|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-228 |
1.14e-95 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 282.34 E-value: 1.14e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 6 LHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAMSSVGAIIE 85
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 86 NPEFYSYLTGFENLELYASMH---DGVSEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTN 162
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYglpRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515936072 163 GLDPAGMKEFREHLQMLVqEEGVSVLFATHLLHEVEELCDRMIIIQKGQIKANTNLRDMegKEQVL 228
Cdd:COG1131 161 GLDPEARRELWELLRELA-AEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL--KARLL 223
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-212 |
3.07e-85 |
|
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: 254.83 E-value: 3.07e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 6 LHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHlKAMSSVGAIIE 85
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI-EALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 86 NPEFYSYLTGFENLELYASMHdGVSEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLD 165
Cdd:cd03268 80 APGFYPNLTARENLRLLARLL-GIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515936072 166 PAGMKEFREHLQMLvQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:cd03268 159 PDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-212 |
7.82e-76 |
|
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: 229.59 E-value: 7.82e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 6 LHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAMSSVGAIIE 85
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 86 NPEFYSYLTGFENLElyasmhdgvseerifevvkrvrlehaihqkvktYSLGMKQRLGIAQAILHKPNLLILDEPTNGLD 165
Cdd:cd03230 81 EPSLYENLTVRENLK---------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLD 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515936072 166 PAGMKEFREHLQMLVQeEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:cd03230 128 PESRREFWELLRELKK-EGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
8-215 |
2.35e-71 |
|
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: 220.50 E-value: 2.35e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 8 IENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAMSSVGAIIENP 87
Cdd:COG4555 4 VENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPDER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 88 EFYSYLTGFENLELYASMHDGVSEE---RIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGL 164
Cdd:COG4555 84 GLYDRLTVRENIRYFAELYGLFDEElkkRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515936072 165 DPAGMKEFREHLQMLvQEEGVSVLFATHLLHEVEELCDRMIIIQKGQIKAN 215
Cdd:COG4555 164 DVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQ 213
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
6-231 |
6.93e-64 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 201.09 E-value: 6.93e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 6 LHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNG--YSQDDdhlkaMSSVGAI 83
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGhpWTRKD-----LHKIGSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 84 IENPEFYSYLTGFENLELYASMhDGVSEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNG 163
Cdd:TIGR03740 76 IESPPLYENLTARENLKVHTTL-LGLPDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515936072 164 LDPAGMKEFREHLQMLvQEEGVSVLFATHLLHEVEELCDRMIIIQKGQIKANTNLRDMEGKEQVLMNI 231
Cdd:TIGR03740 155 LDPIGIQELRELIRSF-PEQGITVILSSHILSEVQQLADHIGIISEGVLGYQGKINKSENLEKLFVEV 221
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-292 |
3.09e-55 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 181.07 E-value: 3.09e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 5 VLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKamsSVGAII 84
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRR---RIGYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 85 ENPEFYSYLTGFENLELYASMHdGVS----EERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEP 160
Cdd:COG4152 78 EERGLYPKMKVGEQLVYLARLK-GLSkaeaKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 161 TNGLDPAG----MKEFREHlqmlvQEEGVSVLFATHLLHEVEELCDRMIIIQKGQIKAN---TNLRDMEGKEQVLMNiqp 233
Cdd:COG4152 157 FSGLDPVNvellKDVIREL-----AAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSgsvDEIRRQFGRNTLRLE--- 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515936072 234 VEKAVSWLDTQG--YTYEQRDQHVLVQLKKDRVPELNKQLVLAEFDVLEMTPQKQSIEEAF 292
Cdd:COG4152 229 ADGDAGWLRALPgvTVVEEDGDGAELKLEDGADAQELLRALLARGPVREFEEVRPSLNEIF 289
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-205 |
6.52e-55 |
|
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: 177.29 E-value: 6.52e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 4 AVLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAMSSVGAI 83
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 84 IENPEFYSYLTGFENLELYASMH-DGVSEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTN 162
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALYgLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 515936072 163 GLDPAGMKEFREHLQMLVQeEGVSVLFATHllHEVEELCDRMI 205
Cdd:COG4133 161 ALDAAGVALLAELIAAHLA-RGGAVLLTTH--QPLELAAARVL 200
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
8-214 |
8.53e-55 |
|
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: 177.56 E-value: 8.53e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 8 IENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAMSSVGAIIENP 87
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 88 EFYSYLTGFENLELYASMHdGVS----EERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNG 163
Cdd:cd03265 83 SVDDELTGWENLYIHARLY-GVPgaerRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515936072 164 LDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQIKA 214
Cdd:cd03265 162 LDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIA 212
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-213 |
9.50e-55 |
|
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: 177.00 E-value: 9.50e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 6 LHIENVDKQIGRHQILQHISMDIRQGeIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAMSSVGAIIE 85
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 86 NPEFYSYLTGFENLELYA---SMHDGVSEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTN 162
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAwlkGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515936072 163 GLDPAGMKEFREHLQMLvqEEGVSVLFATHLLHEVEELCDRMIIIQKGQIK 213
Cdd:cd03264 160 GLDPEERIRFRNLLSEL--GEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
13-296 |
1.18e-54 |
|
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: 179.89 E-value: 1.18e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 13 KQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAMSSVGAIIENPEFYSY 92
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 93 LTGFENLELYASMHD---GVSEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPagm 169
Cdd:TIGR01188 81 LTGRENLEMMGRLYGlpkDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDP--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 170 kEFREHLQMLVQ---EEGVSVLFATHLLHEVEELCDRMIIIQKGQIKAN---TNLRDMEGKE---QVLMNIQPVEKAVSW 240
Cdd:TIGR01188 158 -RTRRAIWDYIRalkEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEgtpEELKRRLGKDtleSRPRDIQSLKVEVSM 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515936072 241 L-----DTQGYTyeqRDQHVLVQLKKDRVPELNKQL--VLAEFD-----VLEMTPQKQSIEEAFMKWT 296
Cdd:TIGR01188 237 LiaelgETGLGL---LAVTVDSDRIKILVPDGDETVpeIVEAAIrngirIRSISTERPSLDDVFLKLT 301
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-214 |
2.85e-53 |
|
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: 173.46 E-value: 2.85e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 6 LHIENVDKQ--IGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAMSSVGAI 83
Cdd:cd03263 1 LQIRNLTKTykKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 84 ienPEF---YSYLTGFENLELYASMHdGVSEERIFEVVKR----VRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLI 156
Cdd:cd03263 81 ---PQFdalFDELTVREHLRFYARLK-GLPKSEIKEEVELllrvLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 157 LDEPTNGLDPAGmkefREHLQMLVQEE--GVSVLFATHLLHEVEELCDRMIIIQKGQIKA 214
Cdd:cd03263 157 LDEPTSGLDPAS----RRAIWDLILEVrkGRSIILTTHSMDEAEALCDRIAIMSDGKLRC 212
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
6-214 |
6.35e-53 |
|
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: 172.55 E-value: 6.35e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 6 LHIENVDKQI----GRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAMSSVG 81
Cdd:cd03266 2 ITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 82 AIIENPEFYSYLTGFENLELYASMHdGVS----EERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLIL 157
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLY-GLKgdelTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515936072 158 DEPTNGLDPAGMKEFREHLQMLvQEEGVSVLFATHLLHEVEELCDRMIIIQKGQIKA 214
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVY 216
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
6-214 |
2.12e-52 |
|
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of this protein family are the ATP-binding subunit of an ABC transporter system that is associated with PQQ biosynthesis and PQQ-dependent alcohol dehydrogenases. While this family shows homology to several efflux ABC transporter subunits, the presence of a periplasmic substrate-binding protein and association with systems for catabolism of alcohols suggests a role in import rather than detoxification. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 274822 [Multi-domain] Cd Length: 236 Bit Score: 171.71 E-value: 2.12e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 6 LHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAMSSVGAIIE 85
Cdd:TIGR03864 2 LEVAGLSFRYGARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVAGHDLRRAPRAALARLGVVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 86 NPEFYSYLTGFENLELYASMHdGVS----EERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPT 161
Cdd:TIGR03864 82 QPTLDLDLSVRQNLRYHAALH-GLSraeaRARIAELLARLGLAERADDKVRELNGGHRRRVEIARALLHRPALLLLDEPT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515936072 162 NGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEElCDRMIIIQKGQIKA 214
Cdd:TIGR03864 161 VGLDPASRAAITAHVRALARDQGLSVLWATHLVDEIEA-SDRLVVLHRGRVLA 212
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-214 |
2.61e-52 |
|
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: 170.92 E-value: 2.61e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 6 LHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAMssvGAIIE 85
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRI---GYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 86 NPEFYSYLTGFENLELYASMHDGVSEE---RIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTN 162
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAQLKGLKKEEarrRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515936072 163 GLDPAGMKEFREHLQMLvQEEGVSVLFATHLLHEVEELCDRMIIIQKGQIKA 214
Cdd:cd03269 158 GLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRAVL 208
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
16-214 |
6.39e-49 |
|
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: 162.50 E-value: 6.39e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 16 GRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAMSS-VGAIIENPE---FYS 91
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRkVGLVFQNPDdqlFAP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 92 ylT-------GFENLelyasmhdGVSEE----RIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEP 160
Cdd:COG1122 92 --TveedvafGPENL--------GLPREeireRVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515936072 161 TNGLDPAGMKEFREHLQMLvQEEGVSVLFATHLLHEVEELCDRMIIIQKGQIKA 214
Cdd:COG1122 162 TAGLDPRGRRELLELLKRL-NKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVA 214
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
19-211 |
3.15e-48 |
|
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: 160.33 E-value: 3.15e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 19 QILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAMS-SVGAIIENPE---FYSYLT 94
Cdd:cd03225 15 PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRrKVGLVFQNPDdqfFGPTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 95 -----GFENLelyasmhdGVSEE----RIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLD 165
Cdd:cd03225 95 eevafGLENL--------GLPEEeieeRVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 515936072 166 PAGMKEFREHLQMLvQEEGVSVLFATHLLHEVEELCDRMIIIQKGQ 211
Cdd:cd03225 167 PAGRRELLELLKKL-KAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-214 |
3.36e-48 |
|
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: 161.30 E-value: 3.36e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 1 MQSAVLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNG---YSQDDDHLKAM 77
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqdiTGLSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 78 -SSVGAIIENPEFYSYLTGFENLELYASMHDGVSEERIFEVV----KRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKP 152
Cdd:COG1127 81 rRRIGMLFQGGALFDSLTVFENVAFPLREHTDLSEAEIRELVleklELVGLPGAADKMPSELSGGMRKRVALARALALDP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515936072 153 NLLILDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQIKA 214
Cdd:COG1127 161 EILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIA 222
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
16-220 |
1.18e-46 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 157.17 E-value: 1.18e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 16 GRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysqdddhlkamsSVGAIIE-----NPEfy 90
Cdd:COG1134 37 EEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG------------RVSALLElgagfHPE-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 91 syLTGFENLELYASMHdGVSEERIFEVVKRVR----LEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDP 166
Cdd:COG1134 103 --LTGRENIYLNGRLL-GLSRKEIDEKFDEIVefaeLGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515936072 167 AGMKEFREHLQMLVqEEGVSVLFATHLLHEVEELCDRMIIIQKGQIKANTNLRD 220
Cdd:COG1134 180 AFQKKCLARIRELR-ESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEE 232
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
8-212 |
1.60e-45 |
|
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: 154.20 E-value: 1.60e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 8 IENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysQDDDHLKAMS------SVG 81
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDG--EDISGLSEAElyrlrrRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 82 AIIENPEFYSYLTGFENLELYASMHDGVSEERIFEVVK----RVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLIL 157
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTRLSEEEIREIVLekleAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 515936072 158 DEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-212 |
2.35e-44 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 151.40 E-value: 2.35e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 1 MQSAVLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKamssV 80
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR----I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 81 GAIIENPEFYSY--LTGFE--NLELYASM-----HDGVSEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHK 151
Cdd:COG1121 78 GYVPQRAEVDWDfpITVRDvvLMGRYGRRglfrrPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515936072 152 PNLLILDEPTNGLDPAGMKEFREHLQMLvQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:COG1121 158 PDLLLLDEPFAGVDAATEEALYELLREL-RREGKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-211 |
3.82e-44 |
|
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: 148.49 E-value: 3.82e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 6 LHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNG---YSQDDDHLKAMSSVGA 82
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedlTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 83 IIENPEFYSYLTGFENLELyasmhdgvseerifevvkrvRLehaihqkvktySLGMKQRLGIAQAILHKPNLLILDEPTN 162
Cdd:cd03229 81 VFQDFALFPHLTVLENIAL--------------------GL-----------SGGQQQRVALARALAMDPDVLLLDEPTS 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 515936072 163 GLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQ 211
Cdd:cd03229 130 ALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-212 |
4.92e-44 |
|
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: 149.56 E-value: 4.92e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 6 LHIENVDKQIG----RHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAMSS-- 79
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAfr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 80 ---VGAIIENPEFYSYLTGFENLEL---YASMHDGVSEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPN 153
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALENVELpllLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515936072 154 LLILDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHlLHEVEELCDRMIIIQKGQI 212
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTH-DPELAEYADRIIELRDGKI 218
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-210 |
2.82e-43 |
|
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: 147.68 E-value: 2.82e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 7 HIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHlkamSSVGAI--I 84
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER----KRIGYVpqR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 85 ENPEFYSYLTGFE----NLELYASMHDGVSEE---RIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLIL 157
Cdd:cd03235 77 RSIDRDFPISVRDvvlmGLYGHKGLFRRLSKAdkaKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515936072 158 DEPTNGLDPAGMKEFREHLQMLvQEEGVSVLFATHLLHEVEELCDRMIIIQKG 210
Cdd:cd03235 157 DEPFAGVDPKTQEDIYELLREL-RREGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
16-214 |
6.14e-42 |
|
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: 144.60 E-value: 6.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 16 GRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysqdddhlkamsSVGAIIE-----NPEfy 90
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------------RVSSLLGlgggfNPE-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 91 syLTGFENLELYASMHdGVSEERIFEVVKRV----RLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDP 166
Cdd:cd03220 99 --LTGRENIYLNGRLL-GLSRKEIDEKIDEIiefsELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 515936072 167 AGMKEFREHLQMLVqEEGVSVLFATHLLHEVEELCDRMIIIQKGQIKA 214
Cdd:cd03220 176 AFQEKCQRRLRELL-KQGKTVILVSHDPSSIKRLCDRALVLEKGKIRF 222
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-212 |
2.06e-41 |
|
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: 150.05 E-value: 2.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 5 VLHIENVDK-----QIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYS----------- 68
Cdd:COG1123 260 LLEVRNLSKrypvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDltklsrrslre 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 69 ---------QDDDH-LKAMSSVGAIIEnpefysyltgfENLELYASMHDGVSEERIFEVVKRVRL--EHA---IHQkvkt 133
Cdd:COG1123 340 lrrrvqmvfQDPYSsLNPRMTVGDIIA-----------EPLRLHGLLSRAERRERVAELLERVGLppDLAdryPHE---- 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515936072 134 YSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:COG1123 405 LSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRI 483
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
3-212 |
7.52e-41 |
|
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: 142.49 E-value: 7.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 3 SAVLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysQDDDHLKAMssvgA 82
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDG--RDITGLPPH----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 83 IIE--------NPEFYSYLTGFENLELYASMHDGVS------------------EERIFEVVKRVRLEHAIHQKVKTYSL 136
Cdd:COG0411 76 IARlgiartfqNPRLFPELTVLENVLVAAHARLGRGllaallrlprarreereaRERAEELLERVGLADRADEPAGNLSY 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515936072 137 GMKQRLGIAQAILHKPNLLILDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:COG0411 156 GQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-216 |
2.51e-40 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 140.18 E-value: 2.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 3 SAVLHIENVDKQIG----RHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNG---YSQDDDHLK 75
Cdd:COG1136 2 SPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGqdiSSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 76 AM--SSVGAIIENPEFYSYLTGFENLEL---YASMHDGVSEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILH 150
Cdd:COG1136 82 RLrrRHIGFVFQFFNLLPELTALENVALpllLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515936072 151 KPNLLILDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHlLHEVEELCDRMIIIQKGQIKANT 216
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTH-DPELAARADRVIRLRDGRIVSDE 226
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-212 |
2.67e-40 |
|
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: 139.96 E-value: 2.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 6 LHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysQDDDHLKAMS-SVGAII 84
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDG--RDVTGVPPERrNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 85 ENPEFYSYLTGFEN----LELyASMHDGVSEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEP 160
Cdd:cd03259 79 QDYALFPHLTVAENiafgLKL-RGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515936072 161 TNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:cd03259 158 LSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
21-215 |
4.42e-40 |
|
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: 140.16 E-value: 4.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 21 LQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNG---YSQDDDHLKAMSSVGAiiENPEFYSYLTGFE 97
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGlvpWKRRKKFLRRIGVVFG--QKTQLWWDLPVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 98 NLELYASMHD---GVSEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPAGMKEFRE 174
Cdd:cd03267 115 SFYLLAAIYDlppARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRN 194
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 515936072 175 HLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQIKAN 215
Cdd:cd03267 195 FLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYD 235
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-211 |
1.63e-39 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 135.84 E-value: 1.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 7 HIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysqdddhlkamssvgaiien 86
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDG-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 87 pefysyltgfenlelyasmhDGVSEERIFEVVKRVRLehaIHQkvktYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDP 166
Cdd:cd00267 61 --------------------KDIAKLPLEELRRRIGY---VPQ----LSGGQRQRVALARALLLNPDLLLLDEPTSGLDP 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 515936072 167 AGMKEFREHLQMLVQeEGVSVLFATHLLHEVEELCDRMIIIQKGQ 211
Cdd:cd00267 114 ASRERLLELLRELAE-EGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-212 |
1.74e-39 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 138.02 E-value: 1.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 5 VLHIENVDK----QIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysQDDDHLK----- 75
Cdd:cd03257 1 LLEVKNLSVsfptGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDG--KDLLKLSrrlrk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 76 ------------AMSS------VGAIIENPefYSYLTGFENLELYasmhdgvsEERIFEVVKRVRLEHAI-----HQkvk 132
Cdd:cd03257 79 irrkeiqmvfqdPMSSlnprmtIGEQIAEP--LRIHGKLSKKEAR--------KEAVLLLLVGVGLPEEVlnrypHE--- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 133 tYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:cd03257 146 -LSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-212 |
1.77e-39 |
|
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: 144.66 E-value: 1.77e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 3 SAVLHIEN--VDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKN---NGRIIMNGYSQDDDHLKAM 77
Cdd:COG1123 2 TPLLEVRDlsVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 78 SS-VGAIIENPEfySYLTGF-------ENLELyASMHDGVSEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAIL 149
Cdd:COG1123 82 GRrIGMVFQDPM--TQLNPVtvgdqiaEALEN-LGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515936072 150 HKPNLLILDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRI 221
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-214 |
2.89e-39 |
|
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: 138.25 E-value: 2.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 5 VLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysQDddhLKAMSS----- 79
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDG--RD---LASLSRrelar 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 80 -VGAIIENPEFYSYLTGFENLEL----YASMHDGVS---EERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHK 151
Cdd:COG1120 76 rIAYVPQEPPAPFGLTVRELVALgrypHLGLFGRPSaedREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515936072 152 PNLLILDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQIKA 214
Cdd:COG1120 156 PPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVA 218
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-212 |
3.34e-39 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 137.18 E-value: 3.34e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 6 LHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysQDDDHLK----AMSSVG 81
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDG--RDITGLPpherARAGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 82 AIIENPEFYSYLTGFENLELYASMHDGVSEERIFEVVKRV--RLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDE 159
Cdd:cd03224 79 YVPEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515936072 160 PTNGLDPAGMKEFREHLQMLvQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:cd03224 159 PSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRV 210
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-212 |
7.61e-39 |
|
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: 136.80 E-value: 7.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 6 LHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysQDDDHLKAMSSVGAII- 84
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDG--EDITGLPPHEIARLGIg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 85 ---ENPEFYSYLTGFENLELYASMHDGVS-------------EERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAI 148
Cdd:cd03219 79 rtfQIPRLFPELTVLENVMVAAQARTGSGlllararreereaRERAEELLERVGLADLADRPAGELSYGQQRRLEIARAL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515936072 149 LHKPNLLILDEPTNGLDPAGMKEFREHLQMLVqEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNPEETEELAELIRELR-ERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
8-214 |
8.01e-39 |
|
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: 134.87 E-value: 8.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 8 IENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysQDDDHLKAMSSVGAIienp 87
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDG--KDLASLSPKELARKI---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 88 efySYLTgfenlelyasmhdgvseerifEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPA 167
Cdd:cd03214 76 ---AYVP---------------------QALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIA 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515936072 168 GMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQIKA 214
Cdd:cd03214 132 HQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVA 178
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-214 |
1.43e-38 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 136.76 E-value: 1.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 1 MQSAVLHIENVDKQ----IGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKa 76
Cdd:COG1116 3 AAAPALELRGVSKRfptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 77 mssVGAIIENPEFYSYLTGFENLELYASMHdGVS----EERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKP 152
Cdd:COG1116 82 ---RGVVFQEPALLPWLTVLDNVALGLELR-GVPkaerRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515936072 153 NLLILDEPTNGLDpAGMKEF-REHLQMLVQEEGVSVLFAThllHEVEE---LCDRMIIIQK--GQIKA 214
Cdd:COG1116 158 EVLLMDEPFGALD-ALTRERlQDELLRLWQETGKTVLFVT---HDVDEavfLADRVVVLSArpGRIVE 221
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-211 |
1.85e-38 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 137.63 E-value: 1.85e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 1 MQSAVLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAMSSV 80
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 81 GAIIE----NPEFysylTGFENLEL---YASMHDGVSEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPN 153
Cdd:PRK13537 83 GVVPQfdnlDPDF----TVRENLLVfgrYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515936072 154 LLILDEPTNGLDPAGMKEFREHLQMLVQeEGVSVLFATHLLHEVEELCDRMIIIQKGQ 211
Cdd:PRK13537 159 VLVLDEPTTGLDPQARHLMWERLRSLLA-RGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-214 |
2.07e-38 |
|
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: 135.29 E-value: 2.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 6 LHIENVDKQ----IGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHlkamSSVG 81
Cdd:cd03293 1 LEVRNVSKTygggGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG----PDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 82 AIIENPEFYSYLTGFENLELYASMHdGVS----EERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLIL 157
Cdd:cd03293 77 YVFQQDALLPWLTVLDNVALGLELQ-GVPkaeaRERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 158 DEPTNGLDpAGMKE-FREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQK--GQIKA 214
Cdd:cd03293 156 DEPFSALD-ALTREqLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVA 214
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-212 |
5.46e-38 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 137.54 E-value: 5.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 1 MQSAVLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysqdddhlKAMSSV 80
Cdd:COG3842 1 MAMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDG--------RDVTGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 81 GaiienPE-------FYSY-----LTGFENLElYASMHDGVS----EERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGI 144
Cdd:COG3842 73 P-----PEkrnvgmvFQDYalfphLTVAENVA-FGLRMRGVPkaeiRARVAELLELVGLEGLADRYPHQLSGGQQQRVAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515936072 145 AQAILHKPNLLILDEPTNGLDpagmKEFREHLQM----LVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:COG3842 147 ARALAPEPRVLLLDEPLSALD----AKLREEMREelrrLQRELGITFIYVTHDQEEALALADRIAVMNDGRI 214
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-227 |
5.80e-38 |
|
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: 134.21 E-value: 5.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 6 LHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGY--SQDDDHLKAMSSVGAI 83
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQdiTKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 84 IENPEFYSYLTGFENLELYASMH---DGVSEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEP 160
