldlyevkdqyvftYSAGMRKKLAIATCLINDPEVVFL 162
Cdd:cd03221 63 -------------------VKIGYFEQ-----------------------------LSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2485612693 163 DEPLSGLDVLAAAELTESIKSWvkemGKTVIIASHRMDFVEKVTNKVLWLKEGK 216
Cdd:cd03221 95 DEPTNHLDLESIEALEEALKEY----PGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-226 |
4.19e-23 |
|
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: 99.06 E-value: 4.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYKRGNQQIkanDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLK-KPEIIRGRF 81
Cdd:COG4988 337 IELEDVSFSYPGGRPAL---DGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDlDPASWRRQI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 82 SflWEGmQNVY-HYLTGEANILyFAylNQVPSsvaRRRCEELLRKLDLYEVKDQYV-----------FTYSAGMRKKLAI 149
Cdd:COG4988 414 A--WVP-QNPYlFAGTIRENLR-LG--RPDAS---DEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLAL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2485612693 150 ATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKemGKTVIIASHRMDFVEKVtNKVLWLKEGKVILEGKTEDL 226
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQA-DRILVLDDGRIVEQGTHEEL 558
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-226 |
4.36e-23 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 97.11 E-value: 4.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVY-------KRGNQQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKP 74
Cdd:COG4608 7 LLEVRDLKKHFpvrgglfGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 75 EIIRGRfsfLWEGMQNVYH--Y------LT-GEanILYFAYLNQ--VPSSVARRRCEELLRKLDLY-EVKDQYVFTYSAG 142
Cdd:COG4608 87 GRELRP---LRRRMQMVFQdpYaslnprMTvGD--IIAEPLRIHglASKAERRERVAELLELVGLRpEHADRYPHEFSGG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 143 MRKKLAIATCLINDPEVVFLDEPLSGLDVlaaaelteSIKSWV--------KEMGKTVIIASHRMDFVEKVTNK--VLWL 212
Cdd:COG4608 162 QRQRIGIARALALNPKLIVCDEPVSALDV--------SIQAQVlnlledlqDELGLTYLFISHDLSVVRHISDRvaVMYL 233
|
250
....*....|....
gi 2485612693 213 keGKVILEGKTEDL 226
Cdd:COG4608 234 --GKIVEIAPRDEL 245
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
3-197 |
5.35e-23 |
|
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: 94.10 E-value: 5.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTkvYKRGNQQIKanDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSL-LKKPEIIRGrf 81
Cdd:cd03231 1 LEADELT--CERDGRALF--SGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLdFQRDSIARG-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 82 sFLWEGMQN-VYHYLTGEANILYFAYLNqvpssvARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVV 160
Cdd:cd03231 75 -LLYLGHAPgIKTTLSVLENLRFWHADH------SDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLW 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 2485612693 161 FLDEPLSGLDVLAAAELTESIKSWVkEMGKTVIIASH 197
Cdd:cd03231 148 ILDEPTTALDKAGVARFAEAMAGHC-ARGGMVVLTTH 183
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
2-228 |
5.54e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 95.44 E-value: 5.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVYkrGNqqIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKP--EIIRg 79
Cdd:PRK11300 5 LLSVSGLMMRF--GG--LLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPghQIAR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 80 rfsflwEGM----QNV--YHYLTGEANIL----------YFAYLNQVPssvARRRCE--------ELLRKLDLYEVKDQY 135
Cdd:PRK11300 80 ------MGVvrtfQHVrlFREMTVIENLLvaqhqqlktgLFSGLLKTP---AFRRAEsealdraaTWLERVGLLEHANRQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 136 VFTYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEG 215
Cdd:PRK11300 151 AGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
250
....*....|...
gi 2485612693 216 KVILEGKTEDLKN 228
Cdd:PRK11300 231 TPLANGTPEEIRN 243
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
23-235 |
5.61e-23 |
|
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: 94.86 E-value: 5.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 23 DNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSL-LKKPEIIRGRFSFLWEgmQNVYHYLTGEANI 101
Cdd:cd03252 19 DNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLaLADPAWLRRQVGVVLQ--ENVLFNRSIRDNI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 102 lyfAYLNQVPSsvaRRRCEELLRKLDLYEVKDQYVFTY-----------SAGMRKKLAIATCLINDPEVVFLDEPLSGLD 170
Cdd:cd03252 97 ---ALADPGMS---MERVIEAAKLAGAHDFISELPEGYdtivgeqgaglSGGQRQRIAIARALIHNPRILIFDEATSALD 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 171 vlaaaelTESIKSWVKEM-----GKTVIIASHRMDFVeKVTNKVLWLKEGKVILEGKTEDLknLSKEEEY 235
Cdd:cd03252 171 -------YESEHAIMRNMhdicaGRTVIIIAHRLSTV-KNADRIIVMEKGRIVEQGSHDEL--LAENGLY 230
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-197 |
7.20e-23 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 95.31 E-value: 7.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 1 MLLEVRNLTKVYKRGNQQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLlKKPEIIRGR 80
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV-TGPGADRGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 81 -FS----FLWegmQNVYhyltgeANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLIN 155
Cdd:COG4525 81 vFQkdalLPW---LNVL------DNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2485612693 156 DPEVVFLDEPLSGLDVLAAAELTESI-KSWvKEMGKTVIIASH 197
Cdd:COG4525 152 DPRFLLMDEPFGALDALTREQMQELLlDVW-QRTGKGVFLITH 193
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
4-226 |
7.75e-23 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 94.21 E-value: 7.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 4 EVRNLTKVYKRGNQQIKandNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEI-IRGRFS 82
Cdd:cd03254 4 EFENVNFSYDEKKPVLK---DINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKsLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 83 ------FLWEGmqnvyhylTGEANILYFAYLNQ---VPSSVARRRCEELLRKL--DLYEVKDQYVFTYSAGMRKKLAIAT 151
Cdd:cd03254 81 vvlqdtFLFSG--------TIMENIRLGRPNATdeeVIEAAKEAGAHDFIMKLpnGYDTVLGENGGNLSQGERQLLAIAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2485612693 152 CLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKemGKTVIIASHRMDFVEKVTnKVLWLKEGKVILEGKTEDL 226
Cdd:cd03254 153 AMLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKNAD-KILVLDDGKIIEEGTHDEL 224
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1-256 |
1.09e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 95.28 E-value: 1.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 1 MLLEVRNLTKVYKRGNQ-QIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSL--------L 71
Cdd:PRK13641 1 MSIKFENVDYIYSPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetgnknL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 72 KKpeiIRGRFSFLWEGMQNVYHYLTGEANILYFAYLNQVPSSVARRRCEELLRKLDLYE-VKDQYVFTYSAGMRKKLAIA 150
Cdd:PRK13641 81 KK---LRKKVSLVFQFPEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 151 TCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEmGKTVIIASHRMDFVEKVTNKVLWLKEGKVIlegKTEDLKNLS 230
Cdd:PRK13641 158 GVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLI---KHASPKEIF 233
|
250 260 270
....*....|....*....|....*....|
gi 2485612693 231 KEEEYIL--YLRNSAKAR--EKLRKYELQF 256
Cdd:PRK13641 234 SDKEWLKkhYLDEPATSRfaSKLEKGGFKF 263
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
7-244 |
1.65e-22 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 94.27 E-value: 1.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 7 NLTKVYKRGNQQiKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKG--------------VSLLK 72
Cdd:PRK10619 7 NVIDLHKRYGEH-EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdgqlkVADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 73 KPEIIRGRFSFLWEGMqNVYHYLTGEANILyfaylnQVPSSV-------ARRRCEELLRKLDLYE-VKDQYVFTYSAGMR 144
Cdd:PRK10619 86 QLRLLRTRLTMVFQHF-NLWSHMTVLENVM------EAPIQVlglskqeARERAVKYLAKVGIDErAQGKYPVHLSGGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 145 KKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTEsIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTE 224
Cdd:PRK10619 159 QRVSIARALAMEPEVLLFDEPTSALDPELVGEVLR-IMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPE 237
|
250 260
....*....|....*....|
gi 2485612693 225 DLKNLSKEEEYILYLRNSAK 244
Cdd:PRK10619 238 QLFGNPQSPRLQQFLKGSLK 257
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3-235 |
1.90e-22 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 97.54 E-value: 1.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYKRGNQQIKandNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLK-KPEIIRGRF 81
Cdd:COG1132 340 IEFENVSFSYPGDRPVLK---DISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDlTLESLRRQI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 82 SFLwegMQNVYHY-LTGEANILYF---AYLNQVpSSVARR-RCEELLRKL-DLYevkDQYV----FTYSAGMRKKLAIAT 151
Cdd:COG1132 417 GVV---PQDTFLFsGTIRENIRYGrpdATDEEV-EEAAKAaQAHEFIEALpDGY---DTVVgergVNLSGGQRQRIAIAR 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 152 CLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKemGKTVIIASHRMDFVEKVtNKVLWLKEGKVILEGKTEDLknLSK 231
Cdd:COG1132 490 ALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRNA-DRILVLDDGRIVEQGTHEEL--LAR 564
|
....
gi 2485612693 232 EEEY 235
Cdd:COG1132 565 GGLY 568
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
2-226 |
2.30e-22 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 93.23 E-value: 2.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVYkrGNQQIKanDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEIIRG-R 80
Cdd:PRK09493 1 MIEFKNVSKHF--GPTQVL--HNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLiR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 81 fsfLWEGM---Q-NVYHYLTGEANILYFaylnqvPSSV-------ARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAI 149
Cdd:PRK09493 77 ---QEAGMvfqQfYLFPHLTALENVMFG------PLRVrgaskeeAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2485612693 150 ATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEmGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDL 226
Cdd:PRK09493 148 ARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVL 223
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
2-226 |
2.84e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 94.65 E-value: 2.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVY--KRG----NQQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPE 75
Cdd:PRK11308 5 LLQAIDLKKHYpvKRGlfkpERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 76 IIRGRfsfLWEGMQNVYHYLTGEAN-------ILYFAYL-NQVPSSVARR-RCEELLRKLDLY-EVKDQYVFTYSAGMRK 145
Cdd:PRK11308 85 EAQKL---LRQKIQIVFQNPYGSLNprkkvgqILEEPLLiNTSLSAAERReKALAMMAKVGLRpEHYDRYPHMFSGGQRQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 146 KLAIATCLINDPEVVFLDEPLSGLDVlaaaelteSIKSWV--------KEMGKTVIIASHRMDFVEKVTNKVLWLKEGKV 217
Cdd:PRK11308 162 RIAIARALMLDPDVVVADEPVSALDV--------SVQAQVlnlmmdlqQELGLSYVFISHDLSVVEHIADEVMVMYLGRC 233
|
....*....
gi 2485612693 218 ILEGKTEDL 226
Cdd:PRK11308 234 VEKGTKEQI 242
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
3-197 |
5.57e-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: 91.27 E-value: 5.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTkvYKRGNQQIKANdnISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEiIRGRfS 82
Cdd:TIGR01189 1 LAARNLA--CSRGERMLFEG--LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD-EPHE-N 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 83 FLWEGMQN-VYHYLTGEANILYFAYLnqvpSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVVF 161
Cdd:TIGR01189 75 ILYLGHLPgLKPELSALENLHFWAAI----HGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWI 150
|
170 180 190
....*....|....*....|....*....|....*.
gi 2485612693 162 LDEPLSGLDVLAAAELTESIKSWVkEMGKTVIIASH 197
Cdd:TIGR01189 151 LDEPTTALDKAGVALLAGLLRAHL-ARGGIVLLTTH 185
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
34-222 |
1.92e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 91.61 E-value: 1.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 34 VLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPE---IIRGRFSFLWEGMQNVYHYLTGEANILYFAYLNQV 110
Cdd:PRK13638 29 VTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRgllALRQQVATVFQDPEQQIFYTDIDSDIAFSLRNLGV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 111 PSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEmGK 190
Cdd:PRK13638 109 PEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQ-GN 187
|
170 180 190
....*....|....*....|....*....|..
gi 2485612693 191 TVIIASHRMDFVEKVTNKVLWLKEGKVILEGK 222
Cdd:PRK13638 188 HVIISSHDIDLIYEISDAVYVLRQGQILTHGA 219
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
2-227 |
2.08e-21 |
|
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: 95.08 E-value: 2.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVYKRGNQqiKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEIIRGRF 81
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSS--PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNM 2014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 82 SFLWEgMQNVYHYLTGEANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVVF 161
Cdd:TIGR01257 2015 GYCPQ-FDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVL 2093
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2485612693 162 LDEPLSGLDVLAAAELTESIKSWVKEmGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDLK 227
Cdd:TIGR01257 2094 LDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLK 2158
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
2-217 |
2.41e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 91.33 E-value: 2.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVYKRgNQQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGvSLLKKPEI--IRG 79
Cdd:PRK13650 4 IIEVKNLTFKYKE-DQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG-DLLTEENVwdIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 80 RFSFLWEGMQNVYHYLTGEANILyFAYLNQ-VPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPE 158
Cdd:PRK13650 82 KIGMVFQNPDNQFVGATVEDDVA-FGLENKgIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2485612693 159 VVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVeKVTNKVLWLKEGKV 217
Cdd:PRK13650 161 IIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQV 218
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
24-226 |
3.09e-21 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 93.96 E-value: 3.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 24 NISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPD---QGDILYKGVSLLKKpeIIRGRFSFLWEGMQNVYHyLTGEAN 100
Cdd:TIGR00955 43 NVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAK--EMRAISAYVQQDDLFIPT-LTVREH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 101 ILYFAYL---NQVPSSVARRRCEELLRKLDLYEVKD------QYVFTYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDV 171
Cdd:TIGR00955 120 LMFQAHLrmpRRVTKKEKRERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDS 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2485612693 172 LAAAELTESIKSwVKEMGKTVIIASHRMDF-VEKVTNKVLWLKEGKVILEGKTEDL 226
Cdd:TIGR00955 200 FMAYSVVQVLKG-LAQKGKTIICTIHQPSSeLFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1-256 |
3.70e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 90.99 E-value: 3.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 1 MLLEVRNLTKVYKRGNQ-QIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPE---- 75
Cdd:PRK13646 1 MTIRFDNVSYTYQKGTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 76 -IIRGRFSFLWEGMQNVYHYLTGEANILYFAYLNQVPSSVARRRCEELLRKLDL-YEVKDQYVFTYSAGMRKKLAIATCL 153
Cdd:PRK13646 81 rPVRKRIGMVFQFPESQLFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFsRDVMSQSPFQMSGGQMRKIAIVSIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 154 INDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDL-KNLSKE 232
Cdd:PRK13646 161 AMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELfKDKKKL 240
|
250 260
....*....|....*....|....*
gi 2485612693 233 EEYILYLRNSAKAREKL-RKYELQF 256
Cdd:PRK13646 241 ADWHIGLPEIVQLQYDFeQKYQTKL 265
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-255 |
3.71e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 90.84 E-value: 3.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVYKrgNQQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLlkKPEIIrgrf 81
Cdd:PRK13635 5 IIRVEHISFRYP--DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVL--SEETV---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 82 sflWE-----GM--QNVYHYLTGE--ANILYFAYLNQ-VPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIAT 151
Cdd:PRK13635 77 ---WDvrrqvGMvfQNPDNQFVGAtvQDDVAFGLENIgVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 152 CLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKvTNKVLWLKEGKVILEGKTEDLKNLSK 231
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKSGH 232
|
250 260
....*....|....*....|....*
gi 2485612693 232 EEEYI-LYLRNSAKAREKLRKYELQ 255
Cdd:PRK13635 233 MLQEIgLDVPFSVKLKELLKRNGIL 257
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-197 |
4.76e-21 |
|
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: 93.31 E-value: 4.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 29 VERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDIlYKGVSLLKKPEIIRGRFSflwegmqnvyhyLTGEAnILYFAYLN 108
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-DEDLKISYKPQYISPDYD------------GTVEE-FLRSANTD 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 109 QVPSSVARrrcEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEM 188
Cdd:COG1245 429 DFGSSYYK---TEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENR 505
|
....*....
