|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-214 |
4.89e-110 |
|
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: 317.62 E-value: 4.89e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 5 VQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTsYEVLGNIGSMIE 84
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKN-IEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 85 YPIFYENLTAEENLDLHCEYMGYhNKKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLD 164
Cdd:cd03268 80 APGFYPNLTARENLRLLARLLGI-RKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 255767068 165 PLGIKKIRQLFQVLsKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEE 214
Cdd:cd03268 159 PDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-231 |
2.13e-98 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 289.27 E-value: 2.13e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 5 VQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNIGSMIE 84
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 85 YPIFYENLTAEENLDLHCEYMG---YHNKKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVN 161
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGlprKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255767068 162 GLDPLGIKKIRQLFQVLSKEyGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDVRGQNTE--YIELV 231
Cdd:COG1131 161 GLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLLEdvFLELT 231
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
6-211 |
2.18e-79 |
|
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: 240.38 E-value: 2.18e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 6 QTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSyevLGNIGSMIEY 85
Cdd:TIGR03740 2 ETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKD---LHKIGSLIES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 86 PIFYENLTAEENLDLHCEYMGYhNKKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLDP 165
Cdd:TIGR03740 79 PPLYENLTARENLKVHTTLLGL-PDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLDP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 255767068 166 LGIKKIRQLFQVLSKEyGMTLLISSHLLGEIEQIADTIGVIRDGRL 211
Cdd:TIGR03740 158 IGIQELRELIRSFPEQ-GITVILSSHILSEVQQLADHIGIISEGVL 202
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-211 |
7.69e-73 |
|
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: 221.89 E-value: 7.69e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 5 VQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNIGSMIE 84
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 85 YPIFYENLTAEENLDLhceymgyhnkkaiqevldmvnlkqidkkpvktfSLGMKQRLGIARAILTKPDLLILDEPVNGLD 164
Cdd:cd03230 81 EPSLYENLTVRENLKL---------------------------------SGGMKQRLALAQALLHDPELLILDEPTSGLD 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 255767068 165 PLGIKKIRQLFQVLSKEyGMTLLISSHLLGEIEQIADTIGVIRDGRL 211
Cdd:cd03230 128 PESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-221 |
6.14e-66 |
|
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: 206.63 E-value: 6.14e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 6 QTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNIGSMIEY 85
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 86 PIFYENLTAEENLDLHCEYMG---YHNKKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVNG 162
Cdd:COG4555 83 RGLYDRLTVRENIRYFAELYGlfdEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 255767068 163 LDPLGIKKIRQLFQVLSKEyGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDVR 221
Cdd:COG4555 163 LDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELR 220
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
12-300 |
5.19e-64 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 203.78 E-value: 5.19e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 12 KTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNIGSMIEYPIFYEN 91
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 92 LTAEENLDLHCEYMGYHNKKA---IQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLDPLGI 168
Cdd:TIGR01188 81 LTGRENLEMMGRLYGLPKDEAeerAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 169 KKIRQLFQVLSKEyGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDVR---GQNTEYIELVTPNQTR------AC 239
Cdd:TIGR01188 161 RAIWDYIRALKEE-GVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKrrlGKDTLESRPRDIQSLKvevsmlIA 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255767068 240 FVLEKELQLTNFKILNEKtIRIYEAEASQAA--ISKALILNDVDIESMNKKYTSLEDYFIKLI 300
Cdd:TIGR01188 240 ELGETGLGLLAVTVDSDR-IKILVPDGDETVpeIVEAAIRNGIRIRSISTERPSLDDVFLKLT 301
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-221 |
7.01e-62 |
|
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: 195.67 E-value: 7.01e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 5 VQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNIGSMIE 84
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 85 YPIFYENLTAEENLDLHCEYMGYHNKKA---IQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVN 161
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERrerIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 162 GLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDVR 221
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-303 |
1.43e-56 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 184.54 E-value: 1.43e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 4 IVQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFThtsYEVLGNIGSMI 83
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD---PEDRRRIGYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 84 E----YPifyeNLTAEENLdlhcEYMG-YHN------KKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPD 152
Cdd:COG4152 78 EerglYP----KMKVGEQL----VYLArLKGlskaeaKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 153 LLILDEPVNGLDPLGIKKIRQLFQVLSKEyGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDVRGQN-TEYIELV 231
Cdd:COG4152 150 LLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFgRNTLRLE 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255767068 232 TPNQTRAcfvLEKELQLTNFKILNEK-TIRIYEAEASQAAISKAliLNDVDIESMNKKYTSLEDYFIKLINGN 303
Cdd:COG4152 229 ADGDAGW---LRALPGVTVVEEDGDGaELKLEDGADAQELLRAL--LARGPVREFEEVRPSLNEIFIEVVGEK 296
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-214 |
1.81e-53 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 173.92 E-value: 1.81e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 5 VQTNGLTKTYQGKEVVSNVSMHIKKGeIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNIGSMIE 84
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 85 YPIFYENLTAEENLDlhceYMGY-------HNKKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILD 157
Cdd:cd03264 80 EFGVYPNFTVREFLD----YIAWlkgipskEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 255767068 158 EPVNGLDPLGIKKIRQLFQVLSKEygMTLLISSHLLGEIEQIADTIGVIRDGRLLEE 214
Cdd:cd03264 156 EPTAGLDPEERIRFRNLLSELGED--RIVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-212 |
1.67e-52 |
|
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: 171.53 E-value: 1.67e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 5 VQTNGLTKTYQGKE--VVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNIGSM 82
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 83 IEYPIFYENLTAEENLDLHCEYMGYHNKKAIQEV---LDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEP 159
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVellLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 255767068 160 VNGLDPLGiKkiRQLFQVLSKEYGM-TLLISSHLLGEIEQIADTIGVIRDGRLL 212
Cdd:cd03263 161 TSGLDPAS-R--RAIWDLILEVRKGrSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-197 |
2.55e-50 |
|
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: 165.34 E-value: 2.55e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 5 VQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNIGSMIE 84
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 85 YPIFYENLTAEENLDLHCEYMGYH-NKKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVNGL 163
Cdd:COG4133 83 ADGLKPELTVRENLRFWAALYGLRaDREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTAL 162
|
170 180 190
....*....|....*....|....*....|....
gi 255767068 164 DPLGIKKIRQLFQVLSKEyGMTLLISSHLLGEIE 197
Cdd:COG4133 163 DAAGVALLAELIAAHLAR-GGAVLLTTHQPLELA 195
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-214 |
2.57e-50 |
|
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: 166.00 E-value: 2.57e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 4 IVQTNGLTKTYQGKE----VVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNI 79
Cdd:cd03266 1 MITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 80 GSMIEYPIFYENLTAEENL----DLHcEYMGYHNKKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLI 155
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLeyfaGLY-GLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 255767068 156 LDEPVNGLDPLGIKKIRQLFQVLsKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEE 214
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-220 |
2.41e-49 |
|
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: 171.24 E-value: 2.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 4 IVQTNGLTKTYQGKE-----VVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGN 78
Cdd:COG1123 260 LLEVRNLSKRYPVRGkggvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 79 IGSMIEYpIF-------------YENLtaEENLDLHCEYMGYHNKKAIQEVLDMVNL--KQIDKKPvKTFSLGMKQRLGI 143
Cdd:COG1123 340 LRRRVQM-VFqdpysslnprmtvGDII--AEPLRLHGLLSRAERRERVAELLERVGLppDLADRYP-HELSGGQRQRVAI 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255767068 144 ARAILTKPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDV 220
Cdd:COG1123 416 ARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEV 492
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-220 |
1.86e-48 |
|
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: 161.35 E-value: 1.86e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 5 VQTNGLTKTYQ-GKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTS-YEVLGNIGSM 82
Cdd:COG1122 1 IELENLSFSYPgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNlRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 83 IEYP---IFYENLTAE-----ENLDLHCEYMgyhnKKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLL 154
Cdd:COG1122 81 FQNPddqLFAPTVEEDvafgpENLGLPREEI----RERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255767068 155 ILDEPVNGLDPLGIKKIRQLFQVLSKEyGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDV 220
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-221 |
1.11e-46 |
|
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: 157.06 E-value: 1.11e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 1 MTYIVQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTS----YEVL 76
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekelYELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 77 GNIGSMieypiF-----YENLTAEEN----LDLHCEYmgyhNKKAIQE----VLDMVNLKQIDKKPVKTFSLGMKQRLGI 143
Cdd:COG1127 82 RRIGML-----FqggalFDSLTVFENvafpLREHTDL----SEAEIRElvleKLELVGLPGAADKMPSELSGGMRKRVAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255767068 144 ARAILTKPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDVR 221
Cdd:COG1127 153 ARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELL 230
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
8-213 |
1.39e-46 |
|
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: 156.14 E-value: 1.39e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 8 NGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEvLGNIGSMIEYPI 87
Cdd:cd03259 4 KGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE-RRNIGMVFQDYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 88 FYENLTAEENLDLHCEYMGYHNKKA---IQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLD 164
Cdd:cd03259 83 LFPHLTVAENIAFGLKLRGVPKAEIrarVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 255767068 165 PLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLE 213
Cdd:cd03259 163 AKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQ 211
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-221 |
2.52e-46 |
|
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: 156.12 E-value: 2.52e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 5 VQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTS----YEVLGNIG 80
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaelYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 81 SMIEYPIFYENLTAEENLDLHCEYMGYHNKKAIQEV----LDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLIL 156
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTRLSEEEIREIvlekLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255767068 157 DEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDVR 221
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELR 225
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
9-220 |
3.45e-46 |
|
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: 155.78 E-value: 3.45e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 9 GLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHtsYEV-----LGnIGSMI 83
Cdd:cd03218 5 NLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITK--LPMhkrarLG-IGYLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 84 EYPIFYENLTAEENLDLHCEYMGYHNK---KAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPV 160
Cdd:cd03218 82 QEASIFRKLTVEENILAVLEIRGLSKKereEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 161 NGLDPLGIKKIRQLFQVLsKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDV 220
Cdd:cd03218 162 AGVDPIAVQDIQKIIKIL-KDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEI 220
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-214 |
1.12e-45 |
|
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: 154.20 E-value: 1.12e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 4 IVQTNGLTKTYQGK----EVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNI 79
Cdd:cd03257 1 LLEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 80 GSMIEYpIFYENLTA-----------EENLDLHCEYMGY-HNKKAIQEVLDMVNL--KQIDKKPVKtFSLGMKQRLGIAR 145
Cdd:cd03257 81 RKEIQM-VFQDPMSSlnprmtigeqiAEPLRIHGKLSKKeARKEAVLLLLVGVGLpeEVLNRYPHE-LSGGQRQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255767068 146 AILTKPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEE 214
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEE 227
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-210 |
3.97e-45 |
|
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: 151.19 E-value: 3.97e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 5 VQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLG---NIGS 81
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPlrrRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 82 MIEYPIFYENLTAEENldlhceymgyhnkkaIQEVLdmvnlkqidkkpvktfSLGMKQRLGIARAILTKPDLLILDEPVN 161
Cdd:cd03229 81 VFQDFALFPHLTVLEN---------------IALGL----------------SGGQQQRVALARALAMDPDVLLLDEPTS 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 255767068 162 GLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGR 210
Cdd:cd03229 130 ALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-211 |
4.34e-45 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 152.26 E-value: 4.34e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 5 VQTNGLTKTYQG----KEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLG--- 77
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 78 --NIGSmieypIF--Y---ENLTAEENLDLHCEYMGYHNKKA---IQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAI 147
Cdd:cd03255 81 rrHIGF-----VFqsFnllPDLTALENVELPLLLAGVPKKERrerAEELLERVGLGDRLNHYPSELSGGQQQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255767068 148 LTKPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLgEIEQIADTIGVIRDGRL 211
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-203 |
4.71e-45 |
|
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: 152.30 E-value: 4.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 6 QTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKfthtsyevLGNIGSMIEY 85
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKP--------LEKERKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 86 -PIFYE-----NLTAEE----NLDLHCEYMGYHNKK---AIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPD 152
Cdd:cd03235 73 vPQRRSidrdfPISVRDvvlmGLYGHKGLFRRLSKAdkaKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 255767068 153 LLILDEPVNGLDPLGIKKIRQLFQVLsKEYGMTLLISSHLLGEIEQIADTI 203
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLREL-RREGMTILVVTHDLGLVLEYFDRV 202
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-210 |
5.02e-45 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 151.85 E-value: 5.02e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 6 QTNGLTKTYQGKE--VVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTS-YEVLGNIGSM 82
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSlKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 83 IEYP---IFyeNLTAEENLDLHCEYMGYHN---KKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLIL 156
Cdd:cd03225 81 FQNPddqFF--GPTVEEEVAFGLENLGLPEeeiEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 255767068 157 DEPVNGLDPLGIKKIRQLFQVLSKEyGMTLLISSHLLGEIEQIADTIGVIRDGR 210
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
14-212 |
2.57e-44 |
|
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: 150.95 E-value: 2.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 14 YQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNIGSMI-EYPIFYENL 92
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFgQKTQLWWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 93 TAEENLDLHCEYMG---YHNKKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLDPLGIK 169
Cdd:cd03267 111 PVIDSFYLLAAIYDlppARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQE 190
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 255767068 170 KIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLL 212
Cdd:cd03267 191 NIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-211 |
6.80e-44 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 150.24 E-value: 6.80e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 1 MTYIVQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHtsyeVLGNIG 80
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR----ARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 81 -----SMIE--YPIfyenlTAEE----NLDLHCEYMGYHNKK---AIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARA 146
Cdd:COG1121 79 yvpqrAEVDwdFPI-----TVRDvvlmGRYGRRGLFRRPSRAdreAVDEALERVGLEDLADRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255767068 147 ILTKPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEyGMTLLISSHLLGEIEQIADTIGVIRDGRL 211
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-210 |
3.45e-43 |
|
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: 147.04 E-value: 3.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 5 VQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFThtsYEVLGNIGSMIE 84
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD---IAARNRIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 85 YPIFYENLTAEENLDLHCEYMGYHNKKA---IQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVN 161
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAQLKGLKKEEArrrIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 255767068 162 GLDPLGIKKIRQLFQVLsKEYGMTLLISSHLLGEIEQIADTIGVIRDGR 210
Cdd:cd03269 158 GLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
8-221 |
6.85e-43 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 147.64 E-value: 6.85e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 8 NGLTKTY----QGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNIGSMI 83
Cdd:COG1124 5 RNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 84 ---EYPIFYENLTAEENLD--LHCEYMGYHNKKaIQEVLDMVNLKQ--IDKKPvKTFSLGMKQRLGIARAILTKPDLLIL 156
Cdd:COG1124 85 fqdPYASLHPRHTVDRILAepLRIHGLPDREER-IAELLEQVGLPPsfLDRYP-HQLSGGQRQRVAIARALILEPELLLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255767068 157 DEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDVR 221
Cdd:COG1124 163 DEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLL 227
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-216 |
2.59e-42 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 145.57 E-value: 2.59e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 1 MTYIVQTNGLTKTYQGKE----VVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVL 76
Cdd:COG1136 1 MSPLLELRNLTKSYGTGEgevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 77 G-----NIGsmieYpIF--Y---ENLTAEENLDLHCEYMGYHNKKA---IQEVLDMVNL-KQIDKKPVKTfSLGMKQRLG 142
Cdd:COG1136 81 ArlrrrHIG----F-VFqfFnllPELTALENVALPLLLAGVSRKERrerARELLERVGLgDRLDHRPSQL-SGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255767068 143 IARAILTKPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLgEIEQIADTIGVIRDGRLLEEVS 216
Cdd:COG1136 155 IARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRIVSDER 227
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-215 |
4.09e-42 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 144.81 E-value: 4.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 4 IVQTNGLTKTY-QGKEVVSNVSMHIKKGEIYgFL-GPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSY-EVLG--- 77
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFV-FLtGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRrEIPYlrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 78 NIGsmieyPIFYE-----NLTAEENLDLHCEYMGYHN---KKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILT 149
Cdd:COG2884 80 RIG-----VVFQDfrllpDRTVYENVALPLRVTGKSRkeiRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255767068 150 KPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEyGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEV 215
Cdd:COG2884 155 RPELLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-220 |
5.53e-42 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 151.33 E-value: 5.53e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 1 MTYIVQTNGLTKTYQGkeVVSN--VSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEV--- 75
Cdd:COG3845 2 MPPALELRGITKRFGG--VVANddVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaia 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 76 LGnIGsMI-EYPIFYENLTAEENLDLHCE--YMGYHNKKA----IQEVLDMVNLKqID-KKPVKTFSLGMKQRLGIARAI 147
Cdd:COG3845 80 LG-IG-MVhQHFMLVPNLTVAENIVLGLEptKGGRLDRKAararIRELSERYGLD-VDpDAKVEDLSVGEQQRVEILKAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255767068 148 LTKPDLLILDEPVNGLDPlgiKKIRQLFQVLS--KEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDV 220
Cdd:COG3845 157 YRGARILILDEPTAVLTP---QEADELFEILRrlAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAET 228
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-220 |
5.98e-42 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 150.94 E-value: 5.98e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 1 MTYIVQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSY---EVLG 77
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPrdaQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 78 nIgSMI--EYPIFyENLTAEENLDLHCEYM--GYHNKKAI----QEVLDMVNLKqID-KKPVKTFSLGMKQRLGIARAIL 148
Cdd:COG1129 81 -I-AIIhqELNLV-PNLSVAENIFLGREPRrgGLIDWRAMrrraRELLARLGLD-IDpDTPVGDLSVAQQQLVEIARALS 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255767068 149 TKPDLLILDEPVNGLDPlgiKKIRQLFQVLS--KEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDV 220
Cdd:COG1129 157 RDARVLILDEPTASLTE---REVERLFRIIRrlKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
4-220 |
7.85e-42 |
|
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: 144.72 E-value: 7.85e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 4 IVQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEV---LGnIG 80
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHErarLG-IG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 81 SMIEYPIFYENLTAEENLDLHCEYMGYHNKKAIQE----VLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLIL 156
Cdd:TIGR04406 80 YLPQEASIFRKLTVEENIMAVLEIRKDLDRAEREErleaLLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255767068 157 DEPVNGLDPLGIKKIRQLFQVLsKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDV 220
Cdd:TIGR04406 160 DEPFAGVDPIAVGDIKKIIKHL-KERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEI 222
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-221 |
2.66e-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: 143.64 E-value: 2.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 1 MTYIVQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTS-YEV--LG 77
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPpHRIarLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 78 ------NIGsmieypIFyENLTAEENLdlhceYMGYHNK-----------------------KAIQEVLDMVNLKQIDKK 128
Cdd:COG0411 81 iartfqNPR------LF-PELTVLENV-----LVAAHARlgrgllaallrlprarreerearERAEELLERVGLADRADE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 129 PVKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRD 208
Cdd:COG0411 149 PAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDF 228
|
250
....*....|...
gi 255767068 209 GRLLEEVSMEDVR 221
Cdd:COG0411 229 GRVIAEGTPAEVR 241
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
6-221 |
9.47e-41 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 141.71 E-value: 9.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 6 QTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTS-YE--VLGnIGsm 82
Cdd:COG1137 5 EAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPmHKraRLG-IG-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 83 ieY-P----IFyENLTAEENLDLHCEYMGYhNKKAIQE----VLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDL 153
Cdd:COG1137 82 --YlPqeasIF-RKLTVEDNILAVLELRKL-SKKEREErleeLLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKF 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255767068 154 LILDEPVNGLDPLGIKKIRQLFQVLsKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEE------VSMEDVR 221
Cdd:COG1137 158 ILLDEPFAGVDPIAVADIQKIIRHL-KERGIGVLITDHNVRETLGICDRAYIISEGKVLAEgtpeeiLNNPLVR 230
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-220 |
1.77e-40 |
|
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: 147.36 E-value: 1.77e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 1 MTYIVQTNGLTKTYQG--KEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPT---SGEIIILGNKFTHTSYEV 75
Cdd:COG1123 1 MTPLLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 76 LGNIGSMI---------EYPIFYENLTAEENLDLHCEYMgyhnKKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARA 146
Cdd:COG1123 81 RGRRIGMVfqdpmtqlnPVTVGDQIAEALENLGLSRAEA----RARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255767068 147 ILTKPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDV 220
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
9-214 |
5.45e-40 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 142.66 E-value: 5.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 9 GLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNIGSMIEYPIF 88
Cdd:PRK13536 46 GVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVVPQFDNL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 89 YENLTAEENLDLHCEYMGYHNKK---AIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLDP 165
Cdd:PRK13536 126 DLEFTVRENLLVFGRYFGMSTREieaVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDP 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 255767068 166 ----LGIKKIRQLfqvLSKeyGMTLLISSHLLGEIEQIADTIGVIRDGRLLEE 214
Cdd:PRK13536 206 harhLIWERLRSL---LAR--GKTILLTTHFMEEAERLCDRLCVLEAGRKIAE 253
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-221 |
1.31e-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: 138.72 E-value: 1.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 6 QTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTS-YEV--LGnIGSM 82
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPpHEIarLG-IGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 83 IEYPIFYENLTAEENLDL--------------HCEYMGYHNKKAiQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAIL 148
Cdd:cd03219 81 FQIPRLFPELTVLENVMVaaqartgsglllarARREEREARERA-EELLERVGLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255767068 149 TKPDLLILDEPVNGLDPLGIKKIRQLFQVLsKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDVR 221
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVR 231
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-161 |
5.17e-39 |
|
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: 134.31 E-value: 5.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 20 VSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVL-GNIGSMIEYPIFYENLTAEENL 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLrKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 99 D--LHCEYMGYHNKKA-IQEVLDMVNLKQIDKKPV----KTFSLGMKQRLGIARAILTKPDLLILDEPVN 161
Cdd:pfam00005 81 RlgLLLKGLSKREKDArAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-221 |
6.02e-39 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 139.45 E-value: 6.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 4 IVQTNGLTKTYQ------G---------------KEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEII 62
Cdd:COG4586 1 IIEVENLSKTYRvyekepGlkgalkglfrreyreVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 63 ILGnkftHTSY----EVLGNIGSmieypIF------YENLTAEENLDLH--------CEYmgyhnKKAIQEVLDMVNLKQ 124
Cdd:COG4586 81 VLG----YVPFkrrkEFARRIGV-----VFgqrsqlWWDLPAIDSFRLLkaiyripdAEY-----KKRLDELVELLDLGE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 125 IDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIG 204
Cdd:COG4586 147 LLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVI 226
|
250
....*....|....*..
gi 255767068 205 VIRDGRLLEEVSMEDVR 221
Cdd:COG4586 227 VIDHGRIIYDGSLEELK 243
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-210 |
1.29e-38 |
|
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: 133.52 E-value: 1.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 8 NGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNigsmieyPI 87
Cdd:cd00267 3 ENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRR-------RI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 88 FYenltaeenldlhceymgyhnkkaiqevldmvnlkqidkkpVKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLDPLG 167
Cdd:cd00267 76 GY----------------------------------------VPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPAS 115
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 255767068 168 IKKIRQLFQVLSKEyGMTLLISSHLLGEIEQIADTIGVIRDGR 210
Cdd:cd00267 116 RERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-214 |
1.71e-38 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 138.01 E-value: 1.71e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 1 MTYIVQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNIG 80
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 81 SMIEYPIFYENLTAEENLDLHCEYMGYHN---KKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILD 157
Cdd:PRK13537 84 VVPQFDNLDPDFTVRENLLVFGRYFGLSAaaaRALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255767068 158 EPVNGLDP----LGIKKIRQLfqvLSKeyGMTLLISSHLLGEIEQIADTIGVIRDGRLLEE 214
Cdd:PRK13537 164 EPTTGLDPqarhLMWERLRSL---LAR--GKTILLTTHFMEEAERLCDRLCVIEEGRKIAE 219
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-220 |
1.97e-38 |
|
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: 135.40 E-value: 1.97e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 4 IVQTNGLTKTYQGK----EVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNI 79
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 80 GSMIEYpIF-----YENLTAEENLDLHCEYMGY---HNKKAIQEVLDMVNLKQ-IDKKPvKTFSLGMKQRLGIARAILTK 150
Cdd:cd03258 81 RRRIGM-IFqhfnlLSSRTVFENVALPLEIAGVpkaEIEERVLELLELVGLEDkADAYP-AQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 151 PDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDV 220
Cdd:cd03258 159 PKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
8-221 |
2.41e-38 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 135.95 E-value: 2.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 8 NGLTKTYQ-GKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVL----GNIGsM 82
Cdd:COG3638 6 RNLSKRYPgGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALrrlrRRIG-M 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 83 I--EYPIFyENLTAEENLdLHcEYMGYHN-------------KKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAI 147
Cdd:COG3638 85 IfqQFNLV-PRLSVLTNV-LA-GRLGRTStwrsllglfppedRERALEALERVGLADKAYQRADQLSGGQQQRVAIARAL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255767068 148 LTKPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLL-----EEVSMEDVR 221
Cdd:COG3638 162 VQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVfdgppAELTDAVLR 240
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-220 |
3.06e-38 |
|
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: 135.60 E-value: 3.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 4 IVQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSG-EIIILGNKFTHTS-YEVLGNIG- 80
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDvWELRKRIGl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 81 ---SMIEYpiFYENLTAEE--------NLDLHCEYmGYHNKKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILT 149
Cdd:COG1119 83 vspALQLR--FPRDETVLDvvlsgffdSIGLYREP-TDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255767068 150 KPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHllgEIEQIADTIG---VIRDGRLLEEVSMEDV 220
Cdd:COG1119 160 DPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTH---HVEEIPPGIThvlLLKDGRVVAAGPKEEV 230
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-211 |
2.55e-37 |
|
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: 130.63 E-value: 2.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 5 VQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYevlgnigsmie 84
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASP----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 85 ypifyenltaeenldlhceymgyhnKKAIQEVLDMVNlkQIdkkpvktfSLGMKQRLGIARAILTKPDLLILDEPVNGLD 164
Cdd:cd03216 70 -------------------------RDARRAGIAMVY--QL--------SVGERQMVEIARALARNARLLILDEPTAALT 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 255767068 165 PlgiKKIRQLFQVLS--KEYGMTLLISSHLLGEIEQIADTIGVIRDGRL 211
Cdd:cd03216 115 P---AEVERLFKVIRrlRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-220 |
3.48e-37 |
|
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: 132.86 E-value: 3.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 4 IVQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSY-EVLGNIGSM 82
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRrELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 83 IEYPIFYENLTAEENLDL----HCEYMGYHNKK---AIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLI 155
Cdd:COG1120 81 PQEPPAPFGLTVRELVALgrypHLGLFGRPSAEdreAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255767068 156 LDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDV 220
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-212 |
4.97e-37 |
|
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: 130.25 E-value: 4.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 6 QTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNIgsmiey 85
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARK------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 86 pifyenltaeenldlhceyMGYhnkkaIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLDP 165
Cdd:cd03214 75 -------------------IAY-----VPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDI 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 255767068 166 LGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLL 212
Cdd:cd03214 131 AHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-221 |
1.10e-36 |
|
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: 130.63 E-value: 1.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 6 QTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNIGsmIEY 85
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAG--IGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 86 -P----IFyENLTAEENLDLHCEYMGYHNKKA-IQEVLDMV-NLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDE 158
Cdd:cd03224 80 vPegrrIF-PELTVEENLLLGAYARRRAKRKArLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255767068 159 PVNGLDPLGIKKIRQLFQVLSKEyGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDVR 221
Cdd:cd03224 159 PSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
8-210 |
2.12e-36 |
|
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: 130.38 E-value: 2.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 8 NGLTKTY-QGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVL----GNIGsM 82
Cdd:cd03256 4 ENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlrRQIG-M 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 83 I--EYPIFyENLTAEENLdLHCEyMGYHN----------KKAIQ---EVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAI 147
Cdd:cd03256 83 IfqQFNLI-ERLSVLENV-LSGR-LGRRStwrslfglfpKEEKQralAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255767068 148 LTKPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGR 210
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-197 |
4.30e-36 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 137.56 E-value: 4.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 20 VSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNIGSMIEYPIFYENLTAEENLD 99
Cdd:NF033858 282 VDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVGYMSQAFSLYGELTVRQNLE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 100 LHCEYmgYHNKKA-----IQEVLDMVNLKQ-IDKKPvKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLDPLGikkiR- 172
Cdd:NF033858 362 LHARL--FHLPAAeiaarVAEMLERFDLADvADALP-DSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVA----Rd 434
|
170 180
....*....|....*....|....*...