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRglsKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515936072 161 TNGLDPAGMKEFREHLQMLVqEEGVSVLFATHLLHEVEELCDRMIIIQKGQIKANTNLRDMEGKEQV 227
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKILK-DRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELV 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-162 |
7.88e-38 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 131.23 E-value: 7.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 21 LQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAMS-SVGAIIENPEFYSYLTGFENL 99
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRkEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 100 ELYASMH---DGVSEERIFEVVKRVRLEHAIHQKV----KTYSLGMKQRLGIAQAILHKPNLLILDEPTN 162
Cdd:pfam00005 81 RLGLLLKglsKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
19-214 |
1.07e-37 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 134.87 E-value: 1.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 19 QILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQ-DDDHLKAM-SSVGAIIENPE-------- 88
Cdd:TIGR04520 16 PALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTlDEENLWEIrKKVGMVFQNPDnqfvgatv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 89 -----FysyltGFENLelyasmhdGVS----EERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDE 159
Cdd:TIGR04520 96 eddvaF-----GLENL--------GVPreemRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 515936072 160 PTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVeELCDRMIIIQKGQIKA 214
Cdd:TIGR04520 163 ATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVA 216
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-212 |
1.28e-37 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 133.25 E-value: 1.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 5 VLHIENVDK-QIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSqdddhLKAMS----- 78
Cdd:COG2884 1 MIRFENVSKrYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQD-----LSRLKrreip 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 79 ----SVGAI------IENpefysyLTGFENLEL---YASMHDGVSEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIA 145
Cdd:COG2884 76 ylrrRIGVVfqdfrlLPD------RTVYENVALplrVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515936072 146 QAILHKPNLLILDEPTNGLDPAGMKEFREHLQMLvQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETSWEIMELLEEI-NRRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-290 |
1.77e-37 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 135.60 E-value: 1.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 21 LQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYS---QDDDHLKAMSSV-G----------AIien 86
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVpfkRRKEFARRIGVVfGqrsqlwwdlpAI--- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 87 pefysyltgfENLELYASMHdGVSE----ERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTN 162
Cdd:COG4586 115 ----------DSFRLLKAIY-RIPDaeykKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 163 GLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQIKANTNLRDMegKEQV----LMNIQPVEKAV 238
Cdd:COG4586 184 GLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEEL--KERFgpykTIVLELAEPVP 261
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 515936072 239 SWLDTQGYTYEQRD--QHVLVQLKKDRVPELNKQLvLAEFDVLEMTPQKQSIEE 290
Cdd:COG4586 262 PLELPRGGEVIEREgnRVRLEVDPRESLAEVLARL-LARYPVRDLTIEEPPIEE 314
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
8-212 |
2.13e-36 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 130.54 E-value: 2.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 8 IENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysQDDDHLKAMS-SVGAIIEN 86
Cdd:cd03296 5 VRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGG--EDATDVPVQErNVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 87 PEFYSYLTGFENLELYASMHDGVS-------EERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDE 159
Cdd:cd03296 83 YALFRHMTVFDNVAFGLRVKPRSErppeaeiRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515936072 160 PTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-212 |
3.06e-36 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 129.17 E-value: 3.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 6 LHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysqdddhlKAMSSVgaiie 85
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDG--------KPLSAM----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 86 NPEFY----SYL---------TGFENLEL-YASMHDGVSEERIFEVVKRVRLEHAI-HQKVKTYSLGMKQRLGIAQAILH 150
Cdd:COG4619 68 PPPEWrrqvAYVpqepalwggTVRDNLPFpFQLRERKFDRERALELLERLGLPPDIlDKPVERLSGGERQRLALIRALLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515936072 151 KPNLLILDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
20-212 |
1.17e-35 |
|
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: 135.73 E-value: 1.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 20 ILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAM-SSVGAIIENPEFYSyltG--F 96
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLrRQIGVVLQDVFLFS---GtiR 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 97 ENLELYasmHDGVSEERIFEVVKRV-------RLEHAIHQKV----KTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLD 165
Cdd:COG2274 567 ENITLG---DPDATDEEIIEAARLAglhdfieALPMGYDTVVgeggSNLSGGQRQRLAIARALLRNPRILILDEATSALD 643
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515936072 166 PAGMKEFREHLQMLVQeeGVSVLFATHLLHEVeELCDRMIIIQKGQI 212
Cdd:COG2274 644 AETEAIILENLRRLLK--GRTVIIIAHRLSTI-RLADRIIVLDKGRI 687
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-232 |
1.31e-35 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 131.11 E-value: 1.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 1 MQSAVLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAMSSV 80
Cdd:PRK13536 37 MSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 81 GAIIE----NPEFysylTGFENLELYA---SMHDGVSEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPN 153
Cdd:PRK13536 117 GVVPQfdnlDLEF----TVRENLLVFGryfGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQ 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515936072 154 LLILDEPTNGLDPAGMKEFREHLQMLVQeEGVSVLFATHLLHEVEELCDRMIIIQKGQIKAntnlrdmEGKEQVLMNIQ 232
Cdd:PRK13536 193 LLILDEPTTGLDPHARHLIWERLRSLLA-RGKTILLTTHFMEEAERLCDRLCVLEAGRKIA-------EGRPHALIDEH 263
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-212 |
1.95e-35 |
|
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: 125.62 E-value: 1.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 6 LHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDddhlkamssvgaiIE 85
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS-------------FA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 86 NPefysyltgfenlelYASMHDGVSeerifevvkrvrlehAIHQkvktYSLGMKQRLGIAQAILHKPNLLILDEPTNGLD 165
Cdd:cd03216 68 SP--------------RDARRAGIA---------------MVYQ----LSVGERQMVEIARALARNARLLILDEPTAALT 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515936072 166 PAGMKEFREHLQMLvQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:cd03216 115 PAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-212 |
2.00e-35 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 128.25 E-value: 2.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 4 AVLHIENVDKQ-IGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysQDDDHLK------A 76
Cdd:COG3638 1 PMLELRNLSKRyPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDG--QDVTALRgralrrL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 77 MSSVGAIienpeFYSY-----LTGFEN--------LELYASMHDGVSEE---RIFEVVKRVRLEHAIHQKVKTYSLGMKQ 140
Cdd:COG3638 79 RRRIGMI-----FQQFnlvprLSVLTNvlagrlgrTSTWRSLLGLFPPEdreRALEALERVGLADKAYQRADQLSGGQQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515936072 141 RLGIAQAILHKPNLLILDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:COG3638 154 RVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRV 225
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
5-227 |
3.64e-35 |
|
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: 127.39 E-value: 3.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 5 VLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDD--HLKAMSSVGA 82
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLpmHERARLGIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 83 IIENPEFYSYLTGFEN----LELYASMHDGVSEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILD 158
Cdd:TIGR04406 81 LPQEASIFRKLTVEENimavLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515936072 159 EPTNGLDPAGMKEFREHLQMLvQEEGVSVLFATHLLHEVEELCDRMIIIQKGQIKANTNLRDMEGKEQV 227
Cdd:TIGR04406 161 EPFAGVDPIAVGDIKKIIKHL-KERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKV 228
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
8-212 |
5.02e-35 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 129.82 E-value: 5.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 8 IENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysQDDDHLKAMS-SVGAIIEN 86
Cdd:PRK10851 5 IANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHG--TDVSRLHARDrKVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 87 PEFYSYLTGFENLELYASM---HDGVSEERIFEVVKR----VRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDE 159
Cdd:PRK10851 83 YALFRHMTVFDNIAFGLTVlprRERPNAAAIKAKVTQllemVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515936072 160 PTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:PRK10851 163 PFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-220 |
5.31e-35 |
|
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: 126.54 E-value: 5.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 5 VLHIENVDK----QIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysQDDDHL------ 74
Cdd:cd03258 1 MIELKNVSKvfgdTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDG--TDLTLLsgkelr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 75 KAMSSVGAIIENPEFYSYLTGFENLElYASMHDGVS----EERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILH 150
Cdd:cd03258 79 KARRRIGMIFQHFNLLSSRTVFENVA-LPLEIAGVPkaeiEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 151 KPNLLILDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQIKANTNLRD 220
Cdd:cd03258 158 NPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEE 227
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-212 |
1.83e-34 |
|
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: 125.37 E-value: 1.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 6 LHIENVDKQIGR-HQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAM----SSV 80
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlrRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 81 GAIIENPEFYSYLTGFEN--------LELYASMHDGVSEERI---FEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAIL 149
Cdd:cd03256 81 GMIFQQFNLIERLSVLENvlsgrlgrRSTWRSLFGLFPKEEKqraLAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515936072 150 HKPNLLILDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFAthlLHEVE---ELCDRMIIIQKGQI 212
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVS---LHQVDlarEYADRIVGLKDGRI 223
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-214 |
2.70e-34 |
|
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: 125.20 E-value: 2.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 3 SAVLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRII------MNGYSQDDdhLKa 76
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrlfgerRGGEDVWE--LR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 77 mSSVGaiIENPEFYSYLTGFENLE------LYASM--HDGVSEE---RIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIA 145
Cdd:COG1119 78 -KRIG--LVSPALQLRFPRDETVLdvvlsgFFDSIglYREPTDEqreRARELLELLGLAHLADRPFGTLSQGEQRRVLIA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515936072 146 QAILHKPNLLILDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQIKA 214
Cdd:COG1119 155 RALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVA 223
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-212 |
5.07e-34 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 127.76 E-value: 5.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 1 MQSAVLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysQDDDHLKA-MSS 79
Cdd:PRK09452 10 SLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDG--QDITHVPAeNRH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 80 VGAIIENPEFYSYLTGFENLELYASMHDGVSEE---RIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLI 156
Cdd:PRK09452 88 VNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEitpRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515936072 157 LDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:PRK09452 168 LDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRI 223
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
7-213 |
6.93e-34 |
|
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: 122.75 E-value: 6.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 7 HIENVDKQIGRHQ-ILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysqDDDHLKA-MSSVGAII 84
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKErRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 85 ENPEFYSYLTGFENlELYASMHD-GVSEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNG 163
Cdd:cd03226 78 QDVDYQLFTDSVRE-ELLLGLKElDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515936072 164 LDPAGMKE----FREhlqmlVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQIK 213
Cdd:cd03226 157 LDYKNMERvgelIRE-----LAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
18-212 |
1.41e-33 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 124.10 E-value: 1.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 18 HQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGY---SQDDDHLKAM-SSVGAIIENPE---FY 90
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRditAKKKKKLKDLrKKVGLVFQFPEhqlFE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 91 syLTGFENLElYASMHDGVSE----ERIFEVVKRVRLEHAIHQKvKTYSL--GMKQRLGIAQAILHKPNLLILDEPTNGL 164
Cdd:TIGR04521 98 --ETVYKDIA-FGPKNLGLSEeeaeERVKEALELVGLDEEYLER-SPFELsgGQMRRVAIAGVLAMEPEVLILDEPTAGL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 515936072 165 DPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:TIGR04521 174 DPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKI 221
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-212 |
2.07e-33 |
|
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: 121.98 E-value: 2.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 6 LHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysQDDDHLKAMS-SVGAII 84
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGG--RDVTDLPPKDrDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 85 ENPEFYSYLTGFENLELYASMHDG---VSEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPT 161
Cdd:cd03301 79 QNYALYPHMTVYDNIAFGLKLRKVpkdEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515936072 162 NGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:cd03301 159 SNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-212 |
3.10e-33 |
|
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: 121.48 E-value: 3.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 6 LHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAM---SSVGA 82
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINelrQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 83 IIENPEFYSYLTGFENLELYASMHDGVS----EERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILD 158
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVKGMSkaeaEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515936072 159 EPTNGLDPAGMKEFREHLQMLVQeEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAE-EGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-211 |
3.44e-33 |
|
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: 119.80 E-value: 3.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 6 LHIENVDKQIG--RHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAM-SSVGA 82
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLrKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 83 IIENPEFYSyLTGFENLelyasmhdgvseerifevvkrvrlehaihqkvktYSLGMKQRLGIAQAILHKPNLLILDEPTN 162
Cdd:cd03228 81 VPQDPFLFS-GTIRENI----------------------------------LSGGQRQRIAIARALLRDPPILILDEATS 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 515936072 163 GLDPAGMKEFREHLQMLvqEEGVSVLFATHLLHEVeELCDRMIIIQKGQ 211
Cdd:cd03228 126 ALDPETEALILEALRAL--AKGKTVIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
16-192 |
5.19e-33 |
|
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: 120.22 E-value: 5.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 16 GRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDH---LKAMSSVGAIIENPE---F 89
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRkglLERRQRVGLVFQDPDdqlF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 90 YSylTGFENLElYASMHDGVSEERIFEVVKR----VRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLD 165
Cdd:TIGR01166 83 AA--DVDQDVA-FGPLNLGLSEAEVERRVREaltaVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLD 159
|
170 180
....*....|....*....|....*..
gi 515936072 166 PAGMKEFREHLQMLVqEEGVSVLFATH 192
Cdd:TIGR01166 160 PAGREQMLAILRRLR-AEGMTVVISTH 185
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
3-212 |
1.06e-32 |
|
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: 120.47 E-value: 1.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 3 SAVLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysQDDDHLKA------ 76
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDG--EDITGLPPhriarl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 77 -MSSVgaiienPE----FySYLTGFENLELYASMHDGVSEERifEVVKRV-----RLEHAIHQKVKTYSLGMKQRLGIAQ 146
Cdd:COG0410 79 gIGYV------PEgrriF-PSLTVEENLLLGAYARRDRAEVR--ADLERVyelfpRLKERRRQRAGTLSGGEQQMLAIGR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515936072 147 AILHKPNLLILDEPTNGLDPAGMKEFREHLQMLvQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:COG0410 150 ALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLERGRI 214
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
4-212 |
1.63e-32 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 122.87 E-value: 1.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 4 AVLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysQDDDHLK------AM 77
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGG--RDVTDLPpkdrniAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 78 ssVgaiienpeFYSY-----LTGFENLELYASMHdGVS----EERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAI 148
Cdd:COG3839 80 --V--------FQSYalyphMTVYENIAFPLKLR-KVPkaeiDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515936072 149 LHKPNLLILDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:COG3839 149 VREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRI 212
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
16-229 |
1.70e-32 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 126.03 E-value: 1.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 16 GRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYS---QDDDHLKAMssVGAIIENPE-FYS 91
Cdd:COG4987 346 AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDlrdLDEDDLRRR--IAVVPQRPHlFDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 92 ylTGFENLELYAsmhDGVSEERIFEVVKRVRLEHAIHQKVKTY-----------SLGMKQRLGIAQAILHKPNLLILDEP 160
Cdd:COG4987 424 --TLRENLRLAR---PDATDEELWAALERVGLGDWLAALPDGLdtwlgeggrrlSGGERRRLALARALLRDAPILLLDEP 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515936072 161 TNGLDPAG----MKEFREHLQmlvqeeGVSVLFATHLLHEVeELCDRMIIIQKGQIKantnlrdMEGKEQVLM 229
Cdd:COG4987 499 TEGLDAATeqalLADLLEALA------GRTVLLITHRLAGL-ERMDRILVLEDGRIV-------EQGTHEELL 557
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
31-212 |
3.93e-32 |
|
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: 118.55 E-value: 3.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 31 GEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAMSS-----VGAIIENPEFYSYLTGFENLElYASM 105
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPpqqrkIGLVFQQYALFPHLNVRENLA-FGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 106 HDGVSEERIF--EVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPAGMKEFREHLQMLVQEE 183
Cdd:cd03297 102 RKRNREDRISvdELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNL 181
|
170 180
....*....|....*....|....*....
gi 515936072 184 GVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:cd03297 182 NIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6-212 |
9.37e-32 |
|
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: 118.21 E-value: 9.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 6 LHIENVDKQIGRHQiLQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysQDDDHLKA-MSSVGAII 84
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNG--KDITNLPPeKRDISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 85 ENPEFYSYLTGFENLElYASMHDGVS----EERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEP 160
Cdd:cd03299 78 QNYALFPHMTVYKNIA-YGLKKRKVDkkeiERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515936072 161 TNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:cd03299 157 FSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
8-212 |
1.02e-31 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 117.67 E-value: 1.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 8 IENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKN-----NGRIIMNG---YSQDDDHLKAMSS 79
Cdd:cd03260 3 LRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGkdiYDLDVDVLELRRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 80 VGAIIENPEFYSyLTGFENLELYASMH----DGVSEERIFEVVKRVRLEHAIHQKVKTYSL--GMKQRLGIAQAILHKPN 153
Cdd:cd03260 83 VGMVFQKPNPFP-GSIYDNVAYGLRLHgiklKEELDERVEEALRKAALWDEVKDRLHALGLsgGQQQRLCLARALANEPE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515936072 154 LLILDEPTNGLDPAGMKEFREHLQMLVQEegVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:cd03260 162 VLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
4-227 |
1.21e-31 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 118.07 E-value: 1.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 4 AVLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNgysqDDD------HLKAM 77
Cdd:PRK10895 2 ATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIID----DEDisllplHARAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 78 SSVGAIIENPEFYSYLTGFENLELYASMHDGVSEE----RIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPN 153
Cdd:PRK10895 78 RGIGYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEqredRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPK 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515936072 154 LLILDEPTNGLDPAGMKEFREHLQMLvQEEGVSVLFATHLLHEVEELCDRMIIIQKGQIKANTNLRDMEGKEQV 227
Cdd:PRK10895 158 FILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHV 230
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-212 |
2.45e-31 |
|
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: 116.95 E-value: 2.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 6 LHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysQDDDHLKAMS-SVGAII 84
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDG--KDITNLPPHKrPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 85 ENPEFYSYLTGFEN----LELyASMHDGVSEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEP 160
Cdd:cd03300 79 QNYALFPHLTVFENiafgLRL-KKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515936072 161 TNGLDpagmKEFREHLQM----LVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:cd03300 158 LGALD----LKLRKDMQLelkrLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
23-204 |
2.78e-31 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 123.31 E-value: 2.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 23 HISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAMSSVGAIIENPEFYSYLTGFENLELY 102
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVGYMSQAFSLYGELTVRQNLELH 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 103 A---SMHDGVSEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPAGMKEFREHLQML 179
Cdd:NF033858 364 ArlfHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIEL 443
|
170 180
....*....|....*....|....*
gi 515936072 180 VQEEGVSVLFATHLLHEVeELCDRM 204
Cdd:NF033858 444 SREDGVTIFISTHFMNEA-ERCDRI 467
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
10-264 |
3.31e-31 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 119.45 E-value: 3.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 10 NVDKQIGRHQIlqHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAMSS-----VGAII 84
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPpekrrIGYVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 85 ENPEFYSYLTGFENLELYASMHDG----VSEERIFEVVKrvrLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEP 160
Cdd:TIGR02142 82 QEARLFPHLSVRGNLRYGMKRARPserrISFERVIELLG---IGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 161 TNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQIKANTNLRDMEGKEQvlMNIQPVEKAVSW 240
Cdd:TIGR02142 159 LAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPD--LPWLAREDQGSL 236
|
250 260 270
....*....|....*....|....*....|...
gi 515936072 241 LD------TQGY---TYEQRDQHVLVQLKKDRV 264
Cdd:TIGR02142 237 IEgvvaehDQHYgltALRLGGGHLWVPENLGPT 269
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
5-212 |
3.70e-31 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 117.01 E-value: 3.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 5 VLHIENVDKQIGR-HQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYS----QDDDHLKAMSS 79
Cdd:TIGR02315 1 MLEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDitklRGKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 80 VGAIIENPEFYSYLTGFEN-----------LELYASMHDGVSEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAI 148
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENvlhgrlgykptWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515936072 149 LHKPNLLILDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEI 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-211 |
4.83e-31 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 121.29 E-value: 4.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 1 MQSAVLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQdddHLKamSSV 80
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV---RIR--SPR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 81 GAI-------------IENpefysyLTGFENLELYASMHDGVS------EERIFEVVKRVRLEHAIHQKVKTYSLGMKQR 141
Cdd:COG3845 76 DAIalgigmvhqhfmlVPN------LTVAENIVLGLEPTKGGRldrkaaRARIRELSERYGLDVDPDAKVEDLSVGEQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 142 LGIAQAILHKPNLLILDEPTNGLDPAGMKEFREHLQMLVqEEGVSVLFATHLLHEVEELCDRMIIIQKGQ 211
Cdd:COG3845 150 VEILKALYRGARILILDEPTAVLTPQEADELFEILRRLA-AEGKSIIFITHKLREVMAIADRVTVLRRGK 218
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
6-212 |
1.00e-30 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 118.33 E-value: 1.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 6 LHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysQD-DDHLKA-MSSVGAI 83
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNG--RDlFTNLPPrERRVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 84 IENPEFYSYLTGFEN----LElyasmHDGVSEERIFEVV----KRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLL 155
Cdd:COG1118 81 FQHYALFPHMTVAENiafgLR-----VRPPSKAEIRARVeellELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515936072 156 ILDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:COG1118 156 LLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRI 212
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
16-233 |
1.85e-30 |
|
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: 120.25 E-value: 1.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 16 GRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKA-MSSVGAIIENPefysYLt 94
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwRRQIAWVPQNP----YL- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 95 gF-----ENLELYASmhdGVSEERIFEVVKRVRLEHAIHQKVKTY-----------SLGMKQRLGIAQAILHKPNLLILD 158
Cdd:COG4988 423 -FagtirENLRLGRP---DASDEELEAALEAAGLDEFVAALPDGLdtplgeggrglSGGQAQRLALARALLRDAPLLLLD 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515936072 159 EPTNGLDPAGMKEFREHLQMLVQeeGVSVLFATHLLHEVEElCDRMIIIQKGQIKAntnlrdmEGKEQVLMNIQP 233
Cdd:COG4988 499 EPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQ-ADRILVLDDGRIVE-------QGTHEELLAKNG 563
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-232 |
2.14e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 115.72 E-value: 2.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 1 MQSAVLHIENVDKQI--GRHQiLQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDH---LK 75
Cdd:PRK13636 1 MEDYILKVEELNYNYsdGTHA-LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRkglMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 76 AMSSVGAIIENPEFYSYLTGFENLELYASMHDGVSE----ERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHK 151
Cdd:PRK13636 80 LRESVGMVFQDPDNQLFSASVYQDVSFGAVNLKLPEdevrKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVME 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 152 PNLLILDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQIKANTNLRDMEGKEQVLMNI 231
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEMLRKV 239
|
.
gi 515936072 232 Q 232
Cdd:PRK13636 240 N 240
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-212 |
3.67e-30 |
|
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: 115.92 E-value: 3.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 5 VLHIENVDKQI----GRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNN---GRIIMNGysQDDDHLK-- 75
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDG--EDLLKLSek 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 76 ----------------AMSS------VGAIIEnpefysyltgfENLELyasmHDGVS----EERIFEVVKRVRLEHAI-- 127
Cdd:COG0444 79 elrkirgreiqmifqdPMTSlnpvmtVGDQIA-----------EPLRI----HGGLSkaeaRERAIELLERVGLPDPErr 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 128 -----HQkvktYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDP---AG-MKEFREhlqmLVQEEGVSVLFATHLLHEVE 198
Cdd:COG0444 144 ldrypHE----LSGGMRQRVMIARALALEPKLLIADEPTTALDVtiqAQiLNLLKD----LQRELGLAILFITHDLGVVA 215
|
250
....*....|....
gi 515936072 199 ELCDRMIIIQKGQI 212
Cdd:COG0444 216 EIADRVAVMYAGRI 229
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-213 |
4.13e-30 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 119.01 E-value: 4.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 5 VLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMN-----GY-SQDDDHLkams 78
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGetvkiGYfDQHQEEL---- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 79 svgaiieNPEfysyLTGFENLELYAsmhDGVSEERIfevvkRVRLEH------AIHQKVKTYSLGMKQRLGIAQAILHKP 152
Cdd:COG0488 391 -------DPD----KTVLDELRDGA---PGGTEQEV-----RGYLGRflfsgdDAFKPVGVLSGGEKARLALAKLLLSPP 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515936072 153 NLLILDEPTNGLDPagmkEFREHLQMLVQE-EGvSVLFATHLLHEVEELCDRMIIIQKGQIK 213
Cdd:COG0488 452 NVLLLDEPTNHLDI----ETLEALEEALDDfPG-TVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
20-192 |
5.95e-30 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 112.66 E-value: 5.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 20 ILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDD----------HLKAMssvgaiieNPEf 89
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPdvaeachylgHRNAM--------KPA- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 90 ysyLTGFENLELYASMHDGvSEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPAGM 169
Cdd:PRK13539 88 ---LTVAENLEFWAAFLGG-EELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAV 163
|
170 180
....*....|....*....|....*..