gi 2485612693 189 GKTVIIASH 197
Cdd:COG1245 506 GKTAMVVDH 514
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
3-232 |
5.44e-21 |
|
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: 88.74 E-value: 5.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTkvYKRGNQQIKanDNISFFVERGDVLGILGPNGAGKTTLIKQIATllIPD----QGDILYKGVSLLKKPEIIR 78
Cdd:cd03217 1 LEIKDLH--VSVGGKEIL--KGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG--HPKyevtEGEILFKGEDITDLPPEER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 79 GRfsflwEGmqnvyhyltgeaniLYFAYlnQVPSSVARRRCEELLRKLDLyevkdqyvfTYSAGMRKKLAIATCLINDPE 158
Cdd:cd03217 75 AR-----LG--------------IFLAF--QYPPEIPGVKNADFLRYVNE---------GFSGGEKKRNEILQLLLLEPD 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2485612693 159 VVFLDEPLSGLDVLAAAELTESIKSWVKEmGKTVIIASHRMDFVEKV-TNKVLWLKEGKVILEGKTEDLKNLSKE 232
Cdd:cd03217 125 LAILDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKELALEIEKK 198
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
4-233 |
5.52e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 90.44 E-value: 5.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 4 EVRNLTkvYKRGNQQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKP-EIIRGRFS 82
Cdd:PRK13632 9 KVENVS--FSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENlKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 83 FLWEGMQNVYHYLTGEANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVVFL 162
Cdd:PRK13632 87 IIFQNPDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIF 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2485612693 163 DEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKvTNKVLWLKEGKVILEGKTEDLKNlSKEE 233
Cdd:PRK13632 167 DESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILN-NKEI 235
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-226 |
5.63e-21 |
|
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: 92.83 E-value: 5.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVY-------KRGNQQIKANDNISFFVERGDVLGILGPNGAGKTTLIKqiATL-LIPDQGDILYKGVSLLKK 73
Cdd:COG4172 275 LLEARDLKVWFpikrglfRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGL--ALLrLIPSEGEIRFDGQDLDGL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 74 P-----------------------------EIIRgrfsflwEGMQnvyhyltgeanilyfayLNQVPSSVA--RRRCEEL 122
Cdd:COG4172 353 SrralrplrrrmqvvfqdpfgslsprmtvgQIIA-------EGLR-----------------VHGPGLSAAerRARVAEA 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 123 LRKLDL-YEVKDQYVFTYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDF 201
Cdd:COG4172 409 LEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAV 488
|
250 260
....*....|....*....|....*
gi 2485612693 202 VEKVTNKVLWLKEGKVILEGKTEDL 226
Cdd:COG4172 489 VRALAHRVMVMKDGKVVEQGPTEQV 513
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
2-226 |
1.12e-20 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 91.05 E-value: 1.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVYkrgnQQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEIIRgRF 81
Cdd:PRK11607 19 LLEIRNLTKSF----DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQR-PI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 82 SFLWEGMQnVYHYLTGEANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVVF 161
Cdd:PRK11607 94 NMMFQSYA-LFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2485612693 162 LDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDL 226
Cdd:PRK11607 173 LDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-210 |
1.78e-20 |
|
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: 88.23 E-value: 1.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 31 RGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEIIRGRFSflwegmQNVYHYLTGEANILY-FAYLNQ 109
Cdd:cd03237 24 ESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADYE------GTVRDLLSSITKDFYtHPYFKT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 110 vpssvarrrceELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMG 189
Cdd:cd03237 98 -----------EIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNE 166
|
170 180
....*....|....*....|.
gi 2485612693 190 KTVIIASHRMDFVEKVTNKVL 210
Cdd:cd03237 167 KTAFVVEHDIIMIDYLADRLI 187
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
2-209 |
3.51e-20 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 87.18 E-value: 3.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVYKRGNQQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLK-----KPEI 76
Cdd:PRK11629 5 LLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlssaaKAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 77 IRGRFSFLWEgmqnvYHYL----TGEANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATC 152
Cdd:PRK11629 85 RNQKLGFIYQ-----FHHLlpdfTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2485612693 153 LINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKV 209
Cdd:PRK11629 160 LVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
2-228 |
3.80e-20 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 87.90 E-value: 3.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTkvYKRGNQQIkaNDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLlkkPEIIRGRf 81
Cdd:PRK11831 7 LVDMRGVS--FTRGNRCI--FDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENI---PAMSRSR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 82 sfLWEGMQNVYHYLTGEAnilYFAYLNqVPSSVA------RRRCEELLR-----KLD---LYEVKDQYVFTYSAGMRKKL 147
Cdd:PRK11831 79 --LYTVRKRMSMLFQSGA---LFTDMN-VFDNVAyplrehTQLPAPLLHstvmmKLEavgLRGAAKLMPSELSGGMARRA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 148 AIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDLK 227
Cdd:PRK11831 153 ALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQ 232
|
.
gi 2485612693 228 N 228
Cdd:PRK11831 233 A 233
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
3-226 |
1.13e-19 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 87.85 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYKRgNQQIkanDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPeiIRGR-F 81
Cdd:PRK11432 7 VVLKNITKRFGS-NTVI---DNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRS--IQQRdI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 82 SFLWEGMQNVYHYLTGEaNILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVVF 161
Cdd:PRK11432 81 CMVFQSYALFPHMSLGE-NVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2485612693 162 LDEPLSGLDvlaaAELTESIKSWVKEMGKTVIIAS----HRMDFVEKVTNKVLWLKEGKVILEGKTEDL 226
Cdd:PRK11432 160 FDEPLSNLD----ANLRRSMREKIRELQQQFNITSlyvtHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
23-197 |
1.37e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 86.29 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 23 DNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLlKKPEIIRGrFSFLWEGM---QNVyhyltgEA 99
Cdd:PRK11248 18 EDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV-EGPGAERG-VVFQNEGLlpwRNV------QD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 100 NILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTE 179
Cdd:PRK11248 90 NVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQT 169
|
170
....*....|....*....
gi 2485612693 180 -SIKSWvKEMGKTVIIASH 197
Cdd:PRK11248 170 lLLKLW-QETGKQVLLITH 187
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-197 |
1.46e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 84.93 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 1 MLLEVRNLTKVykRGNQQIKANdnISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGvsllKKPEIIRGR 80
Cdd:PRK13539 1 MMLEGEDLACV--RGGRVLFSG--LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG----GDIDDPDVA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 81 FSFLWEGMQNVYH-YLTGEANILYFA-YLNQVPSSVarrrcEELLRKLDLYEVKD---QYVftySAGMRKKLAIATCLIN 155
Cdd:PRK13539 73 EACHYLGHRNAMKpALTVAENLEFWAaFLGGEELDI-----AAALEAVGLAPLAHlpfGYL---SAGQKRRVALARLLVS 144
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2485612693 156 DPEVVFLDEPLSGLDVLAAAELTESIKSWVKEmGKTVIIASH 197
Cdd:PRK13539 145 NRPIWILDEPTAALDAAAVALFAELIRAHLAQ-GGIVIAATH 185
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
2-210 |
1.70e-19 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 88.71 E-value: 1.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVYkrgnqqikanDNISFFVE-----RGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKgVSLLKKPEI 76
Cdd:PRK13409 340 LVEYPDLTKKL----------GDFSLEVEggeiyEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKISYKPQY 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 77 IRGRFsflwEGmqNVYHYLTGEANILYFAYLNqvpssvarrrcEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLIND 156
Cdd:PRK13409 409 IKPDY----DG--TVEDLLRSITDDLGSSYYK-----------SEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRD 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2485612693 157 PEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVL 210
Cdd:PRK13409 472 ADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLM 525
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-236 |
1.94e-19 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 85.86 E-value: 1.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTkVYKRGNQQIKandNISFFVERGDVLGILGPNGAGKTTLIKqiaTL-----LIPDQ---GDILYKGVSLLKK- 73
Cdd:COG1117 12 IEVRNLN-VYYGDKQALK---DINLDIPENKVTALIGPSGCGKSTLLR---CLnrmndLIPGArveGEILLDGEDIYDPd 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 74 --PEIIRGRFsflweGM--QN-------VYHyltgeaNILYFAYLNQVPS-SVARRRCEELLRKLDLY-EVKD---QYVF 137
Cdd:COG1117 85 vdVVELRRRV-----GMvfQKpnpfpksIYD------NVAYGLRLHGIKSkSELDEIVEESLRKAALWdEVKDrlkKSAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 138 TYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMgkTVIIASHRMDFVEKVTNKVLWLKEGKV 217
Cdd:COG1117 154 GLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGEL 231
|
250 260
....*....|....*....|..
gi 2485612693 218 ILEGKTEDL-KNLSKE--EEYI 236
Cdd:COG1117 232 VEFGPTEQIfTNPKDKrtEDYI 253
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
2-228 |
4.97e-19 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 84.68 E-value: 4.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVYkrgnQQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQ---------GDILYKGVSLLK 72
Cdd:PRK09984 4 IIRVEKLAKTF----NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellGRTVQREGRLAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 73 KPEIIRGRFSFLWEGMqNVYHYLTGEANILYFAyLNQVP---------SSVARRRCEELLRKLDLYEVKDQYVFTYSAGM 143
Cdd:PRK09984 80 DIRKSRANTGYIFQQF-NLVNRLSVLENVLIGA-LGSTPfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 144 RKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKT 223
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSS 237
|
....*
gi 2485612693 224 EDLKN 228
Cdd:PRK09984 238 QQFDN 242
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
2-226 |
5.31e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 85.04 E-value: 5.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVYKRGNQQIKandNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSL--LKKPEIIRG 79
Cdd:PRK13644 1 MIRLENVSYSYPDGTPALE---NINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdFSKLQGIRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 80 RFSFLWEGMQNVYHYLTGEANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEV 159
Cdd:PRK13644 78 LVGIVFQNPETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPEC 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2485612693 160 VFLDEPLSGLDVLAAAELTESIKSwVKEMGKTVIIASHRMDFVEkVTNKVLWLKEGKVILEGKTEDL 226
Cdd:PRK13644 158 LIFDEVTSMLDPDSGIAVLERIKK-LHEKGKTIVYITHNLEELH-DADRIIVMDRGKIVLEGEPENV 222
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-239 |
8.63e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 83.79 E-value: 8.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVYKrGNQQIkanDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILY--KGVSLLKKPEIIRG 79
Cdd:PRK10895 3 TLTAKNLAKAYK-GRRVV---EDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIddEDISLLPLHARARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 80 RFSFLWEgMQNVYHYLTGEANILYFAYLNQVPSSVARR-RCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPE 158
Cdd:PRK10895 79 GIGYLPQ-EASIFRRLSVYDNLMAVLQIRDDLSAEQREdRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 159 VVFLDEPLSGLDVLAAAELTESIKSwVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDLknLSKEEEYILY 238
Cdd:PRK10895 158 FILLDEPFAGVDPISVIDIKRIIEH-LRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI--LQDEHVKRVY 234
|
.
gi 2485612693 239 L 239
Cdd:PRK10895 235 L 235
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-226 |
1.03e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 85.66 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 1 MLLEVRNLtkVYKRGNQQIKanDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKG--VSLLKKPEIIR 78
Cdd:PRK09536 2 PMIDVSDL--SVEFGDTTVL--DGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddVEALSARAASR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 79 --------GRFSFLWEGMQNVYHYLTGEANILYFAylnqvpSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIA 150
Cdd:PRK09536 78 rvasvpqdTSLSFEFDVRQVVEMGRTPHRSRFDTW------TETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2485612693 151 TCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEmGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDL 226
Cdd:PRK09536 152 RALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-226 |
1.37e-18 |
|
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: 85.89 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVYKRGNQQIKANDNISFFVERGDVLGILGPNGAGK--TTLikqiATL-LIPD-----QGDILYKGVSLLKK 73
Cdd:COG4172 6 LLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKsvTAL----SILrLLPDpaahpSGSILFDGQDLLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 74 PEI----IRGR-----FSflwEGMQ--NVYHylT-----GEANILYFAylnqVPSSVARRRCEELLRKLDLYEVK---DQ 134
Cdd:COG4172 82 SERelrrIRGNriamiFQ---EPMTslNPLH--TigkqiAEVLRLHRG----LSGAAARARALELLERVGIPDPErrlDA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 135 YVFTYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKE 214
Cdd:COG4172 153 YPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQ 232
|
250
....*....|..
gi 2485612693 215 GKVILEGKTEDL 226
Cdd:COG4172 233 GEIVEQGPTAEL 244
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
13-254 |
1.38e-18 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 83.71 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 13 KRGNQQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKG-VSLLKKPEIIRGRFSflweGMQNV 91
Cdd:PRK13546 31 KHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGeVSVIAISAGLSGQLT----GIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 92 yhyltgEANILYFAYlnqvpssvARRRCEELLRKL----DLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVVFLDEPLS 167
Cdd:PRK13546 107 ------EFKMLCMGF--------KRKEIKAMTPKIiefsELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 168 GLDVLAAAELTESIKSWvKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDLknLSKEEEYILYLRNSAKARE 247
Cdd:PRK13546 173 VGDQTFAQKCLDKIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV--LPKYEAFLNDFKKKSKAEQ 249
|
....*..
gi 2485612693 248 KLRKYEL 254
Cdd:PRK13546 250 KEFRNKL 256
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
26-237 |
2.21e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 82.32 E-value: 2.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 26 SFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEIIRgRFSFLWEgMQNVYHYLTGEANIlyfa 105
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRR-PVSMLFQ-ENNLFSHLTVAQNI---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 106 YLNQVP----SSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESI 181
Cdd:PRK10771 93 GLGLNPglklNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2485612693 182 KSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDLKNLSKEEEYIL 237
Cdd:PRK10771 173 SQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKASASALL 228
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
26-228 |
2.34e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 84.70 E-value: 2.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 26 SFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKP-----EIIRGRFSFLWEGMQNVYHyLTGEAN 100
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaelrEVRRKKIAMVFQSFALMPH-MTVLDN 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 101 ILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTES 180
Cdd:PRK10070 127 TAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDE 206
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2485612693 181 IKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDLKN 228
Cdd:PRK10070 207 LVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-197 |
2.68e-18 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 84.23 E-value: 2.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVYkrGNQQIKanDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEIIRgrf 81
Cdd:PRK09452 14 LVELRGISKSF--DGKEVI--SNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENR--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 82 sflweGMQNVY-HY-----LTGEANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLIN 155
Cdd:PRK09452 87 -----HVNTVFqSYalfphMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVN 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2485612693 156 DPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASH 197
Cdd:PRK09452 162 KPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTH 203
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-218 |
3.24e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 84.73 E-value: 3.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVYkrGNQQIKanDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILY-KGVSLlkkpeiirGR 80
Cdd:COG0488 315 VLELEGLSKSY--GDKTLL--DDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLgETVKI--------GY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 81 FSflwegmQNVyHYLTGEANILyfaylnQVPSSVARRRCEELLRKL---------DLYevkdQYVFTYSAGMRKKLAIAT 151
Cdd:COG0488 383 FD------QHQ-EELDPDKTVL------DELRDGAPGGTEQEVRGYlgrflfsgdDAF----KPVGVLSGGEKARLALAK 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2485612693 152 CLINDPEVVFLDEPLSGLDVLAAAELTESIKSWvkemGKTVIIASHRMDFVEKVTNKVLWLKEGKVI 218
Cdd:COG0488 446 LLLSPPNVLLLDEPTNHLDIETLEALEEALDDF----PGTVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2-234 |
3.82e-18 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 84.78 E-value: 3.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVYKRGNQQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKG--VSLLKKPEIIRG 79
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGqdVATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 80 R---FSFLWEGmqnvYH---YLTGEANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCL 153
Cdd:PRK10535 84 RrehFGFIFQR----YHllsHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 154 INDPEVVFLDEPLSGLDVLAAAELTESIKSwVKEMGKTVIIASHRMDfVEKVTNKVLWLKEGKVILEGKTEDLKNLSKEE 233
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEVMAILHQ-LRDRGHTVIIVTHDPQ-VAAQAERVIEIRDGEIVRNPPAQEKVNVAGGT 237
|
.
