|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
16-228 |
6.17e-99 |
|
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: 287.94 E-value: 6.17e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 16 VHAEGLRVRAGRHLAVDGLDLSLGTGVHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVhnRADLHTLRRSLGYLP 95
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV--LKQPQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 96 QHFGFYPRFTVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPT 175
Cdd:cd03264 79 QEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2683828925 176 VGLDPEQRLDFRELLRDLGTDSCVLVSTHLVEDVAVACTDVILINDGQLVHQG 228
Cdd:cd03264 159 AGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
16-234 |
1.94e-89 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 264.62 E-value: 1.94e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 16 VHAEGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVhnRADLHTLRRSLGYL 94
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGeIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDV--ARDPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 95 PQHFGFYPRFTVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEP 174
Cdd:COG1131 79 PQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2683828925 175 TVGLDPEQRLDFRELLRDLGTD-SCVLVSTHLVEDVAVACTDVILINDGQLVHQGTTDDLI 234
Cdd:COG1131 159 TSGLDPEARRELWELLRELAAEgKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELK 219
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
18-241 |
2.84e-73 |
|
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: 223.97 E-value: 2.84e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 18 AEGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRADlhTLRRSLGYLPQ 96
Cdd:COG4555 4 VENLSKKYGKVPALKDVSFTAKDGeITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR--EARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 97 HFGFYPRFTVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTV 176
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2683828925 177 GLDPEQRLDFRELLRDLGT-DSCVLVSTHLVEDVAVACTDVILINDGQLVHQGTTDDLITHGGPDD 241
Cdd:COG4555 162 GLDVMARRLLREILRALKKeGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEEN 227
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
16-224 |
1.43e-63 |
|
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: 196.85 E-value: 1.43e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 16 VHAEGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRAdlHTLRRSLGYL 94
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGeIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP--EEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 95 PQHFGFYPRFTVREFVEYlawlkhlpkatipdavqhaidrvgltakadtrmktlSGGMLRRAGIAQAIVNNPAVLLLDEP 174
Cdd:cd03230 79 PEEPSLYENLTVRENLKL------------------------------------SGGMKQRLALAQALLHDPELLILDEP 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2683828925 175 TVGLDPEQRLDFRELLRDLGTDSC-VLVSTHLVEDVAVACTDVILINDGQL 224
Cdd:cd03230 123 TSGLDPESRREFWELLRELKKEGKtILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
26-233 |
2.95e-59 |
|
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: 187.33 E-value: 2.95e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 26 GRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVhnRADLHTLRRSLGYLPQHFGFYPRF 104
Cdd:cd03263 13 GTKPAVDDLSLNVYKGeIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI--RTDRKAARQSLGYCPQFDALFDEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 105 TVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRL 184
Cdd:cd03263 91 TVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRR 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2683828925 185 DFRELLRDLGTDSCVLVSTHLVEDVAVACTDVILINDGQLVHQGTTDDL 233
Cdd:cd03263 171 AIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
15-233 |
1.72e-58 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 188.01 E-value: 1.72e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 15 VVHAEGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVhNRADlhtlRRSLGY 93
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGeIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL-DPED----RRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 94 LPQHFGFYPRFTVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDE 173
Cdd:COG4152 76 LPEERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2683828925 174 PTVGLDPEQRLDFRELLRDL---GTdsCVLVSTH---LVEDVavaCTDVILINDGQLVHQGTTDDL 233
Cdd:COG4152 156 PFSGLDPVNVELLKDVIRELaakGT--TVIFSSHqmeLVEEL---CDRIVIINKGRKVLSGSVDEI 216
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
15-236 |
3.46e-58 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 185.29 E-value: 3.46e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 15 VVHAEGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRadlhtlRRSLGY 93
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGeFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA------RRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 94 LPQHFGFYPRF--TVREFVE-----YLAWLKHLPKATIpDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNP 166
Cdd:COG1121 80 VPQRAEVDWDFpiTVRDVVLmgrygRRGLFRRPSRADR-EAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2683828925 167 AVLLLDEPTVGLDPEQRLDFRELLRDLGTDSC-VLVSTHLVEDVAVACTDVILINDGqLVHQGTTDDLITH 236
Cdd:COG1121 159 DLLLLDEPFAGVDAATEEALYELLRELRREGKtILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVLTP 228
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
15-235 |
2.17e-55 |
|
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: 178.70 E-value: 2.17e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 15 VVHAEGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHN--RADLhtlRRSL 91
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGeVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlsRREL---ARRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 92 GYLPQHFGFYPRFTVREFVE-----YLAWLKHLPKATIpDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNP 166
Cdd:COG1120 78 AYVPQEPPAPFGLTVRELVAlgrypHLGLFGRPSAEDR-EAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2683828925 167 AVLLLDEPTVGLDPEQRLDFRELLRDLGTDS--CVLVSTHlveDVAVA---CTDVILINDGQLVHQGTTDDLIT 235
Cdd:COG1120 157 PLLLLDEPTSHLDLAHQLEVLELLRRLARERgrTVVMVLH---DLNLAaryADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
16-228 |
6.16e-55 |
|
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: 175.93 E-value: 6.16e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 16 VHAEGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRAdlhtlRRSLGYL 94
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGeIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA-----RNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 95 PQHFGFYPRFTVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEP 174
Cdd:cd03269 76 PEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2683828925 175 TVGLDPEQRLDFRELLRDL-GTDSCVLVSTHLVEDVAVACTDVILINDGQLVHQG 228
Cdd:cd03269 156 FSGLDPVNVELLKDVIRELaRAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
17-220 |
2.86e-54 |
|
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: 174.26 E-value: 2.86e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 17 HAEGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRadlhtlRRSLGYLP 95
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGeFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE------RKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 96 QHFGFYPRF--TVREFVE-----YLAWLKHLPKATIpDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAV 168
Cdd:cd03235 75 QRRSIDRDFpiSVRDVVLmglygHKGLFRRLSKADK-AKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2683828925 169 LLLDEPTVGLDPEQRLDFRELLRDLGTDSC-VLVSTHLVEDVAVACTDVILIN 220
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLRELRREGMtILVVTHDLGLVLEYFDRVLLLN 206
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
19-228 |
5.46e-51 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 165.85 E-value: 5.46e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 19 EGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHpvhNRADLHTLRRSLGYLPQH 97
Cdd:cd03268 4 NDLTKTYGKKRVLDDISLHVKKGeIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK---SYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 98 FGFYPRFTVREFVEYLAWLKHLPKAtipdAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVG 177
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGIRKK----RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2683828925 178 LDPEQRLDFRELLRDLGTDSC-VLVSTHLVEDVAVACTDVILINDGQLVHQG 228
Cdd:cd03268 157 LDPDGIKELRELILSLRDQGItVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
16-233 |
3.40e-50 |
|
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: 164.08 E-value: 3.40e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 16 VHAEGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRADlhTLRRSLGYL 94
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGeIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPR--EVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 95 PQHFGFYPRFTVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEP 174
Cdd:cd03265 79 FQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2683828925 175 TVGLDPEQRLDFRELLRDL--GTDSCVLVSTHLVEDVAVACTDVILINDGQLVHQGTTDDL 233
Cdd:cd03265 159 TIGLDPQTRAHVWEYIEKLkeEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
15-221 |
5.79e-49 |
|
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: 160.34 E-value: 5.79e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 15 VVHAEGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRADlhTLRRSLGY 93
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGeALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARE--DYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 94 LPQHFGFYPRFTVREFVEYLAWLKHLPKATipDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDE 173
Cdd:COG4133 80 LGHADGLKPELTVRENLRFWAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2683828925 174 PTVGLDPEQRLDFRELLRD-LGTDSCVLVSTHlvEDVAVACTDVILIND 221
Cdd:COG4133 158 PFTALDAAGVALLAELIAAhLARGGAVLLTTH--QPLELAAARVLDLGD 204
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
16-236 |
3.11e-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: 159.42 E-value: 3.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 16 VHAEGLRVR-AGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVhNRADLHTLRRSLGY 93
Cdd:COG1122 1 IELENLSFSyPGGTPALDDVSLSIEKGeFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDI-TKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 94 L---PQHFGFYPrfTVREFVEY-LAWLKhLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVL 169
Cdd:COG1122 80 VfqnPDDQLFAP--TVEEDVAFgPENLG-LPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2683828925 170 LLDEPTVGLDPEQRLDFRELLRDL-GTDSCVLVSTHLVEDVAVACTDVILINDGQLVHQGTTDDLITH 236
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSD 224
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
26-233 |
1.50e-47 |
|
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: 159.86 E-value: 1.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 26 GRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRADlhTLRRSLGYLPQHFGFYPRF 104
Cdd:TIGR01188 4 GDFKAVDGVNFKVREGeVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPR--KVRRSIGIVPQYASVDEDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 105 TVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRL 184
Cdd:TIGR01188 82 TGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2683828925 185 DFRELLRDL-GTDSCVLVSTHLVEDVAVACTDVILINDGQLVHQGTTDDL 233
Cdd:TIGR01188 162 AIWDYIRALkEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
16-228 |
2.46e-47 |
|
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: 156.76 E-value: 2.46e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 16 VHAEGL----RVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNraDLHTLRRS 90
Cdd:cd03266 2 ITADALtkrfRDVKKTVQAVDGVSFTVKPGeVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK--EPAEARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 91 LGYLPQHFGFYPRFTVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLL 170
Cdd:cd03266 80 LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2683828925 171 LDEPTVGLDPEQR---LDFRELLRDLGTdsCVLVSTHLVEDVAVACTDVILINDGQLVHQG 228
Cdd:cd03266 160 LDEPTTGLDVMATralREFIRQLRALGK--CILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
15-242 |
3.92e-45 |
|
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: 151.67 E-value: 3.92e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 15 VVHAEGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVH--NRADLHTLRRSL 91