gi 515936072 170 KEF----REHLqmlvqEEGVSVLFATH 192
Cdd:PRK13539 164 ALFaeliRAHL-----AQGGIVIAATH 185
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
8-212 |
1.26e-29 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 115.18 E-value: 1.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 8 IENVDK----QIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysQDddhLKAMS----- 78
Cdd:COG1135 4 LENLSKtfptKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDG--VD---LTALSerelr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 79 ----SVGAIIENPEFYSYLTGFEN----LELyasmhDGVS----EERIFEVVKRVRLEHaihqKVKTY----SLGMKQRL 142
Cdd:COG1135 79 aarrKIGMIFQHFNLLSSRTVAENvalpLEI-----AGVPkaeiRKRVAELLELVGLSD----KADAYpsqlSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 143 GIAQAILHKPNLLILDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:COG1135 150 GIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
10-212 |
1.85e-29 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 112.11 E-value: 1.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 10 NVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAMS---SVGAIIEN 86
Cdd:PRK09493 6 NVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLirqEAGMVFQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 87 PEFYSYLTGFENLELYASMHDGVS----EERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTN 162
Cdd:PRK09493 86 FYLFPHLTALENVMFGPLRVRGASkeeaEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515936072 163 GLDPagmkEFREHLQMLVQ---EEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:PRK09493 166 ALDP----ELRHEVLKVMQdlaEEGMTMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
4-214 |
1.91e-29 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 112.04 E-value: 1.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 4 AVLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysQDDDHLkAM------ 77
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDG--EDITHL-PMhkrarl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 78 --------SSVgaiienpefYSYLTGFENLELYASMHdGVS----EERIFEVVKRVRLEHaiHQKVKTYSL--GMKQRLG 143
Cdd:COG1137 79 gigylpqeASI---------FRKLTVEDNILAVLELR-KLSkkerEERLEELLEEFGITH--LRKSKAYSLsgGERRRVE 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515936072 144 IAQAILHKPNLLILDEPTNGLDPAGMKEFREHLQMLvQEEGVSVLFATHLLHEVEELCDRMIIIQKGQIKA 214
Cdd:COG1137 147 IARALATNPKFILLDEPFAGVDPIAVADIQKIIRHL-KERGIGVLITDHNVRETLGICDRAYIISEGKVLA 216
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-210 |
4.96e-29 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 111.02 E-value: 4.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 21 LQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAMssvgAIIENPEFYSYLTGFENLE 100
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM----VVFQNYSLLPWLTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 101 LY--ASMHDGVSEER---IFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPAGMKEFREH 175
Cdd:TIGR01184 77 LAvdRVLPDLSKSERraiVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEE 156
|
170 180 190
....*....|....*....|....*....|....*
gi 515936072 176 LQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKG 210
Cdd:TIGR01184 157 LMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
21-212 |
5.93e-29 |
|
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: 111.58 E-value: 5.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 21 LQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNG---YSQDDDHLKAMSS--VGAIIENPEFYSYLTG 95
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdiAAMSRKELRELRRkkISMVFQSFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 96 FEN----LELyASMHDGVSEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPAGMKE 171
Cdd:cd03294 120 LENvafgLEV-QGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRRE 198
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 515936072 172 FREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:cd03294 199 MQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-214 |
8.01e-29 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 111.65 E-value: 8.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 1 MQSAVLHIENVDKQI--GRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHL-KAM 77
Cdd:PRK13635 1 MKEEIIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVwDVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 78 SSVGAIIENPEFYSYLTGFENLELYASMHDGVSE----ERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPN 153
Cdd:PRK13635 81 RQVGMVFQNPDNQFVGATVQDDVAFGLENIGVPReemvERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515936072 154 LLILDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEElCDRMIIIQKGQIKA 214
Cdd:PRK13635 161 IIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILE 220
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
20-205 |
1.07e-28 |
|
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: 109.12 E-value: 1.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 20 ILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAMSSVGAIIENPEFYSYLTGFENL 99
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 100 ELYASMHdgvSEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPAGMKEFREHLQML 179
Cdd:cd03231 95 RFWHADH---SDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGH 171
|
170 180
....*....|....*....|....*.
gi 515936072 180 VQEEGvSVLFATHLLHEVEELCDRMI 205
Cdd:cd03231 172 CARGG-MVVLTTHQDLGLSEAGAREL 196
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-212 |
1.67e-28 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 110.49 E-value: 1.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 1 MQSaVLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNN---------GRIIMNGYSQDD 71
Cdd:PRK09984 1 MQT-IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellGRTVQREGRLAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 72 DHLKAMSSVGAIIENPEFYSYLTGFENLELYA-----------SMHDGVSEERIFEVVKRVRLEHAIHQKVKTYSLGMKQ 140
Cdd:PRK09984 80 DIRKSRANTGYIFQQFNLVNRLSVLENVLIGAlgstpfwrtcfSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515936072 141 RLGIAQAILHKPNLLILDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-212 |
3.14e-28 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 108.93 E-value: 3.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 5 VLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNG--YSQDDDHLKAM-SSVG 81
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGedLTDSKKDINKLrRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 82 AIIENPEFYSYLTGFENLELyASMH-DGVS----EERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLI 156
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTL-APIKvKKMSkaeaEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVML 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515936072 157 LDEPTNGLDPagmkEF-REHLQMLVQ--EEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:COG1126 160 FDEPTSALDP----ELvGEVLDVMRDlaKEGMTMVVVTHEMGFAREVADRVVFMDGGRI 214
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
21-214 |
3.31e-28 |
|
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: 108.45 E-value: 3.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 21 LQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDD-DHLKAMSSVGAIIENPE-FYSYLTgfEN 98
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQlDPADLRRNIGYVPQDVTlFYGTLR--DN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 99 LELYASMHDgvsEERIFEVVKRVRLEHAIHQKVKTYSL-----------GMKQRLGIAQAILHKPNLLILDEPTNGLDPA 167
Cdd:cd03245 98 ITLGAPLAD---DERILRAAELAGVTDFVNKHPNGLDLqigergrglsgGQRQAVALARALLNDPPILLLDEPTSAMDMN 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 515936072 168 GMKEFREHLQMLVqeEGVSVLFATH---LLheveELCDRMIIIQKGQIKA 214
Cdd:cd03245 175 SEERLKERLRQLL--GDKTLIIITHrpsLL----DLVDRIIVMDSGRIVA 218
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-212 |
1.15e-27 |
|
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: 107.39 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 6 LHIENVDKQI-GRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYS-QDDDHLKAMSSVGAI 83
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDiREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 84 IENPEFYSYLTGFENLELYASMhDGVSEERI----FEVVKRVRLEHAihQKVKTY----SLGMKQRLGIAQAILHKPNLL 155
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKL-LKWPKEKIreraDELLALVGLDPA--EFADRYphelSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515936072 156 ILDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEI 214
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
21-212 |
1.96e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 108.21 E-value: 1.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 21 LQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAMS---SVGAIIENPEFYSYLTGFE 97
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDirkKVGLVFQYPEYQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 98 NLELYASMHDGVSEERIFEVVKR----VRLEHAIHQKVKTYSL--GMKQRLGIAQAILHKPNLLILDEPTNGLDPAGMKE 171
Cdd:PRK13637 103 KDIAFGPINLGLSEEEIENRVKRamniVGLDYEDYKDKSPFELsgGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDE 182
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 515936072 172 FREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:PRK13637 183 ILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKC 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-213 |
3.22e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 110.92 E-value: 3.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 8 IENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMN-----GY-SQDDDHLKAMSSVG 81
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPkglriGYlPQEPPLDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 82 AIIE-NPEFYSYLTGFENLELYASMHDGVSEE------------------RIFEVVKRVRLEHAIH-QKVKTYSLGMKQR 141
Cdd:COG0488 81 TVLDgDAELRALEAELEELEAKLAEPDEDLERlaelqeefealggweaeaRAEEILSGLGFPEEDLdRPVSELSGGWRRR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515936072 142 LGIAQAILHKPNLLILDEPTNGLDPAGMKEFREHLQmlvQEEGvSVLFATH---LLHEVeelCDRMIIIQKGQIK 213
Cdd:COG0488 161 VALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLK---NYPG-TVLVVSHdryFLDRV---ATRILELDRGKLT 228
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
5-211 |
3.66e-27 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 105.27 E-value: 3.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 5 VLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYS---QDDDHLKAMSSVG 81
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPirrQRDEYHQDLLYLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 82 ---AIieNPEfysyLTGFENLELYASMHDGVSEERIFEVVKRVRL---EHAihqKVKTYSLGMKQRLGIAQAILHKPNLL 155
Cdd:PRK13538 81 hqpGI--KTE----LTALENLRFYQRLHGPGDDEALWEALAQVGLagfEDV---PVRQLSAGQQRRVALARLWLTRAPLW 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515936072 156 ILDEPTNGLDPAGMKEFREHLQMLVQEEGVsVLFATHllHEVEELCDRMIIIQKGQ 211
Cdd:PRK13538 152 ILDEPFTAIDKQGVARLEALLAQHAEQGGM-VILTTH--QDLPVASDKVRKLRLGQ 204
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
21-212 |
1.05e-26 |
|
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: 104.41 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 21 LQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysQDDDHLKAMS------SVGAIIENPEFYSYLT 94
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNG--QDVSDLRGRAipylrrKIGVVFQDFRLLPDRN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 95 GFEN--LELYASMHDG-VSEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPAGMKE 171
Cdd:cd03292 95 VYENvaFALEVTGVPPrEIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 515936072 172 FREHLQMlVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:cd03292 175 IMNLLKK-INKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-221 |
1.22e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 108.95 E-value: 1.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 4 AVLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAMSSVG-A 82
Cdd:COG1129 3 PLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAGiA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 83 IIenpefY------SYLTGFENLEL-----------YASMHdgvseERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIA 145
Cdd:COG1129 83 II-----HqelnlvPNLSVAENIFLgreprrgglidWRAMR-----RRARELLARLGLDIDPDTPVGDLSVAQQQLVEIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515936072 146 QAILHKPNLLILDEPTNGLDPAGMKEFREHLQMLvQEEGVSVLFATHLLHEVEELCDRMIIIQKGQIKANTNLRDM 221
Cdd:COG1129 153 RALSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
31-221 |
1.63e-26 |
|
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: 106.72 E-value: 1.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 31 GEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYS-QDDDHLKAMS----SVGAIIENPEFYSYLTGFENLeLYAsM 105
Cdd:COG4148 25 RGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlQDSARGIFLPphrrRIGYVFQEARLFPHLSVRGNL-LYG-R 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 106 HDGVSEERIF---EVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPAGMKEFREHLQMLVQE 182
Cdd:COG4148 103 KRAPRAERRIsfdEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDE 182
|
170 180 190
....*....|....*....|....*....|....*....
gi 515936072 183 EGVSVLFATHLLHEVEELCDRMIIIQKGQIKANTNLRDM 221
Cdd:COG4148 183 LDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEV 221
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
8-212 |
2.83e-26 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 106.04 E-value: 2.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 8 IENVDK--QIGRHQI--LQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNG---YSQDDDHL-KAMSS 79
Cdd:PRK11153 4 LKNISKvfPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGqdlTALSEKELrKARRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 80 VGAIIENPEFYSYLTGFEN----LELyASMHDGVSEERIFEVVKRVRLEHaihqKVKTY----SLGMKQRLGIAQAILHK 151
Cdd:PRK11153 84 IGMIFQHFNLLSSRTVFDNvalpLEL-AGTPKAEIKARVTELLELVGLSD----KADRYpaqlSGGQKQRVAIARALASN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515936072 152 PNLLILDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:PRK11153 159 PKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
20-192 |
4.80e-26 |
|
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: 102.05 E-value: 4.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 20 ILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNG---YSQDDDHLKAMSSVGaiiENPEFYSYLTGF 96
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGtplAEQRDEPHENILYLG---HLPGLKPELSAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 97 ENLELYASMHDGvSEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPAG----MKEF 172
Cdd:TIGR01189 92 ENLHFWAAIHGG-AQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGvallAGLL 170
|
170 180
....*....|....*....|
gi 515936072 173 REHLQmlvqeEGVSVLFATH 192
Cdd:TIGR01189 171 RAHLA-----RGGIVLLTTH 185
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
16-250 |
6.04e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 103.73 E-value: 6.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 16 GRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAMSS-VGAIIENPEFYSYLT 94
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKfVGLVFQNPDDQIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 95 GFENLELYASMHDGVSEE----RIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPAGMK 170
Cdd:PRK13652 95 TVEQDIAFGPINLGLDEEtvahRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 171 EFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQIKANTNLRDMEGKEQVL----MNIQPVEKAVSWLDTQG- 245
Cdd:PRK13652 175 ELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDLLarvhLDLPSLPKLIRSLQAQGi 254
|
250
....*....|
gi 515936072 246 -----YTYEQ 250
Cdd:PRK13652 255 aidmaYTYQE 264
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
18-221 |
9.15e-26 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 106.90 E-value: 9.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 18 HQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSqdddhlkAMSSVGAIIENPefysyLTGFE 97
Cdd:PRK13545 37 HYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA-------ALIAISSGLNGQ-----LTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 98 NLELYASMHdGVSEERIFEVVKRVrLEHA-----IHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPAGMKEF 172
Cdd:PRK13545 105 NIELKGLMM-GLTKEKIKEIIPEI-IEFAdigkfIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKC 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 515936072 173 REHLQMLvQEEGVSVLFATHLLHEVEELCDRMIIIQKGQIKANTNLRDM 221
Cdd:PRK13545 183 LDKMNEF-KEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEV 230
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
3-201 |
1.65e-25 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 102.11 E-value: 1.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 3 SAVLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMN-----GYSQDDDHLKAM 77
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNgklriGYVPQKLYLDTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 78 SSVgaiienpefysyltgfeNLELYASMHDGVSEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLIL 157
Cdd:PRK09544 82 LPL-----------------TVNRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVL 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 515936072 158 DEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEV-----EELC 201
Cdd:PRK09544 145 DEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVmaktdEVLC 193
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-212 |
2.11e-25 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 101.49 E-value: 2.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 1 MQSAVLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDD-DHLKAMSS 79
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwQTAKIMRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 80 VGAII-ENPEFYSYLTGFENLELYASMHDgvsEERIFEVVKRV-----RLEHAIHQKVKTYSLGMKQRLGIAQAILHKPN 153
Cdd:PRK11614 81 AVAIVpEGRRVFSRMTVEENLAMGGFFAE---RDQFQERIKWVyelfpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515936072 154 LLILDEPTNGLDPAGMKEFREHLQMLvQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:PRK11614 158 LLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
16-212 |
4.03e-25 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 105.25 E-value: 4.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 16 GRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKA-MSSVGAIIENPEFYSyLT 94
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlRRQIGVVPQDTFLFS-GT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 95 GFENLeLYAsmHDGVSEERIFEVVKRVRLEHAIHQKVKTY-----------SLGMKQRLGIAQAILHKPNLLILDEPTNG 163
Cdd:COG1132 430 IRENI-RYG--RPDATDEEVEEAAKAAQAHEFIEALPDGYdtvvgergvnlSGGQRQRIAIARALLKDPPILILDEATSA 506
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 515936072 164 LDPAGMKEFREHLQMLVQeeGVSVLFATHLLHEVEElCDRMIIIQKGQI 212
Cdd:COG1132 507 LDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDGRI 552
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
23-214 |
4.54e-25 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 99.87 E-value: 4.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 23 HISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysQDDDHLK-AMSSVGAIIENPEFYSYLTGFEN--L 99
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING--VDVTAAPpADRPVSMLFQENNLFAHLTVEQNvgL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 100 ELYASMH-DGVSEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPAGMKEFREHLQM 178
Cdd:cd03298 94 GLSPGLKlTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLD 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 515936072 179 LVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQIKA 214
Cdd:cd03298 174 LHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAA 209
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
16-207 |
5.27e-25 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 104.68 E-value: 5.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 16 GRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysQDDDHLKAMS---SVGAIIENPEFYsY 92
Cdd:TIGR02857 333 GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNG--VPLADADADSwrdQIAWVPQHPFLF-A 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 93 LTGFENLELYASmhdGVSEERIFEVVKRV---RLEHAIHQKVKT--------YSLGMKQRLGIAQAILHKPNLLILDEPT 161
Cdd:TIGR02857 410 GTIAENIRLARP---DASDAEIREALERAgldEFVAALPQGLDTpigeggagLSGGQAQRLALARAFLRDAPLLLLDEPT 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 515936072 162 NGLDPAGMKEFREHLQMLVQeeGVSVLFATHLLHeVEELCDRMIII 207
Cdd:TIGR02857 487 AHLDAETEAEVLEALRALAQ--GRTVLLVTHRLA-LAALADRIVVL 529
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
6-215 |
7.75e-25 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 99.83 E-value: 7.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 6 LHIENVDKQIGrHQILqHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysqdDDHLKAMSS---VgA 82
Cdd:COG3840 2 LRLDDLTYRYG-DFPL-RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNG----QDLTALPPAerpV-S 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 83 II--ENPEFySYLTGFENLELyaSMHDG--VSEE---RIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLL 155
Cdd:COG3840 75 MLfqENNLF-PHLTVAQNIGL--GLRPGlkLTAEqraQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPIL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 156 ILDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQIKAN 215
Cdd:COG3840 152 LLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAAD 211
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
6-212 |
1.09e-24 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 100.15 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 6 LHIENVDKQI---------GRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNG--YSQDD--- 71
Cdd:PRK10419 4 LNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGepLAKLNraq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 72 -------------DHLKAM---SSVGAIIENPefYSYLTgfenlelyaSMHDGVSEERIFEVVKRVRLEHAIHQKV-KTY 134
Cdd:PRK10419 84 rkafrrdiqmvfqDSISAVnprKTVREIIREP--LRHLL---------SLDKAERLARASEMLRAVDLDDSVLDKRpPQL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 135 SLGMKQRLGIAQAILHKPNLLILDEPTNGLD---PAGMKEFREHLQmlvQEEGVSVLFATHLLHEVEELCDRMIIIQKGQ 211
Cdd:PRK10419 153 SGGQLQRVCLARALAVEPKLLILDEAVSNLDlvlQAGVIRLLKKLQ---QQFGTACLFITHDLRLVERFCQRVMVMDNGQ 229
|
.
gi 515936072 212 I 212
Cdd:PRK10419 230 I 230
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-211 |
1.31e-24 |
|
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: 96.75 E-value: 1.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 6 LHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIimngysqdddhlkamssvgaiie 85
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 86 npefysyltgfenlelyasmhdgvseerifEVVKRVRLEHaIHQkvktYSLGMKQRLGIAQAILHKPNLLILDEPTNGLD 165
Cdd:cd03221 58 ------------------------------TWGSTVKIGY-FEQ----LSGGEKMRLALAKLLLENPNLLLLDEPTNHLD 102
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515936072 166 PAGmkefREHL-QMLVQEEGvSVLFATHLLHEVEELCDRMIIIQKGQ 211
Cdd:cd03221 103 LES----IEALeEALKEYPG-TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
21-231 |
4.57e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 98.67 E-value: 4.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 21 LQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAM-SSVGAIIENPE--F------YS 91
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLrKHIGIVFQNPDnqFvgsivkYD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 92 YLTGFENLEL-YASMHdgvseERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPAGMK 170
Cdd:PRK13648 105 VAFGLENHAVpYDEMH-----RRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQ 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515936072 171 EFREHLQMLVQEEGVSVLFATHLLHEVEElCDRMIIIQKGQIKANTNLRDMEGKEQVLMNI 231
Cdd:PRK13648 180 NLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAEELTRI 239
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-212 |
4.59e-24 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 100.18 E-value: 4.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 1 MQSAVLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysQDDDHlkamSSv 80
Cdd:PRK11432 2 TQKNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDG--EDVTH----RS- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 81 gaiIENPE----FYSY-----LTGFENLELYASMHdGVSEE----RIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQA 147
Cdd:PRK11432 75 ---IQQRDicmvFQSYalfphMSLGENVGYGLKML-GVPKEerkqRVKEALELVDLAGFEDRYVDQISGGQQQRVALARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515936072 148 ILHKPNLLILDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:PRK11432 151 LILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKI 215
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-214 |
6.49e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 98.16 E-value: 6.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 19 QILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDH---LKAMSSVGAIIENPEFYSYLTG 95
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKrglLALRQQVATVFQDPEQQIFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 96 FENLELYASMHDGVSEE----RIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPAGMKE 171
Cdd:PRK13638 95 IDSDIAFSLRNLGVPEAeitrRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 515936072 172 FREHLQMLVQeEGVSVLFATHLLHEVEELCDRMIIIQKGQIKA 214
Cdd:PRK13638 175 MIAIIRRIVA-QGNHVIISSHDIDLIYEISDAVYVLRQGQILT 216
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-212 |
7.74e-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: 7.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 6 LHIENVDKQIG--RHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNG---YSQDDDHLKAMssV 80
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGadiSQWDPNELGDH--V 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 81 GAIIENPEFYSyltgfenlelyasmhdGVSEERIFevvkrvrlehaihqkvktySLGMKQRLGIAQAILHKPNLLILDEP 160
Cdd:cd03246 79 GYLPQDDELFS----------------GSIAENIL-------------------SGGQRQRLGLARALYGNPRILVLDEP 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515936072 161 TNGLDPAGMKEFREHLQMLvQEEGVSVLFATHLLhEVEELCDRMIIIQKGQI 212
Cdd:cd03246 124 NSHLDVEGERALNQAIAAL-KAAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-212 |
7.81e-24 |
|
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: 95.58 E-value: 7.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 4 AVLHIENvdkqIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysqDDDHLKamsSVGAI 83
Cdd:cd03215 3 PVLEVRG----LSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDG---KPVTRR---SPRDA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 84 IENPEFYsyltgfenlelyasmhdgVSEERIFEVVKrvrLEHAIHQKVKTYSL---GMKQRLGIAQAILHKPNLLILDEP 160
Cdd:cd03215 73 IRAGIAY------------------VPEDRKREGLV---LDLSVAENIALSSLlsgGNQQKVVLARWLARDPRVLILDEP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515936072 161 TNGLDPAGMKEFREHLQMLVqEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:cd03215 132 TRGVDVGAKAEIYRLIRELA-DAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
18-233 |
2.54e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 99.90 E-value: 2.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 18 HQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNG-----YSQDDdhLKAMSSVgaIIENPEFYSY 92
Cdd:PRK11160 353 QPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGqpiadYSEAA--LRQAISV--VSQRVHLFSA 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 93 lTGFENLELYAsmhDGVSEERIFEVVKRVRLEHAIHQKV----------KTYSLGMKQRLGIAQAILHKPNLLILDEPTN 162
Cdd:PRK11160 429 -TLRDNLLLAA---PNASDEALIEVLQQVGLEKLLEDDKglnawlgeggRQLSGGEQRRLGIARALLHDAPLLLLDEPTE 504
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515936072 163 GLDPAgmKEfREHLQMLVQE-EGVSVLFATHLLHEVEELcDRMIIIQKGQIKAntnlrdmEGKEQVLMNIQP 233
Cdd:PRK11160 505 GLDAE--TE-RQILELLAEHaQNKTVLMITHRLTGLEQF-DRICVMDNGQIIE-------QGTHQELLAQQG 565
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
19-212 |
2.66e-23 |
|
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: 94.54 E-value: 2.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 19 QILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMK--KNNGRIIMNGYSQDDDHLKAMSsvGAIIENPEFYSYLTGF 96
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLINGRPLDKRSFRKII--GYVPQDDILHPTLTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 97 ENLELYAsmhdgvseerifevvkrvrlehaihqKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPagmkeFREH- 175
Cdd:cd03213 101 ETLMFAA--------------------------KLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDS-----SSALq 149
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 515936072 176 -LQMLVQ--EEGVSVLFATH-LLHEVEELCDRMIIIQKGQI 212
Cdd:cd03213 150 vMSLLRRlaDTGRTIICSIHqPSSEIFELFDKLLLLSQGRV 190
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-169 |
3.03e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 95.95 E-value: 3.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 1 MQSAVLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysQD----DDHLKA 76
Cdd:COG4674 6 MHGPILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGG--TDltglDEHEIA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 77 MSSVGAIIENPEFYSYLTGFENLELYASMHDGV-----------SEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIA 145
Cdd:COG4674 84 RLGIGRKFQKPTVFEELTVFENLELALKGDRGVfaslfarltaeERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIG 163
|
170 180
....*....|....*....|....
gi 515936072 146 QAILHKPNLLILDEPTngldpAGM 169
Cdd:COG4674 164 MLLAQDPKLLLLDEPV-----AGM 182
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-212 |
5.87e-23 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 95.13 E-value: 5.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 6 LHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMN----GYSQDDDHLkaMssvg 81
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGtaplAEAREDTRL--M---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 82 aiienpefysyltgFENLEL--YASMHDGVS-------EERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKP 152
Cdd:PRK11247 87 --------------FQDARLlpWKKVIDNVGlglkgqwRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 153 NLLILDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:PRK11247 153 GLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
13-212 |
6.09e-23 |
|
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: 98.60 E-value: 6.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 13 KQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMkKNNGRIIMNGysQDDDHL--KAM------------- 77
Cdd:COG4172 294 RTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDG--QDLDGLsrRALrplrrrmqvvfqd 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 78 --SS------VGAIIEnpefysyltgfENLELYasmHDGVS----EERIFEVVKRVRLEHAI-----HQkvktYSLGMKQ 140
Cdd:COG4172 371 pfGSlsprmtVGQIIA-----------EGLRVH---GPGLSaaerRARVAEALEEVGLDPAArhrypHE----FSGGQRQ 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515936072 141 RLGIAQAILHKPNLLILDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:COG4172 433 RIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKV 504
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
12-223 |
1.19e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 94.77 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 12 DKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGY-SQDDDHL-KAMSSVGAIIENPEF 89
Cdd:PRK13633 17 NEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLdTSDEENLwDIRNKAGMVFQNPDN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 90 YSYLT--------GFENLelyasmhdGVSEE----RIFEVVKRVRL----EHAIHqkvkTYSLGMKQRLGIAQAILHKPN 153
Cdd:PRK13633 97 QIVATiveedvafGPENL--------GIPPEeireRVDESLKKVGMyeyrRHAPH----LLSGGQKQRVAIAGILAMRPE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 154 LLILDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEElCDRMIIIQKGQIKantnlrdMEG 223
Cdd:PRK13633 165 CIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVV-------MEG 226
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
21-232 |
1.31e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 95.09 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 21 LQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNG------RIIMNGYSQDDdhLKAM-SSVGAIIENPEFYSYL 93
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGtvtigeRVITAGKKNKK--LKPLrKKVGIVFQFPEHQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 94 TGFENLELYASMHDGVSEE----RIFEVVKRVRLEHAIHQKVK-TYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPAG 168
Cdd:PRK13634 101 ETVEKDICFGPMNFGVSEEdakqKAREMIELVGLPEELLARSPfELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKG 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515936072 169 MKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQIKANTNLRDMEGKEQVLMNIQ 232
Cdd:PRK13634 181 RKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDELEAIG 244
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
20-212 |
2.22e-22 |
|
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: 93.32 E-value: 2.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 20 ILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGY---SQDDDHLKAmsSVGAIIENPEFYSYlTGF 96
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHdlaLADPAWLRR--QVGVVLQENVLFNR-SIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 97 ENLelyASMHDGVSEERIFEVVKRVRLEHAIHQKVKTY-----------SLGMKQRLGIAQAILHKPNLLILDEPTNGLD 165
Cdd:cd03252 94 DNI---ALADPGMSMERVIEAAKLAGAHDFISELPEGYdtivgeqgaglSGGQRQRIAIARALIHNPRILIFDEATSALD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515936072 166 PAGMKEFREHLQMLVqeEGVSVLFATHLLHEVEElCDRMIIIQKGQI 212
Cdd:cd03252 171 YESEHAIMRNMHDIC--AGRTVIIIAHRLSTVKN-ADRIIVMEKGRI 214
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
19-212 |
2.23e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 93.99 E-value: 2.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 19 QILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDH---LKAMSSVGAIIENPEFYSYLTG 95
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKkslLEVRKTVGIVFQNPDDQLFAPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 96 FENLELYASMHDGVSEE----RIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPAGMKE 171
Cdd:PRK13639 96 VEEDVAFGPLNLGLSKEevekRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQ 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 515936072 172 FREHLQMLvQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:PRK13639 176 IMKLLYDL-NKEGITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-229 |
2.74e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 96.78 E-value: 2.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 1 MQSAVLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNG--YSQDDDHLKAMS 78
Cdd:PRK09700 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinYNKLDHKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 79 SVGAIIENPEFYSYLTGFENLEL---------------YASMhdgvsEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLG 143
Cdd:PRK09700 81 GIGIIYQELSVIDELTVLENLYIgrhltkkvcgvniidWREM-----RVRAAMMLLRVGLKVDLDEKVANLSISHKQMLE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 144 IAQAILHKPNLLILDEPTNGLDPAGMkefrEHLQMLVQE---EGVSVLFATHLLHEVEELCDRMIIIQKGQIKANTNLRD 220
Cdd:PRK09700 156 IAKTLMLDAKVIIMDEPTSSLTNKEV----DYLFLIMNQlrkEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSD 231
|
....*....