gi 2485612693 234 E 234
Cdd:PRK10535 238 E 238
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-265 |
4.77e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 84.47 E-value: 4.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYKrgnqQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATL--LIPDQGDILYKgVSLLKKPEIIrGR 80
Cdd:TIGR03269 1 IEVKNLTKKFD----GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYH-VALCEKCGYV-ER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 81 FSF------------------LWEGMQNVYHYLTGEANILY---FAY-------------LNQV--PSSVARRRCEELLR 124
Cdd:TIGR03269 75 PSKvgepcpvcggtlepeevdFWNLSDKLRRRIRKRIAIMLqrtFALygddtvldnvleaLEEIgyEGKEAVGRAVDLIE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 125 KLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEK 204
Cdd:TIGR03269 155 MVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIED 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2485612693 205 VTNKVLWLKEGKVILEGKTEDLKNLSKEeeyilylrnSAKAREKLRKYELQFEILSDVTLK 265
Cdd:TIGR03269 235 LSDKAIWLENGEIKEEGTPDEVVAVFME---------GVSEVEKECEVEVGEPIIKVRNVS 286
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
7-275 |
4.93e-18 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 84.17 E-value: 4.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 7 NLTKVYKRGNQQIK----------------ANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSL 70
Cdd:PRK13545 9 HVTKKYKMYNKPFDklkdlffrskdgeyhyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 71 LKKpeiirgrfsfLWEGMQNvyhYLTGEANIlyfaYLNQVPSSVARRRCEELLRKL----DLYEVKDQYVFTYSAGMRKK 146
Cdd:PRK13545 89 LIA----------ISSGLNG---QLTGIENI----ELKGLMMGLTKEKIKEIIPEIiefaDIGKFIYQPVKTYSSGMKSR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 147 LAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWvKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGkteDL 226
Cdd:PRK13545 152 LGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEF-KEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYG---DI 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2485612693 227 KNLSKEEEYIL--YLRNSAKAREKLRK---YELQFEILSDVT--LKTTLRLGQKEL 275
Cdd:PRK13545 228 KEVVDHYDEFLkkYNQMSVEERKDFREeqiSQFQHGLLQEDQtgRERKRKKGKKTS 283
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-233 |
8.38e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 83.42 E-value: 8.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYKrgnqQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLlkkpeiirgRFS 82
Cdd:PRK11288 5 LSFDGIGKTFP----GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEM---------RFA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 83 ----FLWEGMQNVY---HY---LTGEANIlyfaYLNQVPS-------SVARRRCEELLRKLDLYEVKDQYVFTYSAGMRK 145
Cdd:PRK11288 72 sttaALAAGVAIIYqelHLvpeMTVAENL----YLGQLPHkggivnrRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 146 KLAIATCLINDPEVVFLDEPLSGLdvlaAAELTESIKSWVKEM---GKTVIIASHRMDFVEKVTNKVLWLKEGKVIlegK 222
Cdd:PRK11288 148 MVEIAKALARNARVIAFDEPTSSL----SAREIEQLFRVIRELraeGRVILYVSHRMEEIFALCDAITVFKDGRYV---A 220
|
250
....*....|..
gi 2485612693 223 T-EDLKNLSKEE 233
Cdd:PRK11288 221 TfDDMAQVDRDQ 232
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
3-198 |
1.58e-17 |
|
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: 82.79 E-value: 1.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTkvYKRGNQQIkANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPE-IIRGRF 81
Cdd:TIGR02868 335 LELRDLS--AGYPGAPP-VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQdEVRRRV 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 82 SFLwegMQNVYHYLTGEANILYFAYLNQVPSSV----ARRRCEELLRKLD--LYEVKDQYVFTYSAGMRKKLAIATCLIN 155
Cdd:TIGR02868 412 SVC---AQDAHLFDTTVRENLRLARPDATDEELwaalERVGLADWLRALPdgLDTVLGEGGARLSGGERQRLALARALLA 488
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2485612693 156 DPEVVFLDEPLSGLDVLAAAELTESIksWVKEMGKTVIIASHR 198
Cdd:TIGR02868 489 DAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHH 529
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-198 |
3.08e-17 |
|
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: 81.95 E-value: 3.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYKRGNqqiKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEIIRGRfS 82
Cdd:TIGR02857 322 LEFSGVSVAYPGRR---PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRD-Q 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 83 FLWEGMQNVYHYLTGEANILyFAYLNQVPSSVAR--RRCE--ELLRKLDL---YEVKDQYVfTYSAGMRKKLAIATCLIN 155
Cdd:TIGR02857 398 IAWVPQHPFLFAGTIAENIR-LARPDASDAEIREalERAGldEFVAALPQgldTPIGEGGA-GLSGGQAQRLALARAFLR 475
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2485612693 156 DPEVVFLDEPLSGLDVLAAAELTESIKSWVKemGKTVIIASHR 198
Cdd:TIGR02857 476 DAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHR 516
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-225 |
3.25e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 79.67 E-value: 3.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 1 MLLEVRNLTKVYkrGNQQIKanDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSL--LKKPEIIR 78
Cdd:PRK11231 1 MTLRTENLTVGY--GTKRIL--NDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPIsmLSSRQLAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 79 gRFSFLWEgmqnvyHYLTGEAN-----ILY--FAYLNQVP--SSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAI 149
Cdd:PRK11231 77 -RLALLPQ------HHLTPEGItvrelVAYgrSPWLSLWGrlSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2485612693 150 ATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSwVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTED 225
Cdd:PRK11231 150 AMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRE-LNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEE 224
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
24-226 |
3.78e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 79.78 E-value: 3.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 24 NISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQG-----DILYKGVSLLKKPEIIRGRFSFLWEGMQNVYHYLTGE 98
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGkvtvgDIVVSSTSKQKEIKPVRKKVGVVFQFPESQLFEETVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 99 ANILYFAYLNQVPSSVARRRCEELLRKLDLY-EVKDQYVFTYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAEL 177
Cdd:PRK13643 104 KDVAFGPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEM 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2485612693 178 TESIKSwVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDL 226
Cdd:PRK13643 184 MQLFES-IHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDV 231
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
2-217 |
8.80e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 77.61 E-value: 8.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVYKRGNQQIKAndnISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKG--VSLLKKPEIirg 79
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQALQG---VTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhdITRLKNREV--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 80 rfSFLWE--GMQNVYHYLTGEANIlyfaYLN-QVPSSVA-------RRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAI 149
Cdd:PRK10908 75 --PFLRRqiGMIFQDHHLLMDRTV----YDNvAIPLIIAgasgddiRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2485612693 150 ATCLINDPEVVFLDEPLSGLDvlaaAELTESIKSWVKE---MGKTVIIASHRMDFVEKVTNKVLWLKEGKV 217
Cdd:PRK10908 149 ARAVVNKPAVLLADEPTGNLD----DALSEGILRLFEEfnrVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
6-221 |
1.08e-16 |
|
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: 76.92 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 6 RNLTKVYKRGNQQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPD---QGDILYKGVSLLKKPEIIRGRFS 82
Cdd:cd03233 7 RNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEII 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 83 FLWEGMQNVyHYLTGEaNILYFAylnqvpssvarRRCEellrkldlyevKDQYVFTYSAGMRKKLAIATCLINDPEVVFL 162
Cdd:cd03233 87 YVSEEDVHF-PTLTVR-ETLDFA-----------LRCK-----------GNEFVRGISGGERKRVSIAEALVSRASVLCW 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 163 DEPLSGLDVLAAAELTESIKSWVKEMGKTVIIA-SHRMDFVEKVTNKVLWLKEGKVILEG 221
Cdd:cd03233 143 DNSTRGLDSSTALEILKCIRTMADVLKTTTFVSlYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-226 |
1.41e-16 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 80.15 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVY-KRGNQQIKanDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSL-------LKK 73
Cdd:TIGR00958 478 LIEFQDVSFSYpNRPDVPVL--KGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLvqydhhyLHR 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 74 PEIIRGRFSFLWEGmqnvyhylTGEANILY---FAYLNQVPSSVARRRCEELLRKL--DLYEVKDQYVFTYSAGMRKKLA 148
Cdd:TIGR00958 556 QVALVGQEPVLFSG--------SVRENIAYgltDTPDEEIMAAAKAANAHDFIMEFpnGYDTEVGEKGSQLSGGQKQRIA 627
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2485612693 149 IATCLINDPEVVFLDEPLSGLDvlaaAELTESIKSWVKEMGKTVIIASHRMDFVEKVtNKVLWLKEGKVILEGKTEDL 226
Cdd:TIGR00958 628 IARALVRKPRVLILDEATSALD----AECEQLLQESRSRASRTVLLIAHRLSTVERA-DQILVLKKGSVVEMGTHKQL 700
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
3-235 |
1.48e-16 |
|
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: 77.27 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYkrGNQQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSL-------LKKPE 75
Cdd:cd03251 1 VEFKNVTFRY--PGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVrdytlasLRRQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 76 IIRGRFSFLWEGmqnvyhylTGEANILYFAylnqvpSSVARRRCEELLRKLDLYEVKDQYVFTY-----------SAGMR 144
Cdd:cd03251 79 GLVSQDVFLFND--------TVAENIAYGR------PGATREEVEEAARAANAHEFIMELPEGYdtvigergvklSGGQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 145 KKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKemGKTVIIASHRMDFVEKvTNKVLWLKEGKVILEGKTE 224
Cdd:cd03251 145 QRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHE 221
|
250
....*....|.
gi 2485612693 225 DLknLSKEEEY 235
Cdd:cd03251 222 EL--LAQGGVY 230
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-226 |
1.64e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 77.91 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 1 MLLEVRNLTKV--YKRG---NQQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLlkkpe 75
Cdd:PRK15112 3 TLLEVRNLSKTfrYRTGwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 76 iIRGRFSFLWEGMQNVYHYLTGEAN-------ILYFAY-LNQVPSSVAR-RRCEELLRKLDLY-EVKDQYVFTYSAGMRK 145
Cdd:PRK15112 78 -HFGDYSYRSQRIRMIFQDPSTSLNprqrisqILDFPLrLNTDLEPEQReKQIIETLRQVGLLpDHASYYPHMLAPGQKQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 146 KLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTED 225
Cdd:PRK15112 157 RLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTAD 236
|
.
gi 2485612693 226 L 226
Cdd:PRK15112 237 V 237
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
34-226 |
1.68e-16 |
|
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: 78.99 E-value: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 34 VLGILGPNGAGKTTLIKQIATLLIPDQGDI------LY---KGVSLlkKPEiiRGRFsflweGMqnVY-------HyLTG 97
Cdd:COG4148 27 VTALFGPSGSGKTTLLRAIAGLERPDSGRIrlggevLQdsaRGIFL--PPH--RRRI-----GY--VFqearlfpH-LSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 98 EANILYfaylnqvpssvARRRCEELLRKLDLYEVK---------DQYVFTYSAGMRKKLAIATCLINDPEVVFLDEPLSG 168
Cdd:COG4148 95 RGNLLY-----------GRKRAPRAERRISFDEVVellgighllDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2485612693 169 LDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDL 226
Cdd:COG4148 164 LDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEV 221
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-226 |
2.12e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 79.51 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVYKRGNQQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEIIRGRF 81
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 82 SFLWEGMQNVYH-----------------YLTGEA---NILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSA 141
Cdd:PRK10261 92 EQSAAQMRHVRGadmamifqepmtslnpvFTVGEQiaeSIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 142 GMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEG 221
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETG 251
|
....*
gi 2485612693 222 KTEDL 226
Cdd:PRK10261 252 SVEQI 256
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
25-231 |
2.16e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 77.19 E-value: 2.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 25 ISFFVERGDVLGILGPNGAGKTTLIKQIATLLiPDQGDILYKGVSL--LKKPEIIRGRfSFLweGMQN-------VYHYL 95
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLsdWSAAELARHR-AYL--SQQQsppfampVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 96 TgeaniLYFAylNQVPSSVARRRCEELLRKLDLyevKDQY---VFTYSAG--MRKKLAiATCL-----IN-DPEVVFLDE 164
Cdd:COG4138 91 A-----LHQP--AGASSEAVEQLLAQLAEALGL---EDKLsrpLTQLSGGewQRVRLA-AVLLqvwptINpEGQLLLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2485612693 165 PLSGLDVLAAAELtesiKSWVKEM---GKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDL---KNLSK 231
Cdd:COG4138 160 PMNSLDVAQQAAL----DRLLRELcqqGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVmtpENLSE 228
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
7-221 |
2.48e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 77.74 E-value: 2.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 7 NLTKVY-KRGNQQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDIL---YK---GVSLLKKPEIIRG 79
Cdd:PRK13645 11 NVSYTYaKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIvgdYAipaNLKKIKEVKRLRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 80 RFSFLWEGMQNVYHYLTGEANILYFAYLNQVPSSVARRRCEELLrklDLYEVKDQYV----FTYSAGMRKKLAIATCLIN 155
Cdd:PRK13645 91 EIGLVFQFPEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELL---KLVQLPEDYVkrspFELSGGQKRRVALAGIIAM 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2485612693 156 DPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEG 221
Cdd:PRK13645 168 DGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIG 233
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
3-235 |
4.55e-16 |
|
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: 76.11 E-value: 4.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYKRGNQQIKandNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGV--------SLLKKP 74
Cdd:cd03253 1 IEFENVTFAYDPGRPVLK---DVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQdirevtldSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 75 EIIRgRFSFLWEgmQNVYHyltgeaNILYfAYLNQVPSSVarrrcEELLRKLDLYEVKDQYVFTY-----------SAGM 143
Cdd:cd03253 78 GVVP-QDTVLFN--DTIGY------NIRY-GRPDATDEEV-----IEAAKAAQIHDKIMRFPDGYdtivgerglklSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 144 RKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKemGKTVIIASHRmdfVEKVTN--KVLWLKEGKVILEG 221
Cdd:cd03253 143 KQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHR---LSTIVNadKIIVLKDGRIVERG 217
|
250
....*....|....
gi 2485612693 222 KTEDLknLSKEEEY 235
Cdd:cd03253 218 THEEL--LAKGGLY 229
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-225 |
4.62e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 76.35 E-value: 4.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 1 MLLEVRNLTkvYKRGNQQIKanDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSL--LKKPEIIR 78
Cdd:PRK13548 1 AMLEARNLS--VRLGGRTLL--DDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLadWSPAELAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 79 GR----------FSFLWE---GMQNVYHYLTGEAnilyfaylnqvpssvARRRCEELLRKLDLYEVKDQYVFTYSAGMRK 145
Cdd:PRK13548 77 RRavlpqhsslsFPFTVEevvAMGRAPHGLSRAE---------------DDALVAAALAQVDLAHLAGRDYPQLSGGEQQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 146 KLAIATCLI------NDPEVVFLDEPLSGLD------VLAAAeltesiKSWVKEMGKTVII-------ASHRMDfvekvt 206
Cdd:PRK13548 142 RVQLARVLAqlwepdGPPRWLLLDEPTSALDlahqhhVLRLA------RQLAHERGLAVIVvlhdlnlAARYAD------ 209
|
250
....*....|....*....
gi 2485612693 207 nKVLWLKEGKVILEGKTED 225
Cdd:PRK13548 210 -RIVLLHQGRLVADGTPAE 227
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
18-220 |
6.48e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 75.69 E-value: 6.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 18 QIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKP--EIIRGRFSFLWEGmQNVYHYL 95
Cdd:PRK11614 17 KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQtaKIMREAVAIVPEG-RRVFSRM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 96 TGEANIL---YFAYLNQVPSSVARrrCEELLRKLdlYEVKDQYVFTYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDVL 172
Cdd:PRK11614 96 TVEENLAmggFFAERDQFQERIKW--VYELFPRL--HERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPI 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2485612693 173 AAAELTESIKSwVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILE 220
Cdd:PRK11614 172 IIQQIFDTIEQ-LREQGMTIFLVEQNANQALKLADRGYVLENGHVVLE 218
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-233 |
7.55e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 77.82 E-value: 7.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 1 MLLEVRNLT-------KVYKRGNQQIKANDNISFFVERGDVLGILGPNGAGKTTliKQIATL-LIPDQGDILYKGVSL-- 70
Cdd:PRK15134 274 PLLDVEQLQvafpirkGILKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKST--TGLALLrLINSQGEIWFDGQPLhn 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 71 --LKKPEIIRGRFSFLWegmQNVYHYLTGEANILYFA----YLNQVPSSVARR--RCEELLRKLDL-YEVKDQYVFTYSA 141
Cdd:PRK15134 352 lnRRQLLPVRHRIQVVF---QDPNSSLNPRLNVLQIIeeglRVHQPTLSAAQReqQVIAVMEEVGLdPETRHRYPAEFSG 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 142 GMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEG 221
Cdd:PRK15134 429 GQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQG 508
|
250
....*....|..
gi 2485612693 222 KTEDLKNLSKEE 233
Cdd:PRK15134 509 DCERVFAAPQQE 520
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
25-231 |
1.15e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 74.97 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 25 ISFFVERGDVLGILGPNGAGKTTLIKQIATLLiPDQGDILYKGVSLLKKP----EIIRGRFSflwegmQN--------VY 92
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSaaelARHRAYLS------QQqtppfampVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 93 HYLTgeaniLYFAylNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAG--MRKKLAiATCLINDPEV------VFLDE 164
Cdd:PRK03695 88 QYLT-----LHQP--DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGewQRVRLA-AVVLQVWPDInpagqlLLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 165 PLSGLDVLAAAELTESIKSwVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDL---KNLSK 231
Cdd:PRK03695 160 PMNSLDVAQQAALDRLLSE-LCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVltpENLAQ 228
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
23-198 |
1.23e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 74.22 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 23 DNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEIIRGRFSFLWEgMQNVYHYLTGEANIL 102
Cdd:PRK13540 18 QQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGH-RSGINPYLTLRENCL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 103 YfaylnQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIK 182
Cdd:PRK13540 97 Y-----DIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQ 171
|
170
....*....|....*.