gi 255767068 173 ---QLFQVLSKEYGMTLLISSHLLGEIE 197
Cdd:NF033858 435 mfwRLLIELSREDGVTIFISTHFMNEAE 462
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
4-215 |
7.42e-36 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 129.44 E-value: 7.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 4 IVQTNGLTKTYQGK----EVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVlgni 79
Cdd:COG1116 7 ALELRGVSKRFPTGgggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDR---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 80 gSMIeypiFYEN-----LTAEENLDLHCEYMGYHNKKA---IQEVLDMVNLKQ-IDKKPvKTFSLGMKQRLGIARAILTK 150
Cdd:COG1116 83 -GVV----FQEPallpwLTVLDNVALGLELRGVPKAERrerARELLELVGLAGfEDAYP-HQLSGGMRQRVAIARALAND 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255767068 151 PDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVI--RDGRLLEEV 215
Cdd:COG1116 157 PEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLsaRPGRIVEEI 223
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-215 |
7.54e-36 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 128.36 E-value: 7.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 5 VQTNGLTKTYQGK----EVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGnkfthtsyEVLGNIG 80
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG--------EPVTGPG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 81 SMIEYpIFYEN-----LTAEENLDLHCEYMGYHNKKAIQEV---LDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPD 152
Cdd:cd03293 73 PDRGY-VFQQDallpwLTVLDNVALGLELQGVPKAEARERAeelLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255767068 153 LLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVI--RDGRLLEEV 215
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAEV 216
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-220 |
1.15e-35 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 130.97 E-value: 1.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 4 IVQTNGLTKTYQGK----EVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVL--- 76
Cdd:COG1135 1 MIELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELraa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 77 -GNIGsMieypIFYE-NL----TAEENLDLHCEYMGYhNKKAIQ----EVLDMVNLKqiDKKPVKTFSL--GMKQRLGIA 144
Cdd:COG1135 81 rRKIG-M----IFQHfNLlssrTVAENVALPLEIAGV-PKAEIRkrvaELLELVGLS--DKADAYPSQLsgGQKQRVGIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255767068 145 RAILTKPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDV 220
Cdd:COG1135 153 RALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDV 228
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-212 |
2.54e-35 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 130.60 E-value: 2.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 1 MTYIVQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTS-YEVlgNI 79
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPpEKR--NV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 80 GsMI--EYPIFyENLTAEENLdlhcEY---MGYHNKKAI----QEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTK 150
Cdd:COG3842 80 G-MVfqDYALF-PHLTVAENV----AFglrMRGVPKAEIrarvAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255767068 151 PDLLILDEPVNGLDplgiKKIRQ-----LFQVLsKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLL 212
Cdd:COG3842 154 PRVLLLDEPLSALD----AKLREemreeLRRLQ-RELGITFIYVTHDQEEALALADRIAVMNDGRIE 215
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-220 |
3.10e-35 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 127.51 E-value: 3.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 1 MTYIVQTNGLTKTY----------------------QGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTS 58
Cdd:COG1134 1 MSSMIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 59 GEIiilgnkfthtsyEVLGNIGSMIEY-PIFYENLTAEENLDLHCEYMGYhNKKAIQEVLDMV----NLKQ-IDkKPVKT 132
Cdd:COG1134 81 GRV------------EVNGRVSALLELgAGFHPELTGRENIYLNGRLLGL-SRKEIDEKFDEIvefaELGDfID-QPVKT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 133 FSLGMKQRLGIARAILTKPDLLILDEpvnGL---DPLGIKKIRQLFQVLSKEyGMTLLISSHLLGEIEQIADTIGVIRDG 209
Cdd:COG1134 147 YSSGMRARLAFAVATAVDPDILLVDE---VLavgDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKG 222
|
250
....*....|.
gi 255767068 210 RLLEEVSMEDV 220
Cdd:COG1134 223 RLVMDGDPEEV 233
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
9-211 |
4.48e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 126.08 E-value: 4.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 9 GLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGnigSMIEY--- 85
Cdd:COG4619 5 GLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWR---RQVAYvpq 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 86 -PIFYENlTAEENLDLHCEYMGYH-NKKAIQEVLDMVNLKQID-KKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVNG 162
Cdd:COG4619 82 ePALWGG-TVRDNLPFPFQLRERKfDRERALELLERLGLPPDIlDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 255767068 163 LDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRL 211
Cdd:COG4619 161 LDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-213 |
2.31e-34 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 124.60 E-value: 2.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 5 VQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVK-----PTSGEIIILGNKFTHTSYEVLG-- 77
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDVLElr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 78 -NIGSMIEYP-IFyeNLTAEENLDLHCEYMGYHNKKAI----QEVLDMVNLKQIDKKPVKTFSL--GMKQRLGIARAILT 149
Cdd:cd03260 81 rRVGMVFQKPnPF--PGSIYDNVAYGLRLHGIKLKEELdervEEALRKAALWDEVKDRLHALGLsgGQQQRLCLARALAN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255767068 150 KPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYgmTLLISSHLLGEIEQIADTIGVIRDGRLLE 213
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVE 220
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
10-229 |
3.25e-34 |
|
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: 124.72 E-value: 3.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 10 LTKTYQG-KEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVL-GNIGSMIEYPI 87
Cdd:cd03295 6 VTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELrRKIGYVIQQIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 88 FYENLTAEENLDLHCEYMGYHNKKAIQ---EVLDMVNLkqidkkPVKTF--------SLGMKQRLGIARAILTKPDLLIL 156
Cdd:cd03295 86 LFPHMTVEENIALVPKLLKWPKEKIREradELLALVGL------DPAEFadryphelSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255767068 157 DEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDV-RGQNTEYIE 229
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEIlRSPANDFVA 233
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-220 |
5.09e-34 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 126.32 E-value: 5.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 4 IVQTNGLTKTYQGKE----VVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKP---TSGEIIILGNKFTHTSYEVL 76
Cdd:COG0444 1 LLEVRNLKVYFPTRRgvvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 77 GNI-GSMIEYpIFYENLTA-----------EENLDLHceymGYHNKKA----IQEVLDMVNL----KQIDKKPVkTFSLG 136
Cdd:COG0444 81 RKIrGREIQM-IFQDPMTSlnpvmtvgdqiAEPLRIH----GGLSKAEarerAIELLERVGLpdpeRRLDRYPH-ELSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 137 MKQRLGIARAILTKPDLLILDEPVNGLDPLgI-KKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEV 215
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDVT-IqAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEG 233
|
....*
gi 255767068 216 SMEDV 220
Cdd:COG0444 234 PVEEL 238
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
9-213 |
1.96e-33 |
|
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: 122.35 E-value: 1.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 9 GLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHT-SYEvlGNIGSMIE-YP 86
Cdd:cd03300 5 NVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLpPHK--RPVNTVFQnYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 87 IFyENLTAEENLDLHCEyMGYHNKKAIQ----EVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVNG 162
Cdd:cd03300 83 LF-PHLTVFENIAFGLR-LKKLPKAEIKervaEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 255767068 163 LDplgiKKIRQLFQV----LSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLE 213
Cdd:cd03300 161 LD----LKLRKDMQLelkrLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQ 211
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-211 |
4.37e-33 |
|
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: 122.02 E-value: 4.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 4 IVQTNGLTKTY-QGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNIGSM 82
Cdd:TIGR02315 1 MLEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 83 IEYpIFYE-----NLTAEENLdLHcEYMGYHN-------------KKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIA 144
Cdd:TIGR02315 81 IGM-IFQHynlieRLTVLENV-LH-GRLGYKPtwrsllgrfseedKERALSALERVGLADKAYQRADQLSGGQQQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255767068 145 RAILTKPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRL 211
Cdd:TIGR02315 158 RALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEI 224
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-220 |
9.07e-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: 121.79 E-value: 9.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 5 VQTNGLTKTYQG-----KEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNI 79
Cdd:TIGR04521 1 IKLKNVSYIYQPgtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 80 GSMI-------EYPIFYEnlTAEE-------NLDLHCEymgyHNKKAIQEVLDMVNL--KQIDKKPvktFSL--GMKQRL 141
Cdd:TIGR04521 81 RKKVglvfqfpEHQLFEE--TVYKdiafgpkNLGLSEE----EAEERVKEALELVGLdeEYLERSP---FELsgGQMRRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255767068 142 GIARAILTKPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDV 220
Cdd:TIGR04521 152 AIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREV 230
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
5-212 |
9.10e-33 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 123.64 E-value: 9.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 5 VQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHT------------S 72
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLppkdrniamvfqS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 73 YeVLgnigsmieYPifyeNLTAEENLDLHCEYMGY---HNKKAIQEVLDMVNLKQI-DKKPvKTFSLGMKQRLGIARAIL 148
Cdd:COG3839 84 Y-AL--------YP----HMTVYENIAFPLKLRKVpkaEIDRRVREAAELLGLEDLlDRKP-KQLSGGQRQRVALGRALV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255767068 149 TKPDLLILDEPVNGLDPlgikKIR-----QLFQvLSKEYGMTLLISSHllgeiEQI-----ADTIGVIRDGRLL 212
Cdd:COG3839 150 REPKVFLLDEPLSNLDA----KLRvemraEIKR-LHRRLGTTTIYVTH-----DQVeamtlADRIAVMNDGRIQ 213
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
12-214 |
2.39e-32 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 119.56 E-value: 2.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 12 KTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIiilgnkfthtsyEVLGNIGSMIEYPI-FYE 90
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV------------TVRGRVSSLLGLGGgFNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 91 NLTAEENLDLHCEYMGYHNK---KAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLDPLG 167
Cdd:cd03220 98 ELTGRENIYLNGRLLGLSRKeidEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAF 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 255767068 168 IKKIRQLFQVLSKEyGMTLLISSHLLGEIEQIADTIGVIRDGRLLEE 214
Cdd:cd03220 178 QEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
15-231 |
3.36e-32 |
|
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: 126.10 E-value: 3.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 15 QGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVL-GNIG-SMIEYPIFYENL 92
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLrRQIGvVLQDVFLFSGTI 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 93 taEENLDLHCEYMgyhNKKAIQEVLDMVNLKQ-IDKKP----------VKTFSLGMKQRLGIARAILTKPDLLILDEPVN 161
Cdd:COG2274 566 --RENITLGDPDA---TDEEIIEAARLAGLHDfIEALPmgydtvvgegGSNLSGGQRQRLAIARALLRNPRILILDEATS 640
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255767068 162 GLDPLG----IKKIRQLFQvlskeyGMTLLISSHLLgEIEQIADTIGVIRDGRLLEEVSMEDVRGQNTEYIELV 231
Cdd:COG2274 641 ALDAETeaiiLENLRRLLK------GRTVIIIAHRL-STIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELV 707
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-230 |
3.58e-32 |
|
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: 120.23 E-value: 3.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 5 VQTNGLTKTYQGKE--VVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFT--HTSYEVLGNIG 80
Cdd:TIGR04520 1 IEVENVSFSYPESEkpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLdeENLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 81 SMIEYPifyEN----LTAE-------ENLDLHCEYMgyhnKKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILT 149
Cdd:TIGR04520 81 MVFQNP---DNqfvgATVEddvafglENLGVPREEM----RKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 150 KPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQiADTIGVIRDGRLLEEVSMEDVRGQNTEYIE 229
Cdd:TIGR04520 154 RPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFSQVELLKE 232
|
.
gi 255767068 230 L 230
Cdd:TIGR04520 233 I 233
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
6-220 |
9.97e-32 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 118.01 E-value: 9.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 6 QTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNIGsmIEY 85
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAG--IAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 86 -P----IFyENLTAEENLDLHCEYMGYHNKKAIQEVLDM--VnLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDE 158
Cdd:TIGR03410 80 vPqgreIF-PRLTVEENLLTGLAALPRRSRKIPDEIYELfpV-LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255767068 159 PVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDV 220
Cdd:TIGR03410 158 PTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-229 |
1.53e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 117.91 E-value: 1.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 1 MTYIVQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTS-YEV--LG 77
Cdd:COG4674 7 HGPILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDeHEIarLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 78 nIGSMIEYPIFYENLTAEENLDLHC-----------EYMGYHNKKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARA 146
Cdd:COG4674 87 -IGRKFQKPTVFEELTVFENLELALkgdrgvfaslfARLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGML 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 147 ILTKPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYgmTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDVRgQNTE 226
Cdd:COG4674 166 LAQDPKLLLLDEPVAGMTDAETERTAELLKSLAGKH--SVVVVEHDMEFVRQIARKVTVLHQGSVLAEGSLDEVQ-ADPR 242
|
...
gi 255767068 227 YIE 229
Cdd:COG4674 243 VIE 245
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
20-213 |
3.16e-31 |
|
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: 117.74 E-value: 3.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 20 VSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNIG----SMI--EYPIFyENLT 93
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRrkkiSMVfqSFALL-PHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 94 AEENLDLHCEYMGYHNKKAIQ---EVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLDPLGIKK 170
Cdd:cd03294 119 VLENVAFGLEVQGVPRAEREEraaEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRRE 198
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 255767068 171 IRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLE 213
Cdd:cd03294 199 MQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQ 241
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-220 |
9.56e-31 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 117.98 E-value: 9.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 5 VQTNGLTKTYQGK----EVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLG--- 77
Cdd:PRK11153 2 IELKNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 78 -NIGsMIeypiF-YENL----TAEENLDLHCEYMGYhNKKAIQ----EVLDMVNLK-QIDKKPvKTFSLGMKQRLGIARA 146
Cdd:PRK11153 82 rQIG-MI----FqHFNLlssrTVFDNVALPLELAGT-PKAEIKarvtELLELVGLSdKADRYP-AQLSGGQKQRVAIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255767068 147 ILTKPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDV 220
Cdd:PRK11153 155 LASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEV 228
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-221 |
1.11e-30 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 115.86 E-value: 1.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 1 MTYIVQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFT-HTSYEV--LG 77
Cdd:PRK11300 2 SQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEgLPGHQIarMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 78 NIGSMIEYPIFYEnLTAEENL----DLHCEYMGYHN-------KKAIQEV-------LDMVNLKQIDKKPVKTFSLGMKQ 139
Cdd:PRK11300 82 VVRTFQHVRLFRE-MTVIENLlvaqHQQLKTGLFSGllktpafRRAESEAldraatwLERVGLLEHANRQAGNLAYGQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 140 RLGIARAILTKPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMED 219
Cdd:PRK11300 161 RLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEE 240
|
..
gi 255767068 220 VR 221
Cdd:PRK11300 241 IR 242
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-211 |
1.13e-30 |
|
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: 114.55 E-value: 1.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 5 VQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVL---GNIGs 81
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINelrQKVG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 82 MI--EYPIFyENLTAEENLDLHCEYMGYHNKKAIQE----VLDMVNLK-QIDKKPvKTFSLGMKQRLGIARAILTKPDLL 154
Cdd:cd03262 80 MVfqQFNLF-PHLTVLENITLAPIKVKGMSKAEAEEraleLLEKVGLAdKADAYP-AQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 255767068 155 ILDEPVNGLDPLGIKKIRQLFQVLSKEyGMTLLISSHLLGEIEQIADTIGVIRDGRL 211
Cdd:cd03262 158 LFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
16-191 |
1.36e-30 |
|
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: 113.67 E-value: 1.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 16 GKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTS---YEVLGNIGSMIEYP---IFY 89
Cdd:TIGR01166 4 GPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRkglLERRQRVGLVFQDPddqLFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 90 ENLTAE-----ENLDLHCEYMgyhnKKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLD 164
Cdd:TIGR01166 84 ADVDQDvafgpLNLGLSEAEV----ERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLD 159
|
170 180
....*....|....*....|....*..
gi 255767068 165 PLGIKKIRQLFQVLSKEyGMTLLISSH 191
Cdd:TIGR01166 160 PAGREQMLAILRRLRAE-GMTVVISTH 185
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-211 |
1.96e-30 |
|
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: 113.89 E-value: 1.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 5 VQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTS-YEvlGNIGSMI 83
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPpKD--RDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 84 EYPIFYENLTAEENLDLHCEYMGYHNKKAIQEVLDMVNLKQI----DKKPvKTFSLGMKQRLGIARAILTKPDLLILDEP 159
Cdd:cd03301 79 QNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIehllDRKP-KQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 255767068 160 VNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRL 211
Cdd:cd03301 158 LSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-220 |
2.14e-30 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 116.75 E-value: 2.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 4 IVQTNGLTKTYQ------GKEV-----VSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTS 72
Cdd:COG4608 7 LLEVRDLKKHFPvrgglfGRTVgvvkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 73 ------------------YEVLgN----IGSMIEYPifyenltaeenLDLHceymGYHNKKA----IQEVLDMVNLK--Q 124
Cdd:COG4608 87 grelrplrrrmqmvfqdpYASL-NprmtVGDIIAEP-----------LRIH----GLASKAErrerVAELLELVGLRpeH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 125 IDKKPvKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLDplgiKKIR-Q---LFQVLSKEYGMTLLISSHLLGEIEQIA 200
Cdd:COG4608 151 ADRYP-HEFSGGQRQRIGIARALALNPKLIVCDEPVSALD----VSIQaQvlnLLEDLQDELGLTYLFISHDLSVVRHIS 225
|
250 260
....*....|....*....|
gi 255767068 201 DTIGVIRDGRLLEEVSMEDV 220
Cdd:COG4608 226 DRVAVMYLGKIVEIAPRDEL 245
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
29-212 |
3.31e-30 |
|
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: 113.54 E-value: 3.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 29 KGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILG------NKFTHTSYEVLGnIGSMI-EYPIFyENLTAEENLDlh 101
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsRKKINLPPQQRK-IGLVFqQYALF-PHLNVRENLA-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 102 CEYMGYHNKK---AIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLDPLGIKKIRQLFQVL 178
Cdd:cd03297 98 FGLKRKRNREdriSVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQI 177
|
170 180 190
....*....|....*....|....*....|....
gi 255767068 179 SKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLL 212
Cdd:cd03297 178 KKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
8-210 |
3.32e-30 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 112.09 E-value: 3.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 8 NGLTKTYQG--KEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVL-GNIGSMIE 84
Cdd:cd03228 4 KNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLrKNIAYVPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 85 YPIFYeNLTAEENLdlhceymgyhnkkaiqevldmvnlkqidkkpvktFSLGMKQRLGIARAILTKPDLLILDEPVNGLD 164
Cdd:cd03228 84 DPFLF-SGTIRENI----------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 255767068 165 PLGIKKIRQLFQVLSKeyGMTLLISSHLLGEIEQiADTIGVIRDGR 210
Cdd:cd03228 129 PETEALILEALRALAK--GKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-220 |
4.08e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 114.79 E-value: 4.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 4 IVQTNGLTKTY-QGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTS---YEVLGNI 79
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKkslLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 80 GSMIEYP---IFYEnlTAEE-------NLDLHCEYMgyhnKKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILT 149
Cdd:PRK13639 81 GIVFQNPddqLFAP--TVEEdvafgplNLGLSKEEV----EKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255767068 150 KPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEyGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDV 220
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
8-221 |
5.78e-30 |
|
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: 113.54 E-value: 5.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 8 NGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTS-YEV--LGnIGsmie 84
Cdd:COG0410 7 ENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPpHRIarLG-IG---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 85 Y-P----IFyENLTAEENLDLHCeyMGYHNKKAIQEVLDMV-----NLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLL 154
Cdd:COG0410 82 YvPegrrIF-PSLTVEENLLLGA--YARRDRAEVRADLERVyelfpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255767068 155 ILDEPVNGLDPLGIKKIRQLFQVLSKEyGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDVR 221
Cdd:COG0410 159 LLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELL 224
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
19-220 |
9.88e-30 |
|
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: 112.81 E-value: 9.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 19 VVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEvLGNIGSMIEYPIFYENLTAEENL 98
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE-KRDISYVPQNYALFPHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 99 DL---HCEYMGYHNKKAIQEVLDMVNLKQI-DKKPvKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLDPLGIKKIRQL 174
Cdd:cd03299 93 AYglkKRKVDKKEIERKVLEIAEMLGIDHLlNRKP-ETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 255767068 175 FQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDV 220
Cdd:cd03299 172 LKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEV 217
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
3-220 |
1.59e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 113.36 E-value: 1.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 3 YIVQTNGLTKTYQG-KEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTS-YEVLGNIG 80
Cdd:PRK13652 2 HLIETRDLCYSYSGsKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENiREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 81 SMIEYP---IFyeNLTAEENLDLHCEYMGYHN---KKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLL 154
Cdd:PRK13652 82 LVFQNPddqIF--SPTVEQDIAFGPINLGLDEetvAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255767068 155 ILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDV 220
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
8-219 |
3.63e-29 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 111.39 E-value: 3.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 8 NGLTKTYQGKEVvsNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTS-YE--VlgnigSMie 84
Cdd:COG3840 5 DDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPpAErpV-----SM-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 85 ypIFYEN-----LTAEENLDLhceymGYH--------NKKAIQEVLDMVNLKQI-DKKPvKTFSLGMKQRLGIARAILTK 150
Cdd:COG3840 76 --LFQENnlfphLTVAQNIGL-----GLRpglkltaeQRAQVEQALERVGLAGLlDRLP-GQLSGGQRQRVALARCLVRK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255767068 151 PDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMED 219
Cdd:COG3840 148 RPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAA 216
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
5-230 |
3.93e-29 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 116.40 E-value: 3.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 5 VQTNGLTKTY--QGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNIGSM 82
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 83 I--EYPIFY----ENLT-AEENLDlhceymgyhnKKAIQEVLDMVNLKQ-IDKKPVK----------TFSLGMKQRLGIA 144
Cdd:COG4987 414 VpqRPHLFDttlrENLRlARPDAT----------DEELWAALERVGLGDwLAALPDGldtwlgeggrRLSGGERRRLALA 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 145 RAILTKPDLLILDEPVNGLDPLGIKKIRQLFQVLSKeyGMTLLISSHLLGEIEQiADTIGVIRDGRLLEEVSMEDVRGQN 224
Cdd:COG4987 484 RALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEELLAQN 560
|
....*.
gi 255767068 225 TEYIEL 230
Cdd:COG4987 561 GRYRQL 566
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
16-194 |
5.05e-29 |
|
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: 109.76 E-value: 5.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 16 GKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNIGSMIEYPIFYENLTAE 95
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 96 ENLDLHCEYMGYHnKKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLDPLGIKKIRQLF 175
Cdd:TIGR01189 92 ENLHFWAAIHGGA-QRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLL 170
|
170
....*....|....*....