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGeILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITglSEKELYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 92 GYLPQH---FGFyprFTVREFVEY-LAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPA 167
Cdd:COG1127 85 GMLFQGgalFDS---LTVFENVAFpLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2683828925 168 VLLLDEPTVGLDPEQRLDFRELLRDL----GTdSCVLVsTHLVEDVAVACTDVILINDGQLVHQGTTDDLITHggpDDP 242
Cdd:COG1127 162 ILLYDEPTAGLDPITSAVIDELIRELrdelGL-TSVVV-THDLDSAFAIADRVAVLADGKIIAEGTPEELLAS---DDP 235
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
19-236 |
8.59e-45 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 153.04 E-value: 8.59e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 19 EGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRAdlHTLRRSLGYLPQH 97
Cdd:PRK13537 11 RNVEKRYGDKLVVDGLSFHVQRGeCFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA--RHARQRVGVVPQF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 98 FGFYPRFTVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVG 177
Cdd:PRK13537 89 DNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTG 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 178 LDPEQRLDFRELLRDL-GTDSCVLVSTHLVEDVAVACTDVILINDGQLVHQGTTDDLITH 236
Cdd:PRK13537 169 LDPQARHLMWERLRSLlARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
27-224 |
3.08e-44 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 148.79 E-value: 3.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 27 RHLAVDGLDLSLGTGVH-GLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHN--RADLHTLRR-SLGYLPQHFGFYP 102
Cdd:cd03255 16 KVQALKGVSLSIEKGEFvAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKlsEKELAAFRRrHIGFVFQSFNLLP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 103 RFTVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQ 182
Cdd:cd03255 96 DLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSET 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2683828925 183 RLDFRELLRDL--GTDSCVLVSTHlVEDVAVACTDVILINDGQL 224
Cdd:cd03255 176 GKEVMELLRELnkEAGTTIVVVTH-DPELAEYADRIIELRDGKI 218
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
18-228 |
9.74e-44 |
|
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: 146.04 E-value: 9.74e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 18 AEGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVhNRADLHTLRRSLGYLPQ 96
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGeIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDL-ASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 97 hfgfyprftvrefveylawlkhlpkatipdavqhAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTV 176
Cdd:cd03214 81 ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2683828925 177 GLDPEQRLDFRELLRDLGTDS--CVLVSTHLVEDVAVACTDVILINDGQLVHQG 228
Cdd:cd03214 127 HLDIAHQIELLELLRRLARERgkTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
19-242 |
1.56e-43 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 147.65 E-value: 1.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 19 EGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVH--NRADLHTLRRSLGYLP 95
Cdd:cd03261 4 RGLTKSFGGRTVLKGVDLDVRRGeILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglSEAELYRLRRRMGMLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 96 QHFGFYPRFTVREFVEYlaWLK-H--LPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLD 172
Cdd:cd03261 84 QSGALFDSLTVFENVAF--PLReHtrLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2683828925 173 EPTVGLDPEQRLDFRELLRDL--GTDSCVLVSTHLVEDVAVACTDVILINDGQLVHQGTTDDLITHggpDDP 242
Cdd:cd03261 162 EPTAGLDPIASGVIDDLIRSLkkELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRAS---DDP 230
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
31-176 |
1.56e-43 |
|
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: 144.71 E-value: 1.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 31 VDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRaDLHTLRRSLGYLPQHFGFYPRFTVREF 109
Cdd:pfam00005 1 LKNVSLTLNPGeILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDD-ERKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2683828925 110 VEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTR----MKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTV 176
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
24-236 |
4.18e-43 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 146.19 E-value: 4.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 24 RAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVH--NRADLHTLRRSLGYLPQHFGF 100
Cdd:cd03258 14 TGGKVTALKDVSLSVPKGeIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTllSGKELRKARRRIGMIFQHFNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 101 YPRFTVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDP 180
Cdd:cd03258 94 LSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2683828925 181 EQRLDFRELLRDLG--TDSCVLVSTHLVEDVAVACTDVILINDGQLVHQGTTDDLITH 236
Cdd:cd03258 174 ETTQSILALLRDINreLGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
14-233 |
1.22e-42 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 145.58 E-value: 1.22e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 14 WVVHAEGLRVR-AGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPV--HNRADLHTLRR 89
Cdd:COG3638 1 PMLELRNLSKRyPGGTPALDDVSLEIERGeFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVtaLRGRALRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 90 SLGYLPQHFGFYPRFTVREFV-----EYL----AWLKHLPKATIPDAVQhAIDRVGLTAKADTRMKTLSGGMLRRAGIAQ 160
Cdd:COG3638 81 RIGMIFQQFNLVPRLSVLTNVlagrlGRTstwrSLLGLFPPEDRERALE-ALERVGLADKAYQRADQLSGGQQQRVAIAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2683828925 161 AIVNNPAVLLLDEPTVGLDP---EQRLD-FRELLRDLG-TdscVLVSTHLVeDVAVACTD-VILINDGQLVHQGTTDDL 233
Cdd:COG3638 160 ALVQEPKLILADEPVASLDPktaRQVMDlLRRIAREDGiT---VVVNLHQV-DLARRYADrIIGLRDGRVVFDGPPAEL 234
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
13-235 |
1.23e-42 |
|
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: 145.61 E-value: 1.23e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 13 PWVVHAEGLRVRAGRHLAVDGLDLSLGTGVH-GLLGPNGAGKTTLMRALATVVKPA-GGTLTLLGHPvHNRADLHTLRRS 90
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHwAILGPNGAGKSTLLSLITGDLPPTyGNDVRLFGER-RGGEDVWELRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 91 LGYLPQ--HFGFYPRFTVREFVEYLAWlkhlpkATI-----PDAVQHA-----IDRVGLTAKADTRMKTLSGGMLRRAGI 158
Cdd:COG1119 80 IGLVSPalQLRFPRDETVLDVVLSGFF------DSIglyrePTDEQRErarelLELLGLAHLADRPFGTLSQGEQRRVLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 159 AQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLRDLGTDSC---VLVsTHLVEDVAVACTDVILINDGQLVHQGTTDDLIT 235
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAptlVLV-THHVEEIPPGITHVLLLKDGRVVAAGPKEEVLT 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-236 |
3.56e-42 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 150.44 E-value: 3.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 2 DTAAAIAPTTHPwVVHAEGLRVR-----AGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLG 75
Cdd:COG1123 248 GRAAPAAAAAEP-LLEVRNLSKRypvrgKGGVRAVDDVSLTLRRGeTLGLVGESGSGKSTLARLLLGLLRPTSGSILFDG 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 76 HPVHN--RADLHTLRRSLGYLPQH-FG-FYPRFTVREFVEY-LAWLKHLPKATIPDAVQHAIDRVGLTAKADTRM-KTLS 149
Cdd:COG1123 327 KDLTKlsRRSLRELRRRVQMVFQDpYSsLNPRMTVGDIIAEpLRLHGLLSRAERRERVAELLERVGLPPDLADRYpHELS 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 150 GGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLRDL--GTDSCVLVSTHlveDVAVA---CTDVILINDGQL 224
Cdd:COG1123 407 GGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLqrELGLTYLFISH---DLAVVryiADRVAVMYDGRI 483
|
250
....*....|..
gi 2683828925 225 VHQGTTDDLITH 236
Cdd:COG1123 484 VEDGPTEEVFAN 495
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
15-227 |
3.79e-42 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 143.65 E-value: 3.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 15 VVHAEGLRVR----AGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVH--NRADLHTL 87
Cdd:COG1136 4 LLELRNLTKSygtgEGEVTALRGVSLSIEAGeFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISslSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 88 RR-SLGYLPQHFGFYPRFTVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNP 166
Cdd:COG1136 84 RRrHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2683828925 167 AVLLLDEPTVGLDPEQRLDFRELLRDLGTDS--CVLVSTHlveDVAVA--CTDVILINDGQLVHQ 227
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNRELgtTIVMVTH---DPELAarADRVIRLRDGRIVSD 225
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
16-228 |
9.20e-41 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 139.58 E-value: 9.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 16 VHAEGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRAdlhTLRRSLGYL 94
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGeFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVP---PERRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 95 PQHFGFYPRFTVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEP 174
Cdd:cd03259 78 FQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2683828925 175 TVGLDPEQRLDFRELLRDL--GTDSCVLVSTHLVEDVAVACTDVILINDGQLVHQG 228
Cdd:cd03259 158 LSALDAKLREELREELKELqrELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
19-223 |
2.67e-40 |
|
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: 138.37 E-value: 2.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 19 EGLRVRAGRH--LAVDGLDLSLGTGVH-GLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRaDLHTLRRSLGYLP 95
Cdd:cd03225 3 KNLSFSYPDGarPALDDISLTIKKGEFvLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKL-SLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 96 QH----FgFYPrfTVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLL 171
Cdd:cd03225 82 QNpddqF-FGP--TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2683828925 172 DEPTVGLDPEQRLDFRELLRDLGTD-SCVLVSTHLVEDVAVACTDVILINDGQ 223
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAEgKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
26-225 |
4.41e-40 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 138.26 E-value: 4.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 26 GRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHN--RADLHTLRRSLGYLPQHFGFYP 102
Cdd:COG2884 13 GGREALSDVSLEIEKGeFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlkRREIPYLRRRIGVVFQDFRLLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 103 RFTVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQ 182
Cdd:COG2884 93 DRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPET 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2683828925 183 RLDFRELLRDL---GTdsCVLVSTH---LVEDVAVActdVILINDGQLV 225
Cdd:COG2884 173 SWEIMELLEEInrrGT--TVLIATHdleLVDRMPKR---VLELEDGRLV 216
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
16-233 |
5.20e-40 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 141.39 E-value: 5.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 16 VHAEGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRAdlhTLRRSLGYL 94
Cdd:COG3842 6 LELENVSKRYGDVTALDDVSLSIEPGeFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLP---PEKRNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 95 PQHFGFYPRFTVREFVEY-LAwLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDE 173
Cdd:COG3842 83 FQDYALFPHLTVAENVAFgLR-MRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2683828925 174 PTVGLDP---EQ-RLDFRELLRDLGTdSCVLVsTHLVEDvAVACTD-VILINDGQLVHQGTTDDL 233
Cdd:COG3842 162 PLSALDAklrEEmREELRRLQRELGI-TFIYV-THDQEE-ALALADrIAVMNDGRIEQVGTPEEI 223
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
10-219 |
9.98e-40 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 138.30 E-value: 9.98e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 10 TTHPWVVHAEGLRVR----AGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNradl 84
Cdd:COG1116 2 SAAAPALELRGVSKRfptgGGGVTALDDVSLTVAAGeFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 85 htLRRSLGYLPQHFGFYPRFTVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVN 164
Cdd:COG1116 78 --PGPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2683828925 165 NPAVLLLDEPTVGLDPEQRLDFRELLRDL----GTdSCVLVsTHLVEDvAVACTDVILI 219
Cdd:COG1116 156 DPEVLLMDEPFGALDALTRERLQDELLRLwqetGK-TVLFV-THDVDE-AVFLADRVVV 211
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
18-236 |