gi 2485612693 183 SWVKEmGKTVIIASHR 198
Cdd:PRK13540 172 EHRAK-GGAVLLTSHQ 186
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-218 |
2.26e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 76.43 E-value: 2.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNL-------TKVYKRGNQQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKG--VSLL- 71
Cdd:PRK10261 313 ILQVRNLvtrfplrSGLLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqrIDTLs 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 72 -KKPEIIRGRFSFLWegmQNVYHYLTGEANILY-----FAYLNQVPSSVARRRCEELLRKLDLY-EVKDQYVFTYSAGMR 144
Cdd:PRK10261 393 pGKLQALRRDIQFIF---QDPYASLDPRQTVGDsimepLRVHGLLPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQR 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2485612693 145 KKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVI 218
Cdd:PRK10261 470 QRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
21-173 |
2.47e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 76.32 E-value: 2.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 21 ANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDilykgVSLLKKP----EI-IRGR-------FSflwegm 88
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGE-----AWLFGQPvdagDIaTRRRvgymsqaFS------ 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 89 qnVYHYLTGEANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVVFLDEPLSG 168
Cdd:NF033858 350 --LYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSG 427
|
....*
gi 2485612693 169 LDVLA 173
Cdd:NF033858 428 VDPVA 432
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
24-226 |
2.70e-15 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 76.29 E-value: 2.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 24 NISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLK-KPEIIRGRFSFLwegMQNVYHYLTGEANIL 102
Cdd:PRK10789 333 NVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKlQLDSWRSRLAVV---SQTPFLFSDTVANNI 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 103 YFAYLNQVPSS---VARRRC--EELLRKLDLY--EVKDQYVFtYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAA 175
Cdd:PRK10789 410 ALGRPDATQQEiehVARLASvhDDILRLPQGYdtEVGERGVM-LSGGQKQRISIARALLLNAEILILDDALSAVDGRTEH 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2485612693 176 ELTESIKSWVKemGKTVIIASHRMDFVEKVTNkVLWLKEGKVILEGKTEDL 226
Cdd:PRK10789 489 QILHNLRQWGE--GRTVIISAHRLSALTEASE-ILVMQHGHIAQRGNHDQL 536
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1-210 |
4.33e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 74.74 E-value: 4.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 1 MLLEVRNLtKVY---KRGNQ-------QIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSL 70
Cdd:PRK15079 7 VLLEVADL-KVHfdiKDGKQwfwqppkTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 71 LK-KPEIIRGRFSFLWEGMQNVYHYLTGEANILYF------AYLNQVPSSVARRRCEELLRKLDLYE-VKDQYVFTYSAG 142
Cdd:PRK15079 86 LGmKDDEWRAVRSDIQMIFQDPLASLNPRMTIGEIiaeplrTYHPKLSRQEVKDRVKAMMLKVGLLPnLINRYPHEFSGG 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2485612693 143 MRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVL 210
Cdd:PRK15079 166 QCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVL 233
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
5-224 |
5.32e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 73.76 E-value: 5.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 5 VRNLTKVYKRGNQQIKandNISFFVERGDVLGILGPNGAGKTTLIK-----------QIATLLIPDQGDILYKGVSLLKK 73
Cdd:PRK15056 9 VNDVTVTWRNGHTALR---DASFTVPGGSIAALVGVNGSGKSTLFKalmgfvrlasgKISILGQPTRQALQKNLVAYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 74 PEIIRGRFSFLWEGMQNVYHYltGEANILyfaylnQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCL 153
Cdd:PRK15056 86 SEEVDWSFPVLVEDVVMMGRY--GHMGWL------RRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2485612693 154 INDPEVVFLDEPLSGLDVLAAAELTESIKSwVKEMGKTVIIASHRMDFVEKVTNKVLWLKeGKVILEGKTE 224
Cdd:PRK15056 158 AQQGQVILLDEPFTGVDVKTEARIISLLRE-LRDEGKTMLVSTHNLGSVTEFCDYTVMVK-GTVLASGPTE 226
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-255 |
6.46e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 73.30 E-value: 6.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYKrgNQQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGD---ILYKGVSLLKKPEI-IR 78
Cdd:PRK13640 6 VEFKHVSFTYP--DSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWdIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 79 GRFSFLWEGMQNVYHYLTGEANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPE 158
Cdd:PRK13640 84 EKVGIVFQNPDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 159 VVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEkVTNKVLWLKEGKVILEG-------KTEDLKNLSK 231
Cdd:PRK13640 164 IIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGspveifsKVEMLKEIGL 242
|
250 260 270
....*....|....*....|....*....|....*
gi 2485612693 232 E----EEYILYLRNSA-------KAREKLRKYELQ 255
Cdd:PRK13640 243 DipfvYKLKNKLKEKGisvpqeiNTEEKLVQYLCQ 277
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
23-246 |
7.07e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 74.99 E-value: 7.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 23 DNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKG---VSLLKK--PEIIRGR-FSFLWEGMQNVYHYLT 96
Cdd:PRK11147 20 DNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQdliVARLQQdpPRNVEGTvYDFVAEGIEEQAEYLK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 97 GeanilYFAYLNQV---PSSVARRRCEELLRKLD----------LYEV-------KDQYVFTYSAGMRKKLAIATCLIND 156
Cdd:PRK11147 100 R-----YHDISHLVetdPSEKNLNELAKLQEQLDhhnlwqlenrINEVlaqlgldPDAALSSLSGGWLRKAALGRALVSN 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 157 PEVVFLDEPLSGLDVlaaaELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVI---------LEGKTEDL- 226
Cdd:PRK11147 175 PDVLLLDEPTNHLDI----ETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVsypgnydqyLLEKEEALr 250
|
250 260 270
....*....|....*....|....*....|
gi 2485612693 227 ----------KNLSKEEEYIlylRNSAKAR 246
Cdd:PRK11147 251 veelqnaefdRKLAQEEVWI---RQGIKAR 277
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
2-233 |
7.10e-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: 74.86 E-value: 7.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVYKrgnqQIKANDNISFFVERGDVLGILGPNGAGKTTLIKqIATLLIPD---QGDILYKGVSL----LKKP 74
Cdd:TIGR02633 1 LLEMKGIVKTFG----GVKALDGIDLEVRPGECVGLCGENGAGKSTLMK-ILSGVYPHgtwDGEIYWSGSPLkasnIRDT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 75 E-----IIRGRFSFLWE--GMQNVY--HYLTGEANILYFAYLNqvpssvarRRCEELLRKLDLYEVKD-QYVFTYSAGMR 144
Cdd:TIGR02633 76 EragivIIHQELTLVPElsVAENIFlgNEITLPGGRMAYNAMY--------LRAKNLLRELQLDADNVtRPVGDYGGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 145 KKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSwVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVIlegKTE 224
Cdd:TIGR02633 148 QLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRD-LKAHGVACVYISHKLNEVKAVCDTICVIRDGQHV---ATK 223
|
....*....
gi 2485612693 225 DLKNLSKEE 233
Cdd:TIGR02633 224 DMSTMSEDD 232
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
32-225 |
7.56e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 74.92 E-value: 7.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 32 GDVLGILGPNGAGKTTLIKQIATLLIPD--QGDILYKGVSLLKKpeiIRGRFSFLWEGmQNVYHYLTGEANILYFAYLnQ 109
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQ---ILKRTGFVTQD-DILYPHLTVRETLVFCSLL-R 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 110 VPSSVAR----RRCEELLRKLDLYE-----VKDQYVFTYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTES 180
Cdd:PLN03211 169 LPKSLTKqekiLVAESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLT 248
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2485612693 181 IKSwVKEMGKTVIIASHR-MDFVEKVTNKVLWLKEGKVILEGKTED 225
Cdd:PLN03211 249 LGS-LAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGRCLFFGKGSD 293
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
24-226 |
8.06e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 73.13 E-value: 8.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 24 NISFfvERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDI------LYKGVS------LLKKPEIIrgrFSF----LWEG 87
Cdd:PRK13634 27 NVSI--PSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVtigervITAGKKnkklkpLRKKVGIV---FQFpehqLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 88 mqnvyhylTGEANILyFAYLN-QVPSSVARRRCEELLRKLDLYE-VKDQYVFTYSAGMRKKLAIATCLINDPEVVFLDEP 165
Cdd:PRK13634 102 --------TVEKDIC-FGPMNfGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2485612693 166 LSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDL 226
Cdd:PRK13634 173 TAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
3-218 |
1.32e-14 |
|
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: 71.37 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYkRGNQQiKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKP-EIIRGRF 81
Cdd:cd03244 3 IEFKNVSLRY-RPNLP-PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGlHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 82 S------FLWEGM--QNV--YHYLTGEAnilyfayLNQVPSSVA-RRRCEELLRKLDLYEVKDQYVFtySAGMRKKLAIA 150
Cdd:cd03244 81 SiipqdpVLFSGTirSNLdpFGEYSDEE-------LWQALERVGlKEFVESLPGGLDTVVEEGGENL--SVGQRQLLCLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2485612693 151 TCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKemGKTVIIASHR----MDFvekvtNKVLWLKEGKVI 218
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPETDALIQKTIREAFK--DCTVLTIAHRldtiIDS-----DRILVLDKGRVV 216
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-233 |
1.48e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 71.87 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYkrGNQQIKANDNISffVERGDVLGILGPNGAGKTTLIKQIATL--LIPD---QGDILYKGVSLLKKPEI- 76
Cdd:PRK14247 4 IEIRDLKVSF--GQVEVLDGVNLE--IPDNTITALMGPSGSGKSTLLRVFNRLieLYPEarvSGEVYLDGQDIFKMDVIe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 77 IRGRFSFLWEgMQNVYHYLTGEANILYFAYLNQVPSSVA--RRRCEELLRKLDLY-EVKDQY---VFTYSAGMRKKLAIA 150
Cdd:PRK14247 80 LRRRVQMVFQ-IPNPIPNLSIFENVALGLKLNRLVKSKKelQERVRWALEKAQLWdEVKDRLdapAGKLSGGQQQRLCIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 151 TCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMgkTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDLKNLS 230
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNP 236
|
...
gi 2485612693 231 KEE 233
Cdd:PRK14247 237 RHE 239
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
2-230 |
1.74e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 72.03 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVY-------KRGNQQIKanDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSL--LK 72
Cdd:PRK10419 3 LLNVSGLSHHYahgglsgKHQHQTVL--NNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLakLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 73 KpeiiRGRFSFLWEgMQNVYHYLTGEAN-------ILY--FAYLNQVPSSVARRRCEELLRKLDL-YEVKDQYVFTYSAG 142
Cdd:PRK10419 81 R----AQRKAFRRD-IQMVFQDSISAVNprktvreIIRepLRHLLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 143 MRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGK 222
Cdd:PRK10419 156 QLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQP 235
|
....*...
gi 2485612693 223 TEDLKNLS 230
Cdd:PRK10419 236 VGDKLTFS 243
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-233 |
1.85e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 72.00 E-value: 1.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 4 EVRNLTKVYKRGNQQIKANDnISFFVERGDVLGILGPNGAGKTTLIKQIATLL------IPDQGDILYKGVSLLKKPEI- 76
Cdd:PRK14246 9 DVFNISRLYLYINDKAILKD-ITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIeiydskIKVDGKVLYFGKDIFQIDAIk 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 77 IRGRFSFLWEgMQNVYHYLTGEANILYFAYLNQVPSSVARRR-CEELLRKLDLY-EVKDQY---VFTYSAGMRKKLAIAT 151
Cdd:PRK14246 88 LRKEVGMVFQ-QPNPFPHLSIYDNIAYPLKSHGIKEKREIKKiVEECLRKVGLWkEVYDRLnspASQLSGGQQQRLTIAR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 152 CLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMgkTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDLKNLSK 231
Cdd:PRK14246 167 ALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPK 244
|
..
gi 2485612693 232 EE 233
Cdd:PRK14246 245 NE 246
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
2-225 |
1.87e-14 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 71.69 E-value: 1.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTkvYKRGNQQIKanDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSL--LKKPEIIRG 79
Cdd:COG4559 1 MLEAENLS--VRLGGRTLL--DDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLaaWSPWELARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 80 R----------FSFL-WE--GMqNVYHYLTGEANilyfaylnqvpssvARRRCEELLRKLDLYEVKDQYVFTYSAGMRKK 146
Cdd:COG4559 77 RavlpqhsslaFPFTvEEvvAL-GRAPHGSSAAQ--------------DRQIVREALALVGLAHLAGRSYQTLSGGEQQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 147 --LAIATCLINDPE-----VVFLDEPLSGLD------VLAAAeltesiKSWVKEMGKTVII------ASHRMDfvekvtn 207
Cdd:COG4559 142 vqLARVLAQLWEPVdggprWLFLDEPTSALDlahqhaVLRLA------RQLARRGGGVVAVlhdlnlAAQYAD------- 208
|
250
....*....|....*...
gi 2485612693 208 KVLWLKEGKVILEGKTED 225
Cdd:COG4559 209 RILLLHQGRLVAQGTPEE 226
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-197 |
2.14e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 73.30 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 29 VERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGvsllKKPEIIRgRFSflweG--MQNvyhYLTGEAN-----I 101
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEP----SWDEVLK-RFR----GteLQN---YFKKLYNgeikvV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 102 LYFAYLNQVPSSV------------ARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVVFLDEPLSGL 169
Cdd:PRK13409 164 HKPQYVDLIPKVFkgkvrellkkvdERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYL 243
|
170 180 190
....*....|....*....|....*....|.
gi 2485612693 170 DV---LAAAELtesIKSWVKemGKTVIIASH 197
Cdd:PRK13409 244 DIrqrLNVARL---IRELAE--GKYVLVVEH 269
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-197 |
2.14e-14 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 73.28 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 30 ERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGvsllKKPEIIRgRFSflweGMQnVYHYLTGEAN-----ILYF 104
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEP----SWDEVLK-RFR----GTE-LQDYFKKLANgeikvAHKP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 105 AYLNQVPSSVA------------RRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDV- 171
Cdd:COG1245 167 QYVDLIPKVFKgtvrellekvdeRGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIy 246
|
170 180
....*....|....*....|....*...
gi 2485612693 172 --LAAAELtesIKSWVKEmGKTVIIASH 197
Cdd:COG1245 247 qrLNVARL---IRELAEE-GKYVLVVEH 270
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
2-217 |
3.87e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 72.55 E-value: 3.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTkVYKRGNQQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLiPDQ--GDILYKGVSL-LKKP-EII 77
Cdd:TIGR02633 257 ILEARNLT-CWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAY-PGKfeGNVFINGKPVdIRNPaQAI 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 78 RGRFSFLWEGMQN--------VYHYLTgEANILYFAYLNQVPSSVARRRCEELLRKLDLYEVK-DQYVFTYSAGMRKKLA 148
Cdd:TIGR02633 335 RAGIAMVPEDRKRhgivpilgVGKNIT-LSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASpFLPIGRLSGGNQQKAV 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2485612693 149 IATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEmGKTVIIASHRMDFVEKVTNKVLWLKEGKV 217
Cdd:TIGR02633 414 LAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
6-222 |
4.12e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 71.98 E-value: 4.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 6 RNLTKVYkrGNQQIKANDNISffVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEIIRGRfsflw 85
Cdd:PRK11000 7 RNVTKAY--GDVVISKDINLD--IHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGV----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 86 eGM--QN--VYHYLTGEANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVVF 161
Cdd:PRK11000 78 -GMvfQSyaLYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2485612693 162 LDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHrmDFVEKVT--NKVLWLKEGKVILEGK 222
Cdd:PRK11000 157 LDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTH--DQVEAMTlaDKIVVLDAGRVAQVGK 217
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
7-226 |
4.23e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 70.79 E-value: 4.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 7 NLTKVYkrGNQQIKANDNISffVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKG--VSLLKKPEIIRgRFSFL 84
Cdd:PRK10253 12 QLTLGY--GKYTVAENLTVE--IPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGehIQHYASKEVAR-RIGLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 85 wegMQNVYhyLTGEANILYFAYLNQVPSS--VARRRCEE------LLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLIND 156
Cdd:PRK10253 87 ---AQNAT--TPGDITVQELVARGRYPHQplFTRWRKEDeeavtkAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 157 PEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDL 226
Cdd:PRK10253 162 TAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
24-229 |
5.23e-14 |
|
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: 72.64 E-value: 5.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 24 NISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKG-VSLLKKpeiirgrFSFLWEGmqnvyhylTGEANIL 102
Cdd:TIGR01271 444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGrISFSPQ-------TSWIMPG--------TIKDNII 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 103 YFAYLNQVPSSVARRRCeELLRKLDLYEVKDQYVF-----TYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAEL 177
Cdd:TIGR01271 509 FGLSYDEYRYTSVIKAC-QLEEDIALFPEKDKTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEI 587
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2485612693 178 TESikSWVKEM-GKTVIIASHRMDFVEKvTNKVLWLKEGKVILEGKTEDLKNL 229
Cdd:TIGR01271 588 FES--CLCKLMsNKTRILVTSKLEHLKK-ADKILLLHEGVCYFYGTFSELQAK 637
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-227 |
7.22e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 72.08 E-value: 7.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 4 EVRNLTKVYkrGNQQikANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKP--EIIRGRF 81
Cdd:NF033858 3 RLEGVSHRY--GKTV--ALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARhrRAVCPRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 82 SFLWEGM-QNVYHYLTGEANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVV 160
Cdd:NF033858 79 AYMPQGLgKNLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2485612693 161 FLDEPLSGLDVLAAA---ELTESIKSWVKEMgkTVIIASHRMDFVEKVTnkvlWL---KEGKVILEGKTEDLK 227
Cdd:NF033858 159 ILDEPTTGVDPLSRRqfwELIDRIRAERPGM--SVLVATAYMEEAERFD----WLvamDAGRVLATGTPAELL 225
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-226 |
7.89e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 71.66 E-value: 7.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVYKRGNQQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLL-----IPDQGDILYKGVSLLKKPEI 76
Cdd:PRK15134 5 LLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLpsppvVYPSGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 77 ----IRG-RFSFLW-EGMQNVYHYLTGEANILYFAYLNQVPSSVARRrcEELLRKLDLYEVKD------QYVFTYSAGMR 144
Cdd:PRK15134 85 tlrgVRGnKIAMIFqEPMVSLNPLHTLEKQLYEVLSLHRGMRREAAR--GEILNCLDRVGIRQaakrltDYPHQLSGGER 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 145 KKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTE 224
Cdd:PRK15134 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAA 242
|
..