gi 255767068 176 QVLSKEYGMTLLISSHLLG 194
Cdd:TIGR01189 171 RAHLARGGIVLLTTHQDLG 189
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-214 |
5.42e-29 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 110.85 E-value: 5.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 4 IVQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVL---GNIG 80
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINklrRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 81 sMIeypiF-----YENLTAEENLdlhceyM-------GYHNKKAIQ---EVLDMVNLK-QIDKKPvKTFSLGMKQRLGIA 144
Cdd:COG1126 81 -MV----FqqfnlFPHLTVLENV------TlapikvkKMSKAEAEEramELLERVGLAdKADAYP-AQLSGGQQQRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255767068 145 RAILTKPDLLILDEPVNGLDP------LGIkkIRQlfqvLSKEyGMTLLISSHLLGEIEQIADTIGVIRDGRLLEE 214
Cdd:COG1126 149 RALAMEPKVMLFDEPTSALDPelvgevLDV--MRD----LAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEE 217
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-191 |
6.23e-29 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 115.55 E-value: 6.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 7 TNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNK---------FTHTSYEVLG 77
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLrigylpqepPLDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 78 NIGS--------MIEYPIFYENLTAEENL-----DLHCEY--MGYHNKKA-IQEVLDMVNLKQID-KKPVKTFSLGMKQR 140
Cdd:COG0488 81 TVLDgdaelralEAELEELEAKLAEPDEDlerlaELQEEFeaLGGWEAEArAEEILSGLGFPEEDlDRPVSELSGGWRRR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 255767068 141 LGIARAILTKPDLLILDEPVNGLDplgIKKIRQLFQVLsKEYGMTLLISSH 191
Cdd:COG0488 161 VALARALLSEPDLLLLDEPTNHLD---LESIEWLEEFL-KNYPGTVLVVSH 207
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
16-232 |
8.84e-29 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 115.65 E-value: 8.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 16 GKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILG---NKFTHTSYevLGNIGsMI--EYPIFye 90
Cdd:COG1132 352 DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGvdiRDLTLESL--RRQIG-VVpqDTFLF-- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 91 NLTAEENLdlhceymGYHNKKA----IQEVLDMVNLKQ-IDKKP------V----KTFSLGMKQRLGIARAILTKPDLLI 155
Cdd:COG1132 427 SGTIRENI-------RYGRPDAtdeeVEEAAKAAQAHEfIEALPdgydtvVgergVNLSGGQRQRIAIARALLKDPPILI 499
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255767068 156 LDEPVNGLDPLGIKKIRQLFQVLSKeyGMTLLISSHLLGEIEQiADTIGVIRDGRLLEEVSMEDVRGQNTEYIELVT 232
Cdd:COG1132 500 LDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHEELLARGGLYARLYR 573
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-213 |
3.33e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 113.62 E-value: 3.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 4 IVQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIIlGNKfTHTSYevlgnigsmi 83
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GET-VKIGY---------- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 84 eYP----IFYENLTAEENLdlhCEYMGYHNKKAIQEVL-------DMVNlkqidkKPVKTFSLGMKQRLGIARAILTKPD 152
Cdd:COG0488 383 -FDqhqeELDPDKTVLDEL---RDGAPGGTEQEVRGYLgrflfsgDDAF------KPVGVLSGGEKARLALAKLLLSPPN 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255767068 153 LLILDEPVNGLDplgIKKIRQLFQVLsKEYGMTLLISSH---LLgeiEQIADTIGVIRDGRLLE 213
Cdd:COG0488 453 VLLLDEPTNHLD---IETLEALEEAL-DDFPGTVLLVSHdryFL---DRVATRILEFEDGGVRE 509
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
17-210 |
3.88e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 109.75 E-value: 3.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 17 KEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSY---EVLGNIGSMIEYP---IFYE 90
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVklsDIRKKVGLVFQYPeyqLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 91 NLTAE-----ENLDLHCEYMgyhnKKAIQEVLDMVNLKQIDKKPVKTFSL--GMKQRLGIARAILTKPDLLILDEPVNGL 163
Cdd:PRK13637 100 TIEKDiafgpINLGLSEEEI----ENRVKRAMNIVGLDYEDYKDKSPFELsgGQKRRVAIAGVVAMEPKILILDEPTAGL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 255767068 164 DPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGR 210
Cdd:PRK13637 176 DPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGK 222
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-210 |
7.88e-28 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 110.81 E-value: 7.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 2 TYIVQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYE------V 75
Cdd:PRK09452 12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEnrhvntV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 76 LGNigsmieYPIFyENLTAEENL--DLHCEYMGYHN-KKAIQEVLDMVNLKQ-IDKKPvKTFSLGMKQRLGIARAILTKP 151
Cdd:PRK09452 92 FQS------YALF-PHMTVFENVafGLRMQKTPAAEiTPRVMEALRMVQLEEfAQRKP-HQLSGGQQQRVAIARAVVNKP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255767068 152 DLLILDEPVNGLDplgiKKIRQLFQV----LSKEYGMTLLISSHLLGEIEQIADTIGVIRDGR 210
Cdd:PRK09452 164 KVLLLDESLSALD----YKLRKQMQNelkaLQRKLGITFVFVTHDQEEALTMSDRIVVMRDGR 222
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-213 |
1.11e-27 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 110.31 E-value: 1.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 1 MTYIVQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSyEVLGNIG 80
Cdd:PRK11607 16 LTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP-PYQRPIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 81 SMIEYPIFYENLTAEENL--DLHCEYMGYHNKKA-IQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILD 157
Cdd:PRK11607 95 MMFQSYALFPHMTVEQNIafGLKQDKLPKAEIASrVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 158 EPVNGLDplgiKKIRQLFQV----LSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLE 213
Cdd:PRK11607 175 EPMGALD----KKLRDRMQLevvdILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQ 230
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
10-220 |
2.41e-27 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 106.52 E-value: 2.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 10 LTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFT----HTsyEVLGNIGSMIEY 85
Cdd:PRK10895 9 LAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllplHA--RARRGIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 86 PIFYENLTAEENL--------DLHCEymgyHNKKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILD 157
Cdd:PRK10895 87 ASIFRRLSVYDNLmavlqirdDLSAE----QREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255767068 158 EPVNGLDPLGIKKIRQLFQVLsKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDV 220
Cdd:PRK10895 163 EPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-220 |
2.42e-27 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 111.03 E-value: 2.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 1 MTYIVQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILG---NKFTHTSYEVLG 77
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinyNKLDHKLAAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 78 nIGSMIEYPIFYENLTAEENLdlhceYMGYHNKKAI---------------QEVLDMVNLKQIDKKPVKTFSLGMKQRLG 142
Cdd:PRK09700 82 -IGIIYQELSVIDELTVLENL-----YIGRHLTKKVcgvniidwremrvraAMMLLRVGLKVDLDEKVANLSISHKQMLE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 143 IARAILTKPDLLILDEPVNGLDPlgiKKIRQLFQVLS--KEYGMTLLISSHLLGEIEQIADTIGVIRDG-----RLLEEV 215
Cdd:PRK09700 156 IAKTLMLDAKVIIMDEPTSSLTN---KEVDYLFLIMNqlRKEGTAIVYISHKLAEIRRICDRYTVMKDGssvcsGMVSDV 232
|
....*
gi 255767068 216 SMEDV 220
Cdd:PRK09700 233 SNDDI 237
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-213 |
2.91e-27 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 106.85 E-value: 2.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 1 MTYIVQTNGLTKTY---------QGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHT 71
Cdd:COG4167 1 MSALLEVRNLSKTFkyrtglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 72 SYEVLG------------------NIGSMIEYP-IFYENLTAEENldlhceymgyhnKKAIQEVLDMVNL--KQIDKKPv 130
Cdd:COG4167 81 DYKYRCkhirmifqdpntslnprlNIGQILEEPlRLNTDLTAEER------------EERIFATLRLVGLlpEHANFYP- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 131 KTFSLGMKQRLGIARAILTKPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGR 210
Cdd:COG4167 148 HMLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGE 227
|
...
gi 255767068 211 LLE 213
Cdd:COG4167 228 VVE 230
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
6-200 |
3.05e-27 |
|
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: 105.27 E-value: 3.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 6 QTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNIGSMIEY 85
Cdd:cd03231 2 EADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 86 PIFYENLTAEENLDLHCEYmgyHNKKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLDP 165
Cdd:cd03231 82 PGIKTTLSVLENLRFWHAD---HSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
170 180 190
....*....|....*....|....*....|....*
gi 255767068 166 LGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIA 200
Cdd:cd03231 159 AGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGA 193
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
23-220 |
3.12e-27 |
|
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: 108.66 E-value: 3.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 23 VSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGnkfthtsyEVLGNIGSMIEYP--------IFYE---- 90
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNG--------RTLFDSRKGIFLPpekrrigyVFQEarlf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 91 -NLTAEENLdlhcEY-----MGYHNKKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLD 164
Cdd:TIGR02142 88 pHLSVRGNL----RYgmkraRPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 255767068 165 PLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDV 220
Cdd:TIGR02142 164 DPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
8-224 |
4.69e-27 |
|
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: 110.62 E-value: 4.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 8 NGLTKTY-QGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNigsMIEY- 85
Cdd:COG4988 340 EDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRR---QIAWv 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 86 ---P-IFyeNLTAEENLDLhceymGYHN--KKAIQEVLDMVNLKQ-IDKKPV----------KTFSLGMKQRLGIARAIL 148
Cdd:COG4988 417 pqnPyLF--AGTIRENLRL-----GRPDasDEELEAALEAAGLDEfVAALPDgldtplgeggRGLSGGQAQRLALARALL 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255767068 149 TKPDLLILDEPVNGLDPLGIKKIRQLFQVLSKeyGMTLLISSHLLGEIEQiADTIGVIRDGRLLEEVSMEDVRGQN 224
Cdd:COG4988 490 RDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-220 |
5.17e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 106.86 E-value: 5.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 3 YIVQTNGLTKTY-QGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLG---N 78
Cdd:PRK13636 4 YILKVEELNYNYsDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKlreS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 79 IGSMIEYP---IF----YENLT-AEENLDLHCEYMgyhnKKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTK 150
Cdd:PRK13636 84 VGMVFQDPdnqLFsasvYQDVSfGAVNLKLPEDEV----RKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVME 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 151 PDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDV 220
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-214 |
5.19e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 106.74 E-value: 5.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 1 MTYIVQTNGLTKTYQ-GKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFT-HTSYEVLGN 78
Cdd:PRK13647 1 MDNIIEVEDLHFRYKdGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNaENEKWVRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 79 IGSMIEYP---IFyeNLTAEENLDLHCEYMGYHNKKA---IQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPD 152
Cdd:PRK13647 81 VGLVFQDPddqVF--SSTVWDDVAFGPVNMGLDKDEVerrVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255767068 153 LLILDEPVNGLDPLGIKKIRQLFQVLSKEyGMTLLISSHLLGEIEQIADTIGVIRDGRLLEE 214
Cdd:PRK13647 159 VIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAE 219
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
5-219 |
8.86e-26 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 104.80 E-value: 8.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 5 VQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHT------------S 72
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRsiqqrdicmvfqS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 73 YEVLG--NIGSMIEYPIFYENLTAEEnldlhceymgyhNKKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTK 150
Cdd:PRK11432 87 YALFPhmSLGENVGYGLKMLGVPKEE------------RKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255767068 151 PDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMED 219
Cdd:PRK11432 155 PKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQE 223
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-219 |
1.67e-25 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 105.78 E-value: 1.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 1 MTYIVQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLtSLVKPT---SGEIIILGNKFTHTSYEVLG 77
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVL-SGVYPHgtyEGEIIFEGEELQASNIRDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 78 NIGSMIeypIFYE-----NLTAEENLDLHCEYM--GYHNKKAI----QEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARA 146
Cdd:PRK13549 81 RAGIAI---IHQElalvkELSVLENIFLGNEITpgGIMDYDAMylraQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255767068 147 ILTKPDLLILDEPVNGLDPlgiKKIRQLFQVLS--KEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMED 219
Cdd:PRK13549 158 LNKQARLLILDEPTASLTE---SETAVLLDIIRdlKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAG 229
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
10-220 |
2.04e-25 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 105.65 E-value: 2.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 10 LTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSL--VKPTSGEII-----------------------IL 64
Cdd:TIGR03269 6 LTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpskvgepcpVC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 65 GNKFTH-----------TSYEVLGNIGSMIEYPI-FYENLTAEENLDLHCEYMGYHNKKAIQ---EVLDMVNLKQIDKKP 129
Cdd:TIGR03269 86 GGTLEPeevdfwnlsdkLRRRIRKRIAIMLQRTFaLYGDDTVLDNVLEALEEIGYEGKEAVGravDLIEMVQLSHRITHI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 130 VKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDG 209
Cdd:TIGR03269 166 ARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENG 245
|
250
....*....|.
gi 255767068 210 RLLEEVSMEDV 220
Cdd:TIGR03269 246 EIKEEGTPDEV 256
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
12-209 |
2.25e-25 |
|
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: 100.41 E-value: 2.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 12 KTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKF-----THTSYEVLGNIGsmieYP 86
Cdd:cd03226 8 SYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIkakerRKSIGYVMQDVD----YQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 87 IFYEnlTAEENLDLhcEYMGYHNKKA-IQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLDP 165
Cdd:cd03226 84 LFTD--SVREELLL--GLKELDAGNEqAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDY 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 255767068 166 LGIKKIRQLFQVLSKEyGMTLLISSHLLGEIEQIADTIGVIRDG 209
Cdd:cd03226 160 KNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
8-210 |
3.50e-25 |
|
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: 97.90 E-value: 3.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 8 NGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNkfthtsyevlgnigsmieypi 87
Cdd:cd03221 4 ENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST--------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 88 fyenltaeenldlhcEYMGYhnkkaiqevldmvnLKQidkkpvktFSLGMKQRLGIARAILTKPDLLILDEPVNGLDPLG 167
Cdd:cd03221 63 ---------------VKIGY--------------FEQ--------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLES 105
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 255767068 168 IKKIRQLFqvlsKEYGMTLLISSHLLGEIEQIADTIGVIRDGR 210
Cdd:cd03221 106 IEALEEAL----KEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
9-230 |
9.63e-25 |
|
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: 104.03 E-value: 9.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 9 GLTKTYQG--KEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNIGSMIEYP 86
Cdd:TIGR02203 335 NVTFRYPGrdRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQD 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 87 IFYENLTAEENLdlhcEY--MGYHNKKAIQEVLDMVNLKQ-IDKKP--VKT--------FSLGMKQRLGIARAILTKPDL 153
Cdd:TIGR02203 415 VVLFNDTIANNI----AYgrTEQADRAEIERALAAAYAQDfVDKLPlgLDTpigengvlLSGGQRQRLAIARALLKDAPI 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255767068 154 LILDEPVNGLDPLGIKKIRQLFQVLSKeyGMTLLISSHLLGEIEQiADTIGVIRDGRLLEEVSMEDVRGQNTEYIEL 230
Cdd:TIGR02203 491 LILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNELLARNGLYAQL 564
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-230 |
1.36e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 100.19 E-value: 1.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 1 MTYIVQTNGLTKTY---QGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTS-YEVL 76
Cdd:PRK13650 1 MSNIIEVKNLTFKYkedQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENvWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 77 GNIGSMIEYPifyEN----LTAEENLDLHCEYMGYHN---KKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILT 149
Cdd:PRK13650 81 HKIGMVFQNP---DNqfvgATVEDDVAFGLENKGIPHeemKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 150 KPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIeQIADTIGVIRDGRLLEEVSMEDVRGQNTEYIE 229
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELFSRGNDLLQ 236
|
.
gi 255767068 230 L 230
Cdd:PRK13650 237 L 237
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
24-211 |
1.41e-24 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 98.33 E-value: 1.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 24 SMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIIlgNKFTHTSYEVLGNIGSMIeypiFYEN-----LTAEENL 98
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLI--NGVDVTAAPPADRPVSML----FQENnlfahLTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 99 DLHCE---YMGYHNKKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLDPLGIKKIRQLF 175
Cdd:cd03298 92 GLGLSpglKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 255767068 176 QVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRL 211
Cdd:cd03298 172 LDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
5-214 |
1.57e-24 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 99.32 E-value: 1.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 5 VQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKF-------THTSYEVLG 77
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsqkpsEKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 78 NIGSMIEYPIFYENLTAEENL-DLHCEYMGYHNKKAIQEVLDMVNLKQIDKK----PVKtFSLGMKQRLGIARAILTKPD 152
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENLiEAPCKVLGLSKEQAREKAMKLLARLRLTDKadrfPLH-LSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255767068 153 LLILDEPVNGLDPLGIKKIRQLFQVLSkEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEE 214
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQ 222
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
5-230 |
1.92e-24 |
|
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: 98.84 E-value: 1.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 5 VQTNGLTKTYQGKE--VVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNIGSM 82
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 83 IEYPIFYENLTAEENLdlhcEYmGYHN--KKAIQEVLDMVNLKQ-IDKKP-----------VKtFSLGMKQRLGIARAIL 148
Cdd:cd03251 81 VSQDVFLFNDTVAENI----AY-GRPGatREEVEEAARAANAHEfIMELPegydtvigergVK-LSGGQRQRIAIARALL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 149 TKPDLLILDEPVNGLDPLGIKKIRQLFQVLSKeyGMTLLISSHLLGEIEQiADTIGVIRDGRLLEEVSMEDVRGQNTEYI 228
Cdd:cd03251 155 KDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLAQGGVYA 231
|
..
gi 255767068 229 EL 230
Cdd:cd03251 232 KL 233
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
11-211 |
2.21e-24 |
|
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: 97.86 E-value: 2.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 11 TKTYQGKEV-VSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLG----NIGSMIEY 85
Cdd:cd03292 7 TKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPylrrKIGVVFQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 86 PIFYENLTAEENLDLHCEYMGYHNK---KAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVNG 162
Cdd:cd03292 87 FRLLPDRNVYENVAFALEVTGVPPReirKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGN 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 255767068 163 LDPLGIKKIRQLFQVLSKEyGMTLLISSHLLGEIEQIADTIGVIRDGRL 211
Cdd:cd03292 167 LDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-211 |
2.21e-24 |
|
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: 103.55 E-value: 2.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 5 VQTNGLTKTYQ--GKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIIlGNKFTHTSYEVL-GNIGS 81
Cdd:TIGR01257 929 VCVKNLVKIFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLV-GGKDIETNLDAVrQSLGM 1007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 82 MIEYPIFYENLTAEENLDLHCEYMGYHNKKA---IQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDE 158
Cdd:TIGR01257 1008 CPQHNILFHHLTVAEHILFYAQLKGRSWEEAqleMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDE 1087
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 255767068 159 PVNGLDPLGIKKIRQLfqVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRL 211
Cdd:TIGR01257 1088 PTSGVDPYSRRSIWDL--LLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
8-220 |
2.24e-24 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 100.99 E-value: 2.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 8 NGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEiIILGNK--FTHTSyevLG--NIGSMI 83
Cdd:COG1118 6 RNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGR-IVLNGRdlFTNLP---PRerRVGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 84 -EYPIFyENLTAEEN----LDlhceyMGYHNKKAIQ----EVLDMVNLKQI-DKKPvKTFSLGMKQRLGIARAILTKPDL 153
Cdd:COG1118 82 qHYALF-PHMTVAENiafgLR-----VRPPSKAEIRarveELLELVQLEGLaDRYP-SQLSGGQRQRVALARALAVEPEV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255767068 154 LILDEPVNGLDPLGIKKIRQ-LFQVLsKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDV 220
Cdd:COG1118 155 LLLDEPFGALDAKVRKELRRwLRRLH-DELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-211 |
2.44e-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: 97.12 E-value: 2.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 4 IVQTNGLTktyqGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSyevlgnIGSMI 83
Cdd:cd03215 4 VLEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRS------PRDAI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 84 EYPIFY-----------ENLTAEENLdlhceymgyhnkkAIQEVLdmvnlkqidkkpvktfSLGMKQRLGIARAILTKPD 152
Cdd:cd03215 74 RAGIAYvpedrkreglvLDLSVAENI-------------ALSSLL----------------SGGNQQKVVLARWLARDPR 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 255767068 153 LLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHlLGEIEQIADTIGVIRDGRL 211
Cdd:cd03215 125 VLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSE-LDELLGLCDRILVMYEGRI 182
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
22-209 |
5.74e-24 |
|
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: 97.54 E-value: 5.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 22 NVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYE---VLGNIgSMIEYpifyenLTAEENL 98
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDrmvVFQNY-SLLPW------LTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 99 DLHCEYMGYHNKKA-----IQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLDPLGIKKIRQ 173
Cdd:TIGR01184 76 ALAVDRVLPDLSKSerraiVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQE 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 255767068 174 LFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDG 209
Cdd:TIGR01184 156 ELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
4-217 |
7.69e-24 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 97.19 E-value: 7.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 4 IVQTNGLTKTYQ-GK---EVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILG---NKFTHTSYEVL 76
Cdd:PRK11629 5 LLQCDNLCKRYQeGSvqtDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpmSKLSSAAKAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 77 GN--IGSMIEYPIFYENLTAEENLDLHCEYMGYHNKKAIQEVLDM---VNLKQIDKKPVKTFSLGMKQRLGIARAILTKP 151
Cdd:PRK11629 85 RNqkLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMlaaVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255767068 152 DLLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLgeieQIADTIG---VIRDGRLLEEVSM 217
Cdd:PRK11629 165 RLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDL----QLAKRMSrqlEMRDGRLTAELSL 229
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
5-220 |
9.31e-24 |
|
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: 97.02 E-value: 9.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 5 VQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLgNIGSMIE 84
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER-NVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 85 YPIFYENLTAEENLDLhceymGYHNKKA------------IQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPD 152
Cdd:cd03296 82 HYALFRHMTVFDNVAF-----GLRVKPRserppeaeirakVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255767068 153 LLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDV 220
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
16-224 |
1.10e-23 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 96.53 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 16 GKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNIGSMIEYPIFYENLTAE 95
Cdd:cd03254 15 KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDTFLFSGTIM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 96 ENLDLHCEYMgyhNKKAIQEVLDMVNLKQ-IDKKP----------VKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLD 164
Cdd:cd03254 95 ENIRLGRPNA---TDEEVIEAAKEAGAHDfIMKLPngydtvlgenGGNLSQGERQLLAIARAMLRDPKILILDEATSNID 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 165 PLGIKKIRQLFQVLSKeyGMTLLISSHLLGEIEQiADTIGVIRDGRLLEEVSMEDVRGQN 224
Cdd:cd03254 172 TETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLAKK 228
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-230 |
1.41e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 97.39 E-value: 1.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 4 IVQTNGLTKTYQGKE--VVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFT-HTSYEVLGNIG 80
Cdd:PRK13635 5 IIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSeETVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 81 SMIEYPifyEN----LTAEENLDLHCEYMGYHNK---KAIQEVLDMVNLKQ-IDKKPVKtFSLGMKQRLGIARAILTKPD 152
Cdd:PRK13635 85 MVFQNP---DNqfvgATVQDDVAFGLENIGVPREemvERVDQALRQVGMEDfLNREPHR-LSGGQKQRVAIAGVLALQPD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255767068 153 LLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQiADTIGVIRDGRLLEEVSMEDVRGQNTEYIEL 230
Cdd:PRK13635 161 IIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKSGHMLQEI 237
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
15-220 |
1.84e-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: 100.14 E-value: 1.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 15 QGKEVVSNVSMHIKKGEIYGFLGPNGAGKT----TIMKMLTSLVKPTSGEIIILGNKFTHTSYEVL----GNIGSMIeyp 86
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELrrirGNRIAMI--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 87 iFYENLTA-----------EENLDLHceyMGYHNKKAIQEVLDMVNLKQID--KKPVKTF----SLGMKQRLGIARAILT 149
Cdd:COG4172 98 -FQEPMTSlnplhtigkqiAEVLRLH---RGLSGAAARARALELLERVGIPdpERRLDAYphqlSGGQRQRVMIAMALAN 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255767068 150 KPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDV 220
Cdd:COG4172 174 EPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAEL 244
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-214 |
2.61e-23 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 95.58 E-value: 2.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 4 IVQTNGLTKTYQGKE----VVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVL--- 76
Cdd:COG4181 8 IIELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARarl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 77 --GNIGSMieypiFYE-----NLTAEENLDLHCEYMGYHNKKAI-QEVLDMVNLKQ-IDKKPvKTFSLGMKQRLGIARAI 147
Cdd:COG4181 88 raRHVGFV-----FQSfqllpTLTALENVMLPLELAGRRDARARaRALLERVGLGHrLDHYP-AQLSGGEQQRVALARAF 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255767068 148 LTKPDLLILDEPVNGLD-PLGIKKIRQLFQvLSKEYGMTLLISSHllgeIEQIA---DTIGVIRDGRLLEE 214
Cdd:COG4181 162 ATEPAILFADEPTGNLDaATGEQIIDLLFE-LNRERGTTLVLVTH----DPALAarcDRVLRLRAGRLVED 227
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-212 |
3.36e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 96.23 E-value: 3.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 4 IVQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLG---NIG 80
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLAlrqQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 81 SMIEYP---IFYENLTAE-----ENLDLHCEYMGyhnkKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPD 152
Cdd:PRK13638 81 TVFQDPeqqIFYTDIDSDiafslRNLGVPEAEIT----RRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQAR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 153 LLILDEPVNGLDPLGIKKIRQLFQVLSKEyGMTLLISSHLLGEIEQIADTIGVIRDGRLL 212
Cdd:PRK13638 157 YLLLDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQIL 215
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
17-255 |
4.40e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 95.92 E-value: 4.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 17 KEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIII--LGNKFTHTSYEVLGNIGSMIEYP-------I 87
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVdgLDTSDEENLWDIRNKAGMVFQNPdnqivatI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 88 FYENLT-AEENLDLHCEYMgyhnKKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLDPL 166
Cdd:PRK13633 103 VEEDVAfGPENLGIPPEEI----RERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 167 GIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQiADTIGVIRDGRLLEEVSMEDVRGQNTEY--IELVTPNQTRACFVLEK 244
Cdd:PRK13633 179 GRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKEVEMMkkIGLDVPQVTELAYELKK 257
|
250
....*....|.
gi 255767068 245 ELQLTNFKILN 255
Cdd:PRK13633 258 EGVDIPSDILT 268
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-214 |
5.52e-23 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 94.95 E-value: 5.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 1 MTYIVQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTH--TSYEVLGN 78
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwqTAKIMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 79 IGSMIEYPIFYENLTAEENLDlhceyMG--YHNKKAIQEVLDMV-----NLKQIDKKPVKTFSLGMKQRLGIARAILTKP 151
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLA-----MGgfFAERDQFQERIKWVyelfpRLHERRIQRAGTMSGGEQQMLAIGRALMSQP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255767068 152 DLLILDEPVNGLDPLGIKKIRQLFQVLSKEyGMTLLISSHLLGEIEQIADTIGVIRDGRLLEE 214
Cdd:PRK11614 157 RLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVVLE 218
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
17-211 |
6.09e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 95.44 E-value: 6.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 17 KEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFT-HTSYEVLGNIGsmieypIFYEN---- 91
Cdd:PRK13632 22 NNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISkENLKEIRKKIG------IIFQNpdnq 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 92 ---LTAE-------ENLDLHCEYMgyhnKKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVN 161
Cdd:PRK13632 96 figATVEddiafglENKKVPPKKM----KDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTS 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 255767068 162 GLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQiADTIGVIRDGRL 211
Cdd:PRK13632 172 MLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKL 220
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
8-220 |
8.06e-23 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 98.06 E-value: 8.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 8 NGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGN--KFTHTSyEVLgNIGSMIey 85
Cdd:PRK11288 8 DGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQemRFASTT-AAL-AAGVAI-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 86 pIFYE-----NLTAEENLdlhceYMGY--------HNKKAIQEVLDmvNLKQIDKK-----PVKTFSLGMKQRLGIARAI 147
Cdd:PRK11288 84 -IYQElhlvpEMTVAENL-----YLGQlphkggivNRRLLNYEARE--QLEHLGVDidpdtPLKYLSIGQRQMVEIAKAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255767068 148 LTKPDLLILDEPVNGLDplgIKKIRQLFQVLS--KEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEV-SMEDV 220
Cdd:PRK11288 156 ARNARVIAFDEPTSSLS---AREIEQLFRVIRelRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATFdDMAQV 228
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-220 |
8.99e-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: 98.22 E-value: 8.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 3 YIVQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVkPTSGEIIILGNKFTHTSYEVLG----- 77
Cdd:COG4172 285 FPIKRGLFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRALRplrrr 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 78 ----------------NIGSMIEypifyenltaeENLDLHCEYMGYHNKKA-IQEVLDMVNLKQ--IDKKPvKTFSLGMK 138
Cdd:COG4172 364 mqvvfqdpfgslsprmTVGQIIA-----------EGLRVHGPGLSAAERRArVAEALEEVGLDPaaRHRYP-HEFSGGQR 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 139 QRLGIARAILTKPDLLILDEPVNGLDpLGI-KKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSM 217
Cdd:COG4172 432 QRIAIARALILEPKLLVLDEPTSALD-VSVqAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPT 510
|
...