gi 515936072 221 MEGKEQVLM 229
Cdd:PRK09700 232 VSNDDIVRL 240
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-212 |
5.13e-22 |
|
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: 95.91 E-value: 5.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 1 MQSAVLHIENV----DKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNN----GRIIMNGY---SQ 69
Cdd:COG4172 2 MSMPLLSVEDLsvafGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAahpsGSILFDGQdllGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 70 DDDHLKA-------------MSS------VGAIIEnpefysyltgfENLELYASMHDGVSEERIFEVVKRVRLEHAiHQK 130
Cdd:COG4172 82 SERELRRirgnriamifqepMTSlnplhtIGKQIA-----------EVLRLHRGLSGAAARARALELLERVGIPDP-ERR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 131 VKTY----SLGMKQRLGIAQAILHKPNLLILDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMII 206
Cdd:COG4172 150 LDAYphqlSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAV 229
|
....*.
gi 515936072 207 IQKGQI 212
Cdd:COG4172 230 MRQGEI 235
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
18-231 |
6.75e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 92.87 E-value: 6.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 18 HQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHL-KAMSSVGAIIENPEfysyltgf 96
Cdd:PRK13650 20 KYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVwDIRHKIGMVFQNPD-------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 97 eNLELYASMHDGVS-------------EERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNG 163
Cdd:PRK13650 92 -NQFVGATVEDDVAfglenkgipheemKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSM 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515936072 164 LDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVeELCDRMIIIQKGQIKANTNLRDMEGKEQVLMNI 231
Cdd:PRK13650 171 LDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELFSRGNDLLQL 237
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
28-224 |
7.44e-22 |
|
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: 96.24 E-value: 7.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 28 IRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSqdddhlkAMSSVGAIIEN----PEFYS---YLTGFENLE 100
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKS-------ILTNISDVHQNmgycPQFDAiddLLTGREHLY 2034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 101 LYASMHdGVSEERIFEV----VKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPAGMKEFREHL 176
Cdd:TIGR01257 2035 LYARLR-GVPAEEIEKVanwsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTI 2113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 515936072 177 QMLVQeEGVSVLFATHLLHEVEELCDRMIIIQKGQIKANTNLRDMEGK 224
Cdd:TIGR01257 2114 VSIIR-EGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSK 2160
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
20-212 |
7.99e-22 |
|
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: 91.52 E-value: 7.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 20 ILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAMSSVGAIIENPEFYSYLTGFENL 99
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVSQDVFLFNDTVAENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 100 eLYASmhDGVSEERIFEVVKRVRLEHAIHQKVKTY-----------SLGMKQRLGIAQAILHKPNLLILDEPTNGLDPAG 168
Cdd:cd03251 97 -AYGR--PGATREEVEEAARAANAHEFIMELPEGYdtvigergvklSGGQRQRIAIARALLKDPPILILDEATSALDTES 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 515936072 169 MKEFREHLQMLVqeEGVSVLFATHLLHEVEElCDRMIIIQKGQI 212
Cdd:cd03251 174 ERLVQAALERLM--KNRTTFVIAHRLSTIEN-ADRIVVLEDGKI 214
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-214 |
8.28e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 92.14 E-value: 8.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 4 AVLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAMSSVGAI 83
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 84 IenPEfYSYLTgF-----ENLELYASMHDGVSEER---IFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAIL------ 149
Cdd:PRK13548 81 L--PQ-HSSLS-FpftveEVVAMGRAPHGLSRAEDdalVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepd 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515936072 150 HKPNLLILDEPTNGLDPAgmkefreH----LQM---LVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQIKA 214
Cdd:PRK13548 157 GPPRWLLLDEPTSALDLA-------HqhhvLRLarqLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVA 221
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
17-192 |
8.72e-22 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 91.17 E-value: 8.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 17 RHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKnngriimngysqdddhlKAMSSVGAIIENPeFYSYLTGF 96
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKG-----------------TPVAGCVDVPDNQ-FGREASLI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 97 ENLELYASMHDGVseerifEVVKRVRLEHAI--HQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPAGMKEFRE 174
Cdd:COG2401 104 DAIGRKGDFKDAV------ELLNAVGLSDAVlwLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVAR 177
|
170
....*....|....*...
gi 515936072 175 HLQMLVQEEGVSVLFATH 192
Cdd:COG2401 178 NLQKLARRAGITLVVATH 195
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
6-196 |
9.77e-22 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 92.07 E-value: 9.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 6 LHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysqdddhlKAMSSVGA--- 82
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG--------KPVEGPGAerg 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 83 -IIENPEFYSYLTGFEN----LELyASMHDGVSEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLIL 157
Cdd:PRK11248 74 vVFQNEGLLPWRNVQDNvafgLQL-AGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 515936072 158 DEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHE 196
Cdd:PRK11248 153 DEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEE 191
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
20-194 |
1.10e-21 |
|
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: 95.12 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 20 ILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGY---SQDDDHLKAMSSVGAiiENPEFYSyLTGF 96
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVpvsSLDQDEVRRRVSVCA--QDAHLFD-TTVR 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 97 ENLELYASmhdGVSEERIFEVVKRVRLE-------HAIHQKV----KTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLD 165
Cdd:TIGR02868 427 ENLRLARP---DATDEELWAALERVGLAdwlralpDGLDTVLgeggARLSGGERQRLALARALLADAPILLLDEPTEHLD 503
|
170 180
....*....|....*....|....*....
gi 515936072 166 PAGMKEFREhlQMLVQEEGVSVLFATHLL 194
Cdd:TIGR02868 504 AETADELLE--DLLAALSGRTVVLITHHL 530
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
21-212 |
2.51e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 91.20 E-value: 2.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 21 LQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDD-DHLKAMSS-VGAIIENPE--FYSYLT-- 94
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDfSKLQGIRKlVGIVFQNPEtqFVGRTVee 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 95 ----GFENLELYASMhdgvSEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPAGMK 170
Cdd:PRK13644 98 dlafGPENLCLPPIE----IRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 515936072 171 EFREHLQMLvQEEGVSVLFATHLLHEVEElCDRMIIIQKGQI 212
Cdd:PRK13644 174 AVLERIKKL-HEKGKTIVYITHNLEELHD-ADRIIVMDRGKI 213
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-212 |
2.86e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 93.62 E-value: 2.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 15 IGRHQILQHISMDIRQGEIVGLLGPNGSGKTT----LIRLIvglmkKNNGRIIMNGYSQDDDHLKAMSSVGAIIE----- 85
Cdd:PRK15134 296 VDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLLPVRHRIQvvfqd 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 86 -----NPEFYSYLTGFENLEL-YASMHDGVSEERIFEVVKRVRLEHAIHQKVKT-YSLGMKQRLGIAQAILHKPNLLILD 158
Cdd:PRK15134 371 pnsslNPRLNVLQIIEEGLRVhQPTLSAAQREQQVIAVMEEVGLDPETRHRYPAeFSGGQRQRIAIARALILKPSLIILD 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515936072 159 EPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:PRK15134 451 EPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEV 504
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
19-214 |
4.25e-21 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 88.14 E-value: 4.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 19 QILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGySQDDDHLKAMSS-VGAIIENPEFYSyLTGFE 97
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDG-VPVSDLEKALSSlISVLNQRPYLFD-TTLRN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 98 NLElyasmhdgvseerifevvkrvrlehaihqkvKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPagmKEFREHLQ 177
Cdd:cd03247 94 NLG-------------------------------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDP---ITERQLLS 139
|
170 180 190
....*....|....*....|....*....|....*...
gi 515936072 178 MLVQE-EGVSVLFATHLLHEVEELcDRMIIIQKGQIKA 214
Cdd:cd03247 140 LIFEVlKDKTLIWITHHLTGIEHM-DKILFLENGKIIM 176
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
19-237 |
8.55e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 89.79 E-value: 8.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 19 QILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAM-SSVGAIIENPE---FYSylT 94
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVrSKVGLVFQDPDdqvFSS--T 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 95 GFE-------NLELYASMhdgvSEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPA 167
Cdd:PRK13647 97 VWDdvafgpvNMGLDKDE----VERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPR 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 168 GMKEFREHLQMLVQeEGVSVLFATHLLHEVEELCDRMIIIQKGQIKAntnlrdmEGKEQVLMNIQPVEKA 237
Cdd:PRK13647 173 GQETLMEILDRLHN-QGKTVIVATHDVDLAAEWADQVIVLKEGRVLA-------EGDKSLLTDEDIVEQA 234
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
19-214 |
1.18e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 89.28 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 19 QILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLK-AMSSVGAIIENPefysyltgfE 97
Cdd:PRK13632 23 NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKeIRKKIGIIFQNP---------D 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 98 NLELYASMHDGVS---EER----------IFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGL 164
Cdd:PRK13632 94 NQFIGATVEDDIAfglENKkvppkkmkdiIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSML 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 515936072 165 DPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVeELCDRMIIIQKGQIKA 214
Cdd:PRK13632 174 DPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIA 222
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-218 |
1.45e-20 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 88.33 E-value: 1.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 1 MQSAVLHIENVDK--QIGRHQ--ILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSqdddhLKA 76
Cdd:PRK11629 1 MNKILLQCDNLCKryQEGSVQtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQP-----MSK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 77 MSSVG-AIIENPE------FYSYLTGFENLE------LYASMHDGVSEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLG 143
Cdd:PRK11629 76 LSSAAkAELRNQKlgfiyqFHHLLPDFTALEnvamplLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515936072 144 IAQAILHKPNLLILDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELcDRMIIIQKGQIKANTNL 218
Cdd:PRK11629 156 IARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTAELSL 229
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-244 |
1.70e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 91.27 E-value: 1.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 3 SAVLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDddHLKAMSS--- 79
Cdd:PRK15439 9 PPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCA--RLTPAKAhql 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 80 -VGAIIENPEFYSYLTGFENLELYASMHDGvSEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILD 158
Cdd:PRK15439 87 gIYLVPQEPLLFPNLSVKENILFGLPKRQA-SMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 159 EPTNGLDPAGMKEFREHLQMLvQEEGVSVLFATHLLHEVEELCDRMIIIQKGQIKANTNLRDMEgKEQVLMNIQPVEKAV 238
Cdd:PRK15439 166 EPTASLTPAETERLFSRIREL-LAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLS-TDDIIQAITPAAREK 243
|
....*.
gi 515936072 239 SWLDTQ 244
Cdd:PRK15439 244 SLSASQ 249
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
21-232 |
2.30e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 88.91 E-value: 2.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 21 LQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYS-----QDDDHLKAM-SSVGAIIENPEFYSYLT 94
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAipanlKKIKEVKRLrKEIGLVFQFPEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 95 GFENLELYASMHDGVSEERIF----EVVKRVRL-EHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPAGM 169
Cdd:PRK13645 107 TIEKDIAFGPVNLGENKQEAYkkvpELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGE 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515936072 170 KEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQIKANTNLRDMEGKEQVLMNIQ 232
Cdd:PRK13645 187 EDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQELLTKIE 249
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
8-212 |
2.33e-20 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 87.88 E-value: 2.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 8 IENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDD-HLKAMSS------- 79
Cdd:PRK11264 6 VKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTArSLSQQKGlirqlrq 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 80 -VGAIIENPEFYSYLTGFENL----ELYASMHDGVSEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNL 154
Cdd:PRK11264 86 hVGFVFQNFNLFPHRTVLENIiegpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEV 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515936072 155 LILDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLfATHLLHEVEELCDRMIIIQKGQI 212
Cdd:PRK11264 166 ILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRI 222
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
19-166 |
2.85e-20 |
|
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: 87.33 E-value: 2.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 19 QILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLM---KKNNGRIIMNGYSQDDDHLKamSSVGAIIENPEFYSYLTG 95
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQPRKPDQFQ--KCVAYVRQDDILLPGLTV 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515936072 96 FENLELYA------SMHDGVSEERI-FEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDP 166
Cdd:cd03234 99 RETLTYTAilrlprKSSDAIRKKRVeDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-221 |
3.52e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 90.37 E-value: 3.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 1 MQSAVLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKN--NGRIIMNGYSQDDDHLKAMS 78
Cdd:PRK13549 1 MMEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQASNIRDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 79 SVGAIIENPEF--YSYLTGFENLEL-----------YASMHdgvseERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIA 145
Cdd:PRK13549 81 RAGIAIIHQELalVKELSVLENIFLgneitpggimdYDAMY-----LRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515936072 146 QAILHKPNLLILDEPTNGLDPagmKEFREHLQML--VQEEGVSVLFATHLLHEVEELCDRMIIIQKGQIKANTNLRDM 221
Cdd:PRK13549 156 KALNKQARLLILDEPTASLTE---SETAVLLDIIrdLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGM 230
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
16-197 |
4.05e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 86.13 E-value: 4.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 16 GRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNG---------YSQDDDHLKAmsSVGAIIEn 86
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgarvayvpqRSEVPDSLPL--TVRDLVA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 87 pefysyltgfenLELYASM-----HDGVSEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPT 161
Cdd:NF040873 80 ------------MGRWARRglwrrLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190
....*....|....*....|....*....|....*.
gi 515936072 162 NGLDPAGMKEFREHLQMLVqEEGVSVLFATHLLHEV 197
Cdd:NF040873 148 TGLDAESRERIIALLAEEH-ARGATVVVVTHDLELV 182
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-213 |
6.18e-20 |
|
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: 89.86 E-value: 6.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 6 LHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGL--MKKNNGRIIMN-------GYSQ------- 69
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHvalcekcGYVErpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 70 -------------------DDDHLKAMSSVGAIIENPEF--YSYLTGFENLelYASMHDGVSE-----ERIFEVVKRVRL 123
Cdd:TIGR03269 81 pcpvcggtlepeevdfwnlSDKLRRRIRKRIAIMLQRTFalYGDDTVLDNV--LEALEEIGYEgkeavGRAVDLIEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 124 EHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDR 203
Cdd:TIGR03269 159 SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDK 238
|
250
....*....|
gi 515936072 204 MIIIQKGQIK 213
Cdd:TIGR03269 239 AIWLENGEIK 248
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
23-212 |
8.88e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 89.34 E-value: 8.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 23 HISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAMSSVGaIIENPEFYS----YLTGFEN 98
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARG-LVYLPEDRQssglYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 99 LELYASMHDGVS-------EERIFEVVKR---VRLEHAiHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPAG 168
Cdd:PRK15439 360 WNVCALTHNRRGfwikparENAVLERYRRalnIKFNHA-EQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515936072 169 mkefREHLQMLVQ---EEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:PRK15439 439 ----RNDIYQLIRsiaAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-213 |
1.37e-19 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 86.18 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 1 MQSAVLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYS-----QDDDHLK 75
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlvrDKDGQLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 76 AM---------SSVGAIIENPEFYSYLTGFENLELYASMHDGVSE----ERIFEVVKRVRLEHAIHQKVKTY-SLGMKQR 141
Cdd:PRK10619 81 VAdknqlrllrTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKqearERAVKYLAKVGIDERAQGKYPVHlSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515936072 142 LGIAQAILHKPNLLILDEPTNGLDPAGMKEFREHLQMLVqEEGVSVLFATHLLHEVEELCDRMIIIQKGQIK 213
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLA-EEGKTMVVVTHEMGFARHVSSHVIFLHQGKIE 231
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
23-210 |
1.44e-19 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 85.81 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 23 HISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQD--DDHLKAMSSVGAIIENPEFYSYLTGFENL- 99
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEglPGHQIARMGVVRTFQHVRLFREMTVIENLl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 100 -----ELYASMHDGVSEERIFEVVKRVRLEHAIH------------QKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTN 162
Cdd:PRK11300 103 vaqhqQLKTGLFSGLLKTPAFRRAESEALDRAATwlervgllehanRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAA 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 515936072 163 GLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKG 210
Cdd:PRK11300 183 GLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
20-258 |
1.46e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 86.39 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 20 ILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLM---KKNNGRIIMNGYSQDDDHL-KAMSSVGAIIENP--EFYSYL 93
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVwDIREKVGIVFQNPdnQFVGAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 94 T------GFENlelyasmhDGVSEERIFEVVKRVRLEHAIHQKVKT----YSLGMKQRLGIAQAILHKPNLLILDEPTNG 163
Cdd:PRK13640 102 VgddvafGLEN--------RAVPRPEMIKIVRDVLADVGMLDYIDSepanLSGGQKQRVAIAGILAVEPKIIILDESTSM 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 164 LDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVeELCDRMIIIQKGQIKANTNLRDMEGKEQVL----MNIQPVEKAVS 239
Cdd:PRK13640 174 LDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVEMLkeigLDIPFVYKLKN 252
|
250 260
....*....|....*....|.
gi 515936072 240 WLDTQGYTYEQ--RDQHVLVQ 258
Cdd:PRK13640 253 KLKEKGISVPQeiNTEEKLVQ 273
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-212 |
1.59e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 87.78 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 1 MQSAVLhiENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHlKAMSSV 80
Cdd:PRK11000 1 MASVTL--RNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVP-PAERGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 81 GAIIENPEFYSYLTGFEN----LELyASMHDGVSEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLI 156
Cdd:PRK11000 78 GMVFQSYALYPHLSVAENmsfgLKL-AGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515936072 157 LDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:PRK11000 157 LDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
5-214 |
1.96e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 88.15 E-value: 1.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 5 VLHIENVdkqiGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysqdddHLKAMSSVGAII 84
Cdd:COG1129 256 VLEVEGL----SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDG------KPVRIRSPRDAI 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 85 EN-----PE------FYSYLTGFENLELyASMHDG-----VSEERIFEVVKRV--RLE---HAIHQKVKTYSLGMKQRLG 143
Cdd:COG1129 326 RAgiayvPEdrkgegLVLDLSIRENITL-ASLDRLsrgglLDRRRERALAEEYikRLRiktPSPEQPVGNLSGGNQQKVV 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515936072 144 IAQAILHKPNLLILDEPTNGLDpAGMKefREHLQMLVQ--EEGVSVLFATHLLHEVEELCDRMIIIQKGQIKA 214
Cdd:COG1129 405 LAKWLATDPKVLILDEPTRGID-VGAK--AEIYRLIRElaAEGKAVIVISSELPELLGLSDRILVMREGRIVG 474
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-208 |
2.33e-19 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 84.77 E-value: 2.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 2 QSAVLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysqdddhlKAMSSVg 81
Cdd:PRK10247 4 NSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEG--------EDISTL- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 82 aiieNPEFY----SYL---------TGFENLEL-YASMHDGVSEERIFEVVKRVRL-EHAIHQKVKTYSLGMKQRLGIAQ 146
Cdd:PRK10247 75 ----KPEIYrqqvSYCaqtptlfgdTVYDNLIFpWQIRNQQPDPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515936072 147 AILHKPNLLILDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEElCDRMIIIQ 208
Cdd:PRK10247 151 NLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKVITLQ 211
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
21-212 |
2.50e-19 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 88.23 E-value: 2.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 21 LQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAMSSVGAIIENPEFYSYLTGFENLE 100
Cdd:TIGR02203 348 LDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIA 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 101 lYASMhDGVSEERIFEVVKRV-------RLEHAIHQKVKT----YSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPAGM 169
Cdd:TIGR02203 428 -YGRT-EQADRAEIERALAAAyaqdfvdKLPLGLDTPIGEngvlLSGGQRQRLAIARALLKDAPILILDEATSALDNESE 505
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 515936072 170 KEFREHLQMLVQeeGVSVLFATHLLHEVEElCDRMIIIQKGQI 212
Cdd:TIGR02203 506 RLVQAALERLMQ--GRTTLVIAHRLSTIEK-ADRIVVMDDGRI 545
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
18-212 |
3.92e-19 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 84.06 E-value: 3.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 18 HQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYS-QDDDHLKAMSSVGAIIENPEFYSYlTGF 96
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPiSQYEHKYLHSKVSLVGQEPVLFAR-SLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 97 ENLelyASMHDGVSEERIFEVVKRV-------RLEHAIH----QKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLD 165
Cdd:cd03248 106 DNI---AYGLQSCSFECVKEAAQKAhahsfisELASGYDtevgEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 515936072 166 pagmKEFREHLQMLVQE--EGVSVLFATHLLHEVEElCDRMIIIQKGQI 212
Cdd:cd03248 183 ----AESEQQVQQALYDwpERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
6-212 |
4.23e-19 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 84.29 E-value: 4.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 6 LHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYS---QDDDHLKAMSS--- 79
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdfSQKPSEKAIRLlrq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 80 -VGAIIENPEFYSYLTGFENLeLYA-----SMHDGVSEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPN 153
Cdd:COG4161 83 kVGMVFQQYNLWPHLTVMENL-IEApckvlGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515936072 154 LLILDEPTNGLDPAGMKEFREHLQMLvQEEGVSVLFAThllHEVE---ELCDRMIIIQKGQI 212
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVT---HEVEfarKVASQVVYMEKGRI 219
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
13-212 |
4.24e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 87.41 E-value: 4.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 13 KQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKN---NGRIIMNGYSQDDDHLKAMSsvGAIIENPEF 89
Cdd:TIGR00955 33 RERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRAIS--AYVQQDDLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 90 YSYLTGFENLELYA--SMHDGVSE----ERIFEVVKRVRLEHAIHQK------VKTYSLGMKQRLGIAQAILHKPNLLIL 157
Cdd:TIGR00955 111 IPTLTVREHLMFQAhlRMPRRVTKkekrERVDEVLQALGLRKCANTRigvpgrVKGLSGGERKRLAFASELLTDPPLLFC 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515936072 158 DEPTNGLDPAGMKEFREHLQMLVQeEGVSVLFATHL-LHEVEELCDRMIIIQKGQI 212
Cdd:TIGR00955 191 DEPTSGLDSFMAYSVVQVLKGLAQ-KGKTIICTIHQpSSELFELFDKIILMAEGRV 245
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
18-212 |
4.31e-19 |
|
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: 84.20 E-value: 4.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 18 HQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAM-SSVGAIIENPEFYSYlTGF 96
Cdd:cd03254 16 KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLrSMIGVVLQDTFLFSG-TIM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 97 ENLELYasmHDGVSEERIFEVVKRVRLEHAIHQKVKTY-----------SLGMKQRLGIAQAILHKPNLLILDEPTNGLD 165
Cdd:cd03254 95 ENIRLG---RPNATDEEVIEAAKEAGAHDFIMKLPNGYdtvlgenggnlSQGERQLLAIARAMLRDPKILILDEATSNID 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515936072 166 PAGMKEFREHLQMLVqeEGVSVLFATHLLHEVEElCDRMIIIQKGQI 212
Cdd:cd03254 172 TETEKLIQEALEKLM--KGRTSIIIAHRLSTIKN-ADKILVLDDGKI 215
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
30-212 |
4.48e-19 |
|
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: 87.76 E-value: 4.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 30 QGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAMSSVGAIIENPEFYSYLTGFENLELYASMHDGV 109
Cdd:TIGR01257 955 ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRS 1034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 110 SEERIFE---VVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPAGMKEFREHLqmLVQEEGVS 186
Cdd:TIGR01257 1035 WEEAQLEmeaMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRT 1112
|
170 180
....*....|....*....|....*.