gi 2485612693 225 DL 226
Cdd:PRK15134 243 TL 244
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-217 |
1.02e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 70.88 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 1 MLLEVRNLTKVYkrGNQQIKanDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKG--VSLLKKpeiiR 78
Cdd:PRK10851 1 MSIEIANIKKSF--GRTQVL--NDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGtdVSRLHA----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 79 GR---FSFlwegmQN--VYHYLTGEANI---LYFAYLNQVPSSVA-RRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAI 149
Cdd:PRK10851 73 DRkvgFVF-----QHyaLFRHMTVFDNIafgLTVLPRRERPNAAAiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2485612693 150 ATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKV 217
Cdd:PRK10851 148 ARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-239 |
1.04e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 70.12 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 23 DNISFFVERGDVLGILGPNGAGKTTLIKQIATLliPDQ-------GDILYKGVSLLKKPEII--RGRFSFLWEgMQNVYH 93
Cdd:PRK14271 38 DQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRM--NDKvsgyrysGDVLLGGRSIFNYRDVLefRRRVGMLFQ-RPNPFP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 94 yLTGEANILYFAYLNQ-VPSSVARRRCEELLRKLDLYE-VKDQYV---FTYSAGMRKKLAIATCLINDPEVVFLDEPLSG 168
Cdd:PRK14271 115 -MSIMDNVLAGVRAHKlVPRKEFRGVAQARLTEVGLWDaVKDRLSdspFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2485612693 169 LDVLAAAELTESIKSWVKEMgkTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDLKNLSKEEEYILYL 239
Cdd:PRK14271 194 LDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYV 262
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
2-232 |
1.05e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 70.12 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVYKRgNQQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEI-IRGR 80
Cdd:PRK13642 4 ILEVENLVFKYEK-ESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWnLRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 81 FSFLWEGMQNVYHYLTGEANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVV 160
Cdd:PRK13642 83 IGMVFQNPDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEII 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2485612693 161 FLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKvTNKVLWLKEGKVILEGKTEDLKNLSKE 232
Cdd:PRK13642 163 ILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSED 233
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
23-226 |
1.16e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 69.78 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 23 DNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKP-EIIRGRFSFLWEGMQNVYHYLTGEANI 101
Cdd:PRK13648 26 KDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNfEKLRKHIGIVFQNPDNQFVGSIVKYDV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 102 LYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESI 181
Cdd:PRK13648 106 AFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLV 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2485612693 182 KSWVKEMGKTVIIASHrmDFVEKV-TNKVLWLKEGKVILEGKTEDL 226
Cdd:PRK13648 186 RKVKSEHNITIISITH--DLSEAMeADHVIVMNKGTVYKEGTPTEI 229
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-231 |
1.39e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 69.29 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLtKVYKRGNQQIKandNISFFVERGDVLGILGPNGAGKTTLIKQIA-----TLLipdQGDILYKGVSLLKK-PE 75
Cdd:CHL00131 7 ILEIKNL-HASVNENEILK---GLNLSINKGEIHAIMGPNGSGKSTLSKVIAghpayKIL---EGDILFKGESILDLePE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 76 IIRGRFSFLweGMQNVYHyLTGEANI--LYFAY-----LNQVPSSVARRRCEELLRKLDLyeVKDQYVFT-------YSA 141
Cdd:CHL00131 80 ERAHLGIFL--AFQYPIE-IPGVSNAdfLRLAYnskrkFQGLPELDPLEFLEIINEKLKL--VGMDPSFLsrnvnegFSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 142 GMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSwVKEMGKTVIIASHRMDFVEKVT-NKVLWLKEGKVILE 220
Cdd:CHL00131 155 GEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINK-LMTSENSIILITHYQRLLDYIKpDYVHVMQNGKIIKT 233
|
250
....*....|.
gi 2485612693 221 GKTEDLKNLSK 231
Cdd:CHL00131 234 GDAELAKELEK 244
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
3-216 |
1.61e-13 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 68.26 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYKRGNQQIKAN-DNISFFVERGDVLGILGPNGAGKTTLIKQIAtllipdqGDI-LYKGVSllkkpeIIRGR 80
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTlKDINLEVPKGELVAIVGPVGSGKSSLLSALL-------GELeKLSGSV------SVPGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 81 FSFL----WegMQNvyhyLTGEANILYFAYLNQvpssvarRRCEE------LLRKLDLYEVKDQYV-----FTYSAGMRK 145
Cdd:cd03250 68 IAYVsqepW--IQN----GTIRENILFGKPFDE-------ERYEKvikacaLEPDLEILPDGDLTEigekgINLSGGQKQ 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2485612693 146 KLAIATCLINDPEVVFLDEPLSGLDVLAAAELTES-IKSWVKEmGKTVIIASHRMDFVEKVtNKVLWLKEGK 216
Cdd:cd03250 135 RISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENcILGLLLN-NKTRILVTHQLQLLPHA-DQIVVLDNGR 204
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3-220 |
1.74e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 68.94 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYkrGNQQIKanDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEIIRGRFS 82
Cdd:PRK11247 13 LLLNAVSKRY--GERTVL--NQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRLMFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 83 ----FLWEG-MQNVYHYLTGEAnilyfaylnqvpssvaRRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDP 157
Cdd:PRK11247 89 darlLPWKKvIDNVGLGLKGQW----------------RDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2485612693 158 EVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHrmDFVEKVT--NKVLWLKEGKVILE 220
Cdd:PRK11247 153 GLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTH--DVSEAVAmaDRVLLIEEGKIGLD 215
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-239 |
1.82e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 70.43 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTkvykrGNQQIKandNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSL-LKKP-EIIRG 79
Cdd:COG1129 256 VLEVEGLS-----VGGVVR---DVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVrIRSPrDAIRA 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 80 RFSFLWE--------GMQNVYHYLTGeANILYFAYLNQVPSSVARRRCEELLRKLDlyeVK----DQYVFTYSAGMRKKL 147
Cdd:COG1129 328 GIAYVPEdrkgeglvLDLSIRENITL-ASLDRLSRGGLLDRRRERALAEEYIKRLR---IKtpspEQPVGNLSGGNQQKV 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 148 AIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEmGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDLk 227
Cdd:COG1129 404 VLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIVGELDREEA- 481
|
250
....*....|..
gi 2485612693 228 nlskEEEYILYL 239
Cdd:COG1129 482 ----TEEAIMAA 489
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
2-233 |
1.82e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 70.34 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVYKrgnqQIKANDNISFFVERGDVLGILGPNGAGKTTLIKqIATLLIPD---QGDILYKGVSL----LKKP 74
Cdd:PRK13549 5 LLEMKNITKTFG----GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMK-VLSGVYPHgtyEGEIIFEGEELqasnIRDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 75 E-----IIRGRFSFLWEgmqnvyhyLTGEANIlyfaYLNQVPSSVAR-------RRCEELLRKLDLYEVKDQYVFTYSAG 142
Cdd:PRK13549 80 EragiaIIHQELALVKE--------LSVLENI----FLGNEITPGGImdydamyLRAQKLLAQLKLDINPATPVGNLGLG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 143 MRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSwVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVIlegK 222
Cdd:PRK13549 148 QQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRD-LKAHGIACIYISHKLNEVKAISDTICVIRDGRHI---G 223
|
250
....*....|.
gi 2485612693 223 TEDLKNLSKEE 233
Cdd:PRK13549 224 TRPAAGMTEDD 234
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-228 |
1.98e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 70.58 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVYKrgnqQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEIIRGRF 81
Cdd:PRK09700 5 YISMAGIGKSFG----PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 82 sflweGMQNVYHYLT--GEANILYFAYLNQVPS-----------SVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLA 148
Cdd:PRK09700 81 -----GIGIIYQELSviDELTVLENLYIGRHLTkkvcgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 149 IATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEmGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDLKN 228
Cdd:PRK09700 156 IAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSN 234
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
3-221 |
3.04e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 68.17 E-value: 3.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLT-KVykrGNQQIKanDNISFFVERGDVLGILGPNGAGKTTLIKQIATllIPD----QGDILYKGVSLLKKPEII 77
Cdd:COG0396 1 LEIKNLHvSV---EGKEIL--KGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMG--HPKyevtSGSILLDGEDILELSPDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 78 RGRFS-FLweGMQN--------VYHYLTGEANILYfayLNQVPSSVARRRCEELLRKLDL-YEVKDQYV---FtySAGMR 144
Cdd:COG0396 74 RARAGiFL--AFQYpveipgvsVSNFLRTALNARR---GEELSAREFLKLLKEKMKELGLdEDFLDRYVnegF--SGGEK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 145 KKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSwVKEMGKTVIIASH--RM-DFVekVTNKVLWLKEGKVILEG 221
Cdd:COG0396 147 KRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNK-LRSPDRGILIITHyqRIlDYI--KPDFVHVLVDGRIVKSG 223
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-253 |
3.29e-13 |
|
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: 69.96 E-value: 3.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 7 NLTKVYKrGNQQIKANDNISFFveRGDVLGILGPNGAGKTTLIKQIATLLIPDQGDIL----YKGVSLLKKPEI-----I 77
Cdd:TIGR03719 9 RVSKVVP-PKKEILKDISLSFF--PGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARpqpgIKVGYLPQEPQLdptktV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 78 RGRFSflwEGMQNVYHYLTgEANILYFAY------LNQVPSSVARrrCEELLRKLDLYEV---------------KDQYV 136
Cdd:TIGR03719 86 RENVE---EGVAEIKDALD-RFNEISAKYaepdadFDKLAAEQAE--LQEIIDAADAWDLdsqleiamdalrcppWDADV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 137 FTYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDvlaaAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVL------ 210
Cdd:TIGR03719 160 TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILeldrgr 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2485612693 211 ----------WL--KEGKVILEGKTED--LKNLSKEEEYIlylRNSAKARE-----KLRKYE 253
Cdd:TIGR03719 236 gipwegnyssWLeqKQKRLEQEEKEESarQKTLKRELEWV---RQSPKGRQakskaRLARYE 294
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1-226 |
5.03e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 67.85 E-value: 5.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 1 MLLEVRNLTKVYKRGNQ-QIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLL---KKPEI 76
Cdd:PRK13649 1 MGINLQNVSYTYQAGTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsKNKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 77 --IRGRFSFLWEGMQNvyhYLTGEANILYFAYLNQ---VPSSVARRRCEELLRKLDLYE-VKDQYVFTYSAGMRKKLAIA 150
Cdd:PRK13649 81 kqIRKKVGLVFQFPES---QLFEETVLKDVAFGPQnfgVSQEEAEALAREKLALVGISEsLFEKNPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2485612693 151 TCLINDPEVVFLDEPLSGLDVLAAAELTESIKSwVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDL 226
Cdd:PRK13649 158 GILAMEPKILVLDEPTAGLDPKGRKELMTLFKK-LHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-224 |
6.60e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 67.17 E-value: 6.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLtKVYKRGNQQIKAndnISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQ-----GDILYKGVSLLKK---P 74
Cdd:PRK14267 5 IETVNL-RVYYGSNHVIKG---VDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIYSPdvdP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 75 EIIRGRFSFLWEgMQNVYHYLTGEANILYFAYLNQVPSSVAR--RRCEELLRKLDLY-EVKDQ---YVFTYSAGMRKKLA 148
Cdd:PRK14267 81 IEVRREVGMVFQ-YPNPFPHLTIYDNVAIGVKLNGLVKSKKEldERVEWALKKAALWdEVKDRlndYPSNLSGGQRQRLV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2485612693 149 IATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMgkTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTE 224
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTR 233
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
24-212 |
7.38e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 67.06 E-value: 7.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 24 NISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKG----------VSLLKKPEIIRGRFSFLWEGMQnvyh 93
Cdd:PRK09544 22 DVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGklrigyvpqkLYLDTTLPLTVNRFLRLRPGTK---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 94 yltgEANILyfaylnqvpSSVARRRCEELLrkldlyevkDQYVFTYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDVLA 173
Cdd:PRK09544 98 ----KEDIL---------PALKRVQAGHLI---------DAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNG 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 2485612693 174 AAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWL 212
Cdd:PRK09544 156 QVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL 194
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2-226 |
9.35e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 68.54 E-value: 9.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVYKrGNQQIKAndnISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLK-KPEIIR-- 78
Cdd:PRK15439 11 LLCARSISKQYS-GVEVLKG---IDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARlTPAKAHql 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 79 GRFSFLWEGMqnVYHYLTGEANILYfaylnQVP-SSVARRRCEELLRKLD----------LYEVKDQYVftysagmrkkL 147
Cdd:PRK15439 87 GIYLVPQEPL--LFPNLSVKENILF-----GLPkRQASMQKMKQLLAALGcqldldssagSLEVADRQI----------V 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2485612693 148 AIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSwVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDL 226
Cdd:PRK15439 150 EILRGLMRDSRILILDEPTASLTPAETERLFSRIRE-LLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-200 |
1.18e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 66.28 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 1 MLLEVRNLTkvYKRGNQQIKanDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLK-KPEIIRG 79
Cdd:PRK10247 6 PLLQLQNVG--YLAGDAKIL--NNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTlKPEIYRQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 80 RFSFLWEGMQnvyhyLTGEA--NILYFAYL--NQVPSSVArrrceeLLRKLDLYEVKD----QYVFTYSAGMRKKLAIAT 151
Cdd:PRK10247 82 QVSYCAQTPT-----LFGDTvyDNLIFPWQirNQQPDPAI------FLDDLERFALPDtiltKNIAELSGGEKQRISLIR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2485612693 152 CLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMD 200
Cdd:PRK10247 151 NLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKD 199
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-217 |
1.51e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 67.65 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTkVYKRGNQQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLiPD--QGDILYKGvsllkKPEIIRGR 80
Cdd:PRK13549 260 LEVRNLT-AWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAY-PGrwEGEIFIDG-----KPVKIRNP 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 81 FSFLWEGM---------------QNVYHYLTgEANILYFAYLNQVPSSVARRRCEELLRKLdlyEVK----DQYVFTYSA 141
Cdd:PRK13549 333 QQAIAQGIamvpedrkrdgivpvMGVGKNIT-LAALDRFTGGSRIDDAAELKTILESIQRL---KVKtaspELAIARLSG 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2485612693 142 GMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEmGKTVIIASHRMDFVEKVTNKVLWLKEGKV 217
Cdd:PRK13549 409 GNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-197 |
2.60e-12 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 65.47 E-value: 2.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 32 GDVLGILGPNGAGKTTLIKQIATLLIPDQGdilykgvSLLKKP---EIIRgrfSFLWEGMQNVYHYLTGE--ANILYFAY 106
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLG-------KFDDPPdwdEILD---EFRGSELQNYFTKLLEGdvKVIVKPQY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 107 LNQVPSSVA------------RRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDV--- 171
Cdd:cd03236 96 VDLIPKAVKgkvgellkkkdeRGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIkqr 175
|
170 180
....*....|....*....|....*.