gi 255767068 218 EDV 220
Cdd:COG4172 511 EQV 513
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-213 |
9.62e-23 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 96.19 E-value: 9.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 1 MTYIVQTNGLTKTYQGK----------EVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTH 70
Cdd:PRK11308 2 QQPLLQAIDLKKHYPVKrglfkperlvKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 71 TSYEVLGNIGSMIEypIFYENLTA------------EENLDLHCEYMGYHNKKAIQEVLDMVNLK--QIDKKPvKTFSLG 136
Cdd:PRK11308 82 ADPEAQKLLRQKIQ--IVFQNPYGslnprkkvgqilEEPLLINTSLSAAERREKALAMMAKVGLRpeHYDRYP-HMFSGG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255767068 137 MKQRLGIARAILTKPDLLILDEPVNGLDpLGIK-KIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLE 213
Cdd:PRK11308 159 QRQRIAIARALMLDPDVVVADEPVSALD-VSVQaQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVE 235
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-213 |
1.32e-22 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 94.33 E-value: 1.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 1 MTYIVQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMK----M--LTSLVKpTSGEIIILGNKFTHTSYE 74
Cdd:COG1117 8 LEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrMndLIPGAR-VEGEILLDGEDIYDPDVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 75 VLG---NIGsMIeypiF----------YENLTAeeNLDLHceymGYHNKKAIQEV----LDMVNL----KQIDKKPVKTF 133
Cdd:COG1117 87 VVElrrRVG-MV----FqkpnpfpksiYDNVAY--GLRLH----GIKSKSELDEIveesLRKAALwdevKDRLKKSALGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 134 SLGMKQRLGIARAILTKPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYgmTLLISSHLLGEIEQIADTIGVIRDGRLLE 213
Cdd:COG1117 156 SGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGELVE 233
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
13-253 |
1.40e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 94.81 E-value: 1.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 13 TYQG-----KEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSY-----EVLGNIGSM 82
Cdd:PRK13649 11 TYQAgtpfeGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdikQIRKKVGLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 83 IEYP---IFYEnlTAEENLDLHCEYMGYHNKKAIQ---EVLDMVNLKQ--IDKKPVKtFSLGMKQRLGIARAILTKPDLL 154
Cdd:PRK13649 91 FQFPesqLFEE--TVLKDVAFGPQNFGVSQEEAEAlarEKLALVGISEslFEKNPFE-LSGGQMRRVAIAGILAMEPKIL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 155 ILDEPVNGLDPLGIKKIRQLFQVLSKEyGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDVRgQNTEYIE---LV 231
Cdd:PRK13649 168 VLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF-QDVDFLEekqLG 245
|
250 260
....*....|....*....|...
gi 255767068 232 TPNQTRACFVL-EKELQLTNFKI 253
Cdd:PRK13649 246 VPKITKFAQRLaDRGISFSSLPI 268
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
8-211 |
1.49e-22 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 93.97 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 8 NGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIIlGNKFTHTSYE------------- 74
Cdd:PRK11247 16 NAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLA-GTAPLAEAREdtrlmfqdarllp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 75 ---VLGNIGsmieypifyenltaeenLDLHCEYmgyhnKKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKP 151
Cdd:PRK11247 95 wkkVIDNVG-----------------LGLKGQW-----RDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 152 DLLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRL 211
Cdd:PRK11247 153 GLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-213 |
1.62e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 94.14 E-value: 1.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 1 MTYIVQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVK-----PTSGEIIILGNKFTHTSY-- 73
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVdp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 74 -EVLGNIGSMIEYPIFYENLTAEENLDLHCEYMGY-HNKKAIQEVLDMVNLKQIDKKPVK--------TFSLGMKQRLGI 143
Cdd:PRK14267 81 iEVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLvKSKKELDERVEWALKKAALWDEVKdrlndypsNLSGGQRQRLVI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 144 ARAILTKPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYgmTLLISSHLLGEIEQIADTIGVIRDGRLLE 213
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIE 228
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-201 |
1.88e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 93.95 E-value: 1.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 5 VQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLvKPTSGEIIILGNK--FTHTSYEVLGNIG-- 80
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM-NELESEVRVEGRVefFNQNIYERRVNLNrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 81 ----SMIEYPIFYENLTAEENLDLHCEYMGYHNKKAIQEVLDMV--------NLKQIDKKPVKTFSLGMKQRLGIARAIL 148
Cdd:PRK14258 87 rrqvSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLEIDDIVESAlkdadlwdEIKHKIHKSALDLSGGQQQRLCIARALA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 255767068 149 TKPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIAD 201
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-214 |
1.89e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 97.08 E-value: 1.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 15 QGKEVVSNVSMHIKKGEIYGFLGPNGAGKT----TIMKML-TSLVKPTSGEIIILGNKFTHTSYEVL----GNIGSMIey 85
Cdd:PRK15134 20 TVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLpSPPVVYPSGDIRFHGESLLHASEQTLrgvrGNKIAMI-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 86 piFYENL-------TAE----ENLDLHceyMGYHNKKAIQEV---LDMVNLKQIdKKPVKTF----SLGMKQRLGIARAI 147
Cdd:PRK15134 98 --FQEPMvslnplhTLEkqlyEVLSLH---RGMRREAARGEIlncLDRVGIRQA-AKRLTDYphqlSGGERQRVMIAMAL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255767068 148 LTKPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEE 214
Cdd:PRK15134 172 LTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQ 238
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
21-194 |
2.24e-22 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 92.17 E-value: 2.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 21 SNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGN---IGsmiEYPIFYENLTAEEN 97
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDllyLG---HQPGIKTELTALEN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 98 LDLHCEYMGYHNKKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLDPLGIKKIRQLFQV 177
Cdd:PRK13538 95 LRFYQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQ 174
|
170
....*....|....*..
gi 255767068 178 LSKEYGMTLLISSHLLG 194
Cdd:PRK13538 175 HAEQGGMVILTTHQDLP 191
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-220 |
3.55e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 93.05 E-value: 3.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 5 VQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVK-----PTSGEIIILGNK-FTHTSYEVLGN 78
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDiFKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 79 IGSMIEYPIFYENLTAEENLDLHCEYMGYHNKKA-----IQEVLDMVNL----KQIDKKPVKTFSLGMKQRLGIARAILT 149
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKKelqerVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAF 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255767068 150 KPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEygMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDV 220
Cdd:PRK14247 164 QPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
4-219 |
6.77e-22 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 95.24 E-value: 6.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 4 IVQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLtSLVKPT---SGEIIILGN--KFTHTS-YEVLG 77
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVL-SGVYPHgsyEGEILFDGEvcRFKDIRdSEALG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 78 NIgsmieypIFYENL------TAEENLDLHCEymgyHNKKAI----------QEVLDMVNLKQIDKKPVKTFSLGMKQRL 141
Cdd:NF040905 80 IV-------IIHQELalipylSIAENIFLGNE----RAKRGVidwnetnrraRELLAKVGLDESPDTLVTDIGVGKQQLV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255767068 142 GIARAILTKPDLLILDEPVNGLDPLGIKKIRQLFQVLsKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMED 219
Cdd:NF040905 149 EIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRTIETLDCRA 225
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
16-220 |
7.31e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 95.09 E-value: 7.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 16 GKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFThtsyevLGNIGSMIEYPIFY------ 89
Cdd:COG1129 264 VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVR------IRSPRDAIRAGIAYvpedrk 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 90 -----------ENLTAEeNLDLHCEYMGYHNKKAIQEVLDMVNLKQI----DKKPVKTFSLGMKQRLGIARAILTKPDLL 154
Cdd:COG1129 338 geglvldlsirENITLA-SLDRLSRGGLLDRRRERALAEEYIKRLRIktpsPEQPVGNLSGGNQQKVVLAKWLATDPKVL 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255767068 155 ILDEPVNGLDpLGIKK-IRQLFQVLSKEyGMT-LLISSHlLGEIEQIADTIGVIRDGRLLEEVSMEDV 220
Cdd:COG1129 417 ILDEPTRGID-VGAKAeIYRLIRELAAE-GKAvIVISSE-LPELLGLSDRILVMREGRIVGELDREEA 481
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-236 |
1.09e-21 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 94.73 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 1 MTYIVQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTS---YEVLG 77
Cdd:PRK15439 8 APPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpakAHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 78 nIGSMIEYPIFYENLTAEENLdlhCEYMGYH--NKKAIQEVLDMVNLkQID-KKPVKTFSLGMKQRLGIARAILTKPDLL 154
Cdd:PRK15439 88 -IYLVPQEPLLFPNLSVKENI---LFGLPKRqaSMQKMKQLLAALGC-QLDlDSSAGSLEVADRQIVEILRGLMRDSRIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 155 ILDEPVNGLDPLGIKKI-RQLFQVLSKEYGMTLLisSHLLGEIEQIADTIGVIRDGRLLEEVSMEDVRgqNTEYIELVTP 233
Cdd:PRK15439 163 ILDEPTASLTPAETERLfSRIRELLAQGVGIVFI--SHKLPEIRQLADRISVMRDGTIALSGKTADLS--TDDIIQAITP 238
|
...
gi 255767068 234 NQT 236
Cdd:PRK15439 239 AAR 241
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
20-213 |
1.12e-21 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 93.23 E-value: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 20 VSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLG---------------------N 78
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRavrsdiqmifqdplaslnprmT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 79 IGSMIEYP--IFYENLTAEEnldlhceymgyhNKKAIQEVLDMVNL--KQIDKKPvKTFSLGMKQRLGIARAILTKPDLL 154
Cdd:PRK15079 117 IGEIIAEPlrTYHPKLSRQE------------VKDRVKAMMLKVGLlpNLINRYP-HEFSGGQCQRIGIARALILEPKLI 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 155 ILDEPVNGLDpLGIK-KIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLE 213
Cdd:PRK15079 184 ICDEPVSALD-VSIQaQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVE 242
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
2-209 |
1.15e-21 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 95.47 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 2 TYIVQTNGLTKTYQGKE--VVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNI 79
Cdd:TIGR01257 1935 TDILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNM 2014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 80 GSMIEYPIFYENLTAEENLDLHCEYMGYHNKKaIQEV----LDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLI 155
Cdd:TIGR01257 2015 GYCPQFDAIDDLLTGREHLYLYARLRGVPAEE-IEKVanwsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVL 2093
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 255767068 156 LDEPVNGLDPLGIKKIRQLFQVLSKEyGMTLLISSHLLGEIEQIADTIGVIRDG 209
Cdd:TIGR01257 2094 LDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-228 |
2.03e-21 |
|
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: 94.12 E-value: 2.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 4 IVQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLtSLVKPT---SGEIIILGNKFTHTSYEVLGNIG 80
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKIL-SGVYPHgtwDGEIYWSGSPLKASNIRDTERAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 81 SMIEYP--IFYENLTAEENLDL-----------HCEYMGYHNKKAIQEV-LDMVNlkqiDKKPVKTFSLGMKQRLGIARA 146
Cdd:TIGR02633 80 IVIIHQelTLVPELSVAENIFLgneitlpggrmAYNAMYLRAKNLLRELqLDADN----VTRPVGDYGGGQQQLVEIAKA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 147 ILTKPDLLILDEPVNGLDPLGIKKIRQLFQVLsKEYGMTLLISSHLLGEIEQIADTIGVIRDGRlleEVSMEDVRGQNTE 226
Cdd:TIGR02633 156 LNKQARLLILDEPSSSLTEKETEILLDIIRDL-KAHGVACVYISHKLNEVKAVCDTICVIRDGQ---HVATKDMSTMSED 231
|
..
gi 255767068 227 YI 228
Cdd:TIGR02633 232 DI 233
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
5-214 |
4.10e-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: 4.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 5 VQTNGLTKTY--QGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIiLGNKFTHTSYEVLGNIGSM 82
Cdd:cd03247 1 LSINNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEIT-LDGVPVSDLEKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 83 IEYPIFYENLTAEENLDlhceymgyhnkkaiqevldmvnlkqidkkpvKTFSLGMKQRLGIARAILTKPDLLILDEPVNG 162
Cdd:cd03247 80 LNQRPYLFDTTLRNNLG-------------------------------RRFSGGERQRLALARILLQDAPIVLLDEPTVG 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 255767068 163 LDPLGIKKI-RQLFQVLSkeyGMTLLISSHLLGEIEQiADTIGVIRDGRLLEE 214
Cdd:cd03247 129 LDPITERQLlSLIFEVLK---DKTLIWITHHLTGIEH-MDKILFLENGKIIMQ 177
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-225 |
5.06e-21 |
|
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: 92.94 E-value: 5.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 4 IVQTNGLTKTYQGKE-----VVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEI-IILGNKF---THTSYE 74
Cdd:TIGR03269 279 IIKVRNVSKRYISVDrgvvkAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnVRVGDEWvdmTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 75 VLGNIGSMI-----EYPIF-----YENLTAEENLDLHCEY-----------MGYHNKKAiQEVLDmvnlkqidkKPVKTF 133
Cdd:TIGR03269 359 GRGRAKRYIgilhqEYDLYphrtvLDNLTEAIGLELPDELarmkavitlkmVGFDEEKA-EEILD---------KYPDEL 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 134 SLGMKQRLGIARAILTKPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLE 213
Cdd:TIGR03269 429 SEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVK 508
|
250
....*....|..
gi 255767068 214 EVSMEDVRGQNT 225
Cdd:TIGR03269 509 IGDPEEIVEELT 520
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
5-213 |
5.35e-21 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 89.69 E-value: 5.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 5 VQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTS-------YEVLG 77
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKtpsdkaiRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 78 NIGSMIEYPIFYENLTAEENL-DLHCEYMGYHNKKAIQ---EVLDMVNLKQI-DKKPVKtFSLGMKQRLGIARAILTKPD 152
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLiEAPCRVLGLSKDQALAraeKLLERLRLKPYaDRFPLH-LSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255767068 153 LLILDEPVNGLDPLGIKKIRQLFQVLSkEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLE 213
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVE 221
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-221 |
9.09e-21 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 89.44 E-value: 9.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 1 MTYIVQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTS----YEVL 76
Cdd:PRK11831 4 VANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsrlYTVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 77 GNIGSMIEYPIFYENLTAEEN----LDLHCEYMGYHNKKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPD 152
Cdd:PRK11831 84 KRMSMLFQSGALFTDMNVFDNvaypLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255767068 153 LLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDVR 221
Cdd:PRK11831 164 LIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQ 232
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
8-203 |
9.42e-21 |
|
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: 92.35 E-value: 9.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 8 NGLTKTYQGK-EVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGN-IGSMIEY 85
Cdd:TIGR02857 325 SGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDqIAWVPQH 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 86 PIFYENlTAEENLDLhceYMGYHNKKAIQEVLDMVNL------------KQIDKKPVKtFSLGMKQRLGIARAILTKPDL 153
Cdd:TIGR02857 405 PFLFAG-TIAENIRL---ARPDASDAEIREALERAGLdefvaalpqgldTPIGEGGAG-LSGGQAQRLALARAFLRDAPL 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 255767068 154 LILDEPVNGLDP----LGIKKIRQLFQvlskeyGMTLLISSHLLGEIEQiADTI 203
Cdd:TIGR02857 480 LLLDEPTAHLDAeteaEVLEALRALAQ------GRTVLLVTHRLALAAL-ADRI 526
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
22-252 |
1.03e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 89.89 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 22 NVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFT-HTSYEVLGNI----GSMIEYP--IFYENlTA 94
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpETGNKNLKKLrkkvSLVFQFPeaQLFEN-TV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 95 EENLDLHCEYMGYHNKKAIQEVLD---MVNLKQ--IDKKPVKtFSLGMKQRLGIARAILTKPDLLILDEPVNGLDPLGIK 169
Cdd:PRK13641 104 LKDVEFGPKNFGFSEDEAKEKALKwlkKVGLSEdlISKSPFE-LSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 170 KIRQLFQVLSKEyGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDVRgQNTEYIE---LVTPNQTRacfvLEKEL 246
Cdd:PRK13641 183 EMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIF-SDKEWLKkhyLDEPATSR----FASKL 256
|
....*.
gi 255767068 247 QLTNFK 252
Cdd:PRK13641 257 EKGGFK 262
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
6-214 |
1.18e-20 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 89.36 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 6 QTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNIGSMIEY 85
Cdd:PRK10419 14 AHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRDIQM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 86 pIFYENLTA-----------EENLDlHCEYMGYHNKKA-IQEVLDMVNLKQ--IDKKPvKTFSLGMKQRLGIARAILTKP 151
Cdd:PRK10419 94 -VFQDSISAvnprktvreiiREPLR-HLLSLDKAERLArASEMLRAVDLDDsvLDKRP-PQLSGGQLQRVCLARALAVEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255767068 152 DLLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEE 214
Cdd:PRK10419 171 KLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVET 233
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-198 |
1.25e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 88.99 E-value: 1.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 4 IVQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYE---VLGNIG 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAErgvVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 81 SMieyPifYENLTAEENLDLHCEYMGYHNKKAI-QEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEP 159
Cdd:PRK11248 81 LL---P--WRNVQDNVAFGLQLAGVEKMQRLEIaHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEP 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 255767068 160 VNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHllgEIEQ 198
Cdd:PRK11248 156 FGALDAFTREQMQTLLLKLWQETGKQVLLITH---DIEE 191
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
15-191 |
2.35e-20 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 88.38 E-value: 2.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 15 QGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYE---VLGNIGSMieyPIfyen 91
Cdd:COG4525 18 QPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADrgvVFQKDALL---PW---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 92 LTAEEN--LDLHCEYMGYHNKKAI-QEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLDPLGI 168
Cdd:COG4525 91 LNVLDNvaFGLRLRGVPKAERRARaEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTR 170
|
170 180
....*....|....*....|...
gi 255767068 169 KKIRQLFQVLSKEYGMTLLISSH 191
Cdd:COG4525 171 EQMQELLLDVWQRTGKGVFLITH 193
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-220 |
2.47e-20 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 87.83 E-value: 2.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 5 VQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLG------- 77
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAkrlailr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 78 ---NIGSMI---------EYPIFYENLTAEEnldlhceymgyhnKKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIAR 145
Cdd:COG4604 82 qenHINSRLtvrelvafgRFPYSKGRLTAED-------------REIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 146 AILTKPDLLILDEPVNGLDplgIKKIRQLFQVL---SKEYGMTLLISSHllgeieQI------ADTIGVIRDGRLLEEVS 216
Cdd:COG4604 149 VLAQDTDYVLLDEPLNNLD---MKHSVQMMKLLrrlADELGKTVVIVLH------DInfascyADHIVAMKDGRVVAQGT 219
|
....
gi 255767068 217 MEDV 220
Cdd:COG4604 220 PEEI 223
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
16-230 |
2.61e-20 |
|
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: 87.67 E-value: 2.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 16 GKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILG---NKFTHTSYE----------VLGNigSM 82
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdiREVTLDSLRraigvvpqdtVLFN--DT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 83 IEYPIFYENLTAEEnldlhceymgyhnkkaiQEVLDMVNLKQIDKKpVKTF---------------SLGMKQRLGIARAI 147
Cdd:cd03253 91 IGYNIRYGRPDATD-----------------EEVIEAAKAAQIHDK-IMRFpdgydtivgerglklSGGEKQRVAIARAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 148 LTKPDLLILDEPVNGLDPLGIKKIRQLFQVLSKeyGMTLLISSHLLGEIEQiADTIGVIRDGRLLEEVSMEDVRGQNTEY 227
Cdd:cd03253 153 LKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLAKGGLY 229
|
...
gi 255767068 228 IEL 230
Cdd:cd03253 230 AEM 232
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
5-243 |
2.73e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 89.76 E-value: 2.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 5 VQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLgNIGSMIE 84
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDR-KVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 85 YPIFYENLTAEEN-------LDLHCEYMGYHNKKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILD 157
Cdd:PRK10851 82 HYALFRHMTVFDNiafgltvLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 158 EPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRlleevsmedvrgqnteyIELV-TPNQ- 235
Cdd:PRK10851 162 EPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGN-----------------IEQAgTPDQv 224
|
250
....*....|...
gi 255767068 236 -----TRacFVLE 243
Cdd:PRK10851 225 wrepaTR--FVLE 235
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
16-220 |
3.25e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 90.47 E-value: 3.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 16 GKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSyevlgnIGSMIEYPIFY------ 89
Cdd:COG3845 270 GVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLS------PRERRRLGVAYipedrl 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 90 -----ENLTAEENLDLhceymGYHNKKAIQEVLdMVNLKQIDKK-----------------PVKTFSLGMKQRLGIARAI 147
Cdd:COG3845 344 grglvPDMSVAENLIL-----GRYRRPPFSRGG-FLDRKAIRAFaeelieefdvrtpgpdtPARSLSGGNQQKVILAREL 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255767068 148 LTKPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEyGMT-LLISSHlLGEIEQIADTIGVIRDGRLLEEVSMEDV 220
Cdd:COG3845 418 SRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAvLLISED-LDEILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
16-191 |
5.07e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 86.08 E-value: 5.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 16 GKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYevlgniGSMIEY--------Pi 87
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDV------AEACHYlghrnamkP- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 88 fyeNLTAEENLDLHCEYMGYHNkKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLDPLG 167
Cdd:PRK13539 87 ---ALTVAENLEFWAAFLGGEE-LDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAA 162
|
170 180
....*....|....*....|....
gi 255767068 168 IKKIRQLFQVLSKEYGMtLLISSH 191
Cdd:PRK13539 163 VALFAELIRAHLAQGGI-VIAATH 185
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
4-220 |
5.30e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 87.55 E-value: 5.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 4 IVQTNGLTKTYQG--KEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGE---IIILGNKFTH-TSYEVLG 77
Cdd:PRK13640 5 IVEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAkTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 78 NIGSMIEYPifyEN----LTAEENLDLHCEYMGYHNKKAIQEVLDMVN----LKQIDKKPvKTFSLGMKQRLGIARAILT 149
Cdd:PRK13640 85 KVGIVFQNP---DNqfvgATVGDDVAFGLENRAVPRPEMIKIVRDVLAdvgmLDYIDSEP-ANLSGGQKQRVAIAGILAV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255767068 150 KPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQiADTIGVIRDGRLLEEVSMEDV 220
Cdd:PRK13640 161 EPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEI 230
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
8-187 |
5.55e-20 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 86.06 E-value: 5.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 8 NGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNkfTHTSYEVLGNIGSMIEYPI 87
Cdd:PRK13543 15 HALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK--TATRGDRSRFMAYLGHLPG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 88 FYENLTAEENLDLHCEYMGYHNKKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLDPLG 167
Cdd:PRK13543 93 LKADLSTLENLHFLCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEG 172
|
170 180
....*....|....*....|
gi 255767068 168 IKKIRQLFQVLSKEYGMTLL 187
Cdd:PRK13543 173 ITLVNRMISAHLRGGGAALV 192
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-232 |
5.75e-20 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 86.82 E-value: 5.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 18 EVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKF-THTSYEVLGNIGSMIEYPIFYENlTAEE 96
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIrDLNLRWLRSQIGLVSQEPVLFDG-TIAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 97 NLdlhceymGYHNKKAIQEVLDMVNLKQ-----IDKKPVK----------TFSLGMKQRLGIARAILTKPDLLILDEPVN 161
Cdd:cd03249 96 NI-------RYGKPDATDEEVEEAAKKAnihdfIMSLPDGydtlvgergsQLSGGQKQRIAIARALLRNPKILLLDEATS 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255767068 162 GLDPLGIKKIRQLFQVLSKeyGMTLLISSHLLGEIeQIADTIGVIRDGRLLEEVSMEDVRGQNTEYIELVT 232
Cdd:cd03249 169 ALDAESEKLVQEALDRAMK--GRTTIVIAHRLSTI-RNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVK 236
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-230 |
6.02e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 89.88 E-value: 6.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 5 VQTNGLTKTY--QGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNIGSM 82
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 83 IEYPIFYENLTAEENLDLHCEYMgyhNKKAIQEVLDMVNLKQI--DKKPVKTF--------SLGMKQRLGIARAILTKPD 152
Cdd:PRK11160 419 VSQRVHLFSATLRDNLLLAAPNA---SDEALIEVLQQVGLEKLleDDKGLNAWlgeggrqlSGGEQRRLGIARALLHDAP 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255767068 153 LLILDEPVNGLDPLGIKKIRQLFQVLSKeyGMTLLISSHLLGEIEQIaDTIGVIRDGRLLEEVSMEDVRGQNTEYIEL 230
Cdd:PRK11160 496 LLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-220 |
6.22e-20 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 87.15 E-value: 6.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 1 MTYIVQTNGLTKTY---------QGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTH- 70
Cdd:PRK15112 1 VETLLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 71 -----------------TSYEVLGNIGSMIEYPifyenltaeenLDLHCEYMGYHNKKAIQEVLDMVNLK--QIDKKPvK 131
Cdd:PRK15112 81 dysyrsqrirmifqdpsTSLNPRQRISQILDFP-----------LRLNTDLEPEQREKQIIETLRQVGLLpdHASYYP-H 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 132 TFSLGMKQRLGIARAILTKPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRL 211
Cdd:PRK15112 149 MLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEV 228
|
....*....
gi 255767068 212 LEEVSMEDV 220
Cdd:PRK15112 229 VERGSTADV 237
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
5-213 |
6.69e-20 |
|
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: 86.01 E-value: 6.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 5 VQTNGLTKTY--QGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNIGSM 82
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 83 I-EYPIFYENlTAEENLDLHCEymgyHNKKAIQEVLDMVNLKQ-IDKKPVK----------TFSLGMKQRLGIARAILTK 150
Cdd:cd03244 83 IpQDPVLFSG-TIRSNLDPFGE----YSDEELWQALERVGLKEfVESLPGGldtvveeggeNLSVGQRQLLCLARALLRK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255767068 151 PDLLILDEPVNGLDPLGIKKIRqlfQVLSKEY-GMTLLISSHLLGEIEQiADTIGVIRDGRLLE 213
Cdd:cd03244 158 SKILVLDEATASVDPETDALIQ---KTIREAFkDCTVLTIAHRLDTIID-SDRILVLDKGRVVE 217
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-214 |
6.76e-20 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 86.69 E-value: 6.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 4 IVQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLG---NIG 80
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLirqEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 81 SMIEYPIFYENLTAEENL---DLHCEYMGYHNKKAI-QEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLIL 156
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVmfgPLRVRGASKEEAEKQaRELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 255767068 157 DEPVNGLDPLGIKKIRQLFQVLSKEyGMTLLISSHLLGEIEQIADTIGVIRDGRLLEE 214
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAED 217
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
16-218 |
7.41e-20 |
|
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: 85.27 E-value: 7.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 16 GKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLT--SLVKPTSGEIIILGNKFTHTSYEV---LGnIGSMIEYPIFYE 90
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMghPKYEVTEGEILFKGEDITDLPPEErarLG-IFLAFQYPPEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 91 NLTaeenldlhceymgyhnkkaIQEVLDMVNlkqidkkpvKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLDPLGIKK 170
Cdd:cd03217 91 GVK-------------------NADFLRYVN---------EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 255767068 171 IRQLFQVLSKEyGMTLLISSHLLGEIEQI-ADTIGVIRDGRLLEEVSME 218
Cdd:cd03217 143 VAEVINKLREE-GKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKE 190
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-193 |
8.79e-20 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 86.32 E-value: 8.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 1 MTYIVQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIilgnkftHTSYEVLGNIG 80
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-------RNGKLRIGYVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 81 SMIEYPIFYEnLTAEENLDLHceymGYHNKKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPV 160
Cdd:PRK09544 74 QKLYLDTTLP-LTVNRFLRLR----PGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPT 148
|
170 180 190
....*....|....*....|....*....|...