2.58e-39 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 136.41 E-value: 2.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 18 AEGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGH-----PVHNRAdlhtlRRSL 91
Cdd:cd03219 3 VRGLTKRFGGLVALDDVSFSVRPGeIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEditglPPHEIA-----RLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 92 GYLPQHFGFYPRFTVREFVE----------YLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQA 161
Cdd:cd03219 78 GRTFQIPRLFPELTVLENVMvaaqartgsgLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2683828925 162 IVNNPAVLLLDEPTVGLDPEQRLDFRELLRDLGTDSC-VLVSTHLVEDVAVACTDVILINDGQLVHQGTTDDLITH 236
Cdd:cd03219 158 LATDPKLLLLDEPAAGLNPEETEELAELIRELRERGItVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNN 233
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
15-242 |
1.48e-38 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 134.74 E-value: 1.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 15 VVHAEGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVH-NRADLHTLRRSLG 92
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGeVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdSKKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 93 YLPQHFGFYPRFTVREFVEY-LAWLKHLPKAtipDAVQHAI---DRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAV 168
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLaPIKVKKMSKA---EAEERAMellERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 169 LLLDEPTVGLDPEQRLDFRELLRDLGTD--SCVLVsTH---LVEDVAvactD-VILINDGQLVHQGTTDDLITHggPDDP 242
Cdd:COG1126 158 MLFDEPTSALDPELVGEVLDVMRDLAKEgmTMVVV-THemgFAREVA----DrVVFMDGGRIVEEGPPEEFFEN--PQHE 230
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
20-234 |
2.15e-38 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 137.27 E-value: 2.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 20 GLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRADLhtLRRSLGYLPQHF 98
Cdd:PRK13536 46 GVSKSYGDKAVVNGLSFTVASGeCFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARL--ARARIGVVPQFD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 99 GFYPRFTVRE----FVEYLAWLKHLPKATIPDAVQHAidrvGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEP 174
Cdd:PRK13536 124 NLDLEFTVREnllvFGRYFGMSTREIEAVIPSLLEFA----RLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEP 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2683828925 175 TVGLDPEQRLDFRELLRD-LGTDSCVLVSTHLVEDVAVACTDVILINDGQLVHQGTTDDLI 234
Cdd:PRK13536 200 TTGLDPHARHLIWERLRSlLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALI 260
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
29-233 |
3.42e-38 |
|
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: 133.85 E-value: 3.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 29 LAVDGLDLSLGTGVHGL---------------LGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHN--RADLHTLRRSL 91
Cdd:cd03256 1 IEVENLSKTYPNGKKALkdvslsinpgefvalIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKlkGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 92 GYLPQHFGFYPRFTVRE-----FVEYLAWLKHL----PKATIPDAVqHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAI 162
Cdd:cd03256 81 GMIFQQFNLIERLSVLEnvlsgRLGRRSTWRSLfglfPKEEKQRAL-AALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2683828925 163 VNNPAVLLLDEPTVGLDPEQRLDFRELLRDLGTDS--CVLVSTHLVEDVAVACTDVILINDGQLVHQGTTDDL 233
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINREEgiTVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
22-236 |
4.25e-38 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 136.36 E-value: 4.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 22 RVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVH--NRADLHTLRRSLGYLPQHF 98
Cdd:COG1135 12 PTKGGPVTALDDVSLTIEKGeIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTalSERELRAARRKIGMIFQHF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 99 GFYPRFTVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGL 178
Cdd:COG1135 92 NLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSAL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2683828925 179 DPE---QRLDfreLLRD----LG-TdscVLVSTH---LVEDVavaCTDVILINDGQLVHQGTTDDLITH 236
Cdd:COG1135 172 DPEttrSILD---LLKDinreLGlT---IVLITHemdVVRRI---CDRVAVLENGRIVEQGPVLDVFAN 231
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
17-223 |
1.78e-37 |
|
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: 129.29 E-value: 1.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 17 HAEGLRVRAGRHLAVDGLDLSLGTGVH-GLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHnRADLHTLRRSLGYLP 95
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIvALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIA-KLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 96 QhfgfyprftvrefveylawlkhlpkatipdavqhaidrvgltakadtrmktLSGGMLRRAGIAQAIVNNPAVLLLDEPT 175
Cdd:cd00267 80 Q---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2683828925 176 VGLDPEQRLDFRELLRDLGTDSC-VLVSTHLVEDVAVACTDVILINDGQ 223
Cdd:cd00267 109 SGLDPASRERLLELLRELAEEGRtVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
26-223 |
2.75e-37 |
|
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: 129.61 E-value: 2.75e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 26 GRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVH-NRADLHTLRRSLGYLPQHFGFYPR 103
Cdd:cd03229 11 GQKTVLNDVSLNIEAGeIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdLEDELPPLRRRIGMVFQDFALFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 104 FTVREFVEYLawlkhlpkatipdavqhaidrvgltakadtrmktLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQR 183
Cdd:cd03229 91 LTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITR 136
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2683828925 184 LDFRELLRDLGTDS--CVLVSTHLVEDVAVACTDVILINDGQ 223
Cdd:cd03229 137 REVRALLKSLQAQLgiTVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
18-236 |
3.77e-37 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 130.74 E-value: 3.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 18 AEGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGH-----PVHNRAdlhtlRRSL 91
Cdd:cd03218 3 AENLSKRYGKRKVVNGVSLSVKQGeIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQditklPMHKRA-----RLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 92 GYLPQHFGFYPRFTVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLL 171
Cdd:cd03218 78 GYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2683828925 172 DEPTVGLDPEQRLDFREL---LRDLGTDscVLVSTHLVEDVAVACTDVILINDGQLVHQGTTDDLITH 236
Cdd:cd03218 158 DEPFAGVDPIAVQDIQKIikiLKDRGIG--VLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAAN 223
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
28-236 |
1.21e-36 |
|
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: 130.11 E-value: 1.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 28 HLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHN--RADLHTLRRSLGYLPQHFGFYPRF 104
Cdd:TIGR02315 15 KQALKNINLNINPGeFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKlrGKKLRKLRRRIGMIFQHYNLIERL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 105 TVREFV---------EYLAWLKHLPKATIPDAVQhAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPT 175
Cdd:TIGR02315 95 TVLENVlhgrlgykpTWRSLLGRFSEEDKERALS-ALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPI 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2683828925 176 VGLDPE---QRLD-FRELLRDLGTdsCVLVSTHLVEDVAVACTDVILINDGQLVHQGTTDDLITH 236
Cdd:TIGR02315 174 ASLDPKtskQVMDyLKRINKEDGI--TVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDE 236
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
19-231 |
5.06e-36 |
|
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: 127.90 E-value: 5.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 19 EGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVhNRADLHtlrrSLGYLPQH 97
Cdd:TIGR03740 4 KNLSKRFGKQTAVNNISLTVPKNsVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPW-TRKDLH----KIGSLIES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 98 FGFYPRFTVREFVEYLAWLKHLPKATIpDAVQHAidrVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVG 177
Cdd:TIGR03740 79 PPLYENLTARENLKVHTTLLGLPDSRI-DEVLNI---VDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2683828925 178 LDPEQRLDFRELLRDLGTDS-CVLVSTHLVEDVAVACTDVILINDGQLVHQGTTD 231
Cdd:TIGR03740 155 LDPIGIQELRELIRSFPEQGiTVILSSHILSEVQQLADHIGIISEGVLGYQGKIN 209
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
26-219 |
1.16e-35 |
|
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: 126.82 E-value: 1.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 26 GRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRadlhtlRRSLGYLPQHFGFYPRF 104
Cdd:cd03293 15 GAVTALEDISLSVEEGeFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP------GPDRGYVFQQDALLPWL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 105 TVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRL 184
Cdd:cd03293 89 TVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTRE 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 2683828925 185 DFRELLRDL--GTDSCVLVSTHLVEDvAVACTDVILI 219
Cdd:cd03293 169 QLQEELLDIwrETGKTVLLVTHDIDE-AVFLADRVVV 204
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
16-235 |
1.59e-35 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 127.44 E-value: 1.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 16 VHAEGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRADlHTLRRSLGYL 94
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGkITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSS-RQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 95 PQHFGFYPRFTVREFVEY--LAWLKHLPKATIPD--AVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLL 170
Cdd:PRK11231 82 PQHHLTPEGITVRELVAYgrSPWLSLWGRLSAEDnaRVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2683828925 171 LDEPTVGLDPEQRLDFRELLRDLGTD-SCVLVSTHLVEDVAVACTDVILINDGQLVHQGTTDDLIT 235
Cdd:PRK11231 162 LDEPTTYLDINHQVELMRLMRELNTQgKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
18-234 |
1.71e-35 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 127.01 E-value: 1.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 18 AEGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGH-----PVHNRAdlhtlRRSL 91
Cdd:TIGR04406 4 AENLIKSYKKRKVVNDVSLSVKSGeIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQdithlPMHERA-----RLGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 92 GYLPQHFGFYPRFTVREFVE-YLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLL 170
Cdd:TIGR04406 79 GYLPQEASIFRKLTVEENIMaVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFIL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2683828925 171 LDEPTVGLDPEQRLDFRELLRDLGTDSC-VLVSTHLVEDVAVACTDVILINDGQLVHQGTTDDLI 234
Cdd:TIGR04406 159 LDEPFAGVDPIAVGDIKKIIKHLKERGIgVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIV 223
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
16-224 |
1.80e-35 |
|
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: 126.11 E-value: 1.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 16 VHAEGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPV-HNRADLHTLRRSLGY 93
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGeVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtDDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 94 LPQHFGFYPRFTVREFV-EYLAWLKHLPKAtipDAVQHAI---DRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVL 169
Cdd:cd03262 81 VFQQFNLFPHLTVLENItLAPIKVKGMSKA---EAEERALellEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2683828925 170 LLDEPTVGLDPEQRLDFRELLRDLGTDSC-VLVSTH---LVEDVAvacTDVILINDGQL 224
Cdd:cd03262 158 LFDEPTSALDPELVGEVLDVMKDLAEEGMtMVVVTHemgFAREVA---DRVIFMDDGRI 213
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
18-232 |
6.97e-35 |
|
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: 125.54 E-value: 6.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 18 AEGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGH-----PVHNRADLHtLRRSL 91
Cdd:COG0411 7 VRGLTKRFGGLVAVDDVSLEVERGeIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRditglPPHRIARLG-IARTF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 92 gylpQHFGFYPRFTVREFVE----------YLAWLKHLPK-----ATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRA 156
Cdd:COG0411 86 ----QNPRLFPELTVLENVLvaaharlgrgLLAALLRLPRarreeREARERAEELLERVGLADRADEPAGNLSYGQQRRL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 157 GIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLRDLGTD---SCVLVS--THLVEDVavaCTDVILINDGQLVHQGTTD 231
Cdd:COG0411 162 EIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErgiTILLIEhdMDLVMGL---ADRIVVLDFGRVIAEGTPA 238
|
.