gi 2485612693 172 LAAAELtesIKSWVKEmGKTVIIASH 197
Cdd:cd03236 176 LNAARL---IRELAED-DNYVLVVEH 197
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-217 |
2.80e-12 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 63.99 E-value: 2.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTkvykrgnqQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKP--EIIRg 79
Cdd:cd03215 4 VLEVRGLS--------VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSprDAIR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 80 rfsflwEGMQnvyhYLTGEanilyfaylnqvpssvarRRCEELLRKLDLYE---VKDQYvftySAGMRKKLAIATCLIND 156
Cdd:cd03215 75 ------AGIA----YVPED------------------RKREGLVLDLSVAEniaLSSLL----SGGNQQKVVLARWLARD 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2485612693 157 PEVVFLDEPLSGLDVLAAAELTESIKSwVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKV 217
Cdd:cd03215 123 PRVLILDEPTRGVDVGAKAEIYRLIRE-LADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
32-271 |
3.12e-12 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 67.18 E-value: 3.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 32 GDVLGILGPNGAGKTTLIKQIATLLIPD--QGDILYKGVSllKKPEIIrGRFSFLWEgmQNVYH--YLTGEANILYFAYL 107
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFP--KKQETF-ARISGYCE--QNDIHspQVTVRESLIYSAFL 980
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 108 nQVPSSVAR----RRCEELLRKLDLYEVKDQYV-----FTYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELT 178
Cdd:PLN03140 981 -RLPKEVSKeekmMFVDEVMELVELDNLKDAIVglpgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVM 1059
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 179 ESIKSWVkEMGKTVIIASHR--MDFVEKVTNKVLWLKEGKVILEGKTEdlKNLSKEEEYILYLRNSAKAREKLRKYELQF 256
Cdd:PLN03140 1060 RTVRNTV-DTGRTVVCTIHQpsIDIFEAFDELLLMKRGGQVIYSGPLG--RNSHKIIEYFEAIPGVPKIKEKYNPATWML 1136
|
250
....*....|....*
gi 2485612693 257 EILSdvtLKTTLRLG 271
Cdd:PLN03140 1137 EVSS---LAAEVKLG 1148
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
3-226 |
4.07e-12 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 66.58 E-value: 4.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYKRGNQQikANDNISFFVERGDVLGILGPNGAGKTTlikqIATLLIP----DQGDILYKGVSLLK-KPEII 77
Cdd:PRK11176 342 IEFRNVTFTYPGKEVP--ALRNINFKIPAGKTVALVGRSGSGKST----IANLLTRfydiDEGEILLDGHDLRDyTLASL 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 78 RGRFSFLwegMQNVYHYLTGEANILYFAYLNQVpssvARRRCEELLR---KLDLYEVKDQYVFT--------YSAGMRKK 146
Cdd:PRK11176 416 RNQVALV---SQNVHLFNDTIANNIAYARTEQY----SREQIEEAARmayAMDFINKMDNGLDTvigengvlLSGGQRQR 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 147 LAIATCLINDPEVVFLDEPLSGLDvlaaaelTES---IKSWVKEMGK--TVIIASHRMDFVEKvTNKVLWLKEGKVILEG 221
Cdd:PRK11176 489 IAIARALLRDSPILILDEATSALD-------TESeraIQAALDELQKnrTSLVIAHRLSTIEK-ADEILVVEDGEIVERG 560
|
....*
gi 2485612693 222 KTEDL 226
Cdd:PRK11176 561 THAEL 565
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-208 |
4.36e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 65.19 E-value: 4.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTkVYKRGNQQIKandNISFFVERGDVLGILGPNGAGKTTLIKQIATL--LIPD---QGDILYKGVSLLKK--- 73
Cdd:PRK14243 10 VLRTENLN-VYYGSFLAVK---NVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGfrvEGKVTFHGKNLYAPdvd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 74 PEIIRGRFSFLWEG----MQNVYHyltgeaNILYFAYLNQVPSSVaRRRCEELLRKLDLY-EVKD---QYVFTYSAGMRK 145
Cdd:PRK14243 86 PVEVRRRIGMVFQKpnpfPKSIYD------NIAYGARINGYKGDM-DELVERSLRQAALWdEVKDklkQSGLSLSGGQQQ 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2485612693 146 KLAIATCLINDPEVVFLDEPLSGLDVLAaaelTESIKSWVKEMGK--TVIIASHRMDFVEKVTNK 208
Cdd:PRK14243 159 RLCIARAIAVQPEVILMDEPCSALDPIS----TLRIEELMHELKEqyTIIIVTHNMQQAARVSDM 219
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
24-217 |
1.19e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.07 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 24 NISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKG--VSLLKKPEIIRGRFSFLWEGMQNVYHYLtgEA-- 99
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGkeINALSTAQRLARGLVYLPEDRQSSGLYL--DApl 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 100 --NILYFAYlNQVP----SSVARRRCEELLRKLDL-YEVKDQYVFTYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDVL 172
Cdd:PRK15439 359 awNVCALTH-NRRGfwikPARENAVLERYRRALNIkFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVS 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2485612693 173 AAAELTESIKSwVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKV 217
Cdd:PRK15439 438 ARNDIYQLIRS-IAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
3-218 |
1.24e-11 |
|
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: 62.81 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYkrGNQQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKP-EIIRGRF 81
Cdd:cd03369 7 IEVENLSVRY--APDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPlEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 82 SFlwegmqnvyhyltgeanilyfayLNQVPSSVArrrcEELLRKLDLY-EVKDQYVFT----------YSAGMRKKLAIA 150
Cdd:cd03369 85 TI-----------------------IPQDPTLFS----GTIRSNLDPFdEYSDEEIYGalrvsegglnLSQGQRQLLCLA 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2485612693 151 TCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKemGKTVIIASHRM----DFvekvtNKVLWLKEGKVI 218
Cdd:cd03369 138 RALLKRPRVLVLDEATASIDYATDALIQKTIREEFT--NSTILTIAHRLrtiiDY-----DKILVMDAGEVK 202
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-225 |
2.36e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 64.25 E-value: 2.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKvykrgnqqiKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLL-KKPEiirgrf 81
Cdd:PRK10762 258 LKVDNLSG---------PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVtRSPQ------ 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 82 sflwEGMQNVYHYLT----GEANIL--------------YFAYlnqvpSSVARRRCEELL---RKLDLYEVK----DQYV 136
Cdd:PRK10762 323 ----DGLANGIVYISedrkRDGLVLgmsvkenmsltalrYFSR-----AGGSLKHADEQQavsDFIRLFNIKtpsmEQAI 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 137 FTYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEmGKTVIIASHRMDFVEKVTNKVLWLKEGK 216
Cdd:PRK10762 394 GLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGR 472
|
....*....
gi 2485612693 217 VILEGKTED 225
Cdd:PRK10762 473 ISGEFTREQ 481
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-197 |
2.98e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 62.10 E-value: 2.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVYKRGNQQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEIIRGRF 81
Cdd:PRK10584 6 IVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 82 -----SFLWEGMQNVyHYLTGEANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLIND 156
Cdd:PRK10584 86 rakhvGFVFQSFMLI-PTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2485612693 157 PEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASH 197
Cdd:PRK10584 165 PDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTH 205
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
23-226 |
3.10e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 62.41 E-value: 3.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 23 DNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPD----QGDILYKGVSLLkkPEIIRGRFSFLWegMQ------NVY 92
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGKPVA--PCALRGRKIATI--MQnprsafNPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 93 HYLTGEAnILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDVL 172
Cdd:PRK10418 96 HTMHTHA-RETCLALGKPADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVV 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2485612693 173 AAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDL 226
Cdd:PRK10418 175 AQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
2-236 |
3.30e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 62.49 E-value: 3.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVYKRGnqqiKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATL--LIPD---QGDILYKGVSL------ 70
Cdd:PRK14239 5 ILQVSDLSVYYNKK----KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIysprtd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 71 ---LKKpEIirgrfsflweGM----QNVYHYLTGEaNILYFAYLNQVP-SSVARRRCEELLRKLDLY-EVKDQY---VFT 138
Cdd:PRK14239 81 tvdLRK-EI----------GMvfqqPNPFPMSIYE-NVVYGLRLKGIKdKQVLDEAVEKSLKGASIWdEVKDRLhdsALG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 139 YSAGMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMgkTVIIASHRMDFVEKVTNKVLWLKEGKVI 218
Cdd:PRK14239 149 LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLI 226
|
250 260
....*....|....*....|.
gi 2485612693 219 LEGKTED--LKNLSKE-EEYI 236
Cdd:PRK14239 227 EYNDTKQmfMNPKHKEtEDYI 247
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
2-226 |
4.29e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 62.84 E-value: 4.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVYKRGNQQIKANDNISFFVERGDVLGILGPNGAGKTtlIKQIATL-LIPDQGDIL-----YKGVSLLKKPE 75
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKS--VSSLAIMgLIDYPGRVMaekleFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 76 -----IIRGRFSFLWEG-MQNVYHYLTGEANILYFAYLNQVPSSVARR-RCEELLRKL---DLYEVKDQYVFTYSAGMRK 145
Cdd:PRK11022 81 kerrnLVGAEVAMIFQDpMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRqRAIDLLNQVgipDPASRLDVYPHQLSGGMSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 146 KLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTED 225
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHD 240
|
.
gi 2485612693 226 L 226
Cdd:PRK11022 241 I 241
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
24-232 |
4.96e-11 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 62.18 E-value: 4.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 24 NISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKG-VSLLKKpeiirgrFSFLWEGmqnvyhylTGEANIL 102
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGrISFSSQ-------FSWIMPG--------TIKENII 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 103 YFAYLNQVPSSVARRRCEeLLRKLDLYEVKDQYVF-----TYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAEL 177
Cdd:cd03291 120 FGVSYDEYRYKSVVKACQ-LEEDITKFPEKDNTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEI 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2485612693 178 TESikSWVKEMG-KTVIIASHRMDFVEKvTNKVLWLKEGKVILEGKTEDLKNLSKE 232
Cdd:cd03291 199 FES--CVCKLMAnKTRILVTSKMEHLKK-ADKILILHEGSSYFYGTFSELQSLRPD 251
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-217 |
5.23e-11 |
|
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: 61.33 E-value: 5.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVYK-RGNQQIKanDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSL-LKKPEIIRG 79
Cdd:cd03248 11 IVKFQNVTFAYPtRPDTLVL--QDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIsQYEHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 80 RFSFLweGMQNVYHYLTGEANILY---FAYLNQVPSSVARRRCEELLRKLDL--YEVKDQYVFTYSAGMRKKLAIATCLI 154
Cdd:cd03248 89 KVSLV--GQEPVLFARSLQDNIAYglqSCSFECVKEAAQKAHAHSFISELASgyDTEVGEKGSQLSGGQKQRVAIARALI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2485612693 155 NDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEmgKTVIIASHRMDFVEKVTNkVLWLKEGKV 217
Cdd:cd03248 167 RNPQVLILDEATSALDAESEQQVQQALYDWPER--RTVLVIAHRLSTVERADQ-ILVLDGGRI 226
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
6-197 |
5.52e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.59 E-value: 5.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 6 RNLTKvykrgNQQIKAN-----DNISFFVERGDVLGILGPNGAGKTTLIKQIA---TLLIPDQGDILYKGVSLLKKPEII 77
Cdd:TIGR00956 763 RNLTY-----EVKIKKEkrvilNNVDGWVKPGTLTALMGASGAGKTTLLNVLAervTTGVITGGDRLVNGRPLDSSFQRS 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 78 RGRFSflwegmQNVYHY--LTGEANILYFAYLNQvPSSVAR----RRCEELLRKLDLYEVKDQYVFTYSAGM----RKKL 147
Cdd:TIGR00956 838 IGYVQ------QQDLHLptSTVRESLRFSAYLRQ-PKSVSKsekmEYVEEVIKLLEMESYADAVVGVPGEGLnveqRKRL 910
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2485612693 148 AIATCLINDPE-VVFLDEPLSGLDVLAAAELTESIKSWVKEmGKTVIIASH 197
Cdd:TIGR00956 911 TIGVELVAKPKlLLFLDEPTSGLDSQTAWSICKLMRKLADH-GQAILCTIH 960
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-235 |
7.57e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 62.53 E-value: 7.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVYKrgNQQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPE-IIRGR 80
Cdd:PRK11160 338 SLTLNNVSFTYP--DQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEaALRQA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 81 FSFLwegMQNVYHYLTGEANILYFA-----------YLNQVpssvarrRCEELL---RKLDLY--EVKDQYvftySAGMR 144
Cdd:PRK11160 416 ISVV---SQRVHLFSATLRDNLLLAapnasdealieVLQQV-------GLEKLLeddKGLNAWlgEGGRQL----SGGEQ 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 145 KKLAIATCLINDPEVVFLDEPLSGLDvlaaAElTES-IKSWVKEM--GKTVIIASHRMDFVEKVTNKVLwLKEGKVILEG 221
Cdd:PRK11160 482 RRLGIARALLHDAPLLLLDEPTEGLD----AE-TERqILELLAEHaqNKTVLMITHRLTGLEQFDRICV-MDNGQIIEQG 555
|
250
....*....|....
gi 2485612693 222 KTEDLknLSKEEEY 235
Cdd:PRK11160 556 THQEL--LAQQGRY 567
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
23-223 |
8.16e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 60.74 E-value: 8.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 23 DNISFFVERGDVLGILGPNGAGKTTLIKQIATLL--IPDQGDILYKGVSLLKKPEIIrgrfsflwegmQNVYHYLTGEAN 100
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGREASLI-----------DAIGRKGDFKDA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 101 IlyfAYLNQVPSSVA---RRRCEELlrkldlyevkdqyvftySAGMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAEL 177
Cdd:COG2401 116 V---ELLNAVGLSDAvlwLRRFKEL-----------------STGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRV 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2485612693 178 TESIKSWVKEMGKTVIIASHRMDFVEkvtnkvlWLKEGKVILEGKT 223
Cdd:COG2401 176 ARNLQKLARRAGITLVVATHHYDVID-------DLQPDLLIFVGYG 214
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
29-209 |
8.23e-11 |
|
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: 59.89 E-value: 8.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 29 VERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPeiirgrfsflwegmqnvyhyltgeanilyfayln 108
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKP---------------------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 109 qvpssvarrrceellrkldlyevkdQYVfTYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEM 188
Cdd:cd03222 68 -------------------------QYI-DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEG 121
|
170 180
....*....|....*....|.
gi 2485612693 189 GKTVIIASHRMDFVEKVTNKV 209
Cdd:cd03222 122 KKTALVVEHDLAVLDYLSDRI 142
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
34-225 |
1.56e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 61.04 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 34 VLGILGPNGAGKTTLIKQIATLLIPDQGDI------LY---KGVSLlkKPEiiRGRFSFLWEGMQNVYHYlTGEANILY- 103
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIvlngrvLFdaeKGICL--PPE--KRRIGYVFQDARLFPHY-KVRGNLRYg 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 104 -----FAYLNQVpssVARRRCEELLrkldlyevkDQYVFTYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELT 178
Cdd:PRK11144 101 maksmVAQFDKI---VALLGIEPLL---------DRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2485612693 179 ESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTED 225
Cdd:PRK11144 169 PYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1-223 |
2.91e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.90 E-value: 2.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 1 MLLEVRNLTKVykrgNQ-QIKandNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKP--EII 77
Cdd:PRK10982 249 VILEVRNLTSL----RQpSIR---DVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNanEAI 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 78 RGRFSFLWEGMQN--VYHYLTGEANILYF---AYLNQVPSSVARRRCEELLRKLDLYEVK----DQYVFTYSAGMRKKLA 148
Cdd:PRK10982 322 NHGFALVTEERRStgIYAYLDIGFNSLISnirNYKNKVGLLDNSRMKSDTQWVIDSMRVKtpghRTQIGSLSGGNQQKVI 401
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2485612693 149 IATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEmGKTVIIASHRMDFVEKVTNKVLWLKEGKV--ILEGKT 223
Cdd:PRK10982 402 IGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLVagIVDTKT 477
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
3-198 |
3.21e-10 |
|
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: 57.93 E-value: 3.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYKRGNQQIKandNISFFVERGDVLGILGPNGAGKTTLIKQIA--------TLLIPDQGDILYkgvsLLKKP 74
Cdd:cd03223 1 IELENLSLATPDGRVLLK---DLSFEIKPGDRLLITGPSGTGKSSLFRALAglwpwgsgRIGMPEGEDLLF----LPQRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 75 EIIRGRfsflwegmqnvyhyltgeanilyfaylnqvpssvarrrceelLRKLDLYEVKDqyvfTYSAGMRKKLAIATCLI 154
Cdd:cd03223 74 YLPLGT------------------------------------------LREQLIYPWDD----VLSGGEQQRLAFARLLL 107
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2485612693 155 NDPEVVFLDEPLSGLDVLAAAELTESIkswvKEMGKTVIIASHR 198
Cdd:cd03223 108 HKPKFVFLDEATSALDEESEDRLYQLL----KELGITVISVGHR 147
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
2-226 |
4.68e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 59.74 E-value: 4.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVYKRGNQQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPD---QGDILYKGVSLLKKPEI-- 76
Cdd:PRK09473 12 LLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKel 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 77 --IRG-RFSFLWEG-MQNVYHYL-TGEANILYFAYLNQVPSSVArrrCEELLRKLDlyEVK--------DQYVFTYSAGM 143
Cdd:PRK09473 92 nkLRAeQISMIFQDpMTSLNPYMrVGEQLMEVLMLHKGMSKAEA---FEESVRMLD--AVKmpearkrmKMYPHEFSGGM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 144 RKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKT 223
Cdd:PRK09473 167 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNA 246
|
...