gi 255767068 161 NGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLL 193
Cdd:PRK09544 149 QGVDVNGQVALYDLIDQLRRELDCAVLMVSHDL 181
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
15-211 |
1.21e-19 |
|
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: 85.33 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 15 QGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVL-GNIGSMIEYP-IFYENL 92
Cdd:cd03245 15 QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLrRNIGYVPQDVtLFYGTL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 93 taEENLDLHCeymGYHNKKAIQEVLDMVNLKQIDKKPVKTFSL-----------GMKQRLGIARAILTKPDLLILDEPVN 161
Cdd:cd03245 95 --RDNITLGA---PLADDERILRAAELAGVTDFVNKHPNGLDLqigergrglsgGQRQAVALARALLNDPPILLLDEPTS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 255767068 162 GLDPLGIKK-IRQLFQVLSkeyGMTLLISSH---LLgeieQIADTIGVIRDGRL 211
Cdd:cd03245 170 AMDMNSEERlKERLRQLLG---DKTLIIITHrpsLL----DLVDRIIVMDSGRI 216
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-213 |
1.45e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 85.87 E-value: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 17 KEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVK------PTSGEIIILGNK-FTHTSYEVLGNIGSMIEYPIFY 89
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDiFQIDAIKLRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 90 ENLTAEENLDLHCEYMGYHNKKAI----QEVLDMVNL-KQIDKK---PVKTFSLGMKQRLGIARAILTKPDLLILDEPVN 161
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHGIKEKREIkkivEECLRKVGLwKEVYDRlnsPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 255767068 162 GLDPLGIKKIRQLFQVLSKEygMTLLISSHLLGEIEQIADTIGVIRDGRLLE 213
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVE 232
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
9-211 |
1.86e-19 |
|
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: 83.80 E-value: 1.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 9 GLTKTYQGKE--VVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSyevLGNIGSMIEYP 86
Cdd:cd03246 5 NVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWD---PNELGDHVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 87 IFYENL---TAEENLdlhceymgyhnkkaiqevldmvnlkqidkkpvktFSLGMKQRLGIARAILTKPDLLILDEPVNGL 163
Cdd:cd03246 82 PQDDELfsgSIAENI----------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHL 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 255767068 164 DPLGIKKIRQLFQVLsKEYGMTLLISSHLLGEIEQiADTIGVIRDGRL 211
Cdd:cd03246 128 DVEGERALNQAIAAL-KAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-211 |
2.27e-19 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 85.02 E-value: 2.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 24 SMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTS---YEVlgnigSMieypIFYEN-----LTAE 95
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPpsrRPV-----SM----LFQENnlfshLTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 96 ENLDLhceymGYH--------NKKAIQEVLDMVNLK-QIDKKPVKtFSLGMKQRLGIARAILTKPDLLILDEPVNGLDPL 166
Cdd:PRK10771 90 QNIGL-----GLNpglklnaaQREKLHAIARQMGIEdLLARLPGQ-LSGGQRQRVALARCLVREQPILLLDEPFSALDPA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 255767068 167 GIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRL 211
Cdd:PRK10771 164 LRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
17-166 |
2.34e-19 |
|
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: 84.63 E-value: 2.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 17 KEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLV---KPTSGEIIILGNKFThtSYEVLGNIGSMIEYPIFYENLT 93
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQPRK--PDQFQKCVAYVRQDDILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 94 AEENL--DLHCEyMGYHNKKAI------QEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLDP 165
Cdd:cd03234 98 VRETLtyTAILR-LPRKSSDAIrkkrveDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
.
gi 255767068 166 L 166
Cdd:cd03234 177 F 177
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
22-220 |
2.71e-19 |
|
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: 86.69 E-value: 2.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 22 NVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGnkfthtsyEVLGNIGSMIEYP--------IFYE--- 90
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGG--------EVLQDSARGIFLPphrrrigyVFQEarl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 91 --NLTAEENLdlhcEYmGYHNKKAIQ------EVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVNG 162
Cdd:COG4148 89 fpHLSVRGNL----LY-GRKRAPRAErrisfdEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 255767068 163 LDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDV 220
Cdd:COG4148 164 LDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEV 221
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-213 |
2.77e-19 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 87.40 E-value: 2.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 20 VSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVL-----GNIGSMIEYPIFYENLTA 94
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrrKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 95 EENLDLHCEYMGYHNKKAIQEVLD---MVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLDPLGIKKI 171
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDalrQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 255767068 172 RQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLE 213
Cdd:PRK10070 204 QDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQ 245
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
17-231 |
2.85e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 88.24 E-value: 2.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 17 KEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILG---NKFTHTSYEVlgNIGSMIEYPIFYeNLT 93
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvplVQYDHHYLHR--QVALVGQEPVLF-SGS 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 94 AEENLDLHCEYM------------GYHNkkAIQEVLDMVNlKQIDKKPVKtFSLGMKQRLGIARAILTKPDLLILDEPVN 161
Cdd:TIGR00958 571 VRENIAYGLTDTpdeeimaaakaaNAHD--FIMEFPNGYD-TEVGEKGSQ-LSGGQKQRIAIARALVRKPRVLILDEATS 646
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 162 GLDplgiKKIRQLFQVLSKEYGMTLLISSHLLGEIEQiADTIGVIRDGRLLEEVSMEDVRGQNTEYIELV 231
Cdd:TIGR00958 647 ALD----AECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-231 |
3.83e-19 |
|
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: 84.46 E-value: 3.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 16 GKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVL-GNIGSMIEYPIFYeNLTA 94
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLrRQVGVVLQENVLF-NRSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 95 EENLDLHCEYMGYHNkkaIQEVLDMVNLKQ-IDKKPV----------KTFSLGMKQRLGIARAILTKPDLLILDEPVNGL 163
Cdd:cd03252 93 RDNIALADPGMSMER---VIEAAKLAGAHDfISELPEgydtivgeqgAGLSGGQRQRIAIARALIHNPRILIFDEATSAL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255767068 164 DPLGIKKIRQLFQVLSKeyGMTLLISSHLLGEIEQiADTIGVIRDGRLLEEVSMEDVRGQNTEYIELV 231
Cdd:cd03252 170 DYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAENGLYAYLY 234
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
5-225 |
5.33e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 84.83 E-value: 5.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 5 VQTNGLTKTYQG-----KEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYE----- 74
Cdd:PRK13646 3 IRFDNVSYTYQKgtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDkyirp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 75 VLGNIGSMIEYP---IFYENLTAE-----ENLDLHCEYMgyhNKKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARA 146
Cdd:PRK13646 83 VRKRIGMVFQFPesqLFEDTVEREiifgpKNFKMNLDEV---KNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255767068 147 ILTKPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDVRGQNT 225
Cdd:PRK13646 160 LAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKK 238
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-220 |
8.22e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 86.21 E-value: 8.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 20 VSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKF-THTSYEVLGNigsmieyPIFY--EN----- 91
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvTRSPQDGLAN-------GIVYisEDrkrdg 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 92 ----LTAEENLDL----HCEYMGYHNKKA--IQEVLDMVNLKQID----KKPVKTFSLGMKQRLGIARAILTKPDLLILD 157
Cdd:PRK10762 341 lvlgMSVKENMSLtalrYFSRAGGSLKHAdeQQAVSDFIRLFNIKtpsmEQAIGLLSGGNQQKVAIARGLMTRPKVLILD 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255767068 158 EPVNGLDpLGIKK-IRQLFQVLSKEyGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDV 220
Cdd:PRK10762 421 EPTRGVD-VGAKKeIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTREQA 482
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
9-219 |
8.46e-19 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 86.32 E-value: 8.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 9 GLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFT-HTSYEVLGNIGSMIEypi 87
Cdd:PRK10982 3 NISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVH--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 88 fyenltAEENLDLHCEYMG-------------------YHNKKAIQEVLDMvnlkQID-KKPVKTFSLGMKQRLGIARAI 147
Cdd:PRK10982 80 ------QELNLVLQRSVMDnmwlgryptkgmfvdqdkmYRDTKAIFDELDI----DIDpRAKVATLSVSQMQMIEIAKAF 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255767068 148 LTKPDLLILDEPVNGLDPlgiKKIRQLFQVLSK--EYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMED 219
Cdd:PRK10982 150 SYNAKIVIMDEPTSSLTE---KEVNHLFTIIRKlkERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAG 220
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-219 |
1.09e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 85.83 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 1 MTYIVQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNIG 80
Cdd:PRK10762 1 MQALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 81 SMIeypIFYE-----NLTAEENLDLHCEY---MGYHN-KKAIQE---VLDMVNLKQIDKKPVKTFSLGMKQRLGIARAIL 148
Cdd:PRK10762 81 IGI---IHQElnlipQLTIAENIFLGREFvnrFGRIDwKKMYAEadkLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLS 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255767068 149 TKPDLLILDEPVnglDPLGIKKIRQLFQVLS--KEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMED 219
Cdd:PRK10762 158 FESKVIIMDEPT---DALTDTETESLFRVIRelKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVAD 227
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
6-220 |
1.56e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 83.28 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 6 QTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNIGSM--- 82
Cdd:PRK13548 4 EARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVlpq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 83 ---IEYPifyenLTAEE----NLDLHCEYMGyHNKKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAI--LTKPD- 152
Cdd:PRK13548 84 hssLSFP-----FTVEEvvamGRAPHGLSRA-EDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLaqLWEPDg 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255767068 153 ---LLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDV 220
Cdd:PRK13548 158 pprWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEV 228
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
16-212 |
2.01e-18 |
|
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: 81.44 E-value: 2.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 16 GKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKP--TSGEIIILGNKFTHTSYEVLgnIGSMIEYPIFYENLT 93
Cdd:cd03213 21 GKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDKRSFRKI--IGYVPQDDILHPTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 94 AEENLDLHceymgyhnkkaiqevldmVNLKQIdkkpvktfSLGMKQRLGIARAILTKPDLLILDEPVNGLDPLGIKKIRQ 173
Cdd:cd03213 99 VRETLMFA------------------AKLRGL--------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMS 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 255767068 174 LFQVLSKEyGMTLLISSH-LLGEIEQIADTIGVIRDGRLL 212
Cdd:cd03213 153 LLRRLADT-GRTIICSIHqPSSEIFELFDKLLLLSQGRVI 191
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-230 |
2.13e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 83.22 E-value: 2.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 1 MTYIVQTNGLTKTYQGKEVVSN---VSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFT-HTSYEVL 76
Cdd:PRK13642 1 MNKILEVENLVFKYEKESDVNQlngVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTaENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 77 GNIGSMIEYPIF-YENLTAEENLDLHCEYMGYHNK---KAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPD 152
Cdd:PRK13642 81 RKIGMVFQNPDNqFVGATVEDDVAFGMENQGIPREemiKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255767068 153 LLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQiADTIGVIRDGRLLEEVSMEDVRGQNTEYIEL 230
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDMVEI 237
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
20-270 |
2.14e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 83.52 E-value: 2.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 20 VSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEV---------LGNIGSMIEYPIFYE 90
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIkevkrlrkeIGLVFQFPEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 91 nlTAEENLDLHCEYMGYHNKKAIQEVLDMVNLKQIDKKPVK----TFSLGMKQRLGIARAILTKPDLLILDEPVNGLDPL 166
Cdd:PRK13645 107 --TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKrspfELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPK 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 167 GIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDVRGQnteyIELVTPNQTR--ACFVLEK 244
Cdd:PRK13645 185 GEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN----QELLTKIEIDppKLYQLMY 260
|
250 260
....*....|....*....|....*.
gi 255767068 245 ELQLTNFKILNeKTIRIYEAEASQAA 270
Cdd:PRK13645 261 KLKNKGIDLLN-KNIRTIEEFAKELA 285
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
4-228 |
2.80e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 82.52 E-value: 2.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 4 IVQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSL--VKP---TSGEIIILGnkftHTSY----- 73
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPevtITGSIVYNG----HNIYsprtd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 74 --EVLGNIGSMIEYPIFYEnLTAEENLDLHCEYMGYHNKKAIQEVLDMvNLKQIDK-KPVK--------TFSLGMKQRLG 142
Cdd:PRK14239 81 tvDLRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVEK-SLKGASIwDEVKdrlhdsalGLSGGQQQRVC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 143 IARAILTKPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYgmTLLISSHLLGEIEQIADTIGVIRDGRLLE-----EVSM 217
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEyndtkQMFM 236
|
250
....*....|.
gi 255767068 218 EDVRGQNTEYI 228
Cdd:PRK14239 237 NPKHKETEDYI 247
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
10-211 |
4.27e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 81.07 E-value: 4.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 10 LTKTY-QGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTH-TSYEV---LGNIGSMIE 84
Cdd:PRK10908 7 VSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRlKNREVpflRRQIGMIFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 85 YPIFYENLTAEENLDLHCEYMGYHN---KKAIQEVLDMVNLkqIDKK---PVKtFSLGMKQRLGIARAILTKPDLLILDE 158
Cdd:PRK10908 87 DHHLLMDRTVYDNVAIPLIIAGASGddiRRRVSAALDKVGL--LDKAknfPIQ-LSGGEQQRVGIARAVVNKPAVLLADE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 255767068 159 PVNGLDPLGIKKIRQLFQVLSKeYGMTLLISSHLLGEIEQIADTIGVIRDGRL 211
Cdd:PRK10908 164 PTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
22-244 |
4.97e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 82.47 E-value: 4.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 22 NVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYE-----VLGNIGSMIEYP---IFYENLT 93
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQkeikpVRKKVGVVFQFPesqLFEETVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 94 AE-----ENLDLHCEymgyHNKKAIQEVLDMVNL-KQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLDPLG 167
Cdd:PRK13643 104 KDvafgpQNFGIPKE----KAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 168 IKKIRQLFQVLsKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDVRgQNTEYI---ELVTPNQTRACFVLEK 244
Cdd:PRK13643 180 RIEMMQLFESI-HQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF-QEVDFLkahELGVPKATHFADQLQK 257
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
17-191 |
5.81e-18 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 80.77 E-value: 5.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 17 KEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVK--PTSGEIIILGNKFthtsyevlgnigsmieypifYENLTA 94
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQF--------------------GREASL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 95 EENLDLHceymgyHNKKAIQEVLDMVNLK--QIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLDPLGIKKIR 172
Cdd:COG2401 103 IDAIGRK------GDFKDAVELLNAVGLSdaVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVA 176
|
170
....*....|....*....
gi 255767068 173 QLFQVLSKEYGMTLLISSH 191
Cdd:COG2401 177 RNLQKLARRAGITLVVATH 195
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
10-218 |
5.88e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 82.44 E-value: 5.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 10 LTKTYQGK-----EVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIIL-----GNKFTHTSYEVL--- 76
Cdd:PRK13651 8 IVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIfkdekNKKKTKEKEKVLekl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 77 --------------------GNIGSMIEYPIFYEnlTAEENLDLHCEYMGYHNKKAIQ---EVLDMVNLKQ--IDKKPVK 131
Cdd:PRK13651 88 viqktrfkkikkikeirrrvGVVFQFAEYQLFEQ--TIEKDIIFGPVSMGVSKEEAKKraaKYIELVGLDEsyLQRSPFE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 132 tFSLGMKQRLGIARAILTKPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEyGMTLLISSHLL---------------GEI 196
Cdd:PRK13651 166 -LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLdnvlewtkrtiffkdGKI 243
|
250 260
....*....|....*....|..
gi 255767068 197 EQIADTIGVIRDGRLLEEVSME 218
Cdd:PRK13651 244 IKDGDTYDILSDNKFLIENNME 265
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-214 |
6.52e-18 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 81.33 E-value: 6.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 1 MTYIVQTNgLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTS-----GEIIILGNK-------- 67
Cdd:PRK11264 1 MSAIEVKN-LVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAgtirvGDITIDTARslsqqkgl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 68 -----------------FTHTSyeVLGNIgsmIEYPIFYENLTAEENLDLHceymgyhnkkaiQEVLDMVNLKQIDKKPV 130
Cdd:PRK11264 80 irqlrqhvgfvfqnfnlFPHRT--VLENI---IEGPVIVKGEPKEEATARA------------RELLAKVGLAGKETSYP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 131 KTFSLGMKQRLGIARAILTKPDLLILDEPVNGLDP--LG--IKKIRQLfqvlsKEYGMTLLISSHLLGEIEQIADTIGVI 206
Cdd:PRK11264 143 RRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPelVGevLNTIRQL-----AQEKRTMVIVTHEMSFARDVADRAIFM 217
|
....*...
gi 255767068 207 RDGRLLEE 214
Cdd:PRK11264 218 DQGRIVEQ 225
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-213 |
9.09e-18 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 81.13 E-value: 9.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 1 MTYIVQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVL---- 76
Cdd:PRK11701 3 DQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseae 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 77 ---------------------------GNIGsmieypifyENLTAeenldlhceyMGYHNKKAIQEV----LDMVNL--K 123
Cdd:PRK11701 83 rrrllrtewgfvhqhprdglrmqvsagGNIG---------ERLMA----------VGARHYGDIRATagdwLERVEIdaA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 124 QIDKKPvKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTI 203
Cdd:PRK11701 144 RIDDLP-TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRL 222
|
250
....*....|
gi 255767068 204 GVIRDGRLLE 213
Cdd:PRK11701 223 LVMKQGRVVE 232
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
22-249 |
1.10e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 81.22 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 22 NVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIIlGNKF--THTSYEVLGNI----GSMIEYP---IFYEnl 92
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVitAGKKNKKLKPLrkkvGIVFQFPehqLFEE-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 93 TAEENLDLHCEYMGYHNKKAIQ---EVLDMVNLKQ--IDKKPvktFSL--GMKQRLGIARAILTKPDLLILDEPVNGLDP 165
Cdd:PRK13634 102 TVEKDICFGPMNFGVSEEDAKQkarEMIELVGLPEelLARSP---FELsgGQMRRVAIAGVLAMEPEVLVLDEPTAGLDP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 166 LGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDV--RGQNTEYIELVTPNQTRACFVLE 243
Cdd:PRK13634 179 KGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIfaDPDELEAIGLDLPETVKFKRALE 258
|
....*.
gi 255767068 244 KELQLT 249
Cdd:PRK13634 259 EKFGIS 264
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
9-240 |
1.35e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 82.20 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 9 GLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGN-IGSMIEYPI 87
Cdd:PRK09536 8 DLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRrVASVPQDTS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 88 FYENLTAEENLDL----HCEYMGYH---NKKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPV 160
Cdd:PRK09536 88 LSFEFDVRQVVEMgrtpHRSRFDTWtetDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 161 NGLDPLGIKKIRQLFQVLSKEyGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDVrgqnteyielVTPNQTRACF 240
Cdd:PRK09536 168 ASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV----------LTADTLRAAF 236
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
4-211 |
1.51e-17 |
|
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: 79.82 E-value: 1.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 4 IVQTNGLTKTYQGK---EVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNIG 80
Cdd:cd03248 11 IVKFQNVTFAYPTRpdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 81 SMI-EYPIFYENlTAEENLDL---HCEYM-------GYHNKKAIQEVLDMVNlKQIDKKPVKtFSLGMKQRLGIARAILT 149
Cdd:cd03248 91 SLVgQEPVLFAR-SLQDNIAYglqSCSFEcvkeaaqKAHAHSFISELASGYD-TEVGEKGSQ-LSGGQKQRVAIARALIR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255767068 150 KPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYgmTLLISSHLLGEIEQiADTIGVIRDGRL 211
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-212 |
1.62e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 80.44 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 1 MTYIVQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLvkptsgeiiILGNKFTHTSYEVLGN-- 78
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL---------ITGDKSAGSHIELLGRtv 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 79 ----------------IGSMIEYPIFYENLTAEENLDLHC-----------EYMGYHNKKAIQEVLDMVNLKQIDKKPVK 131
Cdd:PRK09984 72 qregrlardirksranTGYIFQQFNLVNRLSVLENVLIGAlgstpfwrtcfSWFTREQKQRALQALTRVGMVHFAHQRVS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 132 TFSLGMKQRLGIARAILTKPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRL 211
Cdd:PRK09984 152 TLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
.
gi 255767068 212 L 212
Cdd:PRK09984 232 F 232
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
10-223 |
2.24e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 80.01 E-value: 2.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 10 LTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNK-------------FTHTSYEVL 76
Cdd:PRK10619 11 LHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlvrdkdgqlkvADKNQLRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 77 GNIGSMI-EYPIFYENLTAEEN-LDLHCEYMGYHNKKAIQEVLDMVNLKQID-----KKPVKtFSLGMKQRLGIARAILT 149
Cdd:PRK10619 91 RTRLTMVfQHFNLWSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIDeraqgKYPVH-LSGGQQQRVSIARALAM 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255767068 150 KPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEyGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDVRGQ 223
Cdd:PRK10619 170 EPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGN 242
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
22-228 |
2.58e-17 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 79.86 E-value: 2.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 22 NVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIiilgnkfthtsyEVLGNIGSMIEYPIFYENLTAEENLDLH 101
Cdd:PRK13546 42 DISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV------------DRNGEVSVIAISAGLSGQLTGIENIEFK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 102 CEYMGYHNK---KAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVN-GLDPLGIKKIRQLFQV 177
Cdd:PRK13546 110 MLCMGFKRKeikAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSvGDQTFAQKCLDKIYEF 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 255767068 178 lsKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDVRGQNTEYI 228
Cdd:PRK13546 190 --KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKYEAFL 238
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-220 |
3.10e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 79.75 E-value: 3.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 10 LTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEI----IILGNKFTHTSYEVLG---NIGSM 82
Cdd:PRK14271 27 LTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRysgdVLLGGRSIFNYRDVLEfrrRVGML 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 83 IEYP-----IFYENLTA---EENLDLHCEYMGYHNKKAIQEVLDMVNLKQIDKKPVKtFSLGMKQRLGIARAILTKPDLL 154
Cdd:PRK14271 107 FQRPnpfpmSIMDNVLAgvrAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFR-LSGGQQQLLCLARTLAVNPEVL 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255767068 155 ILDEPVNGLDPLGIKKIRQLFQVLSKEygMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDV 220
Cdd:PRK14271 186 LLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
8-201 |
3.20e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 79.93 E-value: 3.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 8 NGLTKTYQ-GKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNIGSMIE-- 84
Cdd:PRK15056 10 NDVTVTWRnGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQSEev 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 85 ---YPIFYENLTAEENLDlhceYMGY------HNKKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLI 155
Cdd:PRK15056 90 dwsFPVLVEDVVMMGRYG----HMGWlrrakkRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVIL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 255767068 156 LDEPVNGLDPLGIKKIRQLFQVLSKEyGMTLLISSHLLGEIEQIAD 201
Cdd:PRK15056 166 LDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCD 210
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
14-193 |
3.23e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 78.45 E-value: 3.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 14 YQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILG---NKFTHTSYEVLGNIG--SMIEypif 88
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERqsiKKDLCTYQKQLCFVGhrSGIN---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 89 yENLTAEEN--LDLHCEymgyHNKKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLDPL 166
Cdd:PRK13540 87 -PYLTLRENclYDIHFS----PGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDEL 161
|
170 180
....*....|....*....|....*..
gi 255767068 167 GIKKIRQLFQVLSKEYGMTLLISSHLL 193
Cdd:PRK13540 162 SLLTIITKIQEHRAKGGAVLLTSHQDL 188
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-210 |
3.82e-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: 3.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 1 MTYIVQTNGLTKTY-----QGKE--VVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIIlgnkftHTSY 73
Cdd:COG4778 1 MTTLLEVENLSKTFtlhlqGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILV------RHDG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 74 EVLgNIGSMIEYPIFY---------------------ENLTAEENLDlhceyMGYHNKKAIQEVLDMVNLKQIDKK---- 128
Cdd:COG4778 75 GWV-DLAQASPREILAlrrrtigyvsqflrviprvsaLDVVAEPLLE-----RGVDREEARARARELLARLNLPERlwdl 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 129 PVKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLDPLGIKKIRQLFQVLsKEYGMTLLISSHLLGEIEQIADTIGVIRD 208
Cdd:COG4778 149 PPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDEEVREAVADRVVDVTP 227
|
..