gi 2683828925 232 D 232
Cdd:COG0411 239 E 239
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
22-240 |
3.12e-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: 123.56 E-value: 3.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 22 RVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVhNRADLHTLRRSLGYLPQHFGF 100
Cdd:cd03295 8 KRYGGGKKAVNNLNLEIAKGeFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDI-REQDPVELRRKIGYVIQQIGL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 101 YPRFTVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAK--ADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGL 178
Cdd:cd03295 87 FPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGAL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2683828925 179 DPEQRL----DFRELLRDLGTdSCVLVsTHLVEDvAVACTDVI-LINDGQLVHQGTTDDLITHGGPD 240
Cdd:cd03295 167 DPITRDqlqeEFKRLQQELGK-TIVFV-THDIDE-AFRLADRIaIMKNGEIVQVGTPDEILRSPAND 230
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
22-228 |
4.81e-34 |
|
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: 122.61 E-value: 4.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 22 RVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHN--RADLHTLRRSLGYLPQH- 97
Cdd:cd03257 12 PTGGGSVKALDDVSFSIKKGeTLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKlsRRLRKIRRKEIQMVFQDp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 98 FG-FYPRFTVRE-FVE-YLAWLKHLPKATIPDAVQHAIDRVGLtakADTRMK----TLSGGMLRRAGIAQAIVNNPAVLL 170
Cdd:cd03257 92 MSsLNPRMTIGEqIAEpLRIHGKLSKKEARKEAVLLLLVGVGL---PEEVLNryphELSGGQRQRVAIARALALNPKLLI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2683828925 171 LDEPTVGLDPEQRLDFRELLRDL----GTdSCVLVsTHlveDVAVA---CTDVILINDGQLVHQG 228
Cdd:cd03257 169 ADEPTSALDVSVQAQILDLLKKLqeelGL-TLLFI-TH---DLGVVakiADRVAVMYAGKIVEEG 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
18-242 |
5.56e-34 |
|
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: 122.99 E-value: 5.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 18 AEGLRVRAG----RHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRADLHtLRRSLG 92
Cdd:COG1124 4 VRNLSVSYGqggrRVPVLKDVSLEVAPGeSFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKA-FRRRVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 93 YLPQH-FG-FYPRFTVREFVEYLawLKHLPKATIPDAVQHAIDRVGLTAK-ADTRMKTLSGGMLRRAGIAQAIVNNPAVL 169
Cdd:COG1124 83 MVFQDpYAsLHPRHTVDRILAEP--LRIHGLPDREERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARALILEPELL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 170 LLDEPTVGLDP---EQRLD-FRELLRDLGTdSCVLVStHlveDVAVA---CTDVILINDGQLVHQGTTDDLitHGGPDDP 242
Cdd:COG1124 161 LLDEPTSALDVsvqAEILNlLKDLREERGL-TYLFVS-H---DLAVVahlCDRVAVMQNGRIVEELTVADL--LAGPKHP 233
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1-238 |
5.71e-34 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 128.72 E-value: 5.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 1 MDTAAAIAPTTHPWVVHAEGLRVR-AGRHLAVDGLDLSLGTGVH-GLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPV 78
Cdd:COG4988 322 APAGTAPLPAAGPPSIELEDVSFSyPGGRPALDGLSLTIPPGERvALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDL 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 79 HNrADLHTLRRSLGYLPQHfgfyPRF---TVREFVeylawLKHLPKATiPDAVQHAIDRVGLTA-------KADTRM--- 145
Cdd:COG4988 402 SD-LDPASWRRQIAWVPQN----PYLfagTIRENL-----RLGRPDAS-DEELEAALEAAGLDEfvaalpdGLDTPLgeg 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 146 -KTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLRDLGTDSCVLVSTHLVEDVAVAcTDVILINDGQL 224
Cdd:COG4988 471 gRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQA-DRILVLDDGRI 549
|
250
....*....|....
gi 2683828925 225 VHQGTTDDLITHGG 238
Cdd:COG4988 550 VEQGTHEELLAKNG 563
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
18-236 |
6.72e-34 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 122.45 E-value: 6.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 18 AEGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGH-----PVHNRAdlhtlRRSL 91
Cdd:COG1137 6 AENLVKSYGKRTVVKDVSLEVNQGeIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdithlPMHKRA-----RLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 92 GYLPQHFGFYPRFTVRE----FVEylawLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPA 167
Cdd:COG1137 81 GYLPQEASIFRKLTVEDnilaVLE----LRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2683828925 168 VLLLDEPTVGLDPEQRLDFRELLRDL-----GtdscVLVSTHLVEDvAVACTD-VILINDGQLVHQGTTDDLITH 236
Cdd:COG1137 157 FILLDEPFAGVDPIAVADIQKIIRHLkergiG----VLITDHNVRE-TLGICDrAYIISEGKVLAEGTPEEILNN 226
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
19-233 |
7.04e-34 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 125.19 E-value: 7.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 19 EGLRVRAGRHLAVDGLDLSLGTG---VhgLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVhnrADLHTLRRSLGYLP 95
Cdd:COG3839 7 ENVSKSYGGVEALKDIDLDIEDGeflV--LLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV---TDLPPKDRNIAMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 96 QHFGFYPRFTVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPT 175
Cdd:COG3839 82 QSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2683828925 176 VGLDPEQRLDFR----ELLRDLGTdSCVLVsTH-LVEDVAVAcTDVILINDGQLVHQGTTDDL 233
Cdd:COG3839 162 SNLDAKLRVEMRaeikRLHRRLGT-TTIYV-THdQVEAMTLA-DRIAVMNDGRIQQVGTPEEL 221
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
45-236 |
9.90e-34 |
|
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: 123.14 E-value: 9.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 45 LLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVH--NRADLHTLRR-SLGYLPQHFGFYPRFTVREFVEYLAWLKHLPK 121
Cdd:cd03294 55 IMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAamSRKELRELRRkKISMVFQSFALLPHRTVLENVAFGLEVQGVPR 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 122 ATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLRDLGTDS---C 198
Cdd:cd03294 135 AEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELqktI 214
|
170 180 190
....*....|....*....|....*....|....*....
gi 2683828925 199 VLVSTHLVEdvAVACTDVILI-NDGQLVHQGTTDDLITH 236
Cdd:cd03294 215 VFITHDLDE--ALRLGDRIAImKDGRLVQVGTPEEILTN 251
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
15-262 |
3.15e-33 |
|
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: 126.17 E-value: 3.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 15 VVHAEGLRVR--AGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAG---GTLTLLGHPVhNRADLHTLR 88
Cdd:COG1123 4 LLEVRDLSVRypGGDVPAVDGVSLTIAPGeTVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDL-LELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 89 RSLGYLPQHFG--FYPRfTVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNP 166
Cdd:COG1123 83 RRIGMVFQDPMtqLNPV-TVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 167 AVLLLDEPTVGLDPEQRLDFRELLRDLG--TDSCVLVSTHLVEDVAVACTDVILINDGQLVHQGTTDDLITHggPDDPGD 244
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELQreRGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAA--PQALAA 239
|
250
....*....|....*...
gi 2683828925 245 SPAERGYSALLRRHRTAA 262
Cdd:COG1123 240 VPRLGAARGRAAPAAAAA 257
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
18-224 |
5.11e-33 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 119.54 E-value: 5.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 18 AEGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVhNRADLHTLRRSLGYLPQ 96
Cdd:COG4619 3 LEGLSFRVGGKPILSPVSLTLEAGeCVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPL-SAMPPPEWRRQVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 97 HFGFYPRfTVREFVEYLAWLKHLPKAtiPDAVQHAIDRVGLTAKA-DTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPT 175
Cdd:COG4619 82 EPALWGG-TVRDNLPFPFQLRERKFD--RERALELLERLGLPPDIlDKPVERLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2683828925 176 VGLDPEQRLDFRELLRDLGTDS--CVLVSTHLVEDVAVACTDVILINDGQL 224
Cdd:COG4619 159 SALDPENTRRVEELLREYLAEEgrAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
19-233 |
5.21e-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: 120.03 E-value: 5.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 19 EGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNradLHTLRRSLGYLPQH 97
Cdd:cd03300 4 ENVSKFYGGFVALDGVSLDIKEGeFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN---LPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 98 FGFYPRFTVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVG 177
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2683828925 178 LDPEQR----LDFRELLRDLGTdSCVLVsTHLVEDvAVACTDVI-LINDGQLVHQGTTDDL 233
Cdd:cd03300 161 LDLKLRkdmqLELKRLQKELGI-TFVFV-THDQEE-ALTMSDRIaVMNKGKIQQIGTPEEI 218
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
34-228 |
1.61e-32 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 118.17 E-value: 1.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 34 LDLSLGTGVHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPV---HNRADLHTLRRSLGYLPQHFGFYPRFTVREFV 110
Cdd:cd03297 17 IDFDLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsRKKINLPPQQRKIGLVFQQYALFPHLNVRENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 111 EYLawLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELL 190
Cdd:cd03297 97 AFG--LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPEL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2683828925 191 RDLGTD---SCVLVSTHLVEdVAVACTDVILINDGQLVHQG 228
Cdd:cd03297 175 KQIKKNlniPVIFVTHDLSE-AEYLADRIVVMEDGRLQYIG 214
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
17-235 |
2.05e-32 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 119.06 E-value: 2.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 17 HAEGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHnRADLHTLRRSLGYLP 95
Cdd:COG4559 3 EAENLSVRLGGRTLLDDVSLTLRPGeLTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLA-AWSPWELARRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 96 QH----FGfyprFTVREFVEY--LAWlkHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRR-------AGIAQAI 162
Cdd:COG4559 82 QHsslaFP----FTVEEVVALgrAPH--GSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRvqlarvlAQLWEPV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 163 VNNPAVLLLDEPTVGLDPEQRLDFRELLRDL----GTDSCVLvstHlveDVAVA---CTDVILINDGQLVHQGTTDDLIT 235
Cdd:COG4559 156 DGGPRWLFLDEPTSALDLAHQHAVLRLARQLarrgGGVVAVL---H---DLNLAaqyADRILLLHQGRLVAQGTPEEVLT 229
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
19-240 |
2.77e-32 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 118.21 E-value: 2.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 19 EGLRvRAGRHLAVDGLDLSLGTGVH-GLLGPNGAGKTTLMRALATVVKPAGGTLTLlghpvhNRADLHTL---RRSLGYL 94
Cdd:cd03299 4 ENLS-KDWKEFKLKNVSLEVERGDYfVILGPTGSGKSVLLETIAGFIKPDSGKILL------NGKDITNLppeKRDISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 95 PQHFGFYPRFTVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEP 174
Cdd:cd03299 77 PQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2683828925 175 TVGLDPEQRLDFRELLRDLGTDSCVLV--STHLVEDVAVACTDVILINDGQLVHQGTTDDLITHGGPD 240
Cdd:cd03299 157 FSALDVRTKEKLREELKKIRKEFGVTVlhVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNE 224
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
15-235 |
3.52e-31 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 116.02 E-value: 3.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 15 VVHAEGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHnRADLHTLRRSLGY 93
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGeVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLA-DWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 94 LPQHF--GFyPrFTVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIV------NN 165
Cdd:PRK13548 81 LPQHSslSF-P-FTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2683828925 166 PAVLLLDEPTVGLDPEQRLDFRELLRDLGTDS--CVLVSTHlveDVAVA---CTDVILINDGQLVHQGTTDDLIT 235
Cdd:PRK13548 159 PRWLLLDEPTSALDLAHQHHVLRLARQLAHERglAVIVVLH---DLNLAaryADRIVLLHQGRLVADGTPAEVLT 230
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
19-233 |
3.70e-31 |
|
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: 114.84 E-value: 3.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 19 EGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRADLHTLRRSLGYLPQH 97
Cdd:cd03224 4 ENLNAGYGKSQILFGVSLTVPEGeIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYVPEG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 98 FGFYPRFTVREFVEYLAWLKHlpkatiPDAVQHAIDRV-----GLTAKADTRMKTLSGG---MLrraGIAQAIVNNPAVL 169
Cdd:cd03224 84 RRIFPELTVEENLLLGAYARR------RAKRKARLERVyelfpRLKERRKQLAGTLSGGeqqML---AIARALMSRPKLL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2683828925 170 LLDEPTVGLDP---EQRLDFRELLRDLGTdsCVLvsthLVE---DVAVACTD-VILINDGQLVHQGTTDDL 233
Cdd:cd03224 155 LLDEPSEGLAPkivEEIFEAIRELRDEGV--TIL----LVEqnaRFALEIADrAYVLERGRVVLEGTAAEL 219
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
18-233 |
5.54e-31 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 114.59 E-value: 5.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 18 AEGLRVRAGRHLAVDGLDLSL-GTGVHGLLGPNGAGKTTLMRALA-----TVVKPAGGTLTLLGHPV-HNRADLHTLRRS 90
Cdd:cd03260 3 LRDLNVYYGDKHALKDISLDIpKGEITALIGPSGCGKSTLLRLLNrlndlIPGAPDEGEVLLDGKDIyDLDVDVLELRRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 91 LGYLPQH---FgfypRFTVREFVEYLAWL-KHLPKATIPDAVQHAIDRVGLTAKADTRMK--TLSGGMLRRAGIAQAIVN 164
Cdd:cd03260 83 VGMVFQKpnpF----PGSIYDNVAYGLRLhGIKLKEELDERVEEALRKAALWDEVKDRLHalGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2683828925 165 NPAVLLLDEPTVGLDPEQRLDFRELLRDLGTDSCVLVSTHLVEDVAVACTDVILINDGQLVHQGTTDDL 233
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
8-204 |
5.77e-31 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 121.00 E-value: 5.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 8 APTTHPWVVHAEGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRaDLHT 86
Cdd:NF033858 259 ADDDDEPAIEARGLTMRFGDFTAVDHVSFRIRRGeIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAG-DIAT 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 87 lRRSLGYLPQHFGFYPRFTVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNP 166
Cdd:NF033858 338 -RRRVGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKP 416
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2683828925 167 AVLLLDEPTVGLDPEQRLDFRELLRDLGTDSCV--LVSTH 204
Cdd:NF033858 417 ELLILDEPTSGVDPVARDMFWRLLIELSREDGVtiFISTH 456
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
44-228 |
1.04e-30 |
|
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: 113.03 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 44 GLLGPNGAGKTTLMRALA--TVVKPAGGTLTLLGHPVHnradLHTLRRSLGYLPQHFGFYPRFTVREFVEYLAwlkhlpk 121
Cdd:cd03213 39 AIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLD----KRSFRKIIGYVPQDDILHPTLTVRETLMFAA------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 122 atipdavqhaidrvgltakadtRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLRDLGTDSC-VL 200
Cdd:cd03213 108 ----------------------KLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRtII 165
|
170 180
....*....|....*....|....*....