gi 515936072 187 VLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:TIGR01257 1113 IIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
11-212 |
8.58e-19 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 85.86 E-value: 8.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 11 VDKQIGRHQILQHI---------SMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGY---SQDDDHLKAM- 77
Cdd:PRK10070 25 IEQGLSKEQILEKTglslgvkdaSLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVdiaKISDAELREVr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 78 -SSVGAIIENPEFYSYLTGFENLELYASMHDGVSEER---IFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPN 153
Cdd:PRK10070 105 rKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERrekALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPD 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515936072 154 LLILDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:PRK10070 185 ILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
21-237 |
9.60e-19 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 83.71 E-value: 9.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 21 LQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysqdddhlkamsSVGAIIENPEFYSYLTGFENLE 100
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG------------EVSVIAISAGLSGQLTGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 101 lYASMHDGVSEERIF----EVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPAGMKEFREHL 176
Cdd:PRK13546 108 -FKMLCMGFKRKEIKamtpKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKI 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515936072 177 QMLvQEEGVSVLFATHLLHEVEELCDRMIIIQKGQIKANTNLRD-MEGKEQVLMNIQPVEKA 237
Cdd:PRK13546 187 YEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDvLPKYEAFLNDFKKKSKA 247
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
8-212 |
1.32e-18 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 83.14 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 8 IENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYS-------QDDDHLKAMSSV 80
Cdd:PRK11124 5 LNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdfsktpSDKAIRELRRNV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 81 GAIIENPEFYSYLTGFENLeLYASMH-DGVSEE----RIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLL 155
Cdd:PRK11124 85 GMVFQQYNLWPHLTVQQNL-IEAPCRvLGLSKDqalaRAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 156 ILDEPTNGLDPAGMKEFREHLQMLvQEEGVSVLFAThllHEVE---ELCDRMIIIQKGQI 212
Cdd:PRK11124 164 LFDEPTAALDPEITAQIVSIIREL-AETGITQVIVT---HEVEvarKTASRVVYMENGHI 219
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
27-245 |
1.33e-18 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 84.39 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 27 DIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKN---------NGRIIMNGYSQDDDHLKAmSSVGAIIENP--EFYSYLTG 95
Cdd:PRK09473 38 SLRAGETLGIVGESGSGKSQTAFALMGLLAANgriggsatfNGREILNLPEKELNKLRA-EQISMIFQDPmtSLNPYMRV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 96 FENLELYASMHDGVSEERIFEvvKRVRLEHAI-----HQKVKTY----SLGMKQRLGIAQAILHKPNLLILDEPTNGLDP 166
Cdd:PRK09473 117 GEQLMEVLMLHKGMSKAEAFE--ESVRMLDAVkmpeaRKRMKMYphefSGGMRQRVMIAMALLCRPKLLIADEPTTALDV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 167 AGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGqikantnlRDME-GK-EQVLMniQPVE-------KA 237
Cdd:PRK09473 195 TVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAG--------RTMEyGNaRDVFY--QPSHpysigllNA 264
|
....*...
gi 515936072 238 VSWLDTQG 245
Cdd:PRK09473 265 VPRLDAEG 272
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-229 |
1.48e-18 |
|
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: 85.65 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 5 VLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKN--NGRIIMNGYSQDDDHLKAMSSVGA 82
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 83 IIENPE--FYSYLTGFENLEL-------YASMHDGVSEERIFEVVKRVRLEHA-IHQKVKTYSLGMKQRLGIAQAILHKP 152
Cdd:TIGR02633 81 VIIHQEltLVPELSVAENIFLgneitlpGGRMAYNAMYLRAKNLLRELQLDADnVTRPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515936072 153 NLLILDEPTNGLDPAGMKEFREHLQMLvQEEGVSVLFATHLLHEVEELCDRMIIIQKGQIKANTNLRDMEGKEQVLM 229
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDL-KAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITM 236
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
19-212 |
1.74e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 85.93 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 19 QILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDD-DHLKAMSSVGAIIENPEFYS------ 91
Cdd:TIGR00958 495 PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQyDHHYLHRQVALVGQEPVLFSgsvren 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 92 --Y-LTGFENLELYASMHDGVSEERIFEVVKRVRLEhaIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDpag 168
Cdd:TIGR00958 575 iaYgLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTE--VGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALD--- 649
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 515936072 169 mKEFREHLQMLVQEEGVSVLFATHLLHEVEElCDRMIIIQKGQI 212
Cdd:TIGR00958 650 -AECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSV 691
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-212 |
1.96e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 82.97 E-value: 1.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 8 IENVDKQI--GRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKN-----NGRIIMNG---YSQDDDHLKAM 77
Cdd:PRK14267 5 IETVNLRVyyGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGrniYSPDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 78 SSVGAIIENPEFYSYLTGFENLELYASMHDGV-SEERIFEVV----KRVRLEHAIHQKVKTY----SLGMKQRLGIAQAI 148
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVkSKKELDERVewalKKAALWDEVKDRLNDYpsnlSGGQRQRLVIARAL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515936072 149 LHKPNLLILDEPTNGLDPAGMKEFREHLQMLVQEegVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:PRK14267 165 AMKPKILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-182 |
2.04e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 85.24 E-value: 2.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 2 QSAVLHIENVDKQIGRHQ-ILQHISMDIRQGEivGLL--GPNGSGKTTLIRLIVGLMKKNNGRIIMNgysQDDDHLkams 78
Cdd:COG4178 359 EDGALALEDLTLRTPDGRpLLEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAGLWPYGSGRIARP---AGARVL---- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 79 svgaiienpeFYS---YL---TGFENLeLYASMHDGVSEERIFEVVKRVRLEHAIHQ--KV----KTYSLGMKQRLGIAQ 146
Cdd:COG4178 430 ----------FLPqrpYLplgTLREAL-LYPATAEAFSDAELREALEAVGLGHLAERldEEadwdQVLSLGEQQRLAFAR 498
|
170 180 190
....*....|....*....|....*....|....*.
gi 515936072 147 AILHKPNLLILDEPTNGLDPAGMKEFrehLQMLVQE 182
Cdd:COG4178 499 LLLHKPDWLFLDEATSALDEENEAAL---YQLLREE 531
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-203 |
2.52e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 82.52 E-value: 2.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 1 MQSAVLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKN-----NGRIIMNG---YSQDDD 72
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGhniYSPRTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 73 HLKAMSSVGAIIENPEFYSyLTGFENLeLYASMHDGVSEERIF-EVVKRVRLEHAIHQKVK--------TYSLGMKQRLG 143
Cdd:PRK14239 81 TVDLRKEIGMVFQQPNPFP-MSIYENV-VYGLRLKGIKDKQVLdEAVEKSLKGASIWDEVKdrlhdsalGLSGGQQQRVC 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 144 IAQAILHKPNLLILDEPTNGLDPAGMKEFREHLQMLVQEegVSVLFATHLLHEVEELCDR 203
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD--YTMLLVTRSMQQASRISDR 216
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-202 |
3.09e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 82.39 E-value: 3.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 6 LHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIvGLMKKNNGRIIMNG---------YSQDDDHLKA 76
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGrveffnqniYERRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 77 MSSVGAIIENPEFYSyLTGFENLELYASM--------HDGVSEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAI 148
Cdd:PRK14258 87 RRQVSMVHPKPNLFP-MSVYDNVAYGVKIvgwrpkleIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARAL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515936072 149 LHKPNLLILDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCD 202
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-191 |
3.33e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 85.18 E-value: 3.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 5 VLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRI-IMNGYSQDDDHLKAmssVGAI 83
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVeVLGGDMADARHRRA---VCPR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 84 I--------ENpeFYSYLTGFENLELYASM--HDGVS-EERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKP 152
Cdd:NF033858 78 IaympqglgKN--LYPTLSVFENLDFFGRLfgQDAAErRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 515936072 153 NLLILDEPTNGLDPAGMKEFREhlqmLV-----QEEGVSVLFAT 191
Cdd:NF033858 156 DLLILDEPTTGVDPLSRRQFWE----LIdriraERPGMSVLVAT 195
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
20-212 |
3.41e-18 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 84.79 E-value: 3.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 20 ILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDD-DHLKAMSSVGAIIENPEFYSYlTGFEN 98
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDiDRHTLRQFINYLPQEPYIFSG-SILEN 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 99 LELYASmhDGVSEERIFEVVKRVRLEHAIHQKVKTY-----------SLGMKQRLGIAQAILHKPNLLILDEPTNGLDPA 167
Cdd:TIGR01193 568 LLLGAK--ENVSQDEIWAACEIAEIKDDIENMPLGYqtelseegssiSGGQKQRIALARALLTDSKVLILDESTSNLDTI 645
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 515936072 168 GMKEFREHLQMLVQEegvSVLFATHLLhEVEELCDRMIIIQKGQI 212
Cdd:TIGR01193 646 TEKKIVNNLLNLQDK---TIIFVAHRL-SVAKQSDKIIVLDHGKI 686
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
19-212 |
3.45e-18 |
|
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: 81.89 E-value: 3.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 19 QILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysQDDDHLKAMS---SVGAIIEN-PEFYSylT 94
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDG--QDIREVTLDSlrrAIGVVPQDtVLFND--T 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 95 GFENLElYASmhDGVSEERIFEVVKRVRlehaIHQKVKTY---------------SLGMKQRLGIAQAILHKPNLLILDE 159
Cdd:cd03253 91 IGYNIR-YGR--PDATDEEVIEAAKAAQ----IHDKIMRFpdgydtivgerglklSGGEKQRVAIARAILKNPPILLLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515936072 160 PTNGLDpagmkefrEHLQMLVQE------EGVSVLFATHLLHEVEElCDRMIIIQKGQI 212
Cdd:cd03253 164 ATSALD--------THTEREIQAalrdvsKGRTTIVIAHRLSTIVN-ADKIIVLKDGRI 213
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
21-212 |
3.53e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 82.57 E-value: 3.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 21 LQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYS----QDDDHLKAM-SSVGAIIENPEfySYLtg 95
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHitpeTGNKNLKKLrKKVSLVFQFPE--AQL-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 96 FENLEL----YASMHDGVSE----ERIFEVVKRVRL-EHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDP 166
Cdd:PRK13641 99 FENTVLkdveFGPKNFGFSEdeakEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 515936072 167 AGMKEFrehLQMLV--QEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:PRK13641 179 EGRKEM---MQLFKdyQKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-212 |
3.80e-18 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 81.90 E-value: 3.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 1 MQSAVLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAMSSV 80
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 81 ----------GAIIENPEfysyltgfENLELYASMHDGVSEeRIFEVVKR----VRlEHAIH--QKV-----------KT 133
Cdd:PRK11701 82 errrllrtewGFVHQHPR--------DGLRMQVSAGGNIGE-RLMAVGARhygdIR-ATAGDwlERVeidaariddlpTT 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515936072 134 YSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:PRK11701 152 FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-211 |
3.92e-18 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 83.73 E-value: 3.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 5 VLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysQDDDHLKA-MSSVGAI 83
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDG--VDLSHVPPyQRPINMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 84 IENPEFYSYLTGFENLElYASMHDGVSE----ERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDE 159
Cdd:PRK11607 97 FQSYALFPHMTVEQNIA-FGLKQDKLPKaeiaSRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515936072 160 PTNGLDpagmKEFREHLQM----LVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQ 211
Cdd:PRK11607 176 PMGALD----KKLRDRMQLevvdILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
23-210 |
4.00e-18 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 83.22 E-value: 4.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 23 HISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYS---QDDDHLKAMSS------------------VG 81
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDllgMKDDEWRAVRSdiqmifqdplaslnprmtIG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 82 AIIENPefysyLTGFenlelYASMHDGVSEERIFEVVKRVRL-EHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEP 160
Cdd:PRK15079 119 EIIAEP-----LRTY-----HPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEP 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 515936072 161 TNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKG 210
Cdd:PRK15079 189 VSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLG 238
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
5-212 |
4.69e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 81.07 E-value: 4.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 5 VLHIENVDKQ-IGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYsqDDDHLKAMS----- 78
Cdd:PRK10908 1 MIRFEHVSKAyLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGH--DITRLKNREvpflr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 79 -SVGAIIENPEFYSYLTGFENLELyASMHDGVSEERIFEVVKRVRLEHAIHQKVKTY----SLGMKQRLGIAQAILHKPN 153
Cdd:PRK10908 79 rQIGMIFQDHHLLMDRTVYDNVAI-PLIIAGASGDDIRRRVSAALDKVGLLDKAKNFpiqlSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515936072 154 LLILDEPTNGLDPAgmkeFREHLQMLVQE---EGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:PRK10908 158 VLLADEPTGNLDDA----LSEGILRLFEEfnrVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-225 |
5.22e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 81.67 E-value: 5.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 6 LHIENVDKQIGR-----HQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysQDDDHLKA---M 77
Cdd:COG1101 2 LELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDG--KDVTKLPEykrA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 78 SSVGAIIENPefysyLTG-------FENLELyASMHD-------GVSEERIFEVVKRVR-----LEHAIHQKVKTYSLGM 138
Cdd:COG1101 80 KYIGRVFQDP-----MMGtapsmtiEENLAL-AYRRGkrrglrrGLTKKRRELFRELLAtlglgLENRLDTKVGLLSGGQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 139 KQRLGIAQAILHKPNLLILDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQIkantnL 218
Cdd:COG1101 154 RQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI-----I 228
|
....*..
gi 515936072 219 RDMEGKE 225
Cdd:COG1101 229 LDVSGEE 235
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
13-212 |
6.91e-18 |
|
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: 80.00 E-value: 6.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 13 KQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKN---NGRIIMNGYSQDDDHLKAMSSVGAIIENPEF 89
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 90 YSYLTGFENLELYASMHDgvseerifevvkrvrlehaiHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPAGM 169
Cdd:cd03233 95 FPTLTVRETLDFALRCKG--------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 515936072 170 KEFREHLQMLVQEEGVSVLFAthLLH---EVEELCDRMIIIQKGQI 212
Cdd:cd03233 155 LEILKCIRTMADVLKTTTFVS--LYQasdEIYDLFDKVLVLYEGRQ 198
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
24-212 |
7.13e-18 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 82.48 E-value: 7.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 24 ISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKkNNGRIIMNGYSQDDDHLKAMSS------VGAIIE----------NP 87
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLID-YPGRVMAEKLEFNGQDLQRISEkerrnlVGAEVAmifqdpmtslNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 88 efySYLTGFENLELYaSMHDGVSE----ERIFEVVKRV-------RLEHAIHQkvktYSLGMKQRLGIAQAILHKPNLLI 156
Cdd:PRK11022 105 ---CYTVGFQIMEAI-KVHQGGNKktrrQRAIDLLNQVgipdpasRLDVYPHQ----LSGGMSQRVMIAMAIACRPKLLI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515936072 157 LDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:PRK11022 177 ADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQV 232
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-212 |
7.74e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 81.11 E-value: 7.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 4 AVLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMK-----KNNGRIIMNGysQD---DDHLK 75
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDG--QDifkMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 76 AMSSVGAIIENPEFYSYLTGFENLELYASMHDGVSEERifEVVKRVR--LEHA-IHQKVK--------TYSLGMKQRLGI 144
Cdd:PRK14247 80 LRRRVQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKK--ELQERVRwaLEKAqLWDEVKdrldapagKLSGGQQQRLCI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515936072 145 AQAILHKPNLLILDEPTNGLDPAGMKEFREHLQMLVQEegVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:PRK14247 158 ARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
20-213 |
7.74e-18 |
|
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: 80.62 E-value: 7.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 20 ILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAM-SSVGAIIENPEFYSYlTGFEN 98
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLrSRISIIPQDPVLFSG-TIRSN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 99 LELYasmhDGVSEERIFEVVKRVRLEHAIHQKVKT-----------YSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPA 167
Cdd:cd03244 98 LDPF----GEYSDEELWQALERVGLKEFVESLPGGldtvveeggenLSVGQRQLLCLARALLRKSKILVLDEATASVDPE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 515936072 168 GMkefrEHLQMLVQEE--GVSVLFATHLLHEVEElCDRMIIIQKGQIK 213
Cdd:cd03244 174 TD----ALIQKTIREAfkDCTVLTIAHRLDTIID-SDRILVLDKGRVV 216
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
4-211 |
9.45e-18 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 82.26 E-value: 9.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 4 AVLHIEN----VDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNnGRIIMNGYSQDDDHLKAMSS 79
Cdd:COG4170 2 PLLDIRNltieIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDN-WHVTADRFRWNGIDLLKLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 80 ----------VGAIIENPEfySYLTGFENL--ELYASMHDGVSEERIFEVvKRVRLEHAI----------HQKV-KTY-- 134
Cdd:COG4170 81 rerrkiigreIAMIFQEPS--SCLDPSAKIgdQLIEAIPSWTFKGKWWQR-FKWRKKRAIellhrvgikdHKDImNSYph 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515936072 135 --SLGMKQRLGIAQAILHKPNLLILDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQ 211
Cdd:COG4170 158 elTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQ 236
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-212 |
1.27e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 80.86 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 5 VLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNG---YSQDD----DHLKAM 77
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGkvlYFGKDifqiDAIKLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 78 SSVGAIIENPEFYSYLTGFENLELYASMHdGVSEER-----IFEVVKRVRLEHAIHQKVKT----YSLGMKQRLGIAQAI 148
Cdd:PRK14246 90 KEVGMVFQQPNPFPHLSIYDNIAYPLKSH-GIKEKReikkiVEECLRKVGLWKEVYDRLNSpasqLSGGQQQRLTIARAL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515936072 149 LHKPNLLILDEPTNGLDPAGMKEFREHLQMLVQEegVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:PRK14246 169 ALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
6-214 |
1.30e-17 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 81.84 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 6 LHIeNVDKQIGRHQiLQhISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKA-----MSSV 80
Cdd:PRK11144 2 LEL-NFKQQLGDLC-LT-VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIclppeKRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 81 GAIIENPEFYSYLTGFENLeLYasmhdGVSEERIFEVVKRVRL---EHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLIL 157
Cdd:PRK11144 79 GYVFQDARLFPHYKVRGNL-RY-----GMAKSMVAQFDKIVALlgiEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLM 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515936072 158 DEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQIKA 214
Cdd:PRK11144 153 DEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKA 209
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
4-212 |
2.25e-17 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 81.43 E-value: 2.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 4 AVLHIENVDKQ-IGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysQDDDHLK------A 76
Cdd:PRK11650 2 AGLKLQAVRKSyDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGG--RVVNELEpadrdiA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 77 MssvgaIIENPEFYSYLTGFENLElYASMHDGVS----EERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKP 152
Cdd:PRK11650 80 M-----VFQNYALYPHMSVRENMA-YGLKIRGMPkaeiEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 153 NLLILDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:PRK11650 154 AVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVA 213
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
18-230 |
2.50e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 80.21 E-value: 2.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 18 HQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNG----YSQDDDHLKAM-SSVGAIIENPEFYSY 92
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDititHKTKDKYIRPVrKRIGMVFQFPESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 93 LTGFENLELYASMHDGVSEERIFEVVKRVRLEHAIHQKVKTYSL-----GMKQRLGIAQAILHKPNLLILDEPTNGLDPA 167
Cdd:PRK13646 100 EDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPfqmsgGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQ 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515936072 168 GMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQIKANTNLRDMEGKEQVLMN 230
Cdd:PRK13646 180 SKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKKLAD 242
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
16-214 |
2.59e-17 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 79.81 E-value: 2.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 16 GRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysqddDHLKAMS---------SVGAIIEN 86
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDG-----ENIPAMSrsrlytvrkRMSMLFQS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 87 PEFYSYLTGFENLELYASMHDGVSEERIFEVV----KRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTN 162
Cdd:PRK11831 93 GALFTDMNVFDNVAYPLREHTQLPAPLLHSTVmmklEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515936072 163 GLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQIKA 214
Cdd:PRK11831 173 GQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVA 224
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
6-224 |
3.66e-17 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 80.55 E-value: 3.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 6 LHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSG--KTTLIRLIVGlmkKNNGR--IIMNGYSQDDDHLKAMSSVG 81
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRrpWRF*TWCANRRALRRTIG*H 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 82 AIIENPEFYSYlTGFENLELYASMHDGVSEE---RIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILD 158
Cdd:NF000106 91 RPVR*GRRESF-SGRENLYMIGR*LDLSRKDaraRADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515936072 159 EPTNGLDPAGMKEFREHLQMLVQeEGVSVLFATHLLHEVEELCDRMIIIQKGQIKANTNLRDMEGK 224
Cdd:NF000106 170 EPTTGLDPRTRNEVWDEVRSMVR-DGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTK 234
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-211 |
3.91e-17 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 78.63 E-value: 3.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 1 MQsAVLHIENVDK-----QIGRHQI--LQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMN-------- 65
Cdd:COG4778 1 MT-TLLEVENLSKtftlhLQGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggwvdl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 66 ----------------GY-SQdddHLKAMSSVGAiienpefysyltgfenLELYAS--MHDGVSEERIFEVVKRV--RLE 124
Cdd:COG4778 80 aqaspreilalrrrtiGYvSQ---FLRVIPRVSA----------------LDVVAEplLERGVDREEARARARELlaRLN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 125 haIHQKV-----KTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPAGmkefREHLQMLVQE---EGVSVLFATHLLHE 196
Cdd:COG4778 141 --LPERLwdlppATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAAN----RAVVVELIEEakaRGTAIIGIFHDEEV 214
|
250
....*....|....*
gi 515936072 197 VEELCDRMIIIQKGQ 211
Cdd:COG4778 215 REAVADRVVDVTPFS 229
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
6-214 |
4.56e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 80.66 E-value: 4.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 6 LHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAMS------- 78
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASrrvasvp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 79 ---------SVGAIIE---NPefysYLTGFenlelyaSMHDGVSEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQ 146
Cdd:PRK09536 84 qdtslsfefDVRQVVEmgrTP----HRSRF-------DTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515936072 147 AILHKPNLLILDEPTNGLDPAGMKEFREHLQMLVqEEGVSVLFATHLLHEVEELCDRMIIIQKGQIKA 214
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLDINHQVRTLELVRRLV-DDGKTAVAAIHDLDLAARYCDELVLLADGRVRA 219
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
3-217 |
5.28e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 81.31 E-value: 5.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 3 SAVLHIENVDK--QIGRHQI--LQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNG--RIIMNGYSQ-DDDHLK 75
Cdd:PRK10535 2 TALLELKDIRRsyPSGEEQVevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGtyRVAGQDVATlDADALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 76 AM--SSVGAIIENPEFYSYLTGFENLEL---YASMHDGVSEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILH 150
Cdd:PRK10535 82 QLrrEHFGFIFQRYHLLSHLTAAQNVEVpavYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515936072 151 KPNLLILDEPTNGLDPAGMKEFREHLQMLvQEEGVSVLFATHlLHEVEELCDRMIIIQKGQIKANTN 217
Cdd:PRK10535 162 GGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTH-DPQVAAQAERVIEIRDGEIVRNPP 226
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
6-214 |
5.42e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 78.90 E-value: 5.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 6 LHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNG--YSQ--DDDHLKAMSSVG 81
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpISMlsSRQLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 82 AIIENPEFYS-----------YLTGFENLelyaSMHDgvsEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILH 150
Cdd:PRK11231 83 QHHLTPEGITvrelvaygrspWLSLWGRL----SAED---NARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515936072 151 KPNLLILDEPTNGLDPAGMKEFREHLQMLvQEEGVSVLFATHLLHEVEELCDRMIIIQKGQIKA 214
Cdd:PRK11231 156 DTPVVLLDEPTTYLDINHQVELMRLMREL-NTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMA 218
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
19-212 |
5.57e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 79.74 E-value: 5.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 19 QILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDH---LKAMSSVGAIIENP-------- 87
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKktkEKEKVLEKLVIQKTrfkkikki 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 88 -----------EFYSYLTGFENLE---LYASMHDGVS----EERIFEVVKRVRLEHAIHQKVK-TYSLGMKQRLGIAQAI 148
Cdd:PRK13651 101 keirrrvgvvfQFAEYQLFEQTIEkdiIFGPVSMGVSkeeaKKRAAKYIELVGLDESYLQRSPfELSGGQKRRVALAGIL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515936072 149 LHKPNLLILDEPTNGLDPAGMKEFREHLQMLvQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:PRK13651 181 AMEPDFLVFDEPTAGLDPQGVKEILEIFDNL-NKQGKTIILVTHDLDNVLEWTKRTIFFKDGKI 243
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
5-212 |
6.23e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 78.98 E-value: 6.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 5 VLHIENV----DKQIGRHQiLQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAMS-S 79
Cdd:PRK13642 4 ILEVENLvfkyEKESDVNQ-LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRrK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 80 VGAIIENPEFYSYLTGFENLELYASMHDGVSEE----RIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLL 155
Cdd:PRK13642 83 IGMVFQNPDNQFVGATVEDDVAFGMENQGIPREemikRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEII 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515936072 156 ILDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEElCDRMIIIQKGQI 212
Cdd:PRK13642 163 ILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEI 218
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
22-212 |
1.06e-16 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 77.70 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 22 QHISM----DIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysqdDDHLKAMSS---VGAIIENPEFYSYLT 94
Cdd:PRK10771 12 HHLPMrfdlTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG----QDHTTTPPSrrpVSMLFQENNLFSHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 95 GFENLELyaSMHDGV-----SEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPAGM 169
Cdd:PRK10771 88 VAQNIGL--GLNPGLklnaaQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALR 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 515936072 170 KEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:PRK10771 166 QEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-211 |
1.12e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 79.96 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 2 QSAVLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAMSSVG 81
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 82 -AIIEN-----PEfysyLTGFENLELYASMHD-GVSEERIFEVVKRVRLEH---AI--HQKVKTYSLGMKQRLGIAQAIL 149
Cdd:PRK11288 81 vAIIYQelhlvPE----MTVAENLYLGQLPHKgGIVNRRLLNYEAREQLEHlgvDIdpDTPLKYLSIGQRQMVEIAKALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515936072 150 HKPNLLILDEPTNGLDPagmkefRE--HLQMLVQE---EGVSVLFATHLLHEVEELCDRMIIIQKGQ 211
Cdd:PRK11288 157 RNARVIAFDEPTSSLSA------REieQLFRVIRElraEGRVILYVSHRMEEIFALCDAITVFKDGR 217
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
5-212 |
2.47e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.92 E-value: 2.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 5 VLHIENVD-KQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysQDDDHLkamsSVGAI 83
Cdd:COG3845 257 VLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDG--EDITGL----SPRER 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 84 IEN---------------PEFysylTGFENLELYASMHDGVSEeRIFEVVKRVRlEHA-------------IHQKVKTYS 135
Cdd:COG3845 331 RRLgvayipedrlgrglvPDM----SVAENLILGRYRRPPFSR-GGFLDRKAIR-AFAeelieefdvrtpgPDTPARSLS 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515936072 136 LGMKQRLGIAQAILHKPNLLILDEPTNGLDPAGMKEFREHLQMLvQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:COG3845 405 GGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-212 |
4.17e-16 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 79.00 E-value: 4.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 19 QILQHISMDIRQGEIVGLLGPNGSGKTTLIRLI----VGLMKKNNGRIIMNGYSQDD--DHLKAmsSVGAIIENPEFYSY 92
Cdd:TIGR00956 75 DILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITPEEikKHYRG--DVVYNAETDVHFPH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 93 LTGFENLELYASMH------DGVSEE----RIFEVVKRVR-LEHAIHQKV-----KTYSLGMKQRLGIAQAILHKPNLLI 156
Cdd:TIGR00956 153 LTVGETLDFAARCKtpqnrpDGVSREeyakHIADVYMATYgLSHTRNTKVgndfvRGVSGGERKRVSIAEASLGGAKIQC 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515936072 157 LDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLL-HEVEELCDRMIIIQKGQI 212
Cdd:TIGR00956 233 WDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCsQDAYELFDKVIVLYEGYQ 289
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
19-213 |
4.41e-16 |
|
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: 75.14 E-value: 4.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 19 QILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysQDDDHL---KAMSSVGAIIENPEFYSYlTG 95
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDG--IDISTIpleDLRSSLTIIPQDPTLFSG-TI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 96 FENLELYasmhDGVSEERIFEVVKrvrlehaIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPAGMKEfreh 175
Cdd:cd03369 99 RSNLDPF----DEYSDEEIYGALR-------VSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDAL---- 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 515936072 176 LQMLVQEE--GVSVLFATHLLHEVEElCDRMIIIQKGQIK 213
Cdd:cd03369 164 IQKTIREEftNSTILTIAHRLRTIID-YDKILVMDAGEVK 202
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
24-212 |
6.22e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 76.32 E-value: 6.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 24 ISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGY-----SQDDDHLKAMSSVGAIIENPEfySYLtgFEN 98
Cdd:PRK13649 26 VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTlitstSKNKDIKQIRKKVGLVFQFPE--SQL--FEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 99 LEL----YASMHDGVSEERIfEVVKRVRL------EHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPAG 168
Cdd:PRK13649 102 TVLkdvaFGPQNFGVSQEEA-EALAREKLalvgisESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 515936072 169 MKEFREHLQMLvQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:PRK13649 181 RKELMTLFKKL-HQSGMTIVLVTHLMDDVANYADFVYVLEKGKL 223
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
24-212 |
6.73e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 76.31 E-value: 6.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 24 ISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGR-----IIMNGYSQDDDHLKAMSSVGAIIENPEFYSYLTGFEN 98
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKvtvgdIVVSSTSKQKEIKPVRKKVGVVFQFPESQLFEETVLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 99 LELYASMHDGVSEERI----FEVVKRVRLEHAIHQKVK-TYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPAGMKEFR 173
Cdd:PRK13643 105 DVAFGPQNFGIPKEKAekiaAEKLEMVGLADEFWEKSPfELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMM 184
|
170 180 190
....*....|....*....|....*....|....*....