gi 255767068 209 GR 210
Cdd:COG4778 228 FS 229
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
4-215 |
5.59e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 78.28 E-value: 5.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 4 IVQTNGLTKTY-QGKEVVS---NVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLG-- 77
Cdd:PRK10584 6 IVEVHHLKKSVgQGEHELSiltGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAkl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 78 ---NIGSMIEYPIFYENLTAEENLDLHCEYMG---YHNKKAIQEVLDMVNL-KQIDKKPVKtFSLGMKQRLGIARAILTK 150
Cdd:PRK10584 86 rakHVGFVFQSFMLIPTLNALENVELPALLRGessRQSRNGAKALLEQLGLgKRLDHLPAQ-LSGGEQQRVALARAFNGR 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255767068 151 PDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHllgeIEQIA---DTIGVIRDGRLLEEV 215
Cdd:PRK10584 165 PDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTH----DLQLAarcDRRLRLVNGQLQEEA 228
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
4-187 |
6.59e-17 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 77.82 E-value: 6.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 4 IVQTNGLTKTY-----QGKE--VVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNK-----FTHT 71
Cdd:TIGR02324 1 LLEVEDLSKTFtlhqqGGVRlpVLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRILVRHEGawvdlAQAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 72 SYEVLGNIGSMIEY-PIFYENLTAEENLDLHCE---YMGYHNKKAIQEVLDMVNLKQIDKK----PVKTFSLGMKQRLGI 143
Cdd:TIGR02324 81 PREVLEVRRKTIGYvSQFLRVIPRVSALEVVAEpllERGVPREAARARARELLARLNIPERlwhlPPATFSGGEQQRVNI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 255767068 144 ARAILTKPDLLILDEPVNGLDPLGIKKIRQLFQVLsKEYGMTLL 187
Cdd:TIGR02324 161 ARGFIADYPILLLDEPTASLDAANRQVVVELIAEA-KARGAALI 203
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
16-232 |
7.75e-17 |
|
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: 80.94 E-value: 7.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 16 GKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVL-GNIGSMIEYPIFYENlTA 94
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLrQFINYLPQEPYIFSG-SI 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 95 EENLdlhceYMGYHNKKAIQEVLDMVNLKQIDKKPVK--------------TFSLGMKQRLGIARAILTKPDLLILDEPV 160
Cdd:TIGR01193 565 LENL-----LLGAKENVSQDEIWAACEIAEIKDDIENmplgyqtelseegsSISGGQKQRIALARALLTDSKVLILDEST 639
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255767068 161 NGLDPLGIKKI-RQLFQVLSKeygmTLLISSHLLgEIEQIADTIGVIRDGRLLEEVSMEDVRGQNTEYIELVT 232
Cdd:TIGR01193 640 SNLDTITEKKIvNNLLNLQDK----TIIFVAHRL-SVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIH 707
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-164 |
1.14e-16 |
|
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: 79.98 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 3 YIVQTNGLTKTYQ-GKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKfthtsyevlgNIGS 81
Cdd:TIGR03719 3 YIYTMNRVSKVVPpKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGI----------KVGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 82 MIEYPIFYENLTAEENLDLHCE------------YMGYHNKKA-----------IQEVLDMVNLKQIDKK---------- 128
Cdd:TIGR03719 73 LPQEPQLDPTKTVRENVEEGVAeikdaldrfneiSAKYAEPDAdfdklaaeqaeLQEIIDAADAWDLDSQleiamdalrc 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 255767068 129 -----PVKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLD 164
Cdd:TIGR03719 153 ppwdaDVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
10-214 |
1.25e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 78.10 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 10 LTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTH-TSYEVLGNIGSMIEYPIF 88
Cdd:PRK10253 13 LTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyASKEVARRIGLLAQNATT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 89 YENLTAEEnLDLHCEY--------MGYHNKKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPV 160
Cdd:PRK10253 93 PGDITVQE-LVARGRYphqplftrWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 255767068 161 NGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEE 214
Cdd:PRK10253 172 TWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQ 225
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
5-211 |
1.29e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 79.30 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 5 VQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIIlGNKFTHTSYEVLGNIGSMIE 84
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFI-GEKRMNDVPPAERGVGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 85 YPIFYENLTAEENLDLHCEYMGYhNKKAIQ-------EVLDMVNLkqIDKKPvKTFSLGMKQRLGIARAILTKPDLLILD 157
Cdd:PRK11000 83 SYALYPHLSVAENMSFGLKLAGA-KKEEINqrvnqvaEVLQLAHL--LDRKP-KALSGGQRQRVAIGRTLVAEPSVFLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 255767068 158 EPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRL 211
Cdd:PRK11000 159 EPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
5-245 |
1.49e-16 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 80.01 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 5 VQTNGLTKTYQGK-EVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVL-GNIGSM 82
Cdd:PRK13657 335 VEFDDVSFSYDNSrQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLrRNIAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 83 IEYPIFYeNLTAEENLDLHCEymgyhnKKAIQEVLDMVNLKQ----IDKKPVK----------TFSLGMKQRLGIARAIL 148
Cdd:PRK13657 415 FQDAGLF-NRSIEDNIRVGRP------DATDEEMRAAAERAQahdfIERKPDGydtvvgergrQLSGGERQRLAIARALL 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 149 TKPDLLILDEPVNGLDPLGIKKIRQLFQVLSKeyGMTLLISSHLLGEIEQiADTIGVIRDGRLLEEVSMEDVRGQNTEYI 228
Cdd:PRK13657 488 KDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFDELVARGGRFA 564
|
250
....*....|....*..
gi 255767068 229 ELVtpnqtRACFVLEKE 245
Cdd:PRK13657 565 ALL-----RAQGMLQED 576
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
4-220 |
2.37e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 77.10 E-value: 2.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 4 IVQTNGLTKTYQGKE--VVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYE------- 74
Cdd:PRK13648 7 IIVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEklrkhig 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 75 -VLGN-----IGSMIEYPIFYenltAEENLDLHCEYMGYHNKKAIQEVlDMVNlkQIDKKPvKTFSLGMKQRLGIARAIL 148
Cdd:PRK13648 87 iVFQNpdnqfVGSIVKYDVAF----GLENHAVPYDEMHRRVSEALKQV-DMLE--RADYEP-NALSGGQKQRVAIAGVLA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255767068 149 TKPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQiADTIGVIRDGRLLEEVSMEDV 220
Cdd:PRK13648 159 LNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEI 229
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
16-214 |
3.84e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 76.26 E-value: 3.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 16 GKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLT--SLVKPTSGEIIILGNkfthtsyevlgNIGSM-IE-------- 84
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMghPKYEVTSGSILLDGE-----------DILELsPDeraragif 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 85 ----YPI------FYENLTAEENLDLHCEYMGYHNKKAIQEVLDMVNLKQ-IDKKPV-KTFSLGMKQRLGIARAILTKPD 152
Cdd:COG0396 81 lafqYPVeipgvsVSNFLRTALNARRGEELSAREFLKLLKEKMKELGLDEdFLDRYVnEGFSGGEKKRNEILQMLLLEPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255767068 153 LLILDEPVNGLDPLGIKKIRQLFQVLSKEyGMTLLISSH---LLGEIEqiADTIGVIRDGRLLEE 214
Cdd:COG0396 161 LAILDETDSGLDIDALRIVAEGVNKLRSP-DRGILIITHyqrILDYIK--PDFVHVLVDGRIVKS 222
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
5-191 |
4.23e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 78.31 E-value: 4.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 5 VQTNGLT-KTYQGKEVVSNVSMHIKKGEiyGFL--GPNGAGKTTIMKMLTSLVKPTSGEIIILGNKftHT------SYEV 75
Cdd:COG4178 363 LALEDLTlRTPDGRPLLEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAGLWPYGSGRIARPAGA--RVlflpqrPYLP 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 76 LGNIGSMIEYPifyenLTAEEnldlhceymgyHNKKAIQEVLDMVNL----KQIDKKPV--KTFSLGMKQRLGIARAILT 149
Cdd:COG4178 439 LGTLREALLYP-----ATAEA-----------FSDAELREALEAVGLghlaERLDEEADwdQVLSLGEQQRLAFARLLLH 502
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 255767068 150 KPDLLILDEPVNGLDPlgiKKIRQLFQVLSKEYGMTLLIS-SH 191
Cdd:COG4178 503 KPDWLFLDEATSALDE---ENEAALYQLLREELPGTTVISvGH 542
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-220 |
4.40e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 76.21 E-value: 4.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 4 IVQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNIGSMI 83
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 84 -EYPIFYENLTAEENLdlhcEY-----------MGYHNKKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKP 151
Cdd:PRK11231 82 pQHHLTPEGITVRELV----AYgrspwlslwgrLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255767068 152 DLLILDEPVNGLDPLGIKKIRQLFQVLSKEyGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDV 220
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
15-192 |
4.65e-16 |
|
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: 78.17 E-value: 4.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 15 QGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSY-EVLGNIGSMIEYP-IFyeNL 92
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQdEVRRRVSVCAQDAhLF--DT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 93 TAEENLDLHCeymGYHNKKAIQEVLDMVNLKQ-IDKKP----------VKTFSLGMKQRLGIARAILTKPDLLILDEPVN 161
Cdd:TIGR02868 424 TVRENLRLAR---PDATDEELWAALERVGLADwLRALPdgldtvlgegGARLSGGERQRLALARALLADAPILLLDEPTE 500
|
170 180 190
....*....|....*....|....*....|..
gi 255767068 162 GLDPLGIKK-IRQLFQVLSKEygMTLLISSHL 192
Cdd:TIGR02868 501 HLDAETADElLEDLLAALSGR--TVVLITHHL 530
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
16-220 |
7.70e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 75.79 E-value: 7.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 16 GKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSY--EVLGNIGSMIEYP-IFYENL 92
Cdd:PRK13644 14 GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlqGIRKLVGIVFQNPeTQFVGR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 93 TAEENLDLHCEYM---GYHNKKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLDPLGIK 169
Cdd:PRK13644 94 TVEEDLAFGPENLclpPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 255767068 170 KIRQLFQVLsKEYGMTLLISSHLLGEIeQIADTIGVIRDGRLLEEVSMEDV 220
Cdd:PRK13644 174 AVLERIKKL-HEKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENV 222
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
8-191 |
8.44e-16 |
|
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: 78.03 E-value: 8.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 8 NGLTKTYQ--GKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKpTSGEIIILGNKFTHTSYEVLGNIGSMIEY 85
Cdd:TIGR01271 1221 QGLTAKYTeaGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQ 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 86 PIFYENLTAEENLDLHCEYmgyhNKKAIQEVLDMVNLKQ-IDKKPVK----------TFSLGMKQRLGIARAILTKPDLL 154
Cdd:TIGR01271 1300 KVFIFSGTFRKNLDPYEQW----SDEEIWKVAEEVGLKSvIEQFPDKldfvlvdggyVLSNGHKQLMCLARSILSKAKIL 1375
|
170 180 190
....*....|....*....|....*....|....*...
gi 255767068 155 ILDEPVNGLDPLGIKKIRQ-LFQVLSKeygMTLLISSH 191
Cdd:TIGR01271 1376 LLDEPSAHLDPVTLQIIRKtLKQSFSN---CTVILSEH 1410
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
17-191 |
1.09e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 77.39 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 17 KEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKP---TSGEIIILGNKFTHTSYEVLGniGSMIEYPIFYENLT 93
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKEMRAIS--AYVQQDDLFIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 94 AEENLDLHCEY-MGYHNKK-----AIQEVLDMVNLKQI------DKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVN 161
Cdd:TIGR00955 116 VREHLMFQAHLrMPRRVTKkekreRVDEVLQALGLRKCantrigVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180 190
....*....|....*....|....*....|
gi 255767068 162 GLDPLGIKKIRQLFQVLSKEyGMTLLISSH 191
Cdd:TIGR00955 196 GLDSFMAYSVVQVLKGLAQK-GKTIICTIH 224
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-229 |
1.14e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 75.20 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 2 TYIVQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMK---MLTSLVKP--TSGEIIILGNKFTHTSY--- 73
Cdd:PRK14243 8 ETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnRLNDLIPGfrVEGKVTFHGKNLYAPDVdpv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 74 EVLGNIGSMIEYPIFYENlTAEENLDLHCEYMGYhnKKAIQEVLDMvNLKQI-------DKKPVKTFSL--GMKQRLGIA 144
Cdd:PRK14243 88 EVRRRIGMVFQKPNPFPK-SIYDNIAYGARINGY--KGDMDELVER-SLRQAalwdevkDKLKQSGLSLsgGQQQRLCIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 145 RAILTKPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYgmTLLISSHLLGEIEQIAD---------TIGVIRDGRLLE-- 213
Cdd:PRK14243 164 RAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDmtaffnvelTEGGGRYGYLVEfd 241
|
250
....*....|....*....
gi 255767068 214 --EVSMEDVRGQNT-EYIE 229
Cdd:PRK14243 242 rtEKIFNSPQQQATrDYVS 260
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
11-230 |
1.15e-15 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 76.98 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 11 TKTYQGKEV--VSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNIGSMIEYPIF 88
Cdd:PRK11176 348 TFTYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVH 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 89 YENLTAEENLDLHCEymGYHNKKAIQEVLDMVN-LKQIDKKP--VKT--------FSLGMKQRLGIARAILTKPDLLILD 157
Cdd:PRK11176 428 LFNDTIANNIAYART--EQYSREQIEEAARMAYaMDFINKMDngLDTvigengvlLSGGQRQRIAIARALLRDSPILILD 505
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255767068 158 EPVNGLDPLGIKKIRQLFQVLSKEygMTLLISSHLLGEIEQiADTIGVIRDGRLLEEVSMEDVRGQNTEYIEL 230
Cdd:PRK11176 506 EATSALDTESERAIQAALDELQKN--RTSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAELLAQNGVYAQL 575
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-197 |
1.28e-15 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 76.85 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 20 VSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKfthtsyeVLGNIGSMIEypifyENLTAEENLD 99
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA-------ALIAISSGLN-----GQLTGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 100 LHCEYMGYhNKKAIQE----VLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLDPLGIKKIRQLF 175
Cdd:PRK13545 108 LKGLMMGL-TKEKIKEiipeIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKM 186
|
170 180
....*....|....*....|..
gi 255767068 176 QVLsKEYGMTLLISSHLLGEIE 197
Cdd:PRK13545 187 NEF-KEQGKTIFFISHSLSQVK 207
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
18-228 |
1.54e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 76.63 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 18 EVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSyevlgnIGSMIEYPIFY-------E 90
Cdd:PRK15439 277 EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALS------TAQRLARGLVYlpedrqsS 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 91 NLTAEENLDLHCEYMGYHNK------KAIQEVLD----MVNLKQIDK-KPVKTFSLGMKQRLGIARAILTKPDLLILDEP 159
Cdd:PRK15439 351 GLYLDAPLAWNVCALTHNRRgfwikpARENAVLEryrrALNIKFNHAeQAARTLSGGNQQKVLIAKCLEASPQLLIVDEP 430
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255767068 160 VNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHlLGEIEQIADTIGVIRDGRLLEEVSMEDVrgqNTEYI 228
Cdd:PRK15439 431 TRGVDVSARNDIYQLIRSIAAQNVAVLFISSD-LEEIEQMADRVLVMHQGEISGALTGAAI---NVDTI 495
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-164 |
1.83e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 76.39 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 27 IKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIII----------LGNKFTHTSYEVLGNIGSMIEYPIFYEnltaee 96
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPelkisykpqyIKPDYDGTVEDLLRSITDDLGSSYYKS------ 435
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255767068 97 nldlhceymgyhnkkaiqEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLD 164
Cdd:PRK13409 436 ------------------EIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-220 |
1.86e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 76.43 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 20 VSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEI--------------IILGNKFTHTSYEVLGNIGSMIEY 85
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqvIELSEQSAAQMRHVRGADMAMIFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 86 -------PIFYENLTAEENLDLHceyMGYHNKKAIQEVLDMVNLKQIDKKPV------KTFSLGMKQRLGIARAILTKPD 152
Cdd:PRK10261 112 epmtslnPVFTVGEQIAESIRLH---QGASREEAMVEAKRMLDQVRIPEAQTilsrypHQLSGGMRQRVMIAMALSCRPA 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255767068 153 LLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDV 220
Cdd:PRK10261 189 VLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-212 |
2.19e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 76.30 E-value: 2.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 1 MTYIVQTNGLTKTYQGKE----VVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVL 76
Cdd:PRK10535 1 MTALLELKDIRRSYPSGEeqveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 77 GNI-----GSMIEYPIFYENLTAEENLDLHCEYMGYHNKKAI---QEVLDMVNL-KQIDKKPVKtFSLGMKQRLGIARAI 147
Cdd:PRK10535 81 AQLrrehfGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLlraQELLQRLGLeDRVEYQPSQ-LSGGQQQRVSIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255767068 148 LTKPDLLILDEPVNGLDPLGIKKIRQLFQVLsKEYGMTLLISSHlLGEIEQIADTIGVIRDGRLL 212
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTH-DPQVAAQAERVIEIRDGEIV 222
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-189 |
3.02e-15 |
|
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: 75.74 E-value: 3.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 4 IVQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIilgnkfthtsyevlgnIGSMI 83
Cdd:TIGR03719 322 VIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIE----------------IGETV 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 84 EypIFYENLTaEENLDlhceymgyHNKKAIQEV---LDMV----------------NLKQIDK-KPVKTFSLGMKQRLGI 143
Cdd:TIGR03719 386 K--LAYVDQS-RDALD--------PNKTVWEEIsggLDIIklgkreipsrayvgrfNFKGSDQqKKVGQLSGGERNRVHL 454
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 255767068 144 ARAILTKPDLLILDEPVNGLDplgIKKIRQLFQVLSKEYGMTLLIS 189
Cdd:TIGR03719 455 AKTLKSGGNVLLLDEPTNDLD---VETLRALEEALLNFAGCAVVIS 497
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-191 |
3.38e-15 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 75.70 E-value: 3.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 5 VQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIiilgnKFTHTSyevlgNIGSMIE 84
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-----KWSENA-----NIGYYAQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 85 --YPIFyenltaEENLDLHcEYMGY-----HNKKAIQEVLDMVNLKQID-KKPVKTFSLGMKQRLGIARAILTKPDLLIL 156
Cdd:PRK15064 390 dhAYDF------ENDLTLF-DWMSQwrqegDDEQAVRGTLGRLLFSQDDiKKSVKVLSGGEKGRMLFGKLMMQKPNVLVM 462
|
170 180 190
....*....|....*....|....*....|....*
gi 255767068 157 DEPVNGLDplgIKKIRQLFQVLSKeYGMTLLISSH 191
Cdd:PRK15064 463 DEPTNHMD---MESIESLNMALEK-YEGTLIFVSH 493
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
5-213 |
3.76e-15 |
|
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: 72.83 E-value: 3.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 5 VQTNGLTKTYQGK--EVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNIGSM 82
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 83 I-EYPIFYENlTAEENLDLHCEYmgyhNKKAIQEVLDMvnlkqidKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVN 161
Cdd:cd03369 87 IpQDPTLFSG-TIRSNLDPFDEY----SDEEIYGALRV-------SEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 255767068 162 GL----DPLGIKKIRQLFQvlskeyGMTLLISSHLLGEIEQIaDTIGVIRDGRLLE 213
Cdd:cd03369 155 SIdyatDALIQKTIREEFT------NSTILTIAHRLRTIIDY-DKILVMDAGEVKE 203
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-223 |
3.86e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 75.93 E-value: 3.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 4 IVQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTimkmLTSLV----KPTSGEIiilgnkfthtsyEVLGni 79
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSS----LLSLIagarKIQQGRV------------EVLG-- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 80 GSM------------IEY-PI-----FYENLTAEENLDLHCEYMGyHNKKA----IQEVLDMVNLKQIDKKPVKTFSLGM 137
Cdd:NF033858 63 GDMadarhrravcprIAYmPQglgknLYPTLSVFENLDFFGRLFG-QDAAErrrrIDELLRATGLAPFADRPAGKLSGGM 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 138 KQRLGIARAILTKPDLLILDEPVNGLDPLG-------IKKIRQlfqvlsKEYGMTLLISSHLLGEIEQIaDTIGVIRDGR 210
Cdd:NF033858 142 KQKLGLCCALIHDPDLLILDEPTTGVDPLSrrqfwelIDRIRA------ERPGMSVLVATAYMEEAERF-DWLVAMDAGR 214
|
250
....*....|...
gi 255767068 211 LLEEVSMEDVRGQ 223
Cdd:NF033858 215 VLATGTPAELLAR 227
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-220 |
3.88e-15 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 73.61 E-value: 3.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 6 QTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNI------ 79
Cdd:COG4559 3 EAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRravlpq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 80 GSMIEYPifyenLTAEE----NLDLHCEyMGYHNKKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAIL------- 148
Cdd:COG4559 83 HSSLAFP-----FTVEEvvalGRAPHGS-SAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvd 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255767068 149 TKPDLLILDEPVNGLDplgikkIRQLFQVLS--KEY---GMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDV 220
Cdd:COG4559 157 GGPRWLFLDEPTSALD------LAHQHAVLRlaRQLarrGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEV 227
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
12-220 |
4.49e-15 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 74.56 E-value: 4.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 12 KTYQGK-EVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTsgeIIILGNKFTHTSYEVLG------------N 78
Cdd:COG4170 14 DTPQGRvKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDN---WHVTADRFRWNGIDLLKlsprerrkiigrE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 79 IgSMI-EYPIFYENLTA------EENLDlHCEYMGY------HNKKAIQEVLDMVNLKQiDKKPVKTF----SLGMKQRL 141
Cdd:COG4170 91 I-AMIfQEPSSCLDPSAkigdqlIEAIP-SWTFKGKwwqrfkWRKKRAIELLHRVGIKD-HKDIMNSYphelTEGECQKV 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255767068 142 GIARAILTKPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDV 220
Cdd:COG4170 168 MIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQI 246
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
15-211 |
1.27e-14 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 74.01 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 15 QGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLG-NIGSM---IEypifye 90
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGrHIGYLpqdVE------ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 91 nL---TAEENLDLhceyMGYHNKKAIQE------VLDMvnlkqIDKKP----------VKTFSLGMKQRLGIARAILTKP 151
Cdd:COG4618 417 -LfdgTIAENIAR----FGDADPEKVVAaaklagVHEM-----ILRLPdgydtrigegGARLSGGQRQRIGLARALYGDP 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 152 DLLILDEPVNGLDPLGIKKIRQLFQVLsKEYGMTLLISSHLLGeIEQIADTIGVIRDGRL 211
Cdd:COG4618 487 RLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPS-LLAAVDKLLVLRDGRV 544
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
14-191 |
1.29e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 74.22 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 14 YQ--GKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIiilgnkfthtsyevlgNIGSMIEYPIF--Y 89
Cdd:PRK11147 327 YQidGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI----------------HCGTKLEVAYFdqH 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 90 -ENL----TAEENL------------DLHCeyMGY------HNKKAIQevldmvnlkqidkkPVKTFSLGMKQRLGIARA 146
Cdd:PRK11147 391 rAELdpekTVMDNLaegkqevmvngrPRHV--LGYlqdflfHPKRAMT--------------PVKALSGGERNRLLLARL 454
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 255767068 147 ILTKPDLLILDEPVNGLDplgIKKIrQLFQVLSKEYGMTLLISSH 191
Cdd:PRK11147 455 FLKPSNLLILDEPTNDLD---VETL-ELLEELLDSYQGTVLLVSH 495
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
11-212 |
1.70e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 73.76 E-value: 1.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 11 TKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTS--GEIIILGNKFTHtsyEVLGNIGSMIEYPIF 88
Cdd:PLN03211 75 TRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK---QILKRTGFVTQDDIL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 89 YENLTAEENLdLHCEYMGYHNKKAIQE-------VLDMVNLKQ-----IDKKPVKTFSLGMKQRLGIARAILTKPDLLIL 156
Cdd:PLN03211 152 YPHLTVRETL-VFCSLLRLPKSLTKQEkilvaesVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLIL 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 255767068 157 DEPVNGLDPLGIKKIRQLFQVLSKEyGMTLLISSHL-LGEIEQIADTIGVIRDGRLL 212
Cdd:PLN03211 231 DEPTSGLDATAAYRLVLTLGSLAQK-GKTIVTSMHQpSSRVYQMFDSVLVLSEGRCL 286
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-164 |
1.74e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 73.61 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 3 YIVQTNGLTKTYQG-KEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIIL-GNKF-----------T 69
Cdd:PRK11819 5 YIYTMNRVSKVVPPkKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPApGIKVgylpqepqldpE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 70 HTsyeVLGNI--------GSMIEYPIFYENLtAEENLDLH--CEYMGyhnkkAIQEVLDMVNLKQIDKK----------- 128
Cdd:PRK11819 85 KT---VRENVeegvaevkAALDRFNEIYAAY-AEPDADFDalAAEQG-----ELQEIIDAADAWDLDSQleiamdalrcp 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 255767068 129 ----PVKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLD 164
Cdd:PRK11819 156 pwdaKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-212 |
2.01e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 72.58 E-value: 2.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 4 IVQTNGLTKTYQGKE-----VVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEI----IILGNKFTHTSYE 74
Cdd:PRK13631 21 ILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 75 VLGN------------IGSMI----EYPIFYEnlTAEENLDLHCEYMGYHNKKAIQEV---LDMVNLKQ--IDKKPVKtF 133
Cdd:PRK13631 101 TNPYskkiknfkelrrRVSMVfqfpEYQLFKD--TIEKDIMFGPVALGVKKSEAKKLAkfyLNKMGLDDsyLERSPFG-L 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255767068 134 SLGMKQRLGIARAILTKPDLLILDEPVNGLDPLGIKKIRQLFQVlSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLL 212
Cdd:PRK13631 178 SGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKIL 255
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-213 |
2.22e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 73.35 E-value: 2.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 17 KEV--VSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNIGSMIEYpIF---YEN 91
Cdd:PRK10261 335 REVhaVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQF-IFqdpYAS 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 92 LTAE--------ENLDLHCEYMGYHNKKAIQEVLDMVNLK--QIDKKPvKTFSLGMKQRLGIARAILTKPDLLILDEPVN 161
Cdd:PRK10261 414 LDPRqtvgdsimEPLRVHGLLPGKAAAARVAWLLERVGLLpeHAWRYP-HEFSGGQRQRICIARALALNPKVIIADEAVS 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 255767068 162 GLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLE 213
Cdd:PRK10261 493 ALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVE 544
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-164 |
2.23e-14 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 73.28 E-value: 2.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 27 IKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIII----------LGNKFTHTSYEVLGN-IGSMIEYPIFYEnltae 95
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEdlkisykpqyISPDYDGTVEEFLRSaNTDDFGSSYYKT----- 437
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255767068 96 enldlhceymgyhnkkaiqEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLD 164
Cdd:COG1245 438 -------------------EIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-164 |
2.24e-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: 71.29 E-value: 2.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 27 IKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVlgnigsMIEYPIFYENLTAEEnLDLHCEYMG 106
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYI------KADYEGTVRDLLSSI-TKDFYTHPY 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 255767068 107 YHNkkaiqEVLDMVNLKQIDKKPVKTFSLGMKQRLGIArAILTKP-DLLILDEPVNGLD 164
Cdd:cd03237 95 FKT-----EIAKPLQIEQILDREVPELSGGELQRVAIA-ACLSKDaDIYLLDEPSAYLD 147
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
4-191 |
2.43e-14 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 73.13 E-value: 2.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 4 IVQTNGLTKtYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSlVKPT--SGEIIILGNKftHTSYEVLGNIGS 81
Cdd:PRK10938 261 IVLNNGVVS-YNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQgySNDLTLFGRR--RGSGETIWDIKK 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 82 MIEYPifyenltaeeNLDLHCEYM-----------GYH-------------NKKAiQEVLDMVNL-KQIDKKPVKTFSLG 136
Cdd:PRK10938 337 HIGYV----------SSSLHLDYRvstsvrnvilsGFFdsigiyqavsdrqQKLA-QQWLDILGIdKRTADAPFHSLSWG 405
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 255767068 137 mKQRLG-IARAILTKPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSH 191
Cdd:PRK10938 406 -QQRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSH 460
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
5-221 |
2.93e-14 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 72.46 E-value: 2.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 5 VQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTiMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNIGSmiE 84
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**R-GALPAHV*GPDAGRRPWRF*TWCANRRALRRTIG*--H 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 85 YPIFY---ENLTAEENLDLHCEYMGYHNKKA---IQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDE 158
Cdd:NF000106 91 RPVR*grrESFSGRENLYMIGR*LDLSRKDArarADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255767068 159 PVNGLDPLGIKKIRQLFQVLSKEyGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDVR 221
Cdd:NF000106 171 PTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELK 232
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
10-193 |
7.82e-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: 70.27 E-value: 7.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 10 LTKTYQ--GKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKpTSGEIIILGNKFTHTSYEVLGNIGSMIEYPI 87
Cdd:cd03289 8 LTAKYTegGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 88 FYENLTAEENLDLHceymGYHNKKAIQEVLDMVNLKQ-IDKKPVK----------TFSLGMKQRLGIARAILTKPDLLIL 156
Cdd:cd03289 87 FIFSGTFRKNLDPY----GKWSDEEIWKVAEEVGLKSvIEQFPGQldfvlvdggcVLSHGHKQLMCLARSVLSKAKILLL 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 255767068 157 DEPVNGLDPLGIKKIRQ-LFQVLSkeyGMTLLISSHLL 193
Cdd:cd03289 163 DEPSAHLDPITYQVIRKtLKQAFA---DCTVILSEHRI 197
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
9-214 |
1.46e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.89 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 9 GLTKTYQG-KEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVkPTSGEIIILGNKFTHTSYEVLGNIGSMIEYpI 87
Cdd:PRK15134 290 GILKRTVDhNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLLPVRHRIQV-V 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 88 FYENLTA-----------EENLDLHCEYMGYHNKKA-IQEVLDMVNLKQIDKKPVKT-FSLGMKQRLGIARAILTKPDLL 154
Cdd:PRK15134 368 FQDPNSSlnprlnvlqiiEEGLRVHQPTLSAAQREQqVIAVMEEVGLDPETRHRYPAeFSGGQRQRIAIARALILKPSLI 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 155 ILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEE 214
Cdd:PRK15134 448 ILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQ 507
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
5-191 |
1.60e-13 |
|
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: 67.18 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 5 VQTNGLT-KTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFT----HTSYEVLGNI 79
Cdd:cd03223 1 IELENLSlATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLlflpQRPYLPLGTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 80 GSMIEYPifyenltaeenldlhceymgyhnkkaiqevLDMVnlkqidkkpvktFSLGMKQRLGIARAILTKPDLLILDEP 159
Cdd:cd03223 81 REQLIYP------------------------------WDDV------------LSGGEQQRLAFARLLLHKPKFVFLDEA 118
|
170 180 190
....*....|....*....|....*....|..