gi 2683828925 201 VSTH-LVEDVAVACTDVILINDGQLVHQG 228
Cdd:cd03213 166 CSIHqPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
8-238 |
3.57e-30 |
|
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: 118.33 E-value: 3.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 8 APTTHPWVVHAEGLRVR--AGRHLAVDGLDLSLGTGVH-GLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHnRADL 84
Cdd:COG4987 326 APAPGGPSLELEDVSFRypGAGRPVLDGLSLTLPPGERvAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLR-DLDE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 85 HTLRRSLGYLPQHFGFyprF--TVREFVeYLAwlkhLPKATiPDAVQHAIDRVGLTA-------KADTRM----KTLSGG 151
Cdd:COG4987 405 DDLRRRIAVVPQRPHL---FdtTLRENL-RLA----RPDAT-DEELWAALERVGLGDwlaalpdGLDTWLgeggRRLSGG 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 152 MLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLRDLGTDSCVLVSTHLVEDVAvACTDVILINDGQLVHQGTTD 231
Cdd:COG4987 476 ERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLE-RMDRILVLEDGRIVEQGTHE 554
|
....*..
gi 2683828925 232 DLITHGG 238
Cdd:COG4987 555 ELLAQNG 561
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
16-236 |
1.12e-29 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 114.09 E-value: 1.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 16 VHAEGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHnrADLHTLRRSLGYL 94
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGeLVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF--TNLPPRERRVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 95 PQHFGFYPRFTVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEP 174
Cdd:COG1118 81 FQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2683828925 175 TVGLD----PEQRLDFRELLRDLGTDScVLVsTHLVEDVAVACTDVILINDGQLVHQGTTDDLITH 236
Cdd:COG1118 161 FGALDakvrKELRRWLRRLHDELGGTT-VFV-THDQEEALELADRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
29-224 |
1.79e-29 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 110.58 E-value: 1.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 29 LAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHN--RADLHTLRRSLGYLPQHFGFYPRFT 105
Cdd:cd03292 15 AALDGINISISAGeFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrGRAIPYLRRKIGVVFQDFRLLPDRN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 106 VREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLD 185
Cdd:cd03292 95 VYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2683828925 186 FRELLRDL---GTdsCVLVSTHLVEDVAVACTDVILINDGQL 224
Cdd:cd03292 175 IMNLLKKInkaGT--TVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
19-236 |
9.07e-29 |
|
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: 109.35 E-value: 9.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 19 EGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVhnrADLHTLRRSLGYLPQH 97
Cdd:cd03296 6 RNVSKRFGDFVALDDVSLDIPSGeLVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA---TDVPVQERNVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 98 FGFYPRFTVREFVEYLAWLKH----LPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDE 173
Cdd:cd03296 83 YALFRHMTVFDNVAFGLRVKPrserPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2683828925 174 PTVGLDPEQRLDFRELLRDLGTD---SCVLVsTHLVEDVAVACTDVILINDGQLVHQGTTDDLITH 236
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRLHDElhvTTVFV-THDQEEALEVADRVVVMNKGRIEQVGTPDEVYDH 227
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
26-229 |
1.31e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 109.94 E-value: 1.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 26 GRHlAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPV-HNRADLHTLRRSLGYL---PQHFGF 100
Cdd:PRK13636 18 GTH-ALKGININIKKGeVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdYSRKGLMKLRESVGMVfqdPDNQLF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 101 YPrfTVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDP 180
Cdd:PRK13636 97 SA--SVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDP 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2683828925 181 EQRLDFRELLRDL--GTDSCVLVSTHLVEDVAVACTDVILINDGQLVHQGT 229
Cdd:PRK13636 175 MGVSEIMKLLVEMqkELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGN 225
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
26-218 |
1.45e-28 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 107.32 E-value: 1.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 26 GRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTllghpvhnradlHTLRRSLGYLPQHFGFYPRF 104
Cdd:NF040873 3 GGRPVLHGVDLTIPAGsLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR------------RAGGARVAYVPQRSEVPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 105 --TVREFVEYLAW----LKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGL 178
Cdd:NF040873 71 plTVRDLVAMGRWarrgLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2683828925 179 DPEQRLDFRELLRDL-GTDSCVLVSTHLVEDVAVACTDVIL 218
Cdd:NF040873 151 DAESRERIIALLAEEhARGATVVVVTHDLELVRRADPCVLL 191
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
22-236 |
1.58e-28 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 111.05 E-value: 1.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 22 RVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGT-------LTLLghpvhNRADLHTLRRSLGY 93
Cdd:PRK11153 12 PQGGRTIHALNNVSLHIPAGeIFGVIGASGAGKSTLIRCINLLERPTSGRvlvdgqdLTAL-----SEKELRKARRQIGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 94 LPQHFGFYPRFTVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDE 173
Cdd:PRK11153 87 IFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2683828925 174 PTVGLDPE---QRLDF-RELLRDLG-TdscVLVSTHLVEDVAVACTDVILINDGQLVHQGTTDDLITH 236
Cdd:PRK11153 167 ATSALDPAttrSILELlKDINRELGlT---IVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSH 231
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
17-225 |
2.88e-28 |
|
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: 106.96 E-value: 2.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 17 HAEGLRVRAGRH-LAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRadlhTLRRSLGYL 94
Cdd:cd03226 1 RIENISFSYKKGtEILDDLSLDLYAGeIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK----ERRKSIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 95 PQHFGFYPRF-TVREfvEYLAWLKHLPKAtiPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDE 173
Cdd:cd03226 77 MQDVDYQLFTdSVRE--ELLLGLKELDAG--NEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2683828925 174 PTVGLDPEQRLDFRELLRDL-GTDSCVLVSTHLVEDVAVACTDVILINDGQLV 225
Cdd:cd03226 153 PTSGLDYKNMERVGELIRELaAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
30-240 |
6.27e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 109.02 E-value: 6.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 30 AVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGH-PVHNRADLhtlRRSLG-----------YLPq 96
Cdd:COG4586 37 AVDDISFTIEPGeIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYvPFKRRKEF---ARRIGvvfgqrsqlwwDLP- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 97 hfgfyprftvreFVEYLAWLKH---LPKATIPDAVQHAIDRVGLTAKADTRMKTLSGG--MlrRAGIAQAIVNNPAVLLL 171
Cdd:COG4586 113 ------------AIDSFRLLKAiyrIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGqrM--RCELAAALLHRPKILFL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2683828925 172 DEPTVGLDPEQRLDFRELLRDLGTDSC--VLVSTHLVEDVAVACTDVILINDGQLVHQGTTDDLITHGGPD 240
Cdd:COG4586 179 DEPTIGLDVVSKEAIREFLKEYNRERGttILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKERFGPY 249
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
30-228 |
6.76e-28 |
|
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: 107.03 E-value: 6.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 30 AVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRADLHTLRRSLgYLPQHFGFYPRFTVRE 108
Cdd:cd03267 36 ALKGISFTIEKGeIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGV-VFGQKTQLWWDLPVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 109 FVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRE 188
Cdd:cd03267 115 SFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRN 194
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2683828925 189 LLRDLG--TDSCVLVSTHLVEDVAVACTDVILINDGQLVHQG 228
Cdd:cd03267 195 FLKEYNreRGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
30-212 |
7.84e-28 |
|
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: 105.58 E-value: 7.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 30 AVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPV-HNRADLHTLRRSLGYL---PQHFGFYPrf 104
Cdd:TIGR01166 7 VLKGLNFAAERGeVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLdYSRKGLLERRQRVGLVfqdPDDQLFAA-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 105 TVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRL 184
Cdd:TIGR01166 85 DVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGRE 164
|
170 180
....*....|....*....|....*....