gi 515936072 174 EHLQMlVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:PRK13643 185 QLFES-IHQSGQTVVLVTHLMDDVADYADYVYLLEKGHI 222
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-212 |
7.81e-16 |
|
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: 75.27 E-value: 7.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 18 HQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAM-SSVGAIIENPEFYSyLTGF 96
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLrSQIGLVSQEPVLFD-GTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 97 ENLELyaSMHDGVSEErifevVKRVRLEHAIH---------------QKVKTYSLGMKQRLGIAQAILHKPNLLILDEPT 161
Cdd:cd03249 95 ENIRY--GKPDATDEE-----VEEAAKKANIHdfimslpdgydtlvgERGSQLSGGQKQRIAIARALLRNPKILLLDEAT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515936072 162 NGLDPAGMKEFREHLQMLVqeEGVSVLFATHLLHEVEElCDRMIIIQKGQI 212
Cdd:cd03249 168 SALDAESEKLVQEALDRAM--KGRTTIVIAHRLSTIRN-ADLIAVLQNGQV 215
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-212 |
1.31e-15 |
|
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: 73.72 E-value: 1.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 6 LHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKN--NGRIIMNGysQDDDHL----KAMSS 79
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKG--EDITDLppeeRARLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 80 VGAIIENPEFYSyltGFENLELYASMHDGvseerifevvkrvrlehaihqkvktYSLGMKQRLGIAQAILHKPNLLILDE 159
Cdd:cd03217 79 IFLAFQYPPEIP---GVKNADFLRYVNEG-------------------------FSGGEKKRNEILQLLLLEPDLAILDE 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515936072 160 PTNGLDPAGMKEFREHLQMLVqEEGVSVLFATH---LLHEVEElcDRMIIIQKGQI 212
Cdd:cd03217 131 PDSGLDIDALRLVAEVINKLR-EEGKSVLIITHyqrLLDYIKP--DRVHVLYDGRI 183
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-166 |
1.68e-15 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 74.69 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 4 AVLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIR-------LIVGLmkKNNGRIIMNG---YSQDDDH 73
Cdd:COG1117 10 PKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGA--RVEGEILLDGediYDPDVDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 74 LKAMSSVGAIIENPefysylTGF-----ENLELYASMHDGVSEERIFEVVKRVrLEHA---------IHQKVKTYSLGMK 139
Cdd:COG1117 88 VELRRRVGMVFQKP------NPFpksiyDNVAYGLRLHGIKSKSELDEIVEES-LRKAalwdevkdrLKKSALGLSGGQQ 160
|
170 180
....*....|....*....|....*..
gi 515936072 140 QRLGIAQAILHKPNLLILDEPTNGLDP 166
Cdd:COG1117 161 QRLCIARALAVEPEVLLMDEPTSALDP 187
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-211 |
2.58e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 75.90 E-value: 2.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 1 MQSAVLHIENVD----KQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKN-----NGRIIMNGYS--- 68
Cdd:PRK15134 1 MTQPLLAIENLSvafrQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESllh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 69 QDDDHLKAM--SSVGAIIENPefYSYLTGFENLE--LYA--SMHDGVSEE----RIFEVVKRV-------RLEHAIHQkv 131
Cdd:PRK15134 81 ASEQTLRGVrgNKIAMIFQEP--MVSLNPLHTLEkqLYEvlSLHRGMRREaargEILNCLDRVgirqaakRLTDYPHQ-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 132 ktYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQ 211
Cdd:PRK15134 157 --LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
2-214 |
2.63e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 74.44 E-value: 2.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 2 QSAVLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAMSSVG 81
Cdd:PRK10575 8 SDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 82 AIIenPEFYSYLTGFENLELYA----SMHDGVSEeriFEVVKRVRLEHAI---------HQKVKTYSLGMKQRLGIAQAI 148
Cdd:PRK10575 88 AYL--PQQLPAAEGMTVRELVAigryPWHGALGR---FGAADREKVEEAIslvglkplaHRLVDSLSGGERQRAWIAMLV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515936072 149 LHKPNLLILDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQIKA 214
Cdd:PRK10575 163 AQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIA 228
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
5-192 |
2.94e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 73.06 E-value: 2.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 5 VLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAMSSVGAII 84
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 85 ENPEFYSYLTGFENleLYASMHDGVSEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGL 164
Cdd:PRK13540 81 HRSGINPYLTLREN--CLYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVAL 158
|
170 180 190
....*....|....*....|....*....|..
gi 515936072 165 DPAG----MKEFREHlqmlvQEEGVSVLFATH 192
Cdd:PRK13540 159 DELSlltiITKIQEH-----RAKGGAVLLTSH 185
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
21-215 |
4.02e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 73.43 E-value: 4.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 21 LQHISMD---------IRQGEIVGLLGPNGSGKTTLIRLIVGLMkKNNGRIIMNGYSQDDDHLKAMSSVGAII---ENPE 88
Cdd:PRK03695 3 LNDVAVStrlgplsaeVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLsqqQTPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 89 F----YSYLTgfenLELYASMHDGVSEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILH-----KPN--LLIL 157
Cdd:PRK03695 82 FampvFQYLT----LHQPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdiNPAgqLLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515936072 158 DEPTNGLDPAGMKEfrehLQMLVQE---EGVSVLFATHLLHEVEELCDRMIIIQKGQIKAN 215
Cdd:PRK03695 158 DEPMNSLDVAQQAA----LDRLLSElcqQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLAS 214
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
24-217 |
4.85e-15 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 75.22 E-value: 4.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 24 ISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKA----MSSVgaiienpefYS--YLtgFE 97
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAyrqlFSAV---------FSdfHL--FD 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 98 nlELYAsMHDGVSEERIFEVVKRVRLEHaihqKVK-------T--YSLGMKQRLGIAQAIL-HKPnLLILDEPTNGLDPa 167
Cdd:COG4615 420 --RLLG-LDGEADPARARELLERLELDH----KVSvedgrfsTtdLSQGQRKRLALLVALLeDRP-ILVFDEWAADQDP- 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515936072 168 gmkEFREH-----LQMLvQEEGVSVLFATH---LLHeveeLCDRMIIIQKGQIKANTN 217
Cdd:COG4615 491 ---EFRRVfytelLPEL-KARGKTVIAISHddrYFD----LADRVLKMDYGKLVELTG 540
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-213 |
5.43e-15 |
|
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: 75.72 E-value: 5.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 20 ILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKkNNGRIIMNGYSQDDDHLKAMSSVGAIIENPEFYSYLTGFENL 99
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNL 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 100 ELYASMhdgvSEERIFEVVKRVRLEHAIHQ---KVK--------TYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPAG 168
Cdd:TIGR01271 1313 DPYEQW----SDEEIWKVAEEVGLKSVIEQfpdKLDfvlvdggyVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVT 1388
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 515936072 169 MKEFREHLQMLVQEegVSVLFATHLLHEVEElCDRMIIIQKGQIK 213
Cdd:TIGR01271 1389 LQIIRKTLKQSFSN--CTVILSEHRVEALLE-CQQFLVIEGSSVK 1430
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
18-192 |
7.69e-15 |
|
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: 71.03 E-value: 7.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 18 HQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysqdDDHLkamssvgaiienpeFY----SYL 93
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE----GEDL--------------LFlpqrPYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 94 TgfenlelyasmhDGVSEERIfevvkrvrlehaIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPAGMKEFR 173
Cdd:cd03223 76 P------------LGTLREQL------------IYPWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLY 131
|
170
....*....|....*....
gi 515936072 174 EHLqmlvQEEGVSVLFATH 192
Cdd:cd03223 132 QLL----KELGITVISVGH 146
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
12-212 |
9.84e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 73.35 E-value: 9.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 12 DKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRI-IMNGYSQDDDHLKAMSS----------- 79
Cdd:PRK13631 33 EKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqVGDIYIGDKKNNHELITnpyskkiknfk 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 80 -----VGAIIENPEFYSYLTGFENLELYASMHDGVSEERifevvkrvrlehaIHQKVKTY------------------SL 136
Cdd:PRK13631 113 elrrrVSMVFQFPEYQLFKDTIEKDIMFGPVALGVKKSE-------------AKKLAKFYlnkmglddsylerspfglSG 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515936072 137 GMKQRLGIAQAILHKPNLLILDEPTNGLDPAGMKEFREhLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:PRK13631 180 GQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQ-LILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKI 254
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-165 |
1.33e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 74.22 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 5 VLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIimngysqdddhlkamsSVGAII 84
Cdd:PRK11147 319 VFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI----------------HCGTKL 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 85 ENPEFYSYLtgfENLELYASMHDGVSEERIfEVVKRVRLEHAI--------HQK-----VKTYSLGMKQRLGIAQAILHK 151
Cdd:PRK11147 383 EVAYFDQHR---AELDPEKTVMDNLAEGKQ-EVMVNGRPRHVLgylqdflfHPKramtpVKALSGGERNRLLLARLFLKP 458
|
170
....*....|....
gi 515936072 152 PNLLILDEPTNGLD 165
Cdd:PRK11147 459 SNLLILDEPTNDLD 472
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
22-235 |
1.35e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 74.05 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 22 QHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGY----SQDDDHLKamSSVGAIIENPE---FYSYLT 94
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdispRSPLDAVK--KGMAYITESRRdngFFPNFS 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 95 GFENLELYASMHDG----------VSEERIFEVVKRVRLE---HAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPT 161
Cdd:PRK09700 358 IAQNMAISRSLKDGgykgamglfhEVDEQRTAENQRELLAlkcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPT 437
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515936072 162 NGLDPAGMKEFREHLQMLVqEEGVSVLFATHLLHEVEELCDRMIIIQKGQIKANTNLRDMEGKEQVLMNIQPVE 235
Cdd:PRK09700 438 RGIDVGAKAEIYKVMRQLA-DDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMSEEEIMAWALPQE 510
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-202 |
1.52e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 72.12 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 3 SAVLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIR-------LIVGLmkKNNGRIIMNG---YSQDDD 72
Cdd:PRK14243 8 ETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGF--RVEGKVTFHGknlYAPDVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 73 HLKAMSSVGAIIENPEFYSYlTGFENLELYASM--HDGVSEERIFEVVKRVRLEHAIHQKVKTYSL----GMKQRLGIAQ 146
Cdd:PRK14243 86 PVEVRRRIGMVFQKPNPFPK-SIYDNIAYGARIngYKGDMDELVERSLRQAALWDEVKDKLKQSGLslsgGQQQRLCIAR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515936072 147 AILHKPNLLILDEPTNGLDPAGMKEFREHLQMLVQEegVSVLFATHLLHEVEELCD 202
Cdd:PRK14243 165 AIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSD 218
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
5-213 |
1.60e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 71.35 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 5 VLHIENVDKQIGR--HQ--ILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGY--SQDDDHLKAM- 77
Cdd:PRK10584 6 IVEVHHLKKSVGQgeHElsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQplHQMDEEARAKl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 78 --SSVGAIIENPEFYSYLTGFENLELYA---SMHDGVSEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKP 152
Cdd:PRK10584 86 raKHVGFVFQSFMLIPTLNALENVELPAllrGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515936072 153 NLLILDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLhEVEELCDRMIIIQKGQIK 213
Cdd:PRK10584 166 DVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDL-QLAARCDRRLRLVNGQLQ 225
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
16-214 |
2.40e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 71.56 E-value: 2.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 16 GRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysqddDHLKAMSS------VGAIIENPEF 89
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDG-----EHIQHYASkevarrIGLLAQNATT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 90 YSYLTGFENLELYASMHDGV-------SEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTN 162
Cdd:PRK10253 93 PGDITVQELVARGRYPHQPLftrwrkeDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515936072 163 GLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQIKA 214
Cdd:PRK10253 173 WLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVA 224
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-206 |
3.15e-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: 72.89 E-value: 3.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 27 DIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMN---GY-----SQD-----DDHLkaMSSVGAIIENPEFYSyl 93
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDlkiSYkpqyiSPDydgtvEEFL--RSANTDDFGSSYYKT-- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 94 tgfenlelyasmhdgvseerifEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDpagmKEFR 173
Cdd:COG1245 438 ----------------------EIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD----VEQR 491
|
170 180 190
....*....|....*....|....*....|....*..
gi 515936072 174 EH----LQMLVQEEGVSVLFATHLLHEVEELCDRMII 206
Cdd:COG1245 492 LAvakaIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
16-213 |
3.51e-14 |
|
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: 71.04 E-value: 3.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 16 GRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMkKNNGRIIMNGYSQDDDHLKAMSSVGAIIENPEFYSYLTG 95
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 96 FENLELYASMHDgvseERIFEVVKRVRLEHAIHQ---KVK--------TYSLGMKQRLGIAQAILHKPNLLILDEPTNGL 164
Cdd:cd03289 94 RKNLDPYGKWSD----EEIWKVAEEVGLKSVIEQfpgQLDfvlvdggcVLSHGHKQLMCLARSVLSKAKILLLDEPSAHL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 515936072 165 DPAGMKEFREHLQMLVQeeGVSVLFATHLLHEVEElCDRMIIIQKGQIK 213
Cdd:cd03289 170 DPITYQVIRKTLKQAFA--DCTVILSEHRIEAMLE-CQRFLVIEENKVR 215
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-212 |
3.56e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 70.83 E-value: 3.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 1 MQSAVLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVG--LMKKNNGRIIMNGYSQDDDHLKAMS 78
Cdd:CHL00131 3 KNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 79 SVGAI------IE-----NPEF----------YSYLTGFENLELYasmhdgvseERIFEVVKRVRL-EHAIHQKV-KTYS 135
Cdd:CHL00131 83 HLGIFlafqypIEipgvsNADFlrlaynskrkFQGLPELDPLEFL---------EIINEKLKLVGMdPSFLSRNVnEGFS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 136 LGMKQRLGIAQAILHKPNLLILDEPTNGLDPAGMKEFREHLQMLVQEEGvSVLFATH---LLHEVEElcDRMIIIQKGQI 212
Cdd:CHL00131 154 GGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSEN-SIILITHyqrLLDYIKP--DYVHVMQNGKI 230
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-212 |
3.68e-14 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 72.62 E-value: 3.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 6 LHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRI-----IMNGY-SQDDDHlkamss 79
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwsenANIGYyAQDHAY------ 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 80 vgaiienpEFYSYLTGFENLELYASMHDGvsEERIFEVVKRVRL-EHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILD 158
Cdd:PRK15064 394 --------DFENDLTLFDWMSQWRQEGDD--EQAVRGTLGRLLFsQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMD 463
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 515936072 159 EPTNGLDpagMkEFREHLQM-LVQEEGvSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:PRK15064 464 EPTNHMD---M-ESIESLNMaLEKYEG-TLIFVSHDREFVSSLATRIIEITPDGV 513
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-211 |
4.44e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 72.34 E-value: 4.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 1 MQsAVLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAMSSV 80
Cdd:PRK10762 1 MQ-ALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 81 G-AIIEN-----PEfysyLTGFENLEL---YASMHDGVSEERIFE----VVKRVRLEHAIHQKVKTYSLGMKQRLGIAQA 147
Cdd:PRK10762 80 GiGIIHQelnliPQ----LTIAENIFLgreFVNRFGRIDWKKMYAeadkLLARLNLRFSSDKLVGELSIGEQQMVEIAKV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515936072 148 ILHKPNLLILDEPTNGL----DPAGMKEFREhlqmlVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQ 211
Cdd:PRK10762 156 LSFESKVIIMDEPTDALtdteTESLFRVIRE-----LKSQGRGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
16-165 |
5.35e-14 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 72.16 E-value: 5.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 16 GRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysQDDDHLKaMSSVGAIIenpefysyltG 95
Cdd:COG5265 369 PERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDG--QDIRDVT-QASLRAAI----------G 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 96 -------------FENLeLYAsmHDGVSEERIFEVVKRVRLEHAIHQKVKTY-----------SLGMKQRLGIAQAILHK 151
Cdd:COG5265 436 ivpqdtvlfndtiAYNI-AYG--RPDASEEEVEAAARAAQIHDFIESLPDGYdtrvgerglklSGGEKQRVAIARTLLKN 512
|
170
....*....|....
gi 515936072 152 PNLLILDEPTNGLD 165
Cdd:COG5265 513 PPILIFDEATSALD 526
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-212 |
6.10e-14 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 70.21 E-value: 6.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 4 AVLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNG-------------YSQD 70
Cdd:COG4598 7 PALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGeeirlkpdrdgelVPAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 71 DDHLKAM-SSVGAIIENPEFYSYLTGFENLeLYASMH-DGVS----EERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGI 144
Cdd:COG4598 87 RRQLQRIrTRLGMVFQSFNLWSHMTVLENV-IEAPVHvLGRPkaeaIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515936072 145 AQAILHKPNLLILDEPTNGLDPAGMKEFREHLQMLVqEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:COG4598 166 ARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLA-EEGRTMLVVTHEMGFARDVSSHVVFLHQGRI 232
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-165 |
6.14e-14 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 71.89 E-value: 6.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 5 VLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMN-----GY-SQDDDHLKAMS 78
Cdd:TIGR03719 322 VIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGetvklAYvDQSRDALDPNK 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 79 SVgaiienpefysyltgfenlelYASMHDGVSEERI--FEV-----VKRVRLEHAIHQK-VKTYSLGMKQRLGIAQAILH 150
Cdd:TIGR03719 402 TV---------------------WEEISGGLDIIKLgkREIpsrayVGRFNFKGSDQQKkVGQLSGGERNRVHLAKTLKS 460
|
170
....*....|....*
gi 515936072 151 KPNLLILDEPTNGLD 165
Cdd:TIGR03719 461 GGNVLLLDEPTNDLD 475
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
6-211 |
6.91e-14 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 69.04 E-value: 6.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 6 LHIENV-----DKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNG----YSQdddhlKA 76
Cdd:cd03250 1 ISVEDAsftwdSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGsiayVSQ-----EP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 77 --MSsvGAIIENPEFYSYLtgfenlelyasmhdgvSEERIFEVVKRVRLEH-----------AIHQKVKTYSLGMKQRLG 143
Cdd:cd03250 76 wiQN--GTIRENILFGKPF----------------DEERYEKVIKACALEPdleilpdgdltEIGEKGINLSGGQKQRIS 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515936072 144 IAQAILHKPNLLILDEPTNGLDPagmkEFREHL-QMLVQEEGVS---VLFATHLLHEVEElCDRMIIIQKGQ 211
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAVDA----HVGRHIfENCILGLLLNnktRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-165 |
7.22e-14 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 69.74 E-value: 7.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 27 DIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIImngysqdddhlkamSSVGAIIENPEFYSYLTGFENLELYASMH 106
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIE--------------IELDTVSYKPQYIKADYEGTVRDLLSSIT 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515936072 107 DGVSEERIF--EVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLD 165
Cdd:cd03237 87 KDFYTHPYFktEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
5-228 |
8.27e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.50 E-value: 8.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 5 VLHIENV---DKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMK-KNNGRIIMNGYSQDDDH-LKAMS- 78
Cdd:PRK13549 259 ILEVRNLtawDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNpQQAIAq 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 79 ------------------SVGAIIENPEFYSYLTGfenlelyaSMHDGVSEER-IFEVVKRVRLEHA-IHQKVKTYSLGM 138
Cdd:PRK13549 339 giamvpedrkrdgivpvmGVGKNITLAALDRFTGG--------SRIDDAAELKtILESIQRLKVKTAsPELAIARLSGGN 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 139 KQRLGIAQAILHKPNLLILDEPTNGLDPAGMKEFREHLQMLVQeEGVSVLFATHLLHEVEELCDRMIIIQKGQIKA---N 215
Cdd:PRK13549 411 QQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQ-QGVAIIVISSELPEVLGLSDRVLVMHEGKLKGdliN 489
|
250
....*....|...