gi 255767068 160 VNGLDPLGIKKIRQLFqvlsKEYGMTLLISSH 191
Cdd:cd03223 119 TSALDEESEDRLYQLL----KELGITVISVGH 146
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-225 |
1.71e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 71.16 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 19 VVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNIGSMI-EYPIFYENlTAEEN 97
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIpQSPVLFSG-TVRFN 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 98 LDLHCEymgyHNKKAIQEVLDMVNLKQ-IDKKPV----------KTFSLGMKQRLGIARAILTKPDLLILDEPVNGL--- 163
Cdd:PLN03232 1330 IDPFSE----HNDADLWEALERAHIKDvIDRNPFgldaevseggENFSVGQRQLLSLARALLRRSKILVLDEATASVdvr 1405
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255767068 164 -DPLGIKKIRQLFQvlskeyGMTLLISSHLLGEIEQiADTIGVIRDGRLLEEVSMEDVRGQNT 225
Cdd:PLN03232 1406 tDSLIQRTIREEFK------SCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDT 1461
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
37-215 |
2.31e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 69.52 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 37 GPNGAGKTTIMKMLTSLVKPTSGEIIILGNkfthtsyeVLGNIGSMIEYP--------IFYE-----NLTAEENLDLHCe 103
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGR--------VLFDAEKGICLPpekrrigyVFQDarlfpHYKVRGNLRYGM- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 104 ymgyhNKKAIQEVLDMVNLKQI----DKKPVkTFSLGMKQRLGIARAILTKPDLLILDEPVNGLDplgIKKIRQL---FQ 176
Cdd:PRK11144 102 -----AKSMVAQFDKIVALLGIepllDRYPG-SLSGGEKQRVAIGRALLTAPELLLMDEPLASLD---LPRKRELlpyLE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 255767068 177 VLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRL-----LEEV 215
Cdd:PRK11144 173 RLAREINIPILYVSHSLDEILRLADRVVVLEQGKVkafgpLEEV 216
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
20-220 |
2.39e-13 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 69.37 E-value: 2.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 20 VSNVSMHIKKGEIYGFLGPNGAGKT----TIMKMLTSLVKpTSGEIIILGNKFTHTSYEVLGNIG----SMIeypiFYEN 91
Cdd:PRK09473 32 VNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGR-IGGSATFNGREILNLPEKELNKLRaeqiSMI----FQDP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 92 LTA-----------EENLDLHceyMGYHNKKAIQE---VLDMVNL----KQIDKKPvKTFSLGMKQRLGIARAILTKPDL 153
Cdd:PRK09473 107 MTSlnpymrvgeqlMEVLMLH---KGMSKAEAFEEsvrMLDAVKMpearKRMKMYP-HEFSGGMRQRVMIAMALLCRPKL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255767068 154 LILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDV 220
Cdd:PRK09473 183 LIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
5-214 |
3.18e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 69.75 E-value: 3.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 5 VQTNGLTKTYQ-GKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNIGSMI 83
Cdd:PRK10790 341 IDIDNVSFAYRdDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 84 EY-PI-----FYENLTAEENLDlhceymgyhnKKAIQEVLDMVNLKQIDKK-----------PVKTFSLGMKQRLGIARA 146
Cdd:PRK10790 421 QQdPVvladtFLANVTLGRDIS----------EEQVWQALETVQLAELARSlpdglytplgeQGNNLSVGQKQLLALARV 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255767068 147 ILTKPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEygMTLLISSHLLGEIEQiADTIGVIRDGRLLEE 214
Cdd:PRK10790 491 LVQTPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAHRLSTIVE-ADTILVLHRGQAVEQ 555
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-213 |
3.95e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 67.74 E-value: 3.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 2 TYIVQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTS--LVKPTSGEIIILGNKFTHTSYEVLGNI 79
Cdd:CHL00131 5 KPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERAHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 80 GSMI--EYPIFYENLTAEENLDLHCEYMGYHNKKA----------IQEVLDMVNLKQ--IDKKPVKTFSLGMKQRLGIAR 145
Cdd:CHL00131 85 GIFLafQYPIEIPGVSNADFLRLAYNSKRKFQGLPeldplefleiINEKLKLVGMDPsfLSRNVNEGFSGGEKKRNEILQ 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 146 AILTKPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSH--LLGEIeqIADTIGVIRDGRLLE 213
Cdd:CHL00131 165 MALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYqrLLDYI--KPDYVHVMQNGKIIK 232
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
13-236 |
5.68e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 69.10 E-value: 5.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 13 TYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVkPTSGEIIILG---NKFTHTSY-EVLGNIG--SMIEYP 86
Cdd:PRK11174 359 SPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGielRELDPESWrKHLSWVGqnPQLPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 87 IFYENLTaeenldlhceyMGYHN--KKAIQEVLDMVNLKQIDKK-------PVK----TFSLGMKQRLGIARAILTKPDL 153
Cdd:PRK11174 438 TLRDNVL-----------LGNPDasDEQLQQALENAWVSEFLPLlpqgldtPIGdqaaGLSVGQAQRLALARALLQPCQL 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 154 LILDEPVNGLDPLGIKKIRQLFQVLSKeyGMTLLISSHLLGEIEQIaDTIGVIRDGRLLEEVSMEDVRGQNTEYIELVTP 233
Cdd:PRK11174 507 LLLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAGGLFATLLAH 583
|
...
gi 255767068 234 NQT 236
Cdd:PRK11174 584 RQE 586
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
16-203 |
6.22e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 66.66 E-value: 6.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 16 GKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVL-GNIGSMIEYPIFYENlTA 94
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYrQQVSYCAQTPTLFGD-TV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 95 EENLDLHCEYMGYH-NKKAIQEVLDMVNLKQ-IDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLDPLGIKKIR 172
Cdd:PRK10247 98 YDNLIFPWQIRNQQpDPAIFLDDLERFALPDtILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVN 177
|
170 180 190
....*....|....*....|....*....|.
gi 255767068 173 QLFQVLSKEYGMTLLISSHLLGEIEQIADTI 203
Cdd:PRK10247 178 EIIHRYVREQNIAVLWVTHDKDEINHADKVI 208
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4-211 |
8.89e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 68.22 E-value: 8.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 4 IVQTNGLTKTYQGKevVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKF-THTSYEVLGN---- 78
Cdd:PRK10982 250 ILEVRNLTSLRQPS--IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKInNHNANEAINHgfal 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 79 -------IGSMIEYPIFYENLTAeeNLDLHCEYMGYHN----KKAIQEVLDMVNLKQIDKK-PVKTFSLGMKQRLGIARA 146
Cdd:PRK10982 328 vteerrsTGIYAYLDIGFNSLIS--NIRNYKNKVGLLDnsrmKSDTQWVIDSMRVKTPGHRtQIGSLSGGNQQKVIIGRW 405
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255767068 147 ILTKPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHlLGEIEQIADTIGVIRDGRL 211
Cdd:PRK10982 406 LLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSE-MPELLGITDRILVMSNGLV 469
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-164 |
1.25e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 67.84 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 4 IVQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIilgnkfthtsyevlgnIGSMI 83
Cdd:PRK11819 324 VIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIK----------------IGETV 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 84 EypIFYENLTaEENLDlhceymgyhNKKAIQEV----LDMVNLKQID-----------------KKPVKTFSLGMKQRLG 142
Cdd:PRK11819 388 K--LAYVDQS-RDALD---------PNKTVWEEisggLDIIKVGNREipsrayvgrfnfkggdqQKKVGVLSGGERNRLH 455
|
170 180
....*....|....*....|..
gi 255767068 143 IARAILTKPDLLILDEPVNGLD 164
Cdd:PRK11819 456 LAKTLKQGGNVLLLDEPTNDLD 477
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
24-223 |
2.13e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 67.35 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 24 SMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEiiiLGNKFTHT---SYEVLgnigsmieypifyENLTAEE---- 96
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGE---RQSQFSHItrlSFEQL-------------QKLVSDEwqrn 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 97 NLDLHCEY---MGYHNKKAIQ-EVLDMVNLKQIDK---------KPVKTFSLGMKQRLGIARAILTKPDLLILDEPVNGL 163
Cdd:PRK10938 87 NTDMLSPGeddTGRTTAEIIQdEVKDPARCEQLAQqfgitalldRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 164 DPLGIKKIRQLFQVLSKEyGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDVRGQ 223
Cdd:PRK10938 167 DVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQ 225
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
20-219 |
2.30e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.12 E-value: 2.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 20 VSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTS-YEVLGN-IGSMIEYPI---FYENLTA 94
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpLDAVKKgMAYITESRRdngFFPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 95 EENLDLHCEY--------MGYHN----KKAIQEVLDMVNLK--QIDKKpVKTFSLGMKQRLGIARAILTKPDLLILDEPV 160
Cdd:PRK09700 359 AQNMAISRSLkdggykgaMGLFHevdeQRTAENQRELLALKchSVNQN-ITELSGGNQQKVLISKWLCCCPEVIIFDEPT 437
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 255767068 161 NGLDPLGIKKIRQLFQVLSKEyGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMED 219
Cdd:PRK09700 438 RGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRD 495
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
23-220 |
3.91e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 64.95 E-value: 3.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 23 VSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVkPTSGEIIILGNKFTHTSYEVLG--------NIGSMIEYPIF-Yenlt 93
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELArhraylsqQQTPPFAMPVFqY---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 94 aeenLDLHcEYMGYHNKKAIQEVLDMVNLKQIDKK---PVKTFSLGMKQRLGIARAIL-----TKPD--LLILDEPVNGL 163
Cdd:PRK03695 90 ----LTLH-QPDKTRTEAVASALNEVAEALGLDDKlgrSVNQLSGGEWQRVRLAAVVLqvwpdINPAgqLLLLDEPMNSL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255767068 164 DplgikkIRQ---LFQVLSK--EYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDV 220
Cdd:PRK03695 165 D------VAQqaaLDRLLSElcQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
19-213 |
5.27e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 66.69 E-value: 5.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 19 VVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILG---NKFTHTsyEVLGNIGSMIEYPIFYENlTAE 95
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGcdiSKFGLM--DLRKVLGIIPQAPVLFSG-TVR 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 96 ENLDLHCEymgyHNKKAIQEVLDMVNLKQ-IDKKPV----------KTFSLGMKQRLGIARAILTKPDLLILDEPVN--- 161
Cdd:PLN03130 1331 FNLDPFNE----HNDADLWESLERAHLKDvIRRNSLgldaevseagENFSVGQRQLLSLARALLRRSKILVLDEATAavd 1406
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 255767068 162 -GLDPLGIKKIRQLFQvlskeyGMTLLISSHLLGEIEQiADTIGVIRDGRLLE 213
Cdd:PLN03130 1407 vRTDALIQKTIREEFK------SCTMLIIAHRLNTIID-CDRILVLDAGRVVE 1452
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
7-191 |
7.39e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 65.68 E-value: 7.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 7 TNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIII-----LG----NKFTHTSYEVLG 77
Cdd:PRK15064 4 TANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLdpnerLGklrqDQFAFEEFTVLD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 78 NI--------GSMIEYPIFYENLTAEENLDLHC--------EYMGYHNKKAIQEVLDMVNlkqIDKK----PVKTFSLGM 137
Cdd:PRK15064 84 TVimghtelwEVKQERDRIYALPEMSEEDGMKVadlevkfaEMDGYTAEARAGELLLGVG---IPEEqhygLMSEVAPGW 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 255767068 138 KQRLGIARAILTKPDLLILDEPVNGLDplgIKKIRQLFQVLSkEYGMTLLISSH 191
Cdd:PRK15064 161 KLRVLLAQALFSNPDILLLDEPTNNLD---INTIRWLEDVLN-ERNSTMIIISH 210
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
5-164 |
7.65e-12 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 65.25 E-value: 7.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 5 VQTNGLTKTYQGK-EVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHtsyevlgnigsmI 83
Cdd:PRK11650 4 LKLQAVRKSYDGKtQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNE------------L 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 84 EyP-------IF-----YENLTAEENldlhceyMGYHNK-----KA-----IQEVLDMVNLKQ-IDKKPvKTFSLGMKQR 140
Cdd:PRK11650 72 E-PadrdiamVFqnyalYPHMSVREN-------MAYGLKirgmpKAeieerVAEAARILELEPlLDRKP-RELSGGQRQR 142
|
170 180
....*....|....*....|....
gi 255767068 141 LGIARAILTKPDLLILDEPVNGLD 164
Cdd:PRK11650 143 VAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
20-212 |
8.73e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 63.71 E-value: 8.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 20 VSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVkPTSGEIIILGNKFTHTSYEVLGNIGSMI---EYPIFyeNLTAEE 96
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAYLsqqQSPPF--AMPVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 97 NLDLHCEYMG--YHNKKAIQEVLDMVNLKqiDK--KPVKTFSLGMKQRLGIARAIL-----TKPD--LLILDEPVNGLDp 165
Cdd:COG4138 89 YLALHQPAGAssEAVEQLLAQLAEALGLE--DKlsRPLTQLSGGEWQRVRLAAVLLqvwptINPEgqLLLLDEPMNSLD- 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 255767068 166 lgikkIRQ---LFQVLSK--EYGMTLLISSHLLGEIEQIADTIGVIRDGRLL 212
Cdd:COG4138 166 -----VAQqaaLDRLLRElcQQGITVVMSSHDLNHTLRHADRVWLLKQGKLV 212
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
15-219 |
1.01e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 65.32 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 15 QGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFthtsyeVLGNIGSMIEYPIFY--ENL 92
Cdd:PRK11288 264 KGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPI------DIRSPRDAIRAGIMLcpEDR 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 93 TAE---------ENLDLHCEymGYH-------NKKAIQEVLDmvnlKQIDKKPVKT---------FSLGMKQRLGIARAI 147
Cdd:PRK11288 338 KAEgiipvhsvaDNINISAR--RHHlragcliNNRWEAENAD----RFIRSLNIKTpsreqlimnLSGGNQQKAILGRWL 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255767068 148 LTKPDLLILDEPVNGLDpLGIK-KIRQLFQVLSKEyGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMED 219
Cdd:PRK11288 412 SEDMKVILLDEPTRGID-VGAKhEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRIAGELAREQ 482
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
8-228 |
2.28e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 62.88 E-value: 2.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 8 NGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNigsmiEYPI 87
Cdd:PRK10575 15 RNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFAR-----KVAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 88 FYENLTAEENLDLH-----CEY--------MGYHNKKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLL 154
Cdd:PRK10575 90 LPQQLPAAEGMTVRelvaiGRYpwhgalgrFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255767068 155 ILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDV-RGQNTEYI 228
Cdd:PRK10575 170 LLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELmRGETLEQI 244
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
17-220 |
2.81e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 62.41 E-value: 2.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 17 KEVVSNVSMHIKKGEIYGFLGPNGAGKT----TIMKMLTSLVKPTSGEIIILGN-------KFTHTSyEVLGNIGSMIEy 85
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKpvapcalRGRKIA-TIMQNPRSAFN- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 86 PIFYENLTAEENldlhCEYMGYH-NKKAIQEVLDMVNLKQiDKKPVKTF----SLGMKQRLGIARAILTKPDLLILDEPV 160
Cdd:PRK10418 94 PLHTMHTHARET----CLALGKPaDDATLTAALEAVGLEN-AARVLKLYpfemSGGMLQRMMIALALLCEAPFIIADEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 161 NGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDV 220
Cdd:PRK10418 169 TDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
18-214 |
2.86e-11 |
|
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: 64.07 E-value: 2.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 18 EVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVL-GNIG----------SMIEYP 86
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLrAAIGivpqdtvlfnDTIAYN 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 87 IFYENLTAEEnldlhceymgyhnkkaiQEVLDMVNLKQID------KKPVKT--------FSLGMKQRLGIARAILTKPD 152
Cdd:COG5265 452 IAYGRPDASE-----------------EEVEAAARAAQIHdfieslPDGYDTrvgerglkLSGGEKQRVAIARTLLKNPP 514
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255767068 153 LLILDEPVNGLDPLGIKKIRQLFQVLSKeyGMTLLISSHLLGEIeQIADTIGVIRDGRLLEE 214
Cdd:COG5265 515 ILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTI-VDADEILVLEAGRIVER 573
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
18-220 |
4.19e-11 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 62.90 E-value: 4.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 18 EVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTsgeIIILGNKFTHTSYEVL-----------GNIGSMIeyp 86
Cdd:PRK15093 21 KAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDN---WRVTADRMRFDDIDLLrlsprerrklvGHNVSMI--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 87 iFYEN---LTAEENLDLHC--------------EYMGYHNKKAIqEVLDMVNLKQiDKKPVKTFSL----GMKQRLGIAR 145
Cdd:PRK15093 95 -FQEPqscLDPSERVGRQLmqnipgwtykgrwwQRFGWRKRRAI-ELLHRVGIKD-HKDAMRSFPYelteGECQKVMIAI 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255767068 146 AILTKPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDV 220
Cdd:PRK15093 172 ALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKEL 246
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1-191 |
4.60e-11 |
|
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: 60.72 E-value: 4.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 1 MTYIVQTNGltktyQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKML-----TSLVKptsGEIIILGNKFTHTSYEV 75
Cdd:cd03232 9 LNYTVPVKG-----GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLagrktAGVIT---GEILINGRPLDKNFQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 76 LGNIGSMieyPIFYENLTAEENLDLHCeymgyhnkkaiqevldmvNLKQIdkkpvktfSLGMKQRLGIARAILTKPDLLI 155
Cdd:cd03232 81 TGYVEQQ---DVHSPNLTVREALRFSA------------------LLRGL--------SVEQRKRLTIGVELAAKPSILF 131
|
170 180 190
....*....|....*....|....*....|....*.
gi 255767068 156 LDEPVNGLDPLGIKKIRQLFQVLSKEyGMTLLISSH 191
Cdd:cd03232 132 LDEPTSGLDSQAAYNIVRFLKKLADS-GQAILCTIH 166
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-209 |
4.72e-10 |
|
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: 60.69 E-value: 4.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 16 GKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGN-KFT-HTSYEVLGNIGSMIEYPIFYEnlt 93
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRiSFSpQTSWIMPGTIKDNIIFGLSYD--- 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 94 aeenldlhcEYMGYHNKKAIQEVLDMVNLKQIDKKPVK----TFSLGMKQRLGIARAILTKPDLLILDEPVNGLDPLGIK 169
Cdd:TIGR01271 515 ---------EYRYTSVIKACQLEEDIALFPEKDKTVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEK 585
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 255767068 170 KI--RQLFQVLSKEygMTLLISSHLlgEIEQIADTIGVIRDG 209
Cdd:TIGR01271 586 EIfeSCLCKLMSNK--TRILVTSKL--EHLKKADKILLLHEG 623
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
20-220 |
8.67e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 58.60 E-value: 8.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 20 VSNVSMHIKKGEIYGFLGPNGAGKT----TIMKMLTSLVKPTSGEIIILGNKFTHTS----YEVLGNIGSMIeypiFYEN 91
Cdd:PRK11022 23 VDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISekerRNLVGAEVAMI----FQDP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 92 LTA-----------EENLDLHceyMGYHNKKAIQEVLDMVNL-------KQIDKKPvKTFSLGMKQRLGIARAILTKPDL 153
Cdd:PRK11022 99 MTSlnpcytvgfqiMEAIKVH---QGGNKKTRRQRAIDLLNQvgipdpaSRLDVYP-HQLSGGMSQRVMIAMAIACRPKL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255767068 154 LILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDV 220
Cdd:PRK11022 175 LIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
5-210 |
9.35e-10 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 57.48 E-value: 9.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 5 VQTNGLTKTYQGKE-----VVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIiilgnkfthtsyEVLGNI 79
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV------------SVPGSI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 80 GSMIEYPiFYENLTAEENLDLHCEYmgyhNKKAIQEVL-------DMVNLKQIDKKPV--KTFSL--GMKQRLGIARAIL 148
Cdd:cd03250 69 AYVSQEP-WIQNGTIRENILFGKPF----DEERYEKVIkacalepDLEILPDGDLTEIgeKGINLsgGQKQRISLARAVY 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255767068 149 TKPDLLILDEPVNGLDP-LGikkiRQLFQVLSKEYGM---TLLISSHLLGEIEQiADTIGVIRDGR 210
Cdd:cd03250 144 SDADIYLLDDPLSAVDAhVG----RHIFENCILGLLLnnkTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
12-210 |
1.03e-09 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 57.27 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 12 KTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPT---SGEIIILGN--KFTHTSYEvlGNIGSMIEYP 86
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIpyKEFAEKYP--GEIIYVSEED 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 87 IFYENLTAEENLDLHCEYMGYHNkkaiqevldmvnlkqidkkpVKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLDPL 166
Cdd:cd03233 93 VHFPTLTVRETLDFALRCKGNEF--------------------VRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSS 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 255767068 167 GIKKIRQLFQVLSKEYGMTLLISshLL---GEIEQIADTIGVIRDGR 210
Cdd:cd03233 153 TALEILKCIRTMADVLKTTTFVS--LYqasDEIYDLFDKVLVLYEGR 197
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
22-203 |
1.04e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.19 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 22 NVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIII-----------------LGNKFTHTSyEVLGNIGSMIE 84
Cdd:PRK11147 21 NAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYeqdlivarlqqdpprnvEGTVYDFVA-EGIEEQAEYLK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 85 YpifYENLTaeenLDLHCEYMGYH-NKKA-IQEVLDMVNLKQIDKK--------------PVKTFSLGMKQRLGIARAIL 148
Cdd:PRK11147 100 R---YHDIS----HLVETDPSEKNlNELAkLQEQLDHHNLWQLENRinevlaqlgldpdaALSSLSGGWLRKAALGRALV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 255767068 149 TKPDLLILDEPVNGLDplgIKKIRQLFQVLsKEYGMTLLISSHLLGEIEQIADTI 203
Cdd:PRK11147 173 SNPDVLLLDEPTNHLD---IETIEWLEGFL-KTFQGSIIFISHDRSFIRNMATRI 223
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
16-164 |
1.05e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 59.10 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 16 GKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMK-MLTSLVK--PTSGEIIilgnkftHTSYEVLGN--------IGSMIE 84
Cdd:PLN03073 189 GRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRyMAMHAIDgiPKNCQIL-------HVEQEVVGDdttalqcvLNTDIE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 85 YPIFYEN----LTAEENLDLHCEY-------MGYHNKKAIQEVLDMV--NLKQID----------------------KKP 129
Cdd:PLN03073 262 RTQLLEEeaqlVAQQRELEFETETgkgkganKDGVDKDAVSQRLEEIykRLELIDaytaearaasilaglsftpemqVKA 341
|
170 180 190
....*....|....*....|....*....|....*
gi 255767068 130 VKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLD 164
Cdd:PLN03073 342 TKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
2-191 |
1.11e-09 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 57.89 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 2 TYIVQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILG---------------- 65
Cdd:COG4598 6 PPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGeeirlkpdrdgelvpa 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 66 -------------------NKFTHTSyeVLGNIgsmIEYPIfyenltaeenldlHCeyMGYHNKKAIQE---VLDMVNLK 123
Cdd:COG4598 86 drrqlqrirtrlgmvfqsfNLWSHMT--VLENV---IEAPV-------------HV--LGRPKAEAIERaeaLLAKVGLA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255767068 124 QI-DKKPVKtFSLGMKQRLGIARAILTKPDLLILDEPVNGLDP--LG--IKKIRQLfqvlsKEYGMTLLISSH 191
Cdd:COG4598 146 DKrDAYPAH-LSGGQQQRAAIARALAMEPEVMLFDEPTSALDPelVGevLKVMRDL-----AEEGRTMLVVTH 212
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
14-164 |
1.25e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 59.03 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 14 YQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEI-----IILGnKFTHTSYEVLGNIGSMIEYPIF 88
Cdd:PRK10636 322 YGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIglakgIKLG-YFAQHQLEFLRADESPLQHLAR 400
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255767068 89 YENLTAEENLDLHCEYMGYHNKKAIQevldmvnlkqidkkPVKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLD 164
Cdd:PRK10636 401 LAPQELEQKLRDYLGGFGFQGDKVTE--------------ETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
17-213 |
1.34e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 58.96 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 17 KEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVL-GNIGSMIEYPIFYENlTAE 95
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWrSRLAVVSQTPFLFSD-TVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 96 ENLDLHCEYMgyhNKKAIQEVL-------DMVNLKQ-----IDKKPVkTFSLGMKQRLGIARAILTKPDLLILDEPVNGL 163
Cdd:PRK10789 407 NNIALGRPDA---TQQEIEHVArlasvhdDILRLPQgydteVGERGV-MLSGGQKQRISIARALLLNAEILILDDALSAV 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 255767068 164 DPlgiKKIRQLFQVLSK-EYGMTLLISSHLLGEIEQiADTIGVIRDGRLLE 213
Cdd:PRK10789 483 DG---RTEHQILHNLRQwGEGRTVIISAHRLSALTE-ASEILVMQHGHIAQ 529
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
13-226 |
1.60e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.89 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 13 TYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIII--------LGNKFTHTSYEVLG------- 77
Cdd:PTZ00265 394 TRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIndshnlkdINLKWWRSKIGVVSqdpllfs 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 78 -NIGSMIEYPIF----YENLTAEENLDLHCEYMGYHNKKAIQ--------------------------EVLDMVNLKQID 126
Cdd:PTZ00265 474 nSIKNNIKYSLYslkdLEALSNYYNEDGNDSQENKNKRNSCRakcagdlndmsnttdsneliemrknyQTIKDSEVVDVS 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 127 KK----------PVKTFSL----------GMKQRLGIARAILTKPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTL 186
Cdd:PTZ00265 554 KKvlihdfvsalPDKYETLvgsnasklsgGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRIT 633
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 255767068 187 LISSHLLGEIeQIADTIGVI----RDGRLLEEVSMEDVRGQNTE 226
Cdd:PTZ00265 634 IIIAHRLSTI-RYANTIFVLsnreRGSTVDVDIIGEDPTKDNKE 676
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-206 |
1.60e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 58.64 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 28 KKGEIYGFLGPNGAGKTTIMKMLtslvkptSGEIII-LGNKFTHTSY-EVL-----------------GNIGS-----MI 83
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKIL-------SGELKPnLGDYDEEPSWdEVLkrfrgtelqdyfkklanGEIKVahkpqYV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 84 EYPIFYENLTAEENLdlhceyMGYHNKKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVNGL 163
Cdd:COG1245 170 DLIPKVFKGTVRELL------EKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYL 243
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 255767068 164 DplgikkIRQ------LFQVLSKEyGMTLLISSHLLGEIEQIADTIGVI 206
Cdd:COG1245 244 D------IYQrlnvarLIRELAEE-GKYVLVVEHDLAILDYLADYVHIL 285
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
37-192 |
1.65e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 56.42 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 37 GPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNIGSMIEYPIfyeNLTAEENLDLHCEYmgYHNKKAIQEV 116
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIGHNLGLKL---EMTVFENLKFWSEI--YNSAETLYAA 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255767068 117 LDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLDPLGIKKIRQLFqVLSKEYGMTLLISSHL 192
Cdd:PRK13541 108 IHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLI-VMKANSGGIVLLSSHL 182
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-206 |
2.97e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.90 E-value: 2.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 27 IKKGEIYGFLGPNGAGKTTIMKMLtslvkptSGEIII-LGNKFTHTSY-EVL-----------------GNIGS-----M 82
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKIL-------SGELIPnLGDYEEEPSWdEVLkrfrgtelqnyfkklynGEIKVvhkpqY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 83 IEY-PIFYENLTAE--ENLDlhceymgyhNKKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEP 159
Cdd:PRK13409 169 VDLiPKVFKGKVREllKKVD---------ERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 255767068 160 VNGLDplgikkIRQLFQV--LSKEY--GMTLLISSHLLGEIEQIADTIGVI 206
Cdd:PRK13409 240 TSYLD------IRQRLNVarLIRELaeGKYVLVVEHDLAVLDYLADNVHIA 284
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
20-213 |
4.24e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 57.29 E-value: 4.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 20 VSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFThtsyevlgnIGSMIEY-----PIF-----Y 89
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT---------AEQPEDYrklfsAVFtdfhlF 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 90 ENLTAEENLDLhceymgyhNKKAIQ---EVLDMVNLKQIDKKPVKT--FSLGMKQRLGIARAILTKPDLLILDEPVNGLD 164
Cdd:PRK10522 410 DQLLGPEGKPA--------NPALVEkwlERLKMAHKLELEDGRISNlkLSKGQKKRLALLLALAEERDILLLDEWAADQD 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 255767068 165 PlgikKIRQLF-QVL---SKEYGMTLLISSHLLGEIEQiADTIGVIRDGRLLE 213
Cdd:PRK10522 482 P----HFRREFyQVLlplLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQLSE 529
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
16-211 |
6.66e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.48 E-value: 6.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 16 GKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSlVKP--TSGEIIILGNKFThtsyevLGNIGSMIEYPIFY---- 89
Cdd:PRK13549 274 HIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFG-AYPgrWEGEIFIDGKPVK------IRNPQQAIAQGIAMvped 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 90 -------------ENLTAEeNLDLHCeYMGYHNKKAIQEVLDmvnlKQIDKKPVKTFSL---------GMKQRLGIARAI 147
Cdd:PRK13549 347 rkrdgivpvmgvgKNITLA-ALDRFT-GGSRIDDAAELKTIL----ESIQRLKVKTASPelaiarlsgGNQQKAVLAKCL 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255767068 148 LTKPDLLILDEPVNGLDpLGIK-KIRQLFQVLSKEyGMTLLISSHLLGEIEQIADTIGVIRDGRL 211
Cdd:PRK13549 421 LLNPKILILDEPTRGID-VGAKyEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-171 |
9.42e-09 |
|
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: 55.25 E-value: 9.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 16 GKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILG--NKFTHTSYEVLGNIGSMIEYPIFYEnlt 93
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGriSFSSQFSWIMPGTIKENIIFGVSYD--- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 94 aeenldlhcEYMGYHNKKAIQEVLDMVNLKQIDKKPVK----TFSLGMKQRLGIARAILTKPDLLILDEPVNGLDPLGIK 169
Cdd:cd03291 126 ---------EYRYKSVVKACQLEEDITKFPEKDNTVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEK 196
|
..