gi 2683828925 185 DFRELLRDLGTD-SCVLVSTHlveDVAVA 212
Cdd:TIGR01166 165 QMLAILRRLRAEgMTVVISTH---DVDLA 190
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
22-238 |
8.55e-28 |
|
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: 111.85 E-value: 8.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 22 RVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNrADLHTLRRSLGYLPQHFGF 100
Cdd:COG2274 482 RYPGDSPPVLDNISLTIKPGeRVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQ-IDPASLRRQIGVVLQDVFL 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 101 YPRfTVRE---FveylawlkHLPKATIpDAVQHAIDRVGLTAKA-------DTRM----KTLSGGMLRRAGIAQAIVNNP 166
Cdd:COG2274 561 FSG-TIREnitL--------GDPDATD-EEIIEAARLAGLHDFIealpmgyDTVVgeggSNLSGGQRQRLAIARALLRNP 630
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2683828925 167 AVLLLDEPTVGLDPEQRLDFRELLRDLGTDSCVLVSTH---LVEDvavaCTDVILINDGQLVHQGTTDDLITHGG 238
Cdd:COG2274 631 RILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHrlsTIRL----ADRIIVLDKGRIVEDGTHEELLARKG 701
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
44-237 |
2.99e-27 |
|
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: 106.00 E-value: 2.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 44 GLLGPNGAGKTTLMRALATVVKPAGGTLTLLGH--PVHNRADLHTLRRSLGYLPQhfgfYPR---F--TVREFVEY---- 112
Cdd:TIGR04521 35 AIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRdiTAKKKKKLKDLRKKVGLVFQ----FPEhqlFeeTVYKDIAFgpkn 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 113 LAwlkhLPKATIPDAVQHAIDRVGLtakaDTRMKT-----LSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFR 187
Cdd:TIGR04521 111 LG----LSEEEAEERVKEALELVGL----DEEYLErspfeLSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEIL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2683828925 188 ELLRDL----GTdSCVLVsTHLVEDVAVACTDVILINDGQLVHQGTTDDLITHG 237
Cdd:TIGR04521 183 DLFKRLhkekGL-TVILV-THSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
42-228 |
3.81e-27 |
|
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: 104.66 E-value: 3.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 42 VHGLLGPNGAGKTTLMRALATVVKPAG---GTLTLLGHPVHNradlHTLRRSLGYLPQHFGFYPRFTVREFVEYLAWLK- 117
Cdd:cd03234 35 VMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKP----DQFQKCVAYVRQDDILLPGLTVRETLTYTAILRl 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 118 --HLPKATI-PDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLRDLG 194
Cdd:cd03234 111 prKSSDAIRkKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLA 190
|
170 180 190
....*....|....*....|....*....|....*.
gi 2683828925 195 TDSC-VLVSTHL-VEDVAVACTDVILINDGQLVHQG 228
Cdd:cd03234 191 RRNRiVILTIHQpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
20-235 |
4.05e-27 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 108.01 E-value: 4.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 20 GLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRaDLHTLRRSLGYLPQHF 98
Cdd:PRK09536 8 DLSVEFGDTTVLDGVDLSVREGsLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEAL-SARAASRRVASVPQDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 99 GFYPRFTVREFVEyLAWLKHLPKATIPD-----AVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDE 173
Cdd:PRK09536 87 SLSFEFDVRQVVE-MGRTPHRSRFDTWTetdraAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2683828925 174 PTVGLDPEQRLDFRELLRDLG-TDSCVLVSTHLVEDVAVACTDVILINDGQLVHQGTTDDLIT 235
Cdd:PRK09536 166 PTASLDINHQVRTLELVRRLVdDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLT 228
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
19-233 |
5.10e-27 |
|
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: 104.29 E-value: 5.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 19 EGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRADLHTLRRSLGYLPQH 97
Cdd:COG0410 7 ENLHAGYGGIHVLHGVSLEVEEGeIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIGYVPEG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 98 FGFYPRFTVREFVEYLAWLKHlpkatIPDAVQHAIDRVG-----LTAKADTRMKTLSGG---MLrraGIAQAIVNNPAVL 169
Cdd:COG0410 87 RRIFPSLTVEENLLLGAYARR-----DRAEVRADLERVYelfprLKERRRQRAGTLSGGeqqML---AIGRALMSRPKLL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2683828925 170 LLDEPTVGLDPEQRLDFRELLRDL---GTdsCVLvsthLVE---DVAVACTD-VILINDGQLVHQGTTDDL 233
Cdd:COG0410 159 LLDEPSLGLAPLIVEEIFEIIRRLnreGV--TIL----LVEqnaRFALEIADrAYVLERGRIVLEGTAAEL 223
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
24-236 |
7.49e-27 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 104.40 E-value: 7.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 24 RAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVH-NRADLHTLRRSLGYLPQHFGFY 101
Cdd:PRK09493 10 HFGPTQVLHNIDLNIDQGeVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdPKVDERLIRQEAGMVFQQFYLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 102 PRFTVREFVEYLAwlKHLPKATIPDAVQHA---IDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGL 178
Cdd:PRK09493 90 PHLTALENVMFGP--LRVRGASKEEAEKQArelLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2683828925 179 DPEQRLDFRELLRDLGTDSCVLV-STHLVEDVAVACTDVILINDGQLVHQGTTDDLITH 236
Cdd:PRK09493 168 DPELRHEVLKVMQDLAEEGMTMViVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKN 226
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
19-228 |
1.32e-26 |
|
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: 102.72 E-value: 1.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 19 EGLRVRAGRHLAVDGLDLSLGTG---VhgLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVhnrADLHTLRRSLGYLP 95
Cdd:cd03301 4 ENVTKRFGNVTALDDLNLDIADGefvV--LLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV---TDLPPKDRDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 96 QHFGFYPRFTVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPT 175
Cdd:cd03301 79 QNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2683828925 176 VGLDP----EQRLDFRELLRDLGTdSCVLVSTHLVEDVAVAcTDVILINDGQLVHQG 228
Cdd:cd03301 159 SNLDAklrvQMRAELKRLQQRLGT-TTIYVTHDQVEAMTMA-DRIAVMNDGQIQQIG 213
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
15-239 |
1.60e-26 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 104.12 E-value: 1.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 15 VVH--AEGLRVRAGRHLAV-DGLDLSLGTGVH-GLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVH--NRADLHTLR 88
Cdd:TIGR02769 8 VTHtyRTGGLFGAKQRAPVlTNVSLSIEEGETvGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYqlDRKQRRAFR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 89 RSLGYLPQ--HFGFYPRFTVREFV-EYLAWLKHLPKATIPDAVQHAIDRVGLTAK-ADTRMKTLSGGMLRRAGIAQAIVN 164
Cdd:TIGR02769 88 RDVQLVFQdsPSAVNPRMTVRQIIgEPLRHLTSLDESEQKARIAELLDMVGLRSEdADKLPRQLSGGQLQRINIARALAV 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2683828925 165 NPAVLLLDEPTVGLDPEQRLDFRELLRDL----GTdSCVLVsTHLVEDVAVACTDVILINDGQLVHQGTTDDLITHGGP 239
Cdd:TIGR02769 168 KPKLIVLDEAVSNLDMVLQAVILELLRKLqqafGT-AYLFI-THDLRLVQSFCQRVAVMDKGQIVEECDVAQLLSFKHP 244
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
24-227 |
3.66e-26 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 103.02 E-value: 3.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 24 RAGRHLAVDGLDLSLGTG---VhgLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVH----NRadlhtlrrslGYLPQ 96
Cdd:COG4525 16 GGQPQPALQDVSLTIESGefvV--ALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTgpgaDR----------GVVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 97 HFGFYPRFTVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTV 176
Cdd:COG4525 84 KDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFG 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2683828925 177 GLDPEQRLDFRELLRDL--GTDSCVLVSTHLVEDVAVACTDVILI--NDGQLVHQ 227
Cdd:COG4525 164 ALDALTREQMQELLLDVwqRTGKGVFLITHSVEEALFLATRLVVMspGPGRIVER 218
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
24-236 |
8.52e-26 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 103.64 E-value: 8.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 24 RAGRHLAVDgLDLSlGTGVHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRADLHTL---RRSLGYLPQHFGF 100
Cdd:COG4148 11 RGGFTLDVD-FTLP-GRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFLpphRRRIGYVFQEARL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 101 YPRFTVREFVEYLAWlkHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDP 180
Cdd:COG4148 89 FPHLSVRGNLLYGRK--RAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2683828925 181 EQR---LDFRELLRDLGTDSCVLVStHLVEDVAVACTDVILINDGQLVHQGTTDDLITH 236
Cdd:COG4148 167 ARKaeiLPYLERLRDELDIPILYVS-HSLDEVARLADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
31-234 |
8.92e-26 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 101.51 E-value: 8.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 31 VDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGH-----PVHNRAdlhtlRRSLGYLPQHFGFYPRF 104
Cdd:PRK10895 19 VEDVSLTVNSGeIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllPLHARA-----RRGIGYLPQEASIFRRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 105 TVRE-FVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQR 183
Cdd:PRK10895 94 SVYDnLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2683828925 184 LDFREL---LRDLGTDscVLVSTHLVEDVAVACTDVILINDGQLVHQGTTDDLI 234
Cdd:PRK10895 174 IDIKRIiehLRDSGLG--VLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
45-229 |
1.02e-25 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 101.24 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 45 LLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRADLHT-----LRRSLGYLPQHFGFYPRFTVRE-FVEYLAWLKH 118
Cdd:COG4161 33 LLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSEkairlLRQKVGMVFQQYNLWPHLTVMEnLIEAPCKVLG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 119 LPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLRDLG-TDS 197
Cdd:COG4161 113 LSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSqTGI 192
|
170 180 190
....*....|....*....|....*....|..
gi 2683828925 198 CVLVSTHLVEDVAVACTDVILINDGQLVHQGT 229
Cdd:COG4161 193 TQVIVTHEVEFARKVASQVVYMEKGRIIEQGD 224
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
45-231 |
1.41e-25 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 100.86 E-value: 1.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 45 LLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVH-----NRADLHTLRRSLGYLPQHFGFYPRFTVRE-FVEYLAWLKH 118
Cdd:PRK11124 33 LLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDfsktpSDKAIRELRRNVGMVFQQYNLWPHLTVQQnLIEAPCRVLG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 119 LPKAtipDAVQHA---IDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLRDL-G 194
Cdd:PRK11124 113 LSKD---QALARAeklLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELaE 189
|
170 180 190
....*....|....*....|....*....|....*..
gi 2683828925 195 TDSCVLVSTHLVEDVAVACTDVILINDGQLVHQGTTD 231
Cdd:PRK11124 190 TGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDAS 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
18-224 |
1.43e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 104.76 E-value: 1.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 18 AEGLRVRAGRHLAVDGLDLSLGTGVH-GLLGPNGAGKTTLMRALATVVKPAGGTLTLlghpvhnRADLhtlrrSLGYLPQ 96
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRiGLVGRNGAGKSTLLKILAGELEPDSGEVSI-------PKGL-----RIGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 97 HFGFYPRFTVREFV-----EYLAWLKHLPKATIPDA-----------VQHAIDRVG---LTAKA--------------DT 143
Cdd:COG0488 69 EPPLDDDLTVLDTVldgdaELRALEAELEELEAKLAepdedlerlaeLQEEFEALGgweAEARAeeilsglgfpeedlDR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 144 RMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLRDLgtDSCVLVSTH---LVEDVavaCTDVILIN 220
Cdd:COG0488 149 PVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNY--PGTVLVVSHdryFLDRV---ATRILELD 223
|
....