gi 515936072 216 TNLRdmegKEQVL 228
Cdd:PRK13549 490 HNLT----QEQVM 498
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
18-212 |
8.76e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 71.41 E-value: 8.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 18 HQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNnGRIIMNGYSQDD----DHLKAMSSVGaiiENPEFysyl 93
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELREldpeSWRKHLSWVG---QNPQL---- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 94 tgfenleLYASMHDGV-------SEERIFEVVKRVR-----------LEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLL 155
Cdd:PRK11174 435 -------PHGTLRDNVllgnpdaSDEQLQQALENAWvseflpllpqgLDTPIGDQAAGLSVGQAQRLALARALLQPCQLL 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515936072 156 ILDEPTNGLDpagMKEFREHLQMLVQE-EGVSVLFATHLLHEVEElCDRMIIIQKGQI 212
Cdd:PRK11174 508 LLDEPTASLD---AHSEQLVMQALNAAsRRQTTLMVTHQLEDLAQ-WDQIWVMQDGQI 561
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
24-212 |
9.60e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 71.54 E-value: 9.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 24 ISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAMSS-VGAIIENPEFYSYLTGFENLEly 102
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKlFSAVFTDFHLFDQLLGPEGKP-- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 103 asmhdgVSEERIFEVVKRVRLEHAIH---QKVKTYSL--GMKQRLGIAQAILHKPNLLILDEPTNGLDPAGMKEFREHLQ 177
Cdd:PRK10522 420 ------ANPALVEKWLERLKMAHKLEledGRISNLKLskGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLL 493
|
170 180 190
....*....|....*....|....*....|....*
gi 515936072 178 MLVQEEGVSVLFATHLLHEVeELCDRMIIIQKGQI 212
Cdd:PRK10522 494 PLLQEMGKTIFAISHDDHYF-IHADRLLEMRNGQL 527
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
5-212 |
1.38e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 69.34 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 5 VLHIENVDKQIGRhQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLM----KKNNGRIIMNGYSQDDDHLKAmSSV 80
Cdd:PRK10418 4 QIELRNIALQAAQ-PLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGRVLLDGKPVAPCALRG-RKI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 81 GAIIENPEfysylTGFENLElyaSMHDGVSE-----------ERIFEVVKRVRLEHAiHQKVKTY----SLGMKQRLGIA 145
Cdd:PRK10418 82 ATIMQNPR-----SAFNPLH---TMHTHAREtclalgkpaddATLTAALEAVGLENA-ARVLKLYpfemSGGMLQRMMIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515936072 146 QAILHKPNLLILDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:PRK10418 153 LALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
6-214 |
1.76e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 68.56 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 6 LHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKN--NGRIIMNGysQDddhLKAMSsvgai 83
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKYEvtSGSILLDG--ED---ILELS----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 84 ienPE-------FYSY-----LTGFENLELYASMHDGVSEERI--FEVVKRVrlehaihqKVKTYSLGM----------- 138
Cdd:COG0396 71 ---PDeraragiFLAFqypveIPGVSVSNFLRTALNARRGEELsaREFLKLL--------KEKMKELGLdedfldryvne 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 139 ------KQRLGIAQAILHKPNLLILDEPTNGLDPAGMKEFREHLQMLvQEEGVSVLFATH---LLHEVEelCDRMIIIQK 209
Cdd:COG0396 140 gfsggeKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKL-RSPDRGILIITHyqrILDYIK--PDFVHVLVD 216
|
....*
gi 515936072 210 GQIKA 214
Cdd:COG0396 217 GRIVK 221
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-165 |
2.02e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 70.61 E-value: 2.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 28 IRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMN-------GYSQDDDHL---KAMSSVGAIIENPEFYSyltgfe 97
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPElkisykpQYIKPDYDGtveDLLRSITDDLGSSYYKS------ 435
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515936072 98 nlelyasmhdgvseerifEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLD 165
Cdd:PRK13409 436 ------------------EIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-165 |
2.12e-13 |
|
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: 70.20 E-value: 2.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 29 RQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRiIMNGYSQDDdhlkamssvgaIIE---NPEFYSYLTGFENLELYASM 105
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGD-YDEEPSWDE-----------VLKrfrGTELQDYFKKLANGEIKVAH 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 106 -----------HDG-VSE------ER--IFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLD 165
Cdd:COG1245 165 kpqyvdlipkvFKGtVREllekvdERgkLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
24-228 |
2.27e-13 |
|
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: 70.24 E-value: 2.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 24 ISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMK-KNNGRIIMNGYsQDDDHLKAMSSVGAIIENPE------FYSYLTGF 96
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGK-PVDIRNPAQAIRAGIAMVPEdrkrhgIVPILGVG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 97 ENLELyASMHDGVSEERIFEVVKRVRLEHAIHQ-KVKTYSL---------GMKQRLGIAQAILHKPNLLILDEPTNGLDP 166
Cdd:TIGR02633 358 KNITL-SVLKSFCFKMRIDAAAELQIIGSAIQRlKVKTASPflpigrlsgGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515936072 167 AGMKEFREHLQMLVQeEGVSVLFATHLLHEVEELCDRMIIIQKGQIKA---NTNLRdmegKEQVL 228
Cdd:TIGR02633 437 GAKYEIYKLINQLAQ-EGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGdfvNHALT----QEQVL 496
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-206 |
3.51e-13 |
|
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: 65.86 E-value: 3.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 30 QGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMngysqdddhlkamssvgaiienpefysyltgfenlelyasmhdgV 109
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY--------------------------------------------I 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 110 SEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPAGMKEFREH-----LQMLVQEEG 184
Cdd:smart00382 37 DGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLLLLKSEKN 116
|
170 180
....*....|....*....|..
gi 515936072 185 VSVLFATHLLHEVEELCDRMII 206
Cdd:smart00382 117 LTVILTTNDEKDLGPALLRRRF 138
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
24-212 |
3.79e-13 |
|
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: 69.45 E-value: 3.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 24 ISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRI--------IMNGYSQDDDHLKAMSSVGAIIENPEFYSYLTG 95
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdewVDMTKPGPDGRGRAKRYIGILHQEYDLYPHRTV 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 96 FENLELYASMH--DGVSEERIFEVVKRV-----RLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPAG 168
Cdd:TIGR03269 383 LDNLTEAIGLElpDELARMKAVITLKMVgfdeeKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPIT 462
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 515936072 169 MKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:TIGR03269 463 KVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
5-270 |
3.98e-13 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 69.81 E-value: 3.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 5 VLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRI-----IMNGY---------SQD 70
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIglakgIKLGYfaqhqleflRAD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 71 DDHLKAMSSVGAIIENPEFYSYLTGFenlelyasmhdGVSEERIFEVVKRvrlehaihqkvktYSLGMKQRLGIAQAILH 150
Cdd:PRK10636 392 ESPLQHLARLAPQELEQKLRDYLGGF-----------GFQGDKVTEETRR-------------FSGGEKARLVLALIVWQ 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 151 KPNLLILDEPTNGLDpagmKEFREHL-QMLVQEEGVSVLfATHLLHEVEELCDRMIIIQKGQIKANTNlrDMEGKEQVLM 229
Cdd:PRK10636 448 RPNLLLLDEPTNHLD----LDMRQALtEALIDFEGALVV-VSHDRHLLRSTTDDLYLVHDGKVEPFDG--DLEDYQQWLS 520
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 515936072 230 NIQPVEKAVSWL--DTQGYTYEQR-DQhvlvqlkKDRVPELNKQ 270
Cdd:PRK10636 521 DVQKQENQTDEApkENNANSAQARkDQ-------KRREAELRTQ 557
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
28-169 |
4.19e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 67.18 E-value: 4.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 28 IRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYS-QDDDHLKAMSSVGAIienPEFYSYLTGFENLELYASMH 106
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTaTRGDRSRFMAYLGHL---PGLKADLSTLENLHFLCGLH 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515936072 107 DGVSEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPAGM 169
Cdd:PRK13543 111 GRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGI 173
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
23-211 |
5.25e-13 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 68.29 E-value: 5.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 23 HISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLmKKNNGRIIMNGYSQDDDHLKAMS----------SVGAIIENPEfySY 92
Cdd:PRK15093 25 RVSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDNWRVTADRMRFDDIDLLRLSprerrklvghNVSMIFQEPQ--SC 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 93 LTGFENL--ELYASMHD-----------GVSEERIFEVVKRVRL-EHAIHQKVKTYSL--GMKQRLGIAQAILHKPNLLI 156
Cdd:PRK15093 102 LDPSERVgrQLMQNIPGwtykgrwwqrfGWRKRRAIELLHRVGIkDHKDAMRSFPYELteGECQKVMIAIALANQPRLLI 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 515936072 157 LDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQ 211
Cdd:PRK15093 182 ADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQ 236
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
18-215 |
9.66e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.22 E-value: 9.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 18 HQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAMssVGAIIENPEF-YSYLTGF 96
Cdd:PRK15056 20 HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL--VAYVPQSEEVdWSFPVLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 97 ENLEL---YASM--------HDgvsEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLD 165
Cdd:PRK15056 98 EDVVMmgrYGHMgwlrrakkRD---RQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 515936072 166 PAGMKEFREHLQMLvQEEGVSVLFATHLLHEVEELCDRMIIIqKGQIKAN 215
Cdd:PRK15056 175 VKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYTVMV-KGTVLAS 222
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-192 |
9.88e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 68.30 E-value: 9.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 28 IRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRiimngYSQD---DDHLKAMSSVgaiienpEFYSYLTGFENLELYAS 104
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGD-----YEEEpswDEVLKRFRGT-------ELQNYFKKLYNGEIKVV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 105 MH-------------------DGVSEERIF-EVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGL 164
Cdd:PRK13409 164 HKpqyvdlipkvfkgkvrellKKVDERGKLdEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYL 243
|
170 180 190
....*....|....*....|....*....|..
gi 515936072 165 DpagmkeFREHLQM--LVQE--EGVSVLFATH 192
Cdd:PRK13409 244 D------IRQRLNVarLIRElaEGKYVLVVEH 269
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-212 |
9.91e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 67.04 E-value: 9.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 20 ILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKK-----NNGRIIMNGYS--QDDDHLKAMSSVGAIIENPEFYSy 92
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSifNYRDVLEFRRRVGMLFQRPNPFP- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 93 LTGFENLELYASMHD--------GVSEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGL 164
Cdd:PRK14271 115 MSIMDNVLAGVRAHKlvprkefrGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSAL 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 515936072 165 DPAGMKEFREHLQMLVQEegVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:PRK14271 195 DPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
21-212 |
1.12e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 68.34 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 21 LQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQD---DDHLKAM-SSVGAIIENPefYSYL--- 93
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDtlsPGKLQALrRDIQFIFQDP--YASLdpr 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 94 --TGF---ENLELYASMHDGVSEERIFEVVKRVRL--EHAIHQKvKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDP 166
Cdd:PRK10261 418 qtVGDsimEPLRVHGLLPGKAAAARVAWLLERVGLlpEHAWRYP-HEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 515936072 167 AGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:PRK10261 497 SIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
8-229 |
1.29e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.83 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 8 IENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAMSSVGAIIENP 87
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 88 EFYSYL--TGFENLEL--YASMHDGVSEERIFEVVKRVRLEHAI----HQKVKTYSLGMKQRLGIAQAILHKPNLLILDE 159
Cdd:PRK10982 81 ELNLVLqrSVMDNMWLgrYPTKGMFVDQDKMYRDTKAIFDELDIdidpRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515936072 160 PTNGLDPagmKEFrEHLQMLVQ---EEGVSVLFATHLLHEVEELCDRMIIIQKGQIKANTNLRDMEGKEQVLM 229
Cdd:PRK10982 161 PTSSLTE---KEV-NHLFTIIRklkERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAM 229
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
8-192 |
1.31e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 67.98 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 8 IENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNN--GRIIMNGYSQDDDHLKamsSVGAIIE 85
Cdd:PLN03211 71 ISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQILK---RTGFVTQ 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 86 NPEFYSYLTGFENL----------ELYASMHDGVSEERIFEvVKRVRLEHAI--HQKVKTYSLGMKQRLGIAQAILHKPN 153
Cdd:PLN03211 148 DDILYPHLTVRETLvfcsllrlpkSLTKQEKILVAESVISE-LGLTKCENTIigNSFIRGISGGERKRVSIAHEMLINPS 226
|
170 180 190
....*....|....*....|....*....|....*....
gi 515936072 154 LLILDEPTNGLDPAGMKEFREHLQMLVQeEGVSVLFATH 192
Cdd:PLN03211 227 LLILDEPTSGLDATAAYRLVLTLGSLAQ-KGKTIVTSMH 264
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-192 |
2.12e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 67.27 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 5 VLHIENVDKQI-GRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRI-----IMNGYSQDDDHLKAMS 78
Cdd:TIGR03719 4 IYTMNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEArpqpgIKVGYLPQEPQLDPTK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 79 SVGAIIEN--PEFYSYLTGFEnlELYASM------HDGVSEE--RIFEVVKRV-------RLEHAIH--------QKVKT 133
Cdd:TIGR03719 84 TVRENVEEgvAEIKDALDRFN--EISAKYaepdadFDKLAAEqaELQEIIDAAdawdldsQLEIAMDalrcppwdADVTK 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515936072 134 YSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPAGMKEFREHLQmlvQEEGvSVLFATH 192
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQ---EYPG-TVVAVTH 216
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
23-214 |
4.39e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.18 E-value: 4.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 23 HISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNG-----------------Y-SQD---DDHLKAMSsvg 81
Cdd:PRK10762 270 DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGhevvtrspqdglangivYiSEDrkrDGLVLGMS--- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 82 aIIENPEfysyLTGFENLElYASMHDGVSEERIfEVVKRVRLEH----AIHQKVKTYSLGMKQRLGIAQAILHKPNLLIL 157
Cdd:PRK10762 347 -VKENMS----LTALRYFS-RAGGSLKHADEQQ-AVSDFIRLFNiktpSMEQAIGLLSGGNQQKVAIARGLMTRPKVLIL 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515936072 158 DEPTNGLDPAGMKEFrehLQMLVQ--EEGVSVLFATHLLHEVEELCDRMIIIQKGQIKA 214
Cdd:PRK10762 420 DEPTRGVDVGAKKEI---YQLINQfkAEGLSIILVSSEMPEVLGMSDRILVMHEGRISG 475
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
5-211 |
5.23e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 66.42 E-value: 5.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 5 VLHIENVD----KQIGRHQILQHISMDIRQGEIVGLLGPNGSGKT----TLIRLI-----------VGLMKKNNGRIIMN 65
Cdd:PRK10261 12 VLAVENLNiafmQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqagglvqcdkMLLRRRSRQVIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 66 GYSQDDDHLKAMSSVGAIIENP--EFYSYLTGFENLELYASMHDGVSEERIFEVVKR----VRLEHAiHQKVKTY----S 135
Cdd:PRK10261 92 EQSAAQMRHVRGADMAMIFQEPmtSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRmldqVRIPEA-QTILSRYphqlS 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515936072 136 LGMKQRLGIAQAILHKPNLLILDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQ 211
Cdd:PRK10261 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGE 246
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
5-210 |
9.38e-12 |
|
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: 63.03 E-value: 9.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 5 VLHIENVDKQI----GRHQILQHISMDIRQGEIVGLLGPNGSGKTTLI-----RLIVGLMKknnGRIIMNGYSQDDDHLK 75
Cdd:cd03232 3 VLTWKNLNYTVpvkgGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLdvlagRKTAGVIT---GEILINGRPLDKNFQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 76 amsSVGAIIENPEFYSYLTGFENLELYAsmhdgvseerifevvkrvrlehaihqKVKTYSLGMKQRLGIAQAILHKPNLL 155
Cdd:cd03232 80 ---STGYVEQQDVHSPNLTVREALRFSA--------------------------LLRGLSVEQRKRLTIGVELAAKPSIL 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 156 ILDEPTNGLDPAGMKEFREHLQMLVqEEGVSVLFATH-----LLheveELCDRMIIIQKG 210
Cdd:cd03232 131 FLDEPTSGLDSQAAYNIVRFLKKLA-DSGQAILCTIHqpsasIF----EKFDRLLLLKRG 185
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-212 |
9.97e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 65.77 E-value: 9.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 20 ILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAMSSVGAII-ENPEFYSYLTGFeN 98
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIpQSPVLFSGTVRF-N 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 99 LELYASMHDG-----VSEERIFEVVKR--VRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDpagmKE 171
Cdd:PLN03232 1330 IDPFSEHNDAdlweaLERAHIKDVIDRnpFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVD----VR 1405
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 515936072 172 FREHLQMLVQEE--GVSVLFATHLLHEVEElCDRMIIIQKGQI 212
Cdd:PLN03232 1406 TDSLIQRTIREEfkSCTMLVIAHRLNTIID-CDKILVLSSGQV 1447
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
21-213 |
1.65e-11 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 64.65 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 21 LQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAMSSVGAIIEnpefysyltgfENLE 100
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVS-----------QNVH 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 101 L----------YASmHDGVSEErifEVVKRVRLEHAIH--QKVK------------TYSLGMKQRLGIAQAILHKPNLLI 156
Cdd:PRK11176 428 LfndtianniaYAR-TEQYSRE---QIEEAARMAYAMDfiNKMDngldtvigengvLLSGGQRQRIAIARALLRDSPILI 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515936072 157 LDEPTNGLDPAGMKEFREHLQMLvQEEGVSVLFAtHLLHEVEElCDRMIIIQKGQIK 213
Cdd:PRK11176 504 LDEATSALDTESERAIQAALDEL-QKNRTSLVIA-HRLSTIEK-ADEILVVEDGEIV 557
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1-212 |
2.46e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 63.97 E-value: 2.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 1 MQSAVLHIENVDKQIGRHQ-ILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYS-QDDDHLKAMS 78
Cdd:PRK10790 336 LQSGRIDIDNVSFAYRDDNlVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPlSSLSHSVLRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 79 SVGAIIENPEFYSYlTGFENLELYASmhdgVSEERIFEVVKRVRL-------EHAIHQKV----KTYSLGMKQRLGIAQA 147
Cdd:PRK10790 416 GVAMVQQDPVVLAD-TFLANVTLGRD----ISEEQVWQALETVQLaelarslPDGLYTPLgeqgNNLSVGQKQLLALARV 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515936072 148 ILHKPNLLILDEPTNGLDpAGMKEFREHLQMLVQEEGVSVLFAtHLLHEVEElCDRMIIIQKGQI 212
Cdd:PRK10790 491 LVQTPQILILDEATANID-SGTEQAIQQALAAVREHTTLVVIA-HRLSTIVE-ADTILVLHRGQA 552
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
21-211 |
3.63e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 63.66 E-value: 3.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 21 LQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKN--NGRIIMNGYSQDDDHLKAMSSVGAIIENPEF--YSYLTGF 96
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGEVCRFKDIRDSEALGIVIIHQELalIPYLSIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 97 ENLEL-YASMHDGV-----SEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGL---DPA 167
Cdd:NF040905 97 ENIFLgNERAKRGVidwneTNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALneeDSA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 515936072 168 G----MKEFREHlqmlvqeeGVSVLFATHLLHEVEELCDRMIIIQKGQ 211
Cdd:NF040905 177 AlldlLLELKAQ--------GITSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
17-212 |
4.13e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 62.11 E-value: 4.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 17 RHQI--LQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYS-----------------QD-DDHLKA 76
Cdd:PRK15112 23 RQTVeaVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPlhfgdysyrsqrirmifQDpSTSLNP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 77 MSSVGAIIENPefysyltgfenLELYASMHDGVSEERIFEVVKRVRL--EHAIHQKvKTYSLGMKQRLGIAQAILHKPNL 154
Cdd:PRK15112 103 RQRISQILDFP-----------LRLNTDLEPEQREKQIIETLRQVGLlpDHASYYP-HMLAPGQKQRLGLARALILRPKV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515936072 155 LILDEPTNGLDpAGMKEFREHLQMLVQEE-GVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:PRK15112 171 IIADEALASLD-MSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEV 228
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
38-193 |
4.91e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 61.04 E-value: 4.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 38 GPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAMSSVGaiiENPEFYSYLTGFENLELYASMHDgvSEERIFEV 117
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIG---HNLGLKLEMTVFENLKFWSEIYN--SAETLYAA 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515936072 118 VKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDpagmKEFREHLQMLV---QEEGVSVLFATHL 193
Cdd:PRK13541 108 IHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS----KENRDLLNNLIvmkANSGGIVLLSSHL 182
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-213 |
1.25e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 62.27 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 20 ILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAMSSVGAII-ENPEFYSYlTGFEN 98
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIpQDPVLFSG-SLRMN 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 99 LELYASMHD-------GVSEERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDpagmKE 171
Cdd:TIGR00957 1380 LDPFSQYSDeevwwalELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVD----LE 1455
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 515936072 172 FREHLQMLV--QEEGVSVLFATHLLHEVEELCdRMIIIQKGQIK 213
Cdd:TIGR00957 1456 TDNLIQSTIrtQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVA 1498
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-165 |
2.06e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 61.29 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 5 VLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMN-----GY-SQDDDHLKAMS 78
Cdd:PRK11819 324 VIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGetvklAYvDQSRDALDPNK 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 79 SVGAIIENPEFYSYLTGFE-NLELYASmhdgvseerifevvkRVRLEHAIHQK-VKTYSLGMKQRLGIAQAILHKPNLLI 156
Cdd:PRK11819 404 TVWEEISGGLDIIKVGNREiPSRAYVG---------------RFNFKGGDQQKkVGVLSGGERNRLHLAKTLKQGGNVLL 468
|
....*....
gi 515936072 157 LDEPTNGLD 165
Cdd:PRK11819 469 LDEPTNDLD 477
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-165 |
2.16e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 61.29 E-value: 2.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 1 MQSAVLHIENVDKQIG-RHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGR-IIMNGYsqdddhlkams 78
Cdd:PRK11819 2 MAQYIYTMNRVSKVVPpKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEaRPAPGI----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 79 SVGAIIENPEFYSYLTGFENLElyasmhDGVSEerIFEVVKRV------------------------------------- 121
Cdd:PRK11819 71 KVGYLPQEPQLDPEKTVRENVE------EGVAE--VKAALDRFneiyaayaepdadfdalaaeqgelqeiidaadawdld 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515936072 122 -RLEHAIH--------QKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLD 165
Cdd:PRK11819 143 sQLEIAMDalrcppwdAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
16-165 |
3.27e-10 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 60.75 E-value: 3.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 16 GRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAM-SSVGAIIENPEFYSYLT 94
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLrRNIAVVFQDAGLFNRSI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 95 GfENLELyasMHDGVSEERIFEVVKRVRLEHAIHQKVKTY-----------SLGMKQRLGIAQAILHKPNLLILDEPTNG 163
Cdd:PRK13657 426 E-DNIRV---GRPDATDEEMRAAAERAQAHDFIERKPDGYdtvvgergrqlSGGERQRLAIARALLKDPPILILDEATSA 501
|
..
gi 515936072 164 LD 165
Cdd:PRK13657 502 LD 503
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-165 |
6.81e-10 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 58.53 E-value: 6.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 29 RQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGySQDDdhlkamssvgaIIEN---PEFYSYLTGFENLELYASM 105
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPP-DWDE-----------ILDEfrgSELQNYFTKLLEGDVKVIV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 106 H-----------DGVSEERIF---------EVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLD 165
Cdd:cd03236 92 KpqyvdlipkavKGKVGELLKkkdergkldELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
20-230 |
2.66e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.21 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 20 ILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAMSSVGAII-ENPEFYSYLTGFeN 98
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIpQAPVLFSGTVRF-N 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 99 LELYASMHDG---VSEER--IFEVVKR--VRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDpAGMKE 171
Cdd:PLN03130 1333 LDPFNEHNDAdlwESLERahLKDVIRRnsLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVD-VRTDA 1411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515936072 172 FrehLQMLVQEE--GVSVLFATHLLHEVEElCDRMIIIQKGQIKantnlrDMEGKEQVLMN 230
Cdd:PLN03130 1412 L---IQKTIREEfkSCTMLIIAHRLNTIID-CDRILVLDAGRVV------EFDTPENLLSN 1462
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
3-210 |
6.07e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.04 E-value: 6.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 3 SAVLHIENVDKQIG----RHQILQHISMDIRQGEIVGLLGPNGSGKTTLI-----RLIVGLMKKN----NG--------R 61
Cdd:TIGR00956 757 EDIFHWRNLTYEVKikkeKRVILNNVDGWVKPGTLTALMGASGAGKTTLLnvlaeRVTTGVITGGdrlvNGrpldssfqR 836
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 62 IImnGYSQDDD-HLKAMSsvgaIIENPEFYSYLTGFENLELYASMhdgvseERIFEVVKRVRLEHAIHQKVKTYSLGM-- 138
Cdd:TIGR00956 837 SI--GYVQQQDlHLPTST----VRESLRFSAYLRQPKSVSKSEKM------EYVEEVIKLLEMESYADAVVGVPGEGLnv 904
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 139 --KQRLGIAQAILHKPNLLI-LDEPTNGLDP----AGMKEFREhlqmlVQEEGVSVLFATH-----LLHEVeelcDRMII 206
Cdd:TIGR00956 905 eqRKRLTIGVELVAKPKLLLfLDEPTSGLDSqtawSICKLMRK-----LADHGQAILCTIHqpsaiLFEEF----DRLLL 975
|
....