gi 255767068 170 KI 171
Cdd:cd03291 197 EI 198
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-231 |
1.15e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.14 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 17 KEVVSNVSMHIKKGEIYGFLGPNGAGKTtimkmltSLVKPTSGEIiilgNKFTHTSYEVLGNIGSMIEYPIFYeNLTAEE 96
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKT-------SLISAMLGEL----SHAETSSVVIRGSVAYVPQVSWIF-NATVRE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 97 NLDLHCEYMGYHNKKAI-----QEVLDMV---NLKQIDKKPVkTFSLGMKQRLGIARAILTKPDLLILDEPVNGLDPlgi 168
Cdd:PLN03232 698 NILFGSDFESERYWRAIdvtalQHDLDLLpgrDLTEIGERGV-NISGGQKQRVSMARAVYSNSDIYIFDDPLSALDA--- 773
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255767068 169 KKIRQLFQVLSKE--YGMTLLISSHLLGEIEQIaDTIGVIRDGRLLEEVSMEDVRGQNTEYIELV 231
Cdd:PLN03232 774 HVAHQVFDSCMKDelKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELSKSGSLFKKLM 837
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
13-219 |
1.20e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 55.95 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 13 TYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKML--TSLVKPTSGEIIILGNKFThtsyevLGNIGSMIEYPIFY- 89
Cdd:NF040905 269 LHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVfgRSYGRNISGTVFKDGKEVD------VSTVSDAIDAGLAYv 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 90 ----------------ENLTAEeNL---------DLHCEYM---GYHNKKAI------QEVldmVNLkqidkkpvktfSL 135
Cdd:NF040905 343 tedrkgyglnliddikRNITLA-NLgkvsrrgviDENEEIKvaeEYRKKMNIktpsvfQKV---GNL-----------SG 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 136 GMKQRLGIARAILTKPDLLILDEPVNGLDpLGIK-KIRQLFQVLSKEYGMTLLISSHlLGEIEQIADTIGVIRDGRLLEE 214
Cdd:NF040905 408 GNQQKVVLSKWLFTDPDVLILDEPTRGID-VGAKyEIYTIINELAAEGKGVIVISSE-LPELLGMCDRIYVMNEGRITGE 485
|
....*
gi 255767068 215 VSMED 219
Cdd:NF040905 486 LPREE 490
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
22-213 |
1.50e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.56 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 22 NVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGN-KFTHTSYEVLGNIGSMIEYPI----FYENLTAEe 96
Cdd:PRK10636 19 NATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwQLAWVNQETPALPQPALEYVIdgdrEYRQLEAQ- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 97 nLDLHCEYMGYHNKKAIQEVLDMVNLKQID-----------------KKPVKTFSLGMKQRLGIARAILTKPDLLILDEP 159
Cdd:PRK10636 98 -LHDANERNDGHAIATIHGKLDAIDAWTIRsraasllhglgfsneqlERPVSDFSGGWRMRLNLAQALICRSDLLLLDEP 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 255767068 160 VNGLDplgIKKIRQLFQVLsKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLE 213
Cdd:PRK10636 177 TNHLD---LDAVIWLEKWL-KSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFE 226
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
36-211 |
2.69e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.87 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 36 LGPNGAGKTTIMKMLTSLVKPTSGEII----ILGNKFTHTSYEVLgnigSMIEYPIFYENL----TAEENLDLHCEYMGY 107
Cdd:PLN03073 541 VGPNGIGKSTILKLISGELQPSSGTVFrsakVRMAVFSQHHVDGL----DLSSNPLLYMMRcfpgVPEQKLRAHLGSFGV 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 108 HNKKAIQevldmvnlkqidkkPVKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLDplgIKKIRQLFQVLSKEYGMTLL 187
Cdd:PLN03073 617 TGNLALQ--------------PMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD---LDAVEALIQGLVLFQGGVLM 679
|
170 180
....*....|....*....|....*.
gi 255767068 188 IS--SHLlgeIEQIADTIGVIRDGRL 211
Cdd:PLN03073 680 VShdEHL---ISGSVDELWVVSEGKV 702
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
17-223 |
2.78e-08 |
|
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: 53.76 E-value: 2.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 17 KEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNIGSMI-EYPIFYENlTAE 95
Cdd:cd03288 34 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIIlQDPILFSG-SIR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 96 ENLDLHCEYmgyhNKKAIQEVLDMVNLKQIDK-----------KPVKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLD 164
Cdd:cd03288 113 FNLDPECKC----TDDRLWEALEIAQLKNMVKslpggldavvtEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASID 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 255767068 165 pLGIKKIRQLFqVLSKEYGMTLLISSHLLGEIEQiADTIGVIRDGRLLEEVSMEDVRGQ 223
Cdd:cd03288 189 -MATENILQKV-VMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQ 244
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-211 |
3.96e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 54.06 E-value: 3.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 20 VSNVSMHIKKGEIYGFLGPNGAGKTTIMKML-TSLVKPTSGEIIILGNKFT---------------------HTSYEVLG 77
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPVDirnpaqairagiamvpedrkrHGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 78 nIGSMIEYPIFyENLTAEENLDLHCEymgyhnKKAIQEVLDMVNLKQIDKK-PVKTFSLGMKQRLGIARAILTKPDLLIL 156
Cdd:TIGR02633 356 -VGKNITLSVL-KSFCFKMRIDAAAE------LQIIGSAIQRLKVKTASPFlPIGRLSGGNQQKAVLAKMLLTNPRVLIL 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 255767068 157 DEPVNGLDPLGIKKIRQLFQVLSKEyGMTLLISSHLLGEIEQIADTIGVIRDGRL 211
Cdd:TIGR02633 428 DEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
10-240 |
1.83e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 51.37 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 10 LTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKM----LTSLVKP----TSGEIIILGNKFTHTSYEVLGNIGS 81
Cdd:PRK13547 7 LHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKAlagdLTGGGAPrgarVTGDVTLNGEPLAAIDAPRLARLRA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 82 MIEY---PIFyeNLTAEENLDL----HCEYMG---YHNKKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAI---- 147
Cdd:PRK13547 87 VLPQaaqPAF--AFSAREIVLLgrypHARRAGaltHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlw 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 148 -----LTKPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQIADTIGVIRDGRLLEEVSMEDVrg 222
Cdd:PRK13547 165 pphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV-- 242
|
250
....*....|....*...
gi 255767068 223 qnteyielVTPNQTRACF 240
Cdd:PRK13547 243 --------LTPAHIARCY 252
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-164 |
2.34e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 52.26 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 19 VVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNIGSMI-EYPIFYENlTAEEN 97
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIpQDPVLFSG-SLRMN 1379
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255767068 98 LDLHCEYmgyhNKKAIQEVLDMVNLKQ-IDKKPVK----------TFSLGMKQRLGIARAILTKPDLLILDEPVNGLD 164
Cdd:TIGR00957 1380 LDPFSQY----SDEEVWWALELAHLKTfVSALPDKldhecaeggeNLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1453
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
4-209 |
2.98e-07 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 50.41 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 4 IVQTNGLTKTYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIiLGNKftHTSYEVLGNIGSMI 83
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVH-WSNK--NESEPSFEATRSRN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 84 EYPIFYE-------NLTAEENLDLHCEYmgyhNKKAIQEVLDMVNLK-QIDKKPVK----------TFSLGMKQRLGIAR 145
Cdd:cd03290 78 RYSVAYAaqkpwllNATVEENITFGSPF----NKQRYKAVTDACSLQpDIDLLPFGdqteigergiNLSGGQRQRICVAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255767068 146 AILTKPDLLILDEPVNGLDplgIKKIRQLFQV----LSKEYGMTLLISSHLLGEIEQiADTIGVIRDG 209
Cdd:cd03290 154 ALYQNTNIVFLDDPFSALD---IHLSDHLMQEgilkFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-206 |
1.93e-06 |
|
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: 48.13 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 28 KKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSG---------EIII------LGNKFThtsyEVLGNIGSMIEYPIFYENL 92
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGkfddppdwdEILDefrgseLQNYFT----KLLEGDVKVIVKPQYVDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 93 ------TAEENLDlhceymGYHNKKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLDpl 166
Cdd:cd03236 100 pkavkgKVGELLK------KKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD-- 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 255767068 167 gIK---KIRQLFQVLSKEyGMTLLISSHLLGEIEQIADTIGVI 206
Cdd:cd03236 172 -IKqrlNAARLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
17-219 |
2.34e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.97 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 17 KEVVSNVSMHIKKGEIYGFLGPNGAGKTT-IMKMLTSLVKPTSGEIIILGNkfthTSYEvlgnigSMIEYpIFyeNLTAE 95
Cdd:PLN03130 630 RPTLSNINLDVPVGSLVAIVGSTGEGKTSlISAMLGELPPRSDASVVIRGT----VAYV------PQVSW-IF--NATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 96 ENLDLHCEYMGYHNKKAI-----QEVLDMV---NLKQIDKKPVkTFSLGMKQRLGIARAILTKPDLLILDEPVNGLDP-L 166
Cdd:PLN03130 697 DNILFGSPFDPERYERAIdvtalQHDLDLLpggDLTEIGERGV-NISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAhV 775
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 255767068 167 GikkiRQLFQVLSKE--YGMTLLISSHLLGEIEQIaDTIGVIRDGRLLEEVSMED 219
Cdd:PLN03130 776 G----RQVFDKCIKDelRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEE 825
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
22-191 |
2.74e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.95 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 22 NVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKP---TSGEIIILGNKFtHTSYEvlGNIGSMIEYPIFYENLTAEENL 98
Cdd:TIGR00956 781 NVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPL-DSSFQ--RSIGYVQQQDLHLPTSTVRESL 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 99 DLHCeYMGYHNKKAIQE-------VLDMVNLKQIDKKPVKTFSLGM----KQRLGIARAILTKPDLLI-LDEPVNGLDPL 166
Cdd:TIGR00956 858 RFSA-YLRQPKSVSKSEkmeyveeVIKLLEMESYADAVVGVPGEGLnveqRKRLTIGVELVAKPKLLLfLDEPTSGLDSQ 936
|
170 180
....*....|....*....|....*
gi 255767068 167 GIKKIRQLFQVLSKeYGMTLLISSH 191
Cdd:TIGR00956 937 TAWSICKLMRKLAD-HGQAILCTIH 960
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-231 |
3.10e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 48.79 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 23 VSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNkfthTSYevlgnigsmIEYPIFYENLTAEENLDLHC 102
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS----VAY---------VPQQAWIQNDSLRENILFGK 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 103 EYMGYHNKKAIQ--------EVLDMVNLKQIDKKPVkTFSLGMKQRLGIARAILTKPDLLILDEPVNGLDPLGIKKIrql 174
Cdd:TIGR00957 724 ALNEKYYQQVLEacallpdlEILPSGDRTEIGEKGV-NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHI--- 799
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255767068 175 FQVLSKEYGM----TLLISSHLLGEIEQIaDTIGVIRDGRLLEEVSMEDVRGQNTEYIELV 231
Cdd:TIGR00957 800 FEHVIGPEGVlknkTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQRDGAFAEFL 859
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-196 |
3.48e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 46.21 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 29 KGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILgnkfthtsyevlgnigsmieypifyenltaeenldlhceymgyh 108
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYI-------------------------------------------- 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 109 NKKAIQEVLDMVNLKQIDKKPVKTFSLGMKQRLGIARAILTKPDLLILDEPVNGLDPLGIKKIRQL-----FQVLSKEYG 183
Cdd:smart00382 37 DGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLLLLKSEKN 116
|
170
....*....|...
gi 255767068 184 MTLLISSHLLGEI 196
Cdd:smart00382 117 LTVILTTNDEKDL 129
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
13-191 |
4.34e-06 |
|
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: 48.21 E-value: 4.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 13 TYQGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSL--------VKPTSGEIIILGNKfthtSYEVLGNIGSMIE 84
Cdd:TIGR00954 461 TPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELwpvyggrlTKPAKGKLFYVPQR----PYMTLGTLRDQII 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 85 YPifyenLTAEENLDlhceyMGYHNKKAIQeVLDMVNLKQIDKKPV---------KTFSLGMKQRLGIARAILTKPDLLI 155
Cdd:TIGR00954 537 YP-----DSSEDMKR-----RGLSDKDLEQ-ILDNVQLTHILEREGgwsavqdwmDVLSGGEKQRIAMARLFYHKPQFAI 605
|
170 180 190
....*....|....*....|....*....|....*.
gi 255767068 156 LDEPVNGLDPlgikKIRQLFQVLSKEYGMTLLISSH 191
Cdd:TIGR00954 606 LDECTSAVSV----DVEGYMYRLCREFGITLFSVSH 637
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
27-61 |
1.02e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 45.26 E-value: 1.02e-05
10 20 30
....*....|....*....|....*....|....*
gi 255767068 27 IKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEI 61
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDND 56
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
51-208 |
1.29e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.95 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 51 TSLVKPTSGEIIILGNKFTHTSYEVLGNIGSMI-EYPIFYeNLTAEENLDLHCEYMGYHNKK------AIQEVLD-MVNL 122
Cdd:PTZ00265 1269 DSTVFKNSGKILLDGVDICDYNLKDLRNLFSIVsQEPMLF-NMSIYENIKFGKEDATREDVKrackfaAIDEFIEsLPNK 1347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 123 KQIDKKPV-KTFSLGMKQRLGIARAILTKPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSHLLGEIEQiAD 201
Cdd:PTZ00265 1348 YDTNVGPYgKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SD 1426
|
....*..
gi 255767068 202 TIGVIRD 208
Cdd:PTZ00265 1427 KIVVFNN 1433
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
15-164 |
2.61e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 44.78 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 15 QGKEVVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSL--VKPTSGEIIILGNKFTHTSYEVLGNIGSM------IEYP 86
Cdd:PRK09580 12 EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGIFmafqypVEIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 87 IFYENLTAEENLDLHCEYMGyhnkkaiQEVLDMVNLKQIDKKPVKT---------------FSLGMKQRLGIARAILTKP 151
Cdd:PRK09580 92 GVSNQFFLQTALNAVRSYRG-------QEPLDRFDFQDLMEEKIALlkmpedlltrsvnvgFSGGEKKRNDILQMAVLEP 164
|
170
....*....|...
gi 255767068 152 DLLILDEPVNGLD 164
Cdd:PRK09580 165 ELCILDESDSGLD 177
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
133-191 |
3.89e-05 |
|
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: 44.69 E-value: 3.89e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255767068 133 FSLGMKQRLGIARAIL---TKPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYGmTLLISSH 191
Cdd:pfam13304 237 LSDGTKRLLALLAALLsalPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGA-QLILTTH 297
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-213 |
8.46e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 44.38 E-value: 8.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 19 VVSNVSMHIKKGEIYGFLGPNGAGKTTIMKMLTSLVKPTSGEIIILGNKFTHTSYEVLGNIGSMI-EYPIFYENlTAEEN 97
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIpQDPVLFDG-TVRQN 1403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 98 LDLHCEymgyhnkKAIQEV---LDMVNLKQ--------IDKKPVK---TFSLGMKQRLGIARAILTKPDLLIL-DEPVNG 162
Cdd:PTZ00243 1404 VDPFLE-------ASSAEVwaaLELVGLRErvasesegIDSRVLEggsNYSVGQRQLMCMARALLKKGSGFILmDEATAN 1476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 255767068 163 LDPLGIKKIRQlfQVLSKEYGMTLLISSHLLGEIEQIaDTIGVIRDGRLLE 213
Cdd:PTZ00243 1477 IDPALDRQIQA--TVMSAFSAYTVITIAHRLHTVAQY-DKIIVMDHGAVAE 1524
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
91-203 |
3.07e-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: 41.45 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 91 NLTAEENLDLHCEYMGYHNK-KAIQEV-LDMVNLKQidkkPVKTFSLGMKQRLGIARAIL---TKPDLLILDEPVNGLDP 165
Cdd:cd03271 130 DMTVEEALEFFENIPKIARKlQTLCDVgLGYIKLGQ----PATTLSGGEAQRIKLAKELSkrsTGKTLYILDEPTTGLHF 205
|
90 100 110
....*....|....*....|....*....|....*...
gi 255767068 166 LGIKKIRQLFQVLSkEYGMTLLISSHLLgEIEQIADTI 203
Cdd:cd03271 206 HDVKKLLEVLQRLV-DKGNTVVVIEHNL-DVIKCADWI 241
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
128-225 |
7.38e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 7.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 128 KPVKTFSLGMKQRLGIARAILT---KPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEyGMTLLISSHLLgEIEQIADTI- 203
Cdd:PRK00635 805 RPLSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQ-GHTVVIIEHNM-HVVKVADYVl 882
|
90 100
....*....|....*....|....*..
gi 255767068 204 -----GVIRDGRLLEEVSMEDVRGQNT 225
Cdd:PRK00635 883 elgpeGGNLGGYLLASCSPEELIHLHT 909
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
111-203 |
3.30e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.23 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 111 KAIQEVLDMV---------NLKQIDKK----------------PVKTFSLGMKQRLGIARAIL---TKPDLLILDEPVNG 162
Cdd:TIGR00630 783 KNIADVLDMTveeayeffeAVPSISRKlqtlcdvglgyirlgqPATTLSGGEAQRIKLAKELSkrsTGRTLYILDEPTTG 862
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 255767068 163 LDplgIKKIRQLFQVLSK--EYGMTLLISSHLLGEIEQiADTI 203
Cdd:TIGR00630 863 LH---FDDIKKLLEVLQRlvDKGNTVVVIEHNLDVIKT-ADYI 901
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
129-201 |
4.77e-03 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 38.10 E-value: 4.77e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255767068 129 PVKTFSLGMKQRLGIARAILT---KPDLLILDEPVNGLDPLGIKKIRQLFQVLSKEYGMTLLISSH---LLGEIEQIAD 201
Cdd:COG1106 199 PLSEESDGTKRLLALAGALLDalaKGGVLLIDEIEASLHPSLLRKLLKLFLDLANKNNAQLIFTTHsteLLDAFLELLR 277
|
|
| IstB_IS21 |
pfam01695 |
IstB-like ATP binding protein; This protein contains an ATP/GTP binding P-loop motif. It is ... |
140-199 |
6.47e-03 |
|
IstB-like ATP binding protein; This protein contains an ATP/GTP binding P-loop motif. It is found associated with IS21 family insertion sequences. The function of this protein is unknown, but it may perform a transposase function.
Pssm-ID: 426385 [Multi-domain] Cd Length: 238 Bit Score: 37.42 E-value: 6.47e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255767068 140 RLGIARAILTKPDLLILDEPvnGLDPLGIKKIRQLFQVLSKEYGMT-LLISSHL-LGEIEQI 199
Cdd:pfam01695 143 KLTRKLQQLLKPDVLILDEW--GYLPLDQAEANLLFQVISKRYEHRsIILTSNLpFGEWGQV 202
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
22-203 |
6.68e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 36.92 E-value: 6.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 22 NVSMHIKKGEIYGFLGPNGAGKTTIMkmLTSLVKPTSGEIIILGNKFTHTSYEVLGNIGSMIEYPIFYenLTAEENLdlh 101
Cdd:cd03238 13 NLDVSIPLNVLVVVTGVSGSGKSTLV--NEGLYASGKARLISFLPKFSRNKLIFIDQLQFLIDVGLGY--LTLGQKL--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 102 ceymgyhnkkaiqevldmvnlkqidkkpvKTFSLGMKQRLGIARAIL--TKPDLLILDEPVNGLDPlgiKKIRQLFQVLS 179
Cdd:cd03238 86 -----------------------------STLSGGELQRVKLASELFsePPGTLFILDEPSTGLHQ---QDINQLLEVIK 133
|
170 180
....*....|....*....|....*.
gi 255767068 180 K--EYGMTLLISSHLLGEIEQiADTI 203
Cdd:cd03238 134 GliDLGNTVILIEHNLDVLSS-ADWI 158
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
37-210 |
7.64e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 36.82 E-value: 7.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 37 GPNGAGKTTIM---KMLTSLVKPTSGEIIILGNKFThTSYEVLGNIgsmieypifYENLTAEENLDLHCeymgyHNKKAI 113
Cdd:cd03240 29 GQNGAGKTTIIealKYALTGELPPNSKGGAHDPKLI-REGEVRAQV---------KLAFENANGKKYTI-----TRSLAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255767068 114 QEVLDMVNLKQIDK---KPVKTFSLGMKQ------RLGIARAILTKPDLLILDEPVNGLDPLGI-KKIRQLFQVLSKEYG 183
Cdd:cd03240 94 LENVIFCHQGESNWpllDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIeESLAEIIEERKSQKN 173
|
170 180
....*....|....*....|....*...
gi 255767068 184 MTLLISSHlLGEIEQIADTI-GVIRDGR 210
Cdd:cd03240 174 FQLIVITH-DEELVDAADHIyRVEKDGR 200
|
|
| |