gi 2683828925 221 DGQL 224
Cdd:COG0488 224 RGKL 227
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
15-230 |
1.71e-25 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 101.24 E-value: 1.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 15 VVHAEGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVV---KPAGGTLTLLGHPVHNRA----DLHT 86
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGeMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQREGrlarDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 87 LRRSLGYLPQHFGFYPRFTVREFV------------EYLAWLKHLPKAtipDAVQhAIDRVGLTAKADTRMKTLSGGMLR 154
Cdd:PRK09984 84 SRANTGYIFQQFNLVNRLSVLENVligalgstpfwrTCFSWFTREQKQ---RALQ-ALTRVGMVHFAHQRVSTLSGGQQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2683828925 155 RAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLRDLGTDS--CVLVSTHLVEDVAVACTDVILINDGQLVHQGTT 230
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDYALRYCERIVALRQGHVFYDGSS 237
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
24-233 |
1.78e-25 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 102.88 E-value: 1.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 24 RAGRHLAVDGLDLSL--GTGVhGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRAdlhTLRRSLGYLPQHFGFY 101
Cdd:PRK11432 15 RFGSNTVIDNLNLTIkqGTMV-TLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRS---IQQRDICMVFQSYALF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 102 PRFTVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPE 181
Cdd:PRK11432 91 PHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDAN 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2683828925 182 QRLDFRELLRDLGT--DSCVLVSTH-LVEDVAVACTdVILINDGQLVHQGTTDDL 233
Cdd:PRK11432 171 LRRSMREKIRELQQqfNITSLYVTHdQSEAFAVSDT-VIVMNKGKIMQIGSPQEL 224
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
45-233 |
1.90e-25 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 104.74 E-value: 1.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 45 LLGPNGAGKTTLMRALATVVKPA---GGTLTLLGHPVhnraDLHTLRRSLGYLPQHFGFYPRFTVREFVEYLAWLK---H 118
Cdd:TIGR00955 56 VMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPI----DAKEMRAISAYVQQDDLFIPTLTVREHLMFQAHLRmprR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 119 LPKATIPDAVQHAIDRVGLTAKADT------RMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLRD 192
Cdd:TIGR00955 132 VTKKEKRERVDEVLQALGLRKCANTrigvpgRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKG 211
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2683828925 193 LGTD-SCVLVSTH-----LVEDVavacTDVILINDGQLVHQGTTDDL 233
Cdd:TIGR00955 212 LAQKgKTIICTIHqpsseLFELF----DKIILMAEGRVAYLGSPDQA 254
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
18-227 |
2.30e-25 |
|
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: 98.27 E-value: 2.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 18 AEGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRADLHTLRRSLGYLPQ 96
Cdd:cd03216 3 LRGITKRFGGVKALDGVSLSVRRGeVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMVYQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 97 hfgfyprftvrefveylawlkhlpkatipdavqhaidrvgltakadtrmktLSGGMLRRAGIAQAIVNNPAVLLLDEPTV 176
Cdd:cd03216 83 ---------------------------------------------------LSVGERQMVEIARALARNARLLILDEPTA 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2683828925 177 GLDPEQRLDFRELLRDLGTD--SCVLVSTHLVEDVAVaCTDVILINDGQLVHQ 227
Cdd:cd03216 112 ALTPAEVERLFKVIRRLRAQgvAVIFISHRLDEVFEI-ADRVTVLRDGRVVGT 163
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
15-236 |
2.48e-25 |
|
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: 101.67 E-value: 2.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 15 VVHAEGLRV----RAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKP---AGGTLTLLGHPVHN--RADL 84
Cdd:COG0444 1 LLEVRNLKVyfptRRGVVKAVDGVSFDVRRGeTLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKlsEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 85 HTLR-RSLGYLPQH-FG-FYPRFTVRE-FVEYLAWLKHLPKATIPDAVQHAIDRVGLTAkADTRMK----TLSGGMLRRA 156
Cdd:COG0444 81 RKIRgREIQMIFQDpMTsLNPVMTVGDqIAEPLRIHGGLSKAEARERAIELLERVGLPD-PERRLDryphELSGGMRQRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 157 GIAQAIVNNPAVLLLDEPTVGLDPE---QRLD-FRELLRDLGTdSCVLVsTHlveDVAVA---CTDVILINDGQLVHQGT 229
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTiqaQILNlLKDLQRELGL-AILFI-TH---DLGVVaeiADRVAVMYAGRIVEEGP 234
|
....*..
gi 2683828925 230 TDDLITH 236
Cdd:COG0444 235 VEELFEN 241
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
30-229 |
2.52e-25 |
|
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: 105.10 E-value: 2.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 30 AVDGLDLSL-GTGVHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRADlhTLRRSLGYLPQHFGFYPRFTVRE 108
Cdd:TIGR01257 945 AVDRLNITFyENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLD--AVRQSLGMCPQHNILFHHLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 109 FVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRE 188
Cdd:TIGR01257 1023 HILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWD 1102
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2683828925 189 LLRDLGTDSCVLVSTHLVEDVAVACTDVILINDGQLVHQGT 229
Cdd:TIGR01257 1103 LLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
30-229 |
3.08e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 100.92 E-value: 3.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 30 AVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPV-HNRADLHTLRRSLGYL---PQHFGFYPrf 104
Cdd:PRK13639 17 ALKGINFKAEKGeMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkYDKKSLLEVRKTVGIVfqnPDDQLFAP-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 105 TVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRL 184
Cdd:PRK13639 95 TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGAS 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2683828925 185 DFRELLRDLGTDS-CVLVSTHLVEDVAVACTDVILINDGQLVHQGT 229
Cdd:PRK13639 175 QIMKLLYDLNKEGiTIIISTHDVDLVPVYADKVYVMSDGKIIKEGT 220
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
7-229 |
3.48e-25 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 102.33 E-value: 3.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 7 IAPTTHPWVVHAEGLRVRAGRHLAVDGLDLSLgtgVHG----LLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVhnrA 82
Cdd:PRK09452 6 KQPSSLSPLVELRGISKSFDGKEVISNLDLTI---NNGefltLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI---T 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 83 DLHTLRRSLGYLPQHFGFYPRFTVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAI 162
Cdd:PRK09452 80 HVPAENRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2683828925 163 VNNPAVLLLDEPTVGLD----PEQRLDFRELLRDLGTdSCVLVsTHLVEDvAVACTD-VILINDGQLVHQGT 229
Cdd:PRK09452 160 VNKPKVLLLDESLSALDyklrKQMQNELKALQRKLGI-TFVFV-THDQEE-ALTMSDrIVVMRDGRIEQDGT 228
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
33-236 |
5.12e-25 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 99.44 E-value: 5.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 33 GLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTL------LGHPV-HNRADLHTLRRSLGYLPQHFGFYPRF 104
Cdd:PRK11264 21 GIDLEVKPGeVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidTARSLsQQKGLIRQLRQHVGFVFQNFNLFPHR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 105 TVRE-FVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQR 183
Cdd:PRK11264 101 TVLEnIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELV 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2683828925 184 LDFRELLRDLGTDSCVLV-STH---LVEDVAvacTDVILINDGQLVHQGTTDDLITH 236
Cdd:PRK11264 181 GEVLNTIRQLAQEKRTMViVTHemsFARDVA---DRAIFMDQGRIVEQGPAKALFAD 234
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
16-235 |
6.70e-25 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 99.68 E-value: 6.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 16 VHAEGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRADLHTLRRsLGYL 94
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGhFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR-IGLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 95 PQHFGFYPRFTVREFVEYLAWlKHLPKATI-----PDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVL 169
Cdd:PRK10253 87 AQNATTPGDITVQELVARGRY-PHQPLFTRwrkedEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIM 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2683828925 170 LLDEPTVGLDPEQRLDFRELLRDLGTDSCVLVSThLVEDVAVAC---TDVILINDGQLVHQGTTDDLIT 235
Cdd:PRK10253 166 LLDEPTTWLDISHQIDLLELLSELNREKGYTLAA-VLHDLNQACryaSHLIALREGKIVAQGAPKEIVT 233
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
28-223 |
1.35e-24 |
|
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: 96.30 E-value: 1.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 28 HLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNrADLHTLRRSLGYLPQHFGFYPRfTV 106
Cdd:cd03228 15 KPVLKDVSLTIKPGeKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRD-LDLESLRKNIAYVPQDPFLFSG-TI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 107 REFVeylawlkhlpkatipdavqhaidrvgltakadtrmktLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDF 186
Cdd:cd03228 93 RENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALI 135
|
170 180 190
....*....|....*....|....*....|....*..
gi 2683828925 187 RELLRDLGTDSCVLVSTHLVEDVAvACTDVILINDGQ 223
Cdd:cd03228 136 LEALRALAKGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
19-246 |
1.77e-24 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 98.14 E-value: 1.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 19 EGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRADLHTLRRSLGYLPQH 97
Cdd:PRK11300 9 SGLMMRFGGLLAVNNVNLEVREQeIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRTFQH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 98 FGFYPRFTVrefVEYL--AWLKHLPKATIP-------------DAVQHA---IDRVGLTAKADTRMKTLSGGMLRRAGIA 159
Cdd:PRK11300 89 VRLFREMTV---IENLlvAQHQQLKTGLFSgllktpafrraesEALDRAatwLERVGLLEHANRQAGNLAYGQQRRLEIA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 160 QAIVNNPAVLLLDEPTVGLDPEQRLDFRELLRDLGTD--SCVLVSTH---LVEDVavacTDVILIndgqlVHQGTTddlI 234
Cdd:PRK11300 166 RCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhnVTVLLIEHdmkLVMGI----SDRIYV-----VNQGTP---L 233
|
250
....*....|..
gi 2683828925 235 THGGPDDPGDSP 246
Cdd:PRK11300 234 ANGTPEEIRNNP 245
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
30-236 |
2.02e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 101.25 E-value: 2.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 30 AVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRADLHTLRRSLGYLPQHFGFYPRFTVRE 108
Cdd:COG1129 19 ALDGVSLELRPGeVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAGIAIIHQELNLVPNLSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 109 FVeylaWLKHLP--------KATIPDAvQHAIDRVGLTAKADTRMKTLSGG---MLRragIAQAIVNNPAVLLLDEPTVG 177
Cdd:COG1129 99 NI----FLGREPrrgglidwRAMRRRA-RELLARLGLDIDPDTPVGDLSVAqqqLVE---IARALSRDARVLILDEPTAS 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2683828925 178 LDPE--QRLdFReLLRDL---GTdSCVLVSTHLvEDVAVACTDVILINDGQLVHQG-----TTDDLITH 236
Cdd:COG1129 171 LTERevERL-FR-IIRRLkaqGV-AIIYISHRL-DEVFEIADRVTVLRDGRLVGTGpvaelTEDELVRL 235
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
35-239 |
2.72e-24 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 97.13 E-value: 2.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 35 DLSLGTGVH-GLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVhnrADLHTLRRSLGYLPQHFGFYPRFTVREFVeYL 113
Cdd:COG3840 19 DLTIAAGERvAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL---TALPPAERPVSMLFQENNLFPHLTVAQNI-GL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 114 AWLKHLpKATIPD--AVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLR 191
Cdd:COG3840 95 GLRPGL-KLTAEQraQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2683828925 192 DLG--TDSCVLVSTHLVEDVAVACTDVILINDGQLVHQGTTDDLITHGGP 239
Cdd:COG3840 174 ELCreRGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPP 223
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
29-237 |
3.66e-24 |
|
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: 97.50 E-value: 3.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 29 LAVDGLDLSLGTG--VhGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRADLHTLRRSLGYLPQHfgfyP--RF 104
Cdd:TIGR04520 16 PALKNVSLSIEKGefV-AIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWEIRKKVGMVFQN----PdnQF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 105 ---TVREFV----EYLAwlkhLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVG 177
Cdd:TIGR04520 91 vgaTVEDDVafglENLG----VPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSM 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2683828925 178 LDPEQRLDFRELLRDLGTDS--CVLVSTHLVEDVAVActD-VILINDGQLVHQGTTDDLITHG 237
Cdd:TIGR04520 167 LDPKGRKEVLETIRKLNKEEgiTVISITHDMEEAVLA--DrVIVMNKGKIVAEGTPREIFSQV 227
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
21-242 |
3.72e-24 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 97.35 E-value: 3.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 21 LRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVH------------NRADLHTL 87
Cdd:PRK10619 11 LHKRYGEHEVLKGVSLQANAGdVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvaDKNQLRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 88 RRSLGYLPQHFGFYPRFTVREFV-EYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKT-LSGGMLRRAGIAQAIVNN 165
Cdd:PRK10619 91 RTRLTMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVhLSGGQQQRVSIARALAME 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2683828925 166 PAVLLLDEPTVGLDPEQRLDFRELLRDLGTD-SCVLVSTHLVEDVAVACTDVILINDGQLVHQGTTDDLIthGGPDDP 242
Cdd:PRK10619 171 PEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLF--GNPQSP 246
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
21-251 |
3.75e-24 |
|
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: 99.42 E-value: 3.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 21 LRVRAGRHLAVDGLDLSL---GTGVHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHN---RADLHTLRRSLGYL 94
Cdd:TIGR02142 1 LSARFSKRLGDFSLDADFtlpGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkGIFLPPEKRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 95 PQHFGFYPRFTVREFVEYLAWLKHLPKATI-PDAVqhaIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDE 173
Cdd:TIGR02142 81 FQEARLFPHLSVRGNLRYGMKRARPSERRIsFERV---IELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 174 PTVGLDPEQR---LDFRELLRDLGTDSCVLVStHLVEDVAVACTDVILINDGQLVHQGTTDDLIthGGPDDPGDSPAERG 250
Cdd:TIGR02142 158 PLAALDDPRKyeiLPYLERLHAEFGIPILYVS-HSLQEVLRLADRVVVLEDGRVAAAGPIAEVW--ASPDLPWLAREDQG 234
|
.