gi 2485612693 224 EDL 226
Cdd:PRK09473 247 RDV 249
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
32-226 |
5.25e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 59.03 E-value: 5.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 32 GDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLK-KPEIIRGRFSFL------WEGMqnVYHYLTGEANILYF 104
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARKVAYLpqqlpaAEGM--TVRELVAIGRYPWH 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 105 AYLNQVpSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSW 184
Cdd:PRK10575 115 GALGRF-GAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRL 193
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2485612693 185 VKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDL 226
Cdd:PRK10575 194 SQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
23-235 |
5.28e-10 |
|
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: 58.71 E-value: 5.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 23 DNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLK-KPEIIRGRFSF------LWEGmqnvyhyl 95
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlNLRWLRSQIGLvsqepvLFDG-------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 96 TGEANILYFAylNQVPSSVARRRCE-----ELLRKL-DLYE-VKDQYVFTYSAGMRKKLAIATCLINDPEVVFLDEPLSG 168
Cdd:cd03249 92 TIAENIRYGK--PDATDEEVEEAAKkanihDFIMSLpDGYDtLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2485612693 169 LDvlaaaelTESIKSwVKE------MGKTVIIASHRMDFVEKVtNKVLWLKEGKVILEGKTEDLknLSKEEEY 235
Cdd:cd03249 170 LD-------AESEKL-VQEaldramKGRTTIVIAHRLSTIRNA-DLIAVLQNGQVVEQGTHDEL--MAQKGVY 231
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
23-228 |
6.25e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 59.86 E-value: 6.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 23 DNISFFVERGDVLGILGPNGAGKTTLIKqiaTLL--IPDQGDILYKGVSLLK-KPEIIRGRFSflWEGmQNVyHYLTG-- 97
Cdd:PRK11174 367 GPLNFTLPAGQRIALVGPSGAGKTSLLN---ALLgfLPYQGSLKINGIELRElDPESWRKHLS--WVG-QNP-QLPHGtl 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 98 EANIL---YFAYLNQVPSSVARRRCEELLRKLDL---YEVKDQYVfTYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDV 171
Cdd:PRK11174 440 RDNVLlgnPDASDEQLQQALENAWVSEFLPLLPQgldTPIGDQAA-GLSVGQAQRLALARALLQPCQLLLLDEPTASLDA 518
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2485612693 172 LAAAELTESIKSWVKemGKTVIIASHRMDFVEKVtNKVLWLKEGKVILEGKTEDLKN 228
Cdd:PRK11174 519 HSEQLVMQALNAASR--RQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQ 572
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
3-198 |
1.09e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 59.05 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTkVYKRGNQQIKANDNISffVERGDVLGILGPNGAGKTTLIKQIA--------TLLIPDQGDILYkgvsLLKKP 74
Cdd:COG4178 363 LALEDLT-LRTPDGRPLLEDLSLS--LKPGERLLITGPSGSGKSTLLRAIAglwpygsgRIARPAGARVLF----LPQRP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 75 EIIRGrfsflwegmqnvyhylTGEANILYfaylNQVPSSVARRRCEELLRKL-------DLYEVKD-QYVFtySAGMRKK 146
Cdd:COG4178 436 YLPLG----------------TLREALLY----PATAEAFSDAELREALEAVglghlaeRLDEEADwDQVL--SLGEQQR 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2485612693 147 LAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKswvKEMGKTVIIA-SHR 198
Cdd:COG4178 494 LAFARLLLHKPDWLFLDEATSALDEENEAALYQLLR---EELPGTTVISvGHR 543
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
23-197 |
1.30e-09 |
|
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: 56.87 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 23 DNISFFVERGDVLGILGPNGAGKTTLIKQIA----TLLIpdQGDILYKGvslLKKPEIIRGRFSFLwegMQNVYHY--LT 96
Cdd:cd03232 24 NNISGYVKPGTLTALMGESGAGKTTLLDVLAgrktAGVI--TGEILING---RPLDKNFQRSTGYV---EQQDVHSpnLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 97 GEANILYFAYLnqvpssvarrrceellRKLDLYEvkdqyvftysagmRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAE 176
Cdd:cd03232 96 VREALRFSALL----------------RGLSVEQ-------------RKRLTIGVELAAKPSILFLDEPTSGLDSQAAYN 146
|
170 180
....*....|....*....|.
gi 2485612693 177 LTESIKSwVKEMGKTVIIASH 197
Cdd:cd03232 147 IVRFLKK-LADSGQAILCTIH 166
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
23-226 |
2.03e-09 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 58.43 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 23 DNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSllkkpeiIRGRfsflweGMQNVYHYL------- 95
Cdd:PRK13657 352 EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTD-------IRTV------TRASLRRNIavvfqda 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 96 -----TGEANIlyfaylnqvpsSVAR--------RRCEELLRKLDLYEVKDQYVFTY--------SAGMRKKLAIATCLI 154
Cdd:PRK13657 419 glfnrSIEDNI-----------RVGRpdatdeemRAAAERAQAHDFIERKPDGYDTVvgergrqlSGGERQRLAIARALL 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2485612693 155 NDPEVVFLDEPLSGLDVLAAAELTESIKSWVKemGKTVIIASHRMDFVEKVTnKVLWLKEGKVILEGKTEDL 226
Cdd:PRK13657 488 KDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRNAD-RILVFDNGRVVESGSFDEL 556
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-237 |
2.35e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 56.97 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYKrgNQQIKanDNISFFVERGDVLGILGPNGAGKTTLIKQIATLlipdqgdilykgvSLLKKPEIIRGRFS 82
Cdd:PRK14258 8 IKVNNLSFYYD--TQKIL--EGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM-------------NELESEVRVEGRVE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 83 FLwegMQNVYHYltgEANI--------LYFAYLNQVPSSVARRRC------------------EELLRKLDLY-EVKDQY 135
Cdd:PRK14258 71 FF---NQNIYER---RVNLnrlrrqvsMVHPKPNLFPMSVYDNVAygvkivgwrpkleiddivESALKDADLWdEIKHKI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 136 ---VFTYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWL 212
Cdd:PRK14258 145 hksALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFF 224
|
250 260 270
....*....|....*....|....*....|...
gi 2485612693 213 KE-----GKVILEGKTEDLKNL---SKEEEYIL 237
Cdd:PRK14258 225 KGnenriGQLVEFGLTKKIFNSphdSRTREYVL 257
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
24-202 |
2.66e-09 |
|
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: 56.19 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 24 NISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGV---SLLKKPEIIRGRFSFLWEGMQNVYHYLTGEAN 100
Cdd:cd03290 19 NINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKnesEPSFEATRSRNRYSVAYAAQKPWLLNATVEEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 101 ILYFAYLNQVPSSVARRRCEeLLRKLDLYEVKDQYVF-----TYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDV-LAA 174
Cdd:cd03290 99 ITFGSPFNKQRYKAVTDACS-LQPDIDLLPFGDQTEIgergiNLSGGQRQRICVARALYQNTNIVFLDDPFSALDIhLSD 177
|
170 180
....*....|....*....|....*...
gi 2485612693 175 AELTESIKSWVKEMGKTVIIASHRMDFV 202
Cdd:cd03290 178 HLMQEGILKFLQDDKRTLVLVTHKLQYL 205
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
23-210 |
2.93e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 57.87 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 23 DNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKG----------VSLLKKPEI---IRG--RFSFLWEG 87
Cdd:PRK10636 18 DNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawvnqeTPALPQPALeyvIDGdrEYRQLEAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 88 MQNVYHYLTGEANILYFAYLNQVPSSVARRRCEELLRKLDLYEVK-DQYVFTYSAGMRKKLAIATCLINDPEVVFLDEPL 166
Cdd:PRK10636 98 LHDANERNDGHAIATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQlERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPT 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2485612693 167 SGLDVLAAAELtesiKSWVKEMGKTVIIASHRMDFVEKVTNKVL 210
Cdd:PRK10636 178 NHLDLDAVIWL----EKWLKSYQGTLILISHDRDFLDPIVDKII 217
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-63 |
3.29e-09 |
|
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: 57.64 E-value: 3.29e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2485612693 3 LEVRNLTKVYkrGNQQIKanDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDI 63
Cdd:TIGR03719 323 IEAENLTKAF--GDKLLI--DDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI 379
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
19-233 |
3.51e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.43 E-value: 3.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 19 IKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGvsllkKPEIIRGRFSFLWEGMQNVYHYL--T 96
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQG-----KEIDFKSSKEALENGISMVHQELnlV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 97 GEANILYFAYLNQVPS-------SVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVVFLDEPLSGL 169
Cdd:PRK10982 86 LQRSVMDNMWLGRYPTkgmfvdqDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2485612693 170 DVLAAAELTESIKSwVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVIlegKTEDLKNLSKEE 233
Cdd:PRK10982 166 TEKEVNHLFTIIRK-LKERGCGIVYISHKMEEIFQLCDEITILRDGQWI---ATQPLAGLTMDK 225
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
25-170 |
3.84e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 55.63 E-value: 3.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 25 ISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSlLKKPEiiRGRF-SFL---------WEGMQNVyHY 94
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKT-ATRGD--RSRFmAYLghlpglkadLSTLENL-HF 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2485612693 95 LTGeaniLYFAYLNQVPSSVarrrceelLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVVFLDEPLSGLD 170
Cdd:PRK13543 106 LCG----LHGRRAKQMPGSA--------LAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-63 |
4.19e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.44 E-value: 4.19e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2485612693 3 LEVRNLTKVYkrGNQQIKanDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDI 63
Cdd:PRK11819 325 IEAENLSKSF--GDRLLI--DDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI 381
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
36-296 |
4.64e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 57.18 E-value: 4.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 36 GILGPNGAGKTTLIKQIATLLI---PDQGDILY-------KGVSLLK--------KPEIIRGRFSFLWEGMQNVYHYLTG 97
Cdd:PLN03073 207 GLVGRNGTGKTTFLRYMAMHAIdgiPKNCQILHveqevvgDDTTALQcvlntdieRTQLLEEEAQLVAQQRELEFETETG 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 98 EANILYFAYLNQVPSSvarRRCEELLRKLDLY--------------------EVKDQYVFTYSAGMRKKLAIATCLINDP 157
Cdd:PLN03073 287 KGKGANKDGVDKDAVS---QRLEEIYKRLELIdaytaearaasilaglsftpEMQVKATKTFSGGWRMRIALARALFIEP 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 158 EVVFLDEPLSGLDVLAAAELTESIKSWvkemGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDLKNLSKEEEyil 237
Cdd:PLN03073 364 DLLLLDEPTNHLDLHAVLWLETYLLKW----PKTFIVVSHAREFLNTVVTDILHLHGQKLVTYKGDYDTFERTREEQ--- 436
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2485612693 238 yLRNSAKA---REKLR----------KYELQFEILSDVTLKTTLRLGQKElfySVFSDPDFEvlnLEKKSPD 296
Cdd:PLN03073 437 -LKNQQKAfesNERSRshmqafidkfRYNAKRASLVQSRIKALDRLGHVD---AVVNDPDYK---FEFPTPD 501
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
23-273 |
1.21e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.95 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 23 DNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDI-LYKGVSLlkkpeiirGRFSflwegmQNVYHYLTGEANI 101
Cdd:PRK10636 329 DSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKL--------GYFA------QHQLEFLRADESP 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 102 LyfaylnQVPSSVARRRCEELLRK-LDLYEVKDQYVFT----YSAGMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAE 176
Cdd:PRK10636 395 L------QHLARLAPQELEQKLRDyLGGFGFQGDKVTEetrrFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQA 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 177 LTESIkswvKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKV-ILEGKTED----LKNLSKEE-----EYILYLRNSAKAR 246
Cdd:PRK10636 469 LTEAL----IDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVePFDGDLEDyqqwLSDVQKQEnqtdeAPKENNANSAQAR 544
|
250 260
....*....|....*....|....*..
gi 2485612693 247 EKLRKYELQFEILSDVTLKTTLRLGQK 273
Cdd:PRK10636 545 KDQKRREAELRTQTQPLRKEIARLEKE 571
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
2-226 |
1.50e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 55.57 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVYKrgnqQIKANDNISFFVERGDVLGILGPNGAGKTTLIKqIATLLIPD---QGDILYKG----VSLLKKP 74
Cdd:NF040905 1 ILEMRGITKTFP----GVKALDDVNLSVREGEIHALCGENGAGKSTLMK-VLSGVYPHgsyEGEILFDGevcrFKDIRDS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 75 E-----IIrgrfsflwegmqnvyH-------YLTGEANIlyfaYLNQVPSS-------VARRRCEELLRKLDLYEVKDQY 135
Cdd:NF040905 76 EalgivII---------------HqelalipYLSIAENI----FLGNERAKrgvidwnETNRRARELLAKVGLDESPDTL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 136 VFTYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSwVKEMGKTVIIASHRMDFVEKVTNKVLWLKEG 215
Cdd:NF040905 137 VTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLE-LKAQGITSIIISHKLNEIRRVADSITVLRDG 215
|
250
....*....|...
gi 2485612693 216 KVI--LEGKTEDL 226
Cdd:NF040905 216 RTIetLDCRADEV 228
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
31-201 |
1.54e-08 |
|
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: 52.76 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 31 RGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILykgvsllkkpeiirgrfsflwegmqnvyhYLTGEANIlyfaylnqv 110
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI-----------------------------YIDGEDIL--------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 111 pssvarrrceELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEM-- 188
Cdd:smart00382 43 ----------EEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLlk 112
|
170
....*....|....*.
gi 2485612693 189 ---GKTVIIASHRMDF 201
Cdd:smart00382 113 sekNLTVILTTNDEKD 128
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-233 |
1.67e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.56 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKvykRGNQQIKandNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKPEI--IRG 79
Cdd:PRK09700 265 VFEVRNVTS---RDRKKVR---DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLdaVKK 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 80 RFSFLWEGMQN--VYHYLTGEANIL---------YFAYLNQVPSSVARRRCEELLRKLDLY-EVKDQYVFTYSAGMRKKL 147
Cdd:PRK09700 339 GMAYITESRRDngFFPNFSIAQNMAisrslkdggYKGAMGLFHEVDEQRTAENQRELLALKcHSVNQNITELSGGNQQKV 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 148 AIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSwVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKV--ILEGKTEd 225
Cdd:PRK09700 419 LISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQ-LADDGKVILMVSSELPEIITVCDRIAVFCEGRLtqILTNRDD- 496
|
....*...
gi 2485612693 226 lknLSKEE 233
Cdd:PRK09700 497 ---MSEEE 501
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
2-226 |
2.66e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 54.42 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVYKRGNQQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQI-----------ATLLIPDQGDILYkgVSL 70
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAIcgvtkdnwrvtADRMRFDDIDLLR--LSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 71 LKKPEIIRGRFSFLWEGMQ-------NVYHYLTgeANILYFAYLNQVPSSVA--RRRCEELLRKLDLYEVKD---QYVFT 138
Cdd:PRK15093 81 RERRKLVGHNVSMIFQEPQscldpseRVGRQLM--QNIPGWTYKGRWWQRFGwrKRRAIELLHRVGIKDHKDamrSFPYE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 139 YSAGMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVI 218
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
....*...
gi 2485612693 219 LEGKTEDL 226
Cdd:PRK15093 239 ETAPSKEL 246
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-227 |
5.33e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 53.85 E-value: 5.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVYKrgnqQIKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSL-LKKPE----- 75
Cdd:PRK10762 4 LLQLKGIDKAFP----GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtFNGPKssqea 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 76 ---IIRGRFSFLWEgmqnvyhyLTGEANIlyfaYLNQVPSS--------VARRRCEELLRKLDLYEVKDQYVFTYSAGMR 144
Cdd:PRK10762 80 gigIIHQELNLIPQ--------LTIAENI----FLGREFVNrfgridwkKMYAEADKLLARLNLRFSSDKLVGELSIGEQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 145 KKLAIATCLINDPEVVFLDEPlsgLDVLAAAElTESIKSWVKEM---GKTVIIASHRMDFVEKVTNKVLWLKEGKVILEG 221
Cdd:PRK10762 148 QMVEIAKVLSFESKVIIMDEP---TDALTDTE-TESLFRVIRELksqGRGIVYISHRLKEIFEICDDVTVFRDGQFIAER 223
|
....*.