gi 515936072 207 IQKG 210
Cdd:TIGR00956 976 LQKG 979
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
21-212 |
6.08e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 56.66 E-value: 6.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 21 LQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDD-DHLKAMSSVGAIIENPE----FYSYLT- 94
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNhNANEAINHGFALVTEERrstgIYAYLDi 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 95 GFE----NLELYASMHDGVSEERIFE----VVKRVRLEHAIHQ-KVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLD 165
Cdd:PRK10982 344 GFNslisNIRNYKNKVGLLDNSRMKSdtqwVIDSMRVKTPGHRtQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGID 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 515936072 166 PAGMKEFREHLQMLVQEEGVSVLFAThllhEVEEL---CDRMIIIQKGQI 212
Cdd:PRK10982 424 VGAKFEIYQLIAELAKKDKGIIIISS----EMPELlgiTDRILVMSNGLV 469
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
6-165 |
7.18e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 56.79 E-value: 7.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 6 LHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIR-----LIVGLMKknNGRIIMNGYSQDDDHLKAMSSV 80
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRymamhAIDGIPK--NCQILHVEQEVVGDDTTALQCV 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 81 -GAIIENPEF---------------YSYLTGFENLELYASMHDGVSEERIFEVVKRVRLEHAI----------------- 127
Cdd:PLN03073 256 lNTDIERTQLleeeaqlvaqqreleFETETGKGKGANKDGVDKDAVSQRLEEIYKRLELIDAYtaearaasilaglsftp 335
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 515936072 128 ---HQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLD 165
Cdd:PLN03073 336 emqVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
18-221 |
8.59e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 55.60 E-value: 8.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 18 HQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKN--------NGRIIMNG---YSQDDDHLKAMSSVGAIIEN 86
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGeplAAIDAPRLARLRAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 87 PEFYSYLTGFENLELY--------ASMHDGvseERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAI--LHK----- 151
Cdd:PRK13547 94 PAFAFSAREIVLLGRYpharragaLTHRDG---EIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqLWPphdaa 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515936072 152 --PNLLILDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCDRMIIIQKGQIKANTNLRDM 221
Cdd:PRK13547 171 qpPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
24-215 |
1.41e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 55.69 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 24 ISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGysqdddhlKAMS--SVGAIIEN-----PE------FY 90
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDG--------KPIDirSPRDAIRAgimlcPEdrkaegII 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 91 SYLTGFENLELYASMH--------DGVSEERIFEV-VKRVRLEHA-IHQKVKTYSLGMKQRlgiaqAILHK-----PNLL 155
Cdd:PRK11288 344 PVHSVADNINISARRHhlragcliNNRWEAENADRfIRSLNIKTPsREQLIMNLSGGNQQK-----AILGRwlsedMKVI 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 156 ILDEPTNGLDPAGMKEFREHLQMLVqEEGVSVLFATHLLHEVEELCDRMIIIQKGQIKAN 215
Cdd:PRK11288 419 LLDEPTRGIDVGAKHEIYNVIYELA-AQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGE 477
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
57-165 |
2.69e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.04 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 57 KNNGRIIMNGYSQDDDHLKAMSSVGAII-ENPEFYsyltgfeNLELYASMHDGvSEERIFEVVKRVRLEHAIHQKV---- 131
Cdd:PTZ00265 1274 KNSGKILLDGVDICDYNLKDLRNLFSIVsQEPMLF-------NMSIYENIKFG-KEDATREDVKRACKFAAIDEFIeslp 1345
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 515936072 132 -----------KTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLD 165
Cdd:PTZ00265 1346 nkydtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLD 1390
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-212 |
2.70e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 54.80 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 19 QILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLM--KKNNGRIIMNGYSQDddhlkaMSSVGAIIENPefYSYLT-- 94
Cdd:NF040905 274 KVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTVFKDGKEVD------VSTVSDAIDAG--LAYVTed 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 95 ----GF-------ENLELYA----SMHDGVSEERIFEVVKRVRLE-----HAIHQKVKTYSLGMKQRLGIAQAILHKPNL 154
Cdd:NF040905 346 rkgyGLnliddikRNITLANlgkvSRRGVIDENEEIKVAEEYRKKmniktPSVFQKVGNLSGGNQQKVVLSKWLFTDPDV 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515936072 155 LILDEPTNGLDpAGMK-EFREHLQMLVqEEGVSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:NF040905 426 LILDEPTRGID-VGAKyEIYTIINELA-AEGKGVIVISSELPELLGMCDRIYVMNEGRI 482
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
17-212 |
3.21e-08 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 54.72 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 17 RHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAMSSVGAIIENPEFYSYLTGF 96
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 97 ENLELyasMHDGVSEERIFEVVKRVRLEHAIHQKVKTY-----------SLGMKQRLGIAQAILHKPNLLILDEPTNGLD 165
Cdd:PRK10789 407 NNIAL---GRPDATQQEIEHVARLASVHDDILRLPQGYdtevgergvmlSGGQKQRISIARALLLNAEILILDDALSAVD 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 515936072 166 paGMKEfREHLQMLVQ-EEGVSVLFATHLLHEVEElCDRMIIIQKGQI 212
Cdd:PRK10789 484 --GRTE-HQILHNLRQwGEGRTVIISAHRLSALTE-ASEILVMQHGHI 527
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
32-218 |
3.96e-08 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 52.75 E-value: 3.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 32 EIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIImnGYSQDDDHLKAMSSVgaiienpefYSYLTGFENLELYASMHDGVSE 111
Cdd:PRK15177 14 EHIGILAAPGSGKTTLTRLLCGLDAPDEGDFI--GLRGDALPLGANSFI---------LPGLTGEENARMMASLYGLDGD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 112 ERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLfaT 191
Cdd:PRK15177 83 EFSHFCYQLTQLEQCYTDRVSEYSVTMKTHLAFAINLLLPCRLYIADGKLYTGDNATQLRMQAALACQLQQKGLIVL--T 160
|
170 180
....*....|....*....|....*..
gi 515936072 192 HLLHEVEELCDRMIIIQKGQIKANTNL 218
Cdd:PRK15177 161 HNPRLIKEHCHAFGVLLHGKITMCEDL 187
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
9-192 |
5.59e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 53.98 E-value: 5.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 9 ENVDKQIGRHQIL-QHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIimngySQDDDhlkamssvGAIIENP 87
Cdd:TIGR00954 455 ENIPLVTPNGDVLiESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRL-----TKPAK--------GKLFYVP 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 88 EF-YSYLTGFENLELYASMHD-----GVSEERIFEVVKRVRLEH---------AIHQKVKTYSLGMKQRLGIAQAILHKP 152
Cdd:TIGR00954 522 QRpYMTLGTLRDQIIYPDSSEdmkrrGLSDKDLEQILDNVQLTHilereggwsAVQDWMDVLSGGEKQRIAMARLFYHKP 601
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 515936072 153 NLLILDEPTNGLDPagmkEFREHLQMLVQEEGVSVLFATH 192
Cdd:TIGR00954 602 QFAILDECTSAVSV----DVEGYMYRLCREFGITLFSVSH 637
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
24-212 |
8.41e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.33 E-value: 8.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 24 ISMDIRqgeiVGLLGPNGSGKTTLIRLIVGLMKKNNG------RIIMNGYSQDddHLKAMSsvgaIIENPEFYsyltgfe 97
Cdd:PLN03073 532 IDLDSR----IAMVGPNGIGKSTILKLISGELQPSSGtvfrsaKVRMAVFSQH--HVDGLD----LSSNPLLY------- 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 98 nlelYASMHDGVSEERI------FEVVKRVRLehaihQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPAGMKE 171
Cdd:PLN03073 595 ----MMRCFPGVPEQKLrahlgsFGVTGNLAL-----QPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEA 665
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 515936072 172 FrehLQMLVQEEGvSVLFATHLLHEVEELCDRMIIIQKGQI 212
Cdd:PLN03073 666 L---IQGLVLFQG-GVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
20-192 |
1.32e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.71 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 20 ILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVG-----------LM--KKNNGRIIMN-----GYSQDDDHL--KAMSS 79
Cdd:PRK10938 275 ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndltLFgrRRGSGETIWDikkhiGYVSSSLHLdyRVSTS 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 80 VGAIIenpefysyLTG-FENLELYASMHDgvsEERIF--EVVKRVRLEHAIHQK-VKTYSLGmKQRLG-IAQAILHKPNL 154
Cdd:PRK10938 355 VRNVI--------LSGfFDSIGIYQAVSD---RQQKLaqQWLDILGIDKRTADApFHSLSWG-QQRLAlIVRALVKHPTL 422
|
170 180 190
....*....|....*....|....*....|....*...
gi 515936072 155 LILDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATH 192
Cdd:PRK10938 423 LILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSH 460
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
16-165 |
1.58e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 52.65 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 16 GRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIImngYSQD------------------------- 70
Cdd:PRK11147 14 SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRII---YEQDlivarlqqdpprnvegtvydfvaeg 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 71 ----DDHLKAMSSVGAIIENPEFYSYLTGFENLELYASMHDGVS-EERIFEVVKRVRLEHaiHQKVKTYSLGMKQRLGIA 145
Cdd:PRK11147 91 ieeqAEYLKRYHDISHLVETDPSEKNLNELAKLQEQLDHHNLWQlENRINEVLAQLGLDP--DAALSSLSGGWLRKAALG 168
|
170 180
....*....|....*....|
gi 515936072 146 QAILHKPNLLILDEPTNGLD 165
Cdd:PRK11147 169 RALVSNPDVLLLDEPTNHLD 188
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
19-165 |
3.19e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.95 E-value: 3.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 19 QILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMN-GYSQDDDHLKA-MSSVGAIIENPEFYS----- 91
Cdd:PTZ00265 399 EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKDINLKWwRSKIGVVSQDPLLFSnsikn 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 92 -------------YLTGFENLELYASMHDG-----------------------------------VSEERIFEVVKRV-- 121
Cdd:PTZ00265 479 nikyslyslkdleALSNYYNEDGNDSQENKnkrnscrakcagdlndmsnttdsneliemrknyqtIKDSEVVDVSKKVli 558
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515936072 122 ---------RLEHAIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLD 165
Cdd:PTZ00265 559 hdfvsalpdKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
20-167 |
3.72e-07 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 50.29 E-value: 3.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 20 ILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAMSS-VGAIIENPEFYSYLTGFeN 98
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSrLSIILQDPILFSGSIRF-N 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 99 LELYASMHDgvseERIFEVVKRVRLEH-----------AIHQKVKTYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPA 167
Cdd:cd03288 115 LDPECKCTD----DRLWEALEIAQLKNmvkslpggldaVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMA 190
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
5-192 |
4.24e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 50.17 E-value: 4.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 5 VLHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGL--MKKNNGRIIMNGysQDDDHLKAMSSVG- 81
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKG--KDLLELSPEDRAGe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 82 AIIENPEFYSYLTGFENLELYASMHDGVSEERIFEVVKRVRLEHAIHQKVKT---------------YSLGMKQRLGIAQ 146
Cdd:PRK09580 79 GIFMAFQYPVEIPGVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALlkmpedlltrsvnvgFSGGEKKRNDILQ 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 515936072 147 AILHKPNLLILDEPTNGLDPAGMKEFREHLQMLvQEEGVSVLFATH 192
Cdd:PRK09580 159 MAVLEPELCILDESDSGLDIDALKIVADGVNSL-RDGKRSFIIVTH 203
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-174 |
5.04e-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: 51.06 E-value: 5.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 20 ILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIimngysqdddhlkamSSVGAIIENPEFYSYLTGF--E 97
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI---------------KHSGRISFSPQTSWIMPGTikD 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 98 NLeLYASMHDgvsEERIFEVVKRVRLEHAIH---QKVK--------TYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDP 166
Cdd:TIGR01271 506 NI-IFGLSYD---EYRYTSVIKACQLEEDIAlfpEKDKtvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
....*...
gi 515936072 167 AGMKEFRE 174
Cdd:TIGR01271 582 VTEKEIFE 589
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
24-202 |
5.57e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 50.35 E-value: 5.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 24 ISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNG-----YSQDDDH----------------LKAMSSVGA 82
Cdd:PRK11308 34 VSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGqdllkADPEAQKllrqkiqivfqnpygsLNPRKKVGQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 83 IIENPefysyltgfenLELYASMHDGVSEERIFEVVKRV--RLEHAihqkvKTY----SLGMKQRLGIAQAILHKPNLLI 156
Cdd:PRK11308 114 ILEEP-----------LLINTSLSAAERREKALAMMAKVglRPEHY-----DRYphmfSGGQRQRIAIARALMLDPDVVV 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 515936072 157 LDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFATHLLHEVEELCD 202
Cdd:PRK11308 178 ADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIAD 223
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
27-208 |
6.85e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 48.72 E-value: 6.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 27 DIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIimngysqdddhlkamssvgaiienpefysyltgfenlelyasmh 106
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDND-------------------------------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 107 dgvSEERIFEVVKRvrlehaihQKVKtYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDPAGMKEFREHLQMLVQEEGVS 186
Cdd:cd03222 57 ---EWDGITPVYKP--------QYID-LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKT 124
|
170 180
....*....|....*....|..
gi 515936072 187 VLFATHLLHEVEELCDRMIIIQ 208
Cdd:cd03222 125 ALVVEHDLAVLDYLSDRIHVFE 146
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
21-211 |
8.26e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 48.47 E-value: 8.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 21 LQHISMDIRQGEIVGLLGPNGSGKTTLirLIVGLMKKNNGRIIMNGYSQDDDHLKAMSSVGAIIENPefYSYLTgfenle 100
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLYASGKARLISFLPKFSRNKLIFIDQLQFLIDVG--LGYLT------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 101 lyasmhdgvseerifevvkrvrlehaIHQKVKTYSLGMKQRLGIAQAIL--HKPNLLILDEPTNGLDPAGMKEFREHLQM 178
Cdd:cd03238 81 --------------------------LGQKLSTLSGGELQRVKLASELFsePPGTLFILDEPSTGLHQQDINQLLEVIKG 134
|
170 180 190
....*....|....*....|....*....|...
gi 515936072 179 LVQeEGVSVLFATHLLhEVEELCDRMIIIQKGQ 211
Cdd:cd03238 135 LID-LGNTVILIEHNL-DVLSSADWIIDFGPGS 165
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
20-174 |
9.15e-07 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 49.47 E-value: 9.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 20 ILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNGYSQDDDHLKAMSSvGAIIENPEFysyltgfenl 99
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMP-GTIKENIIF---------- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 100 elyasmhdGVS--EERIFEVVKRVRLEHAIHQKVK-----------TYSLGMKQRLGIAQAILHKPNLLILDEPTNGLDP 166
Cdd:cd03291 121 --------GVSydEYRYKSVVKACQLEEDITKFPEkdntvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
....*...
gi 515936072 167 AGMKEFRE 174
Cdd:cd03291 193 FTEKEIFE 200
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
70-192 |
1.85e-06 |
|
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: 48.54 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 70 DDDHLKAMSSVGAIIENPEFYSYLTGFENLELYASMHDGVSEERIFEVVKRVRLEHAIHQKVKTY--------SLGMKQR 141
Cdd:pfam13304 165 DWAVLDLAADLALFPDLKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGgelpafelSDGTKRL 244
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 515936072 142 LGIAQAIL---HKPNLLILDEPTNGLDPAGMKEFREHLQMLvQEEGVSVLFATH 192
Cdd:pfam13304 245 LALLAALLsalPKGGLLLIDEPESGLHPKLLRRLLELLKEL-SRNGAQLILTTH 297
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
6-188 |
2.83e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.47 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 6 LHIENVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMkknngrIIMNGYSQDD-DHLKAMS--SVGA 82
Cdd:PRK10938 4 LQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGEL------PLLSGERQSQfSHITRLSfeQLQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 83 IIE------NPEFYSYL---TGFENLELyasMHDGVS-EERIFEVVKRVRLEHAIHQKVKTYSLGMKQRLGIAQAILHKP 152
Cdd:PRK10938 78 LVSdewqrnNTDMLSPGeddTGRTTAEI---IQDEVKdPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEP 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 515936072 153 NLLILDEPTNGLDPAGMKEFREHLQMLVQEEGVSVL 188
Cdd:PRK10938 155 DLLILDEPFDGLDVASRQQLAELLASLHQSGITLVL 190
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
20-165 |
4.78e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.86 E-value: 4.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 20 ILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMNG------YSQDDDHLkAMSSVGAIIENPEFYSYL 93
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawVNQETPAL-PQPALEYVIDGDREYRQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 94 -------TGFENLELYASMHDGVSEERIFEVVKRV-RLEHAI-------HQKVKTYSLGMKQRLGIAQAILHKPNLLILD 158
Cdd:PRK10636 95 eaqlhdaNERNDGHAIATIHGKLDAIDAWTIRSRAaSLLHGLgfsneqlERPVSDFSGGWRMRLNLAQALICRSDLLLLD 174
|
....*..
gi 515936072 159 EPTNGLD 165
Cdd:PRK10636 175 EPTNHLD 181
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
17-165 |
2.55e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 45.99 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 17 RHQILQHISMDIRQGEIVGLLGPNGSGKTTL----------------IRlIVGLMKKNNGRIIMNGY-SQDDDHLKAMSS 79
Cdd:PLN03140 892 RLQLLREVTGAFRPGVLTALMGVSGAGKTTLmdvlagrktggyiegdIR-ISGFPKKQETFARISGYcEQNDIHSPQVTV 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 80 VGAIIenpefYSyltGFENLELYASMHDGVS-EERIFEVVKRVRLEHAI--HQKVKTYSLGMKQRLGIAQAILHKPNLLI 156
Cdd:PLN03140 971 RESLI-----YS---AFLRLPKEVSKEEKMMfVDEVMELVELDNLKDAIvgLPGVTGLSTEQRKRLTIAVELVANPSIIF 1042
|
....*....
gi 515936072 157 LDEPTNGLD 165
Cdd:PLN03140 1043 MDEPTSGLD 1051
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
10-165 |
2.83e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.27 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 10 NVDKQIGRHQILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIIMN-----GY-SQD------------- 70
Cdd:PRK15064 6 NITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDpnerlGKlRQDqfafeeftvldtv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 71 ---DDHL-KAMSSVGAIIENPEFySYLTGFENLEL---YASMhDGVS-EERIFEVVKRVRLEHAIHQ-KVKTYSLGMKQR 141
Cdd:PRK15064 86 imgHTELwEVKQERDRIYALPEM-SEEDGMKVADLevkFAEM-DGYTaEARAGELLLGVGIPEEQHYgLMSEVAPGWKLR 163
|
170 180
....*....|....*....|....
gi 515936072 142 LGIAQAILHKPNLLILDEPTNGLD 165
Cdd:PRK15064 164 VLLAQALFSNPDILLLDEPTNNLD 187
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
20-212 |
3.41e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 45.61 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 20 ILQHISMDIRQGEIVGLLGPNGSGKTTLIRLIVGLMKKN---NGRIIMNGY--------------SQDDDHLKAMSsvga 82
Cdd:PLN03140 180 ILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYrlnefvprktsayiSQNDVHVGVMT---- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 83 IIENPEFYSYLTGFenlelyASMHDGVSE----ER---IF---EV---VKRVRLEHAIHQKVKTYSL------------- 136
Cdd:PLN03140 256 VKETLDFSARCQGV------GTRYDLLSElarrEKdagIFpeaEVdlfMKATAMEGVKSSLITDYTLkilgldickdtiv 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 137 ----------GMKQRLGIAQAILHKPNLLILDEPTNGLDPAGMKEFREHLQMLVQEEGVSVLFAthLLH---EVEELCDR 203
Cdd:PLN03140 330 gdemirgisgGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMS--LLQpapETFDLFDD 407
|
....*....
gi 515936072 204 MIIIQKGQI 212
Cdd:PLN03140 408 IILLSEGQI 416
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
6-192 |
6.06e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 43.80 E-value: 6.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 6 LHIENVDKqigrhqiLQHISMDIRQGEIvgLLGPNGSGKTTLIRLIVGLMKKN-----NGRI-IMNGYSQDDDHLkamSS 79
Cdd:COG4938 4 ISIKNFGP-------FKEAELELKPLTL--LIGPNGSGKSTLIQALLLLLQSNfiylpAERSgPARLYPSLVREL---SD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 80 VGAIIENpeFYSYLTGFENLEL----YASMHDGVSE--ERIFEVV-------KRVRLEHAIHQKVKTYSL-----GMKQR 141
Cdd:COG4938 72 LGSRGEY--TADFLAELENLEIlddkSKELLEQVEEwlEKIFPGKvevdassDLVRLVFRPSGNGKRIPLsnvgsGVSEL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515936072 142 LGIAQAILH---KPNLLILDEPTNGLDPAGMKEFREHLQMLVQeEGVSVLFATH 192
Cdd:COG4938 150 LPILLALLSaakPGSLLIIEEPEAHLHPKAQSALAELLAELAN-SGVQVIIETH 202
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
21-192 |
8.47e-05 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 43.84 E-value: 8.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 21 LQHISMDIRQGeIVGLLGPNGSGKTTLIRLIVGLMKKNNGRIImngySQDDDHLKAMSSVGAIIENPEFYSYLTGFENLE 100
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSRKF----DEEDFYLGDDPDLPEIEIELTFGSLLSRLLRLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 101 LYASMHDGVSE------ERIFEVVKRV--RLEHAIHQKVKTY---------------------------------SLGMK 139
Cdd:COG3593 89 LKEEDKEELEEaleelnEELKEALKALneLLSEYLKELLDGLdlelelsldeledllkslslriedgkelpldrlGSGFQ 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 140 QRLGIA--QAILH-----KPNLLILDEPTNGLDPAGMKEFREHLQMLVqEEGVSVLFATH 192
Cdd:COG3593 169 RLILLAllSALAElkrapANPILLIEEPEAHLHPQAQRRLLKLLKELS-EKPNQVIITTH 227
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
17-205 |
1.46e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 42.60 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 17 RHQILQHISMDIRQGEIVGLLGPNGSGKTTLIR--LIVGLMKKNNGRIIMNGYSQDDDHLKAMSSVGAIIE--------- 85
Cdd:cd03271 7 RENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINdtLYPALARRLHLKKEQPGNHDRIEGLEHIDKVIVIDQspigrtprs 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 86 NPEFYsylTGF-------------------ENLE-LY--ASMHD----GVSE-----------ERIFEVVKRVRLEH-AI 127
Cdd:cd03271 87 NPATY---TGVfdeirelfcevckgkrynrETLEvRYkgKSIADvldmTVEEaleffenipkiARKLQTLCDVGLGYiKL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 128 HQKVKTYSLGMKQRLGIAQAILHK---PNLLILDEPTNGLDPAGMKEFREHLQMLVqEEGVSVLFATHLLHeVEELCDRM 204
Cdd:cd03271 164 GQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLV-DKGNTVVVIEHNLD-VIKCADWI 241
|
.
gi 515936072 205 I 205
Cdd:cd03271 242 I 242
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
127-205 |
2.01e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 127 IHQKVKT---------------YSL--GMKQRLGIAQAILH---KPNLLILDEPTNGLDPAGMKEFREHLQMLVQeEGVS 186
Cdd:PRK00635 786 IHEKIHAlcslgldylplgrplSSLsgGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTH-QGHT 864
|
90
....*....|....*....
gi 515936072 187 VLFATHLLHEVeELCDRMI 205
Cdd:PRK00635 865 VVIIEHNMHVV-KVADYVL 882
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
109-209 |
1.48e-03 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 39.64 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 109 VSEERIFEVVKRVRLEHAIHQKV---KTYSLGMKQRLGIAQAI---LHKPNLLILDEPTNGLDPAGMKEFREHLQMLVQE 182
Cdd:COG1106 175 EEEEIEDLVERKLIFKHKGGNVPlplSEESDGTKRLLALAGALldaLAKGGVLLIDEIEASLHPSLLRKLLKLFLDLANK 254
|
90 100 110
....*....|....*....|....*....|..
gi 515936072 183 EGVSVLFATH---LLHEVEEL--CDRMIIIQK 209
Cdd:COG1106 255 NNAQLIFTTHsteLLDAFLELlrRDQIWFVEK 286
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
6-179 |
3.88e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 37.68 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 6 LHIENvdkqIGRHQILQHIsmDIRQGeIVGLLGPNGSGKTTLIRLI-------VGLMKKNNGRIIMNG---------YSQ 69
Cdd:COG0419 5 LRLEN----FRSYRDTETI--DFDDG-LNLIVGPNGAGKSTILEAIryalygkARSRSKLRSDLINVGseeasveleFEH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515936072 70 DDDHLKAMSSVGAIIE-----NPEFYSYLTGFENLELYASMHDGVS------EERIFEVVKRVRLEHAIHQK------VK 132
Cdd:COG0419 78 GGKRYRIERRQGEFAEfleakPSERKEALKRLLGLEIYEELKERLKeleealESALEELAELQKLKQEILAQlsgldpIE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515936072 133 TYSLGMKQRLGIAQAIlhkpnLLILDepTNGLDPAGMKEFREHLQML 179
Cdd:COG0419 158 TLSGGERLRLALADLL-----SLILD--FGSLDEERLERLLDALEEL 197
|
|
| |