gi 2485612693 222 KTEDLK 227
Cdd:PRK10762 224 EVADLT 229
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
3-197 |
1.02e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 53.05 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYKRGNQQIKAndnISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSL-LKKPEIIRGRF 81
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGP---INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVtAEQPEDYRKLF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 82 SFLWEGMQNVYHYLTGE----ANILYFAYLNQVpssvarrrceELLRKLdlyEVKDQYVFT--YSAGMRKKLAIATCLIN 155
Cdd:PRK10522 400 SAVFTDFHLFDQLLGPEgkpaNPALVEKWLERL----------KMAHKL---ELEDGRISNlkLSKGQKKRLALLLALAE 466
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2485612693 156 DPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASH 197
Cdd:PRK10522 467 ERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISH 508
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-63 |
1.26e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.59 E-value: 1.26e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2485612693 3 LEVRNLTKVYKRGnqqiKANDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDI 63
Cdd:PRK15064 320 LEVENLTKGFDNG----PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
3-249 |
1.71e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 52.64 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYKRGNQQIKanDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGvSLLKKPEIIrgrfs 82
Cdd:TIGR00957 637 ITVHNATFTWARDLPPTL--NGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-SVAYVPQQA----- 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 83 flWegMQNVyhylTGEANILYFAYLNQVPSSVARRRCE-----ELLRKLDLYEVKDQYVfTYSAGMRKKLAIATCLINDP 157
Cdd:TIGR00957 709 --W--IQND----SLRENILFGKALNEKYYQQVLEACAllpdlEILPSGDRTEIGEKGV-NLSGGQKQRVSLARAVYSNA 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 158 EVVFLDEPLSGLDVLAAAELTESI---KSWVKemGKTVIIASHRMDFVEKVtNKVLWLKEGKVILEGKTEDLknLSKEEE 234
Cdd:TIGR00957 780 DIYLFDDPLSAVDAHVGKHIFEHVigpEGVLK--NKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQEL--LQRDGA 854
|
250
....*....|....*
gi 2485612693 235 YILYLRNSAKAREKL 249
Cdd:TIGR00957 855 FAEFLRTYAPDEQQG 869
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
32-227 |
1.94e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.42 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 32 GDVLGILGPNGAGKTTLIKQIAT----LLIPDQGDILYKGVSLLKKPEIIRGRFSFLWEGMQNVYHYLTGEAniLYFAYL 107
Cdd:TIGR00956 87 GELTVVLGRPGSGCSTLLKTIASntdgFHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVHFPHLTVGET--LDFAAR 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 108 NQVPS---------SVARRRCEELLRKLDL-----YEVKDQYVFTYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDVLA 173
Cdd:TIGR00956 165 CKTPQnrpdgvsreEYAKHIADVYMATYGLshtrnTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSAT 244
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2485612693 174 AAELTESIKSWVKEMGKTVIIASHR-MDFVEKVTNKVLWLKEGKVILEGKTEDLK 227
Cdd:TIGR00956 245 ALEFIRALKTSANILDTTPLVAIYQcSQDAYELFDKVIVLYEGYQIYFGPADKAK 299
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
25-203 |
2.95e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 49.28 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 25 ISFFveRGDVLGILGPNGAGKTTLIKQIAtllipdqgdilykgvsllkkpeiirgrfsflwegmqnvyhYLTGeanilyF 104
Cdd:cd03227 16 VTFG--EGSLTIITGPNGSGKSTILDAIG----------------------------------------LALG------G 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 105 AYLNQVPSSVARRRCEELLRKLDLYEVKDQYvftySAGMRKKLAIAT----CLINDPEVVFLDEPLSGLDVLAAAELTES 180
Cdd:cd03227 48 AQSATRRRSGVKAGCIVAAVSAELIFTRLQL----SGGEKELSALALilalASLKPRPLYILDEIDRGLDPRDGQALAEA 123
|
170 180
....*....|....*....|...
gi 2485612693 181 IKSWVKEmGKTVIIASHRMDFVE 203
Cdd:cd03227 124 ILEHLVK-GAQVIVITHLPELAE 145
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-253 |
4.60e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.89 E-value: 4.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 6 RNLTKVYKrGNQQIKANDNISFFveRGDVLGILGPNGAGKTTLIKQIATLLIPDQGD-ILYKGVS---LLKKPEI----- 76
Cdd:PRK11819 10 NRVSKVVP-PKKQILKDISLSFF--PGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEaRPAPGIKvgyLPQEPQLdpekt 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 77 IRGRFSflwEGMQNVYHYLTgEANILYFAYLNQVPSS--VARR--RCEELLRKLDLYEV---------------KDQYVF 137
Cdd:PRK11819 87 VRENVE---EGVAEVKAALD-RFNEIYAAYAEPDADFdaLAAEqgELQEIIDAADAWDLdsqleiamdalrcppWDAKVT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 138 TYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDvlaaaelTESIkSW----VKEMGKTVIIASHRMDFVEKVTNKVL--- 210
Cdd:PRK11819 163 KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD-------AESV-AWleqfLHDYPGTVVAVTHDRYFLDNVAGWILeld 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2485612693 211 -------------WL--KEGKVILEGKTED--LKNLSKEEEYIlylRNSAKARE-----KLRKYE 253
Cdd:PRK11819 235 rgrgipwegnyssWLeqKAKRLAQEEKQEAarQKALKRELEWV---RQSPKARQakskaRLARYE 296
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
3-250 |
5.01e-07 |
|
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: 50.24 E-value: 5.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYKRGNQQIKanDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLiPDQGDILYKGVSLLKKP-EIIRGRF 81
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVL--ENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGDIQIDGVSWNSVPlQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 82 S------FLWEGM--QNVYHYLTGEANILYfaylnQVPSSVARRRC-EELLRKLDLYEVKDQYVFtySAGMRKKLAIATC 152
Cdd:cd03289 80 GvipqkvFIFSGTfrKNLDPYGKWSDEEIW-----KVAEEVGLKSViEQFPGQLDFVLVDGGCVL--SHGHKQLMCLARS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 153 LINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKemGKTVIIASHRMDFVEKVtNKVLWLKEGKV--------ILEGKTE 224
Cdd:cd03289 153 VLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFA--DCTVILSEHRIEAMLEC-QRFLVIEENKVrqydsiqkLLNEKSH 229
|
250 260
....*....|....*....|....*..
gi 2485612693 225 DLKNLSKEEEYILY-LRNSAKAREKLR 250
Cdd:cd03289 230 FKQAISPSDRLKLFpRRNSSKSKRKPR 256
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
3-200 |
9.98e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 50.29 E-value: 9.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYKRGNQQIKanDNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDqGDILYKGVS----LLKKpeiIR 78
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRAVL--QDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSwnsvTLQT---WR 1291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 79 GRFSFLwegMQNVYhYLTG--EANI-LYFAYLNQVPSSVA-----RRRCEELLRKLDLYEVKDQYVFtySAGMRKKLAIA 150
Cdd:TIGR01271 1292 KAFGVI---PQKVF-IFSGtfRKNLdPYEQWSDEEIWKVAeevglKSVIEQFPDKLDFVLVDGGYVL--SNGHKQLMCLA 1365
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2485612693 151 TCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMgkTVIIASHRMD 200
Cdd:TIGR01271 1366 RSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNC--TVILSEHRVE 1413
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
2-232 |
1.29e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 48.63 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLtKVYKRGNQQIKAndnISFFVERGDVLGILGPNGAGKTTLIKQIATL--LIPDQGDILYKGVSLLK-KPEIIR 78
Cdd:PRK09580 1 MLSIKDL-HVSVEDKAILRG---LNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLElSPEDRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 79 GrfsflwEGMQNVYHY---LTGEANILyfaYLNQVPSSVARRRCEELLRKLDLYEVKDQYV---------------FTYS 140
Cdd:PRK09580 77 G------EGIFMAFQYpveIPGVSNQF---FLQTALNAVRSYRGQEPLDRFDFQDLMEEKIallkmpedlltrsvnVGFS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 141 AGMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSwVKEMGKTVIIASHR---MDFVEKVTNKVLWlkEGKV 217
Cdd:PRK09580 148 GGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNS-LRDGKRSFIIVTHYqriLDYIKPDYVHVLY--QGRI 224
|
250
....*....|....*
gi 2485612693 218 ILEGKTEDLKNLSKE 232
Cdd:PRK09580 225 VKSGDFTLVKQLEEQ 239
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
25-232 |
1.47e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 49.97 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 25 ISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYK-------GVSLLKKPEIIRGRFSFLWEGmqnvyhylTG 97
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDdcdvakfGLTDLRRVLSIIPQSPVLFSG--------TV 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 98 EANILYFAYLNQVP--SSVARRRCEELLRKLDLYevKDQYVF----TYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDV 171
Cdd:PLN03232 1327 RFNIDPFSEHNDADlwEALERAHIKDVIDRNPFG--LDAEVSeggeNFSVGQRQLLSLARALLRRSKILVLDEATASVDV 1404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2485612693 172 LAAAELTESIKSWVKEMgkTVIIASHRMDFVEKVtNKVLWLKEGKVILEGKTEDLknLSKE 232
Cdd:PLN03232 1405 RTDSLIQRTIREEFKSC--TMLVIAHRLNTIIDC-DKILVLSSGQVLEYDSPQEL--LSRD 1460
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
3-170 |
1.52e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 49.07 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 3 LEVRNLTKVYKRGNQQIKAndnISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKG--VSLLKKPEiiRGR 80
Cdd:PRK11650 4 LKLQAVRKSYDGKTQVIKG---IDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGrvVNELEPAD--RDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 81 fsflweGM--QN--VYHYLTGEANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLIND 156
Cdd:PRK11650 79 ------AMvfQNyaLYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVRE 152
|
170
....*....|....
gi 2485612693 157 PEVVFLDEPLSGLD 170
Cdd:PRK11650 153 PAVFLFDEPLSNLD 166
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1-199 |
1.55e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 46.32 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 1 MLLEVRNLTkVYKRGNQQIKANDNISFFVERGDVLGILGPNGAGKTTLI---------KQIAtllipdqGDILYKG--VS 69
Cdd:NF040905 256 VVFEVKNWT-VYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAmsvfgrsygRNIS-------GTVFKDGkeVD 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 70 LLKKPEIIRGRFSFLWEG--------MQNVYHYLTGeANILYFAYLNQVPSSVARRRCEELLRKLDlyeVK----DQYVF 137
Cdd:NF040905 328 VSTVSDAIDAGLAYVTEDrkgyglnlIDDIKRNITL-ANLGKVSRRGVIDENEEIKVAEEYRKKMN---IKtpsvFQKVG 403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2485612693 138 TYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEmGKTVIIASHRM 199
Cdd:NF040905 404 NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVISSEL 464
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
118-226 |
1.72e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.16 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 118 RCEELLRKLDLYEVKDQYvFTY-SAGMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEmGKTVIIAS 196
Cdd:PRK10938 115 RCEQLAQQFGITALLDRR-FKYlSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVL 192
|
90 100 110
....*....|....*....|....*....|
gi 2485612693 197 HRMDFVEKVTNKVLWLKEGKVILEGKTEDL 226
Cdd:PRK10938 193 NRFDEIPDFVQFAGVLADCTLAETGEREEI 222
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
23-63 |
2.75e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 45.71 E-value: 2.75e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2485612693 23 DNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDI 63
Cdd:PRK11147 336 KDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI 376
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-196 |
1.25e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 43.48 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 2 LLEVRNLTKVYKRGNQQIKandNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSLLKKP--EIIRG 79
Cdd:COG3845 257 VLEVENLSVRDDRGVPALK---DVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSprERRRL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 80 RFSF-----LWEGM-------QNV---YHYLTGEANilyFAYLNQvpsSVARRRCEELLRKldlYEVK----DQYVFTYS 140
Cdd:COG3845 334 GVAYipedrLGRGLvpdmsvaENLilgRYRRPPFSR---GGFLDR---KAIRAFAEELIEE---FDVRtpgpDTPARSLS 404
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2485612693 141 AGMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSwVKEMGKTVIIAS 196
Cdd:COG3845 405 GGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLE-LRDAGAAVLLIS 459
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
23-226 |
1.44e-04 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 42.35 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 23 DNISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYkgvslLKKPEIIRGRFSFLWEGmqnvyhyLTGEANIL 102
Cdd:PRK15177 4 DKTDFVMGYHEHIGILAAPGSGKTTLTRLLCGLDAPDEGDFIG-----LRGDALPLGANSFILPG-------LTGEENAR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 103 YFAYLNQVPSSVARRRCEELLRkldLYEVKDQYVFTYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIK 182
Cdd:PRK15177 72 MMASLYGLDGDEFSHFCYQLTQ---LEQCYTDRVSEYSVTMKTHLAFAINLLLPCRLYIADGKLYTGDNATQLRMQAALA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2485612693 183 SWVKEMGktVIIASHRMDFVEKVTNKVLWLKEGKVILegkTEDL 226
Cdd:PRK15177 149 CQLQQKG--LIVLTHNPRLIKEHCHAFGVLLHGKITM---CEDL 187
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
25-217 |
2.70e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 42.21 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 25 ISFFVERGDVLGILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSL-LKKP-EIIRgrfsflwEGM---------QNVYH 93
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIdIRSPrDAIR-------AGImlcpedrkaEGIIP 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 94 YLTGEANILYFAYLNQVPSSV---ARRRCEELLRKLDLYEVK----DQYVFTYSAGMRKKLAIATCLINDPEVVFLDEPL 166
Cdd:PRK11288 345 VHSVADNINISARRHHLRAGClinNRWEAENADRFIRSLNIKtpsrEQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPT 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2485612693 167 SGLDVLAAAELTESIKSwVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKV 217
Cdd:PRK11288 425 RGIDVGAKHEIYNVIYE-LAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
30-60 |
3.14e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 38.35 E-value: 3.14e-04
10 20 30
....*....|....*....|....*....|.
gi 2485612693 30 ERGDVLgILGPNGAGKTTLIKQIATLLIPDQ 60
Cdd:pfam13555 21 PRGNTL-LTGPSGSGKSTLLDAIQTLLVPAK 50
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
23-226 |
4.55e-04 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 40.97 E-value: 4.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 23 DNISFFVERGDVLGILGPNGAGKTTLIKQIATLL--------IPDQGDILYKGVSL--LKKPEIIRGRfSFLWEGMQNVY 92
Cdd:PRK13547 18 RDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggaprgARVTGDVTLNGEPLaaIDAPRLARLR-AVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 93 HYLTGEAnILYFAYLNQVPSSVARRRCEEL----LRKLDLYEVKDQYVFTYSAGMRKKLAIATCL---------INDPEV 159
Cdd:PRK13547 97 AFSAREI-VLLGRYPHARRAGALTHRDGEIawqaLALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPPRY 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2485612693 160 VFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEKVTNKVLWLKEGKVILEGKTEDL 226
Cdd:PRK13547 176 LLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
135-204 |
7.42e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.17 E-value: 7.42e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 135 YVFTYSAGMRKKLAIATCLINDPEVVFLDEPLSGLDVLAAAELTESIKSWVKEMGKTVIIASHRMDFVEK 204
Cdd:PTZ00265 1355 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR 1424
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
37-170 |
1.05e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.47 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 37 ILGPNGAGKTTLIKQIATLLIPDQGDILYKGVSL--LKKP--EIIRGRFSFLWEgmqnvyhyLTGEANILYFAYL----N 108
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNInnIAKPycTYIGHNLGLKLE--------MTVFENLKFWSEIynsaE 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2485612693 109 QVPSSVARRRCEELLrkldlyevkDQYVFTYSAGMRKKLAIATCLINDPEVVFLDEPLSGLD 170
Cdd:PRK13541 103 TLYAAIHYFKLHDLL---------DEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
89-197 |
6.58e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 37.75 E-value: 6.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485612693 89 QNVYHYLTGEANILYFAYLNQVPSSVARRRCEELLRKLDLYEVKDQYVFTYSAGMRKKLAIATCLINDPE---VVFLDEP 165
Cdd:pfam13304 187 RLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGELPAFELSDGTKRLLALLAALLSALPkggLLLIDEP 266
|
90 100 110
....*....|....*....|....*....|..
gi 2485612693 166 LSGLDVLAAAELTESIKSwVKEMGKTVIIASH 197
Cdd:pfam13304 267 ESGLHPKLLRRLLELLKE-LSRNGAQLILTTH 297
|
|
| |