gi 2683828925 251 Y 251
Cdd:TIGR02142 235 S 235
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
19-235 |
4.36e-24 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 97.08 E-value: 4.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 19 EGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHnRADLHTLRRSLGYLPQH 97
Cdd:COG4604 5 KNVSKRYGGKVVLDDVSLTIPKGgITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVA-TTPSRELAKRLAILRQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 98 FGFYPRFTVREFVEYLAWLKHLPKATIPD--AVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPT 175
Cdd:COG4604 84 NHINSRLTVRELVAFGRFPYSKGRLTAEDreIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2683828925 176 VGLDPE------QRLdfRELLRDLGTdSCVLVsthlVEDV--AVACTDVIL-INDGQLVHQGTTDDLIT 235
Cdd:COG4604 164 NNLDMKhsvqmmKLL--RRLADELGK-TVVIV----LHDInfASCYADHIVaMKDGRVVAQGTPEEIIT 225
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
8-212 |
6.14e-24 |
|
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: 100.44 E-value: 6.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 8 APTTHPWVVHAEGLRVR-AGRHLAVDGLDLSLGTGVH-GLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNrADLH 85
Cdd:TIGR02857 314 VTAAPASSLEFSGVSVAyPGRRPALRPVSFTVPPGERvALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLAD-ADAD 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 86 TLRRSLGYLPQHFGFYPRfTVREFVEyLAwlkhLPKATiPDAVQHAIDRV-----------GLTAKADTRMKTLSGGMLR 154
Cdd:TIGR02857 393 SWRDQIAWVPQHPFLFAG-TIAENIR-LA----RPDAS-DAEIREALERAgldefvaalpqGLDTPIGEGGAGLSGGQAQ 465
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2683828925 155 RAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLRDLGTDSCVLVSTHLVEDVAVA 212
Cdd:TIGR02857 466 RLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALA 523
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
15-259 |
1.36e-23 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 99.81 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 15 VVHAEGLRVRAGRHLAVDGLDLSL--GTGVhGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRAdlHtlRRSLG 92
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIpaGCMV-GLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADAR--H--RRAVC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 93 ----YLPQHFG--FYPRFTVREFVEYLAWLKHLPKAtipdAVQHAIDRV----GLTAKADTRMKTLSGGMLRRAGIAQAI 162
Cdd:NF033858 76 priaYMPQGLGknLYPTLSVFENLDFFGRLFGQDAA----ERRRRIDELlratGLAPFADRPAGKLSGGMKQKLGLCCAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 163 VNNPAVLLLDEPTVGLDPEQRLDFRELLRDLGTDS---CVLVSTHLVE-----DVAVActdvilINDGQLVHQGTTDDLI 234
Cdd:NF033858 152 IHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERpgmSVLVATAYMEeaerfDWLVA------MDAGRVLATGTPAELL 225
|
250 260 270
....*....|....*....|....*....|
gi 2683828925 235 THGGPDDPgdspaERGYSALL-----RRHR 259
Cdd:NF033858 226 ARTGADTL-----EAAFIALLpeekrRGHQ 250
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
22-236 |
1.36e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 95.53 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 22 RVRAGRHLAVDGLDLSLGTGVH-GLLGPNGAGKTTLMRALATVVKPAGGTLT-------LLGhpvhnradlhtlrrsLGy 93
Cdd:COG1134 33 RTRREEFWALKDVSFEVERGESvGIIGRNGAGKSTLLKLIAGILEPTSGRVEvngrvsaLLE---------------LG- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 94 lpqhFGFYPRFTVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDE 173
Cdd:COG1134 97 ----AGFHPELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 174 PT-VGlDPE------QRldFRELLRDLGTdscVLVSTHLVEDVAVACTDVILINDGQLVHQGTTDDLITH 236
Cdd:COG1134 173 VLaVG-DAAfqkkclAR--IRELRESGRT---VIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-236 |
4.67e-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: 97.83 E-value: 4.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 4 AAAIAPTTHPWVVHAEGLRV-----------RAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVkPAGGTL 71
Cdd:COG4172 264 DPRPVPPDAPPLLEARDLKVwfpikrglfrrTVGHVKAVDGVSLTLRRGeTLGLVGESGSGKSTLGLALLRLI-PSEGEI 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 72 TLLGHPVH--NRADLHTLRRSLGYLPQH-FG-FYPRFTVREFV-EYLAWLK-HLPKATIPDAVQHAIDRVGLTAkaDTRM 145
Cdd:COG4172 343 RFDGQDLDglSRRALRPLRRRMQVVFQDpFGsLSPRMTVGQIIaEGLRVHGpGLSAAERRARVAEALEEVGLDP--AARH 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 146 K---TLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLRDLGTD---SCVLVStHlveDVAVA---CTDV 216
Cdd:COG4172 421 RyphEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREhglAYLFIS-H---DLAVVralAHRV 496
|
250 260
....*....|....*....|
gi 2683828925 217 ILINDGQLVHQGTTDDLITH 236
Cdd:COG4172 497 MVMKDGKVVEQGPTEQVFDA 516
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
30-254 |
7.17e-23 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 97.78 E-value: 7.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 30 AVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPV-HNRADLHtlrRSLGYLPQHFGFYPRFTVR 107
Cdd:TIGR01257 1954 AVDRLCVGVRPGeCFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISDVH---QNMGYCPQFDAIDDLLTGR 2030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 108 EFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPE-QRLDF 186
Cdd:TIGR01257 2031 EHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQaRRMLW 2110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 187 RELLRDLGTDSCVLVSTHLVEDVAVACTDVILINDGQLVHQGT---------------------TDDLITHGGPDD---- 241
Cdd:TIGR01257 2111 NTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTiqhlkskfgdgyivtmkikspKDDLLPDLNPVEqffq 2190
|
250
....*....|....*.
gi 2683828925 242 ---PGDSPAERGYSAL 254
Cdd:TIGR01257 2191 gnfPGSVQRERHYNML 2206
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
45-235 |
1.01e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 94.10 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 45 LLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVhNRADLHTLRRSLGYLPQHFG---FYPrfTVREFVEYLAWLKHLPK 121
Cdd:PRK13652 35 VIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPI-TKENIREVRKFVGLVFQNPDdqiFSP--TVEQDIAFGPINLGLDE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 122 ATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLRDLGTD--SCV 199
Cdd:PRK13652 112 ETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTV 191
|
170 180 190
....*....|....*....|....*....|....*.
gi 2683828925 200 LVSTHLVEDVAVACTDVILINDGQLVHQGTTDDLIT 235
Cdd:PRK13652 192 IFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFL 227
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
20-235 |
1.57e-22 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 93.21 E-value: 1.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 20 GLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVH--NRADLHTLRRSLGYLPQ 96
Cdd:PRK10419 17 GLSGKHQHQTVLNNVSLSLKSGeTVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAklNRAQRKAFRRDIQMVFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 97 HF--GFYPRFTVREFV-EYLAWLKHLPKATIPDAVQHAIDRVGLTAK-ADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLD 172
Cdd:PRK10419 97 DSisAVNPRKTVREIIrEPLRHLLSLDKAERLARASEMLRAVDLDDSvLDKRPPQLSGGQLQRVCLARALAVEPKLLILD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2683828925 173 EPTVGLDPEQRLDFRELLRDL----GTdSCVLVsTHLVEDVAVACTDVILINDGQLVHQGTTDDLIT 235
Cdd:PRK10419 177 EAVSNLDLVLQAGVIRLLKKLqqqfGT-ACLFI-THDLRLVERFCQRVMVMDNGQIVETQPVGDKLT 241
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
18-222 |
1.94e-22 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 92.84 E-value: 1.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 18 AEGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRAdlhtlrRSLGYLPQ 96
Cdd:PRK11248 4 ISHLYADYGGKPALEDINLTLESGeLLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG------AERGVVFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 97 HFGFYPRFTVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTV 176
Cdd:PRK11248 78 NEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2683828925 177 GLDPEQRLDFRELLRDL--GTDSCVLVSTHLVEDVAVACTDVILINDG 222
Cdd:PRK11248 158 ALDAFTREQMQTLLLKLwqETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
28-228 |
2.42e-22 |
|
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: 91.88 E-value: 2.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 28 HLAVDGLDLSLGTGVH-GLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVhNRADLHTLRRSLGYLPQHFG-FYPrfT 105
Cdd:cd03245 17 IPALDNVSLTIRAGEKvAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDI-RQLDPADLRRNIGYVPQDVTlFYG--T 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 106 VREFVEYLAwlkhlPKATiPDAVQHAIDRVGLTAKADT-----------RMKTLSGGMLRRAGIAQAIVNNPAVLLLDEP 174
Cdd:cd03245 94 LRDNITLGA-----PLAD-DERILRAAELAGVTDFVNKhpngldlqigeRGRGLSGGQRQAVALARALLNDPPILLLDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2683828925 175 TVGLDPEQRLDFRELLRDLGTDSCVLVSTHLVEDVAVaCTDVILINDGQLVHQG 228
Cdd:cd03245 168 TSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDL-VDRIIVMDSGRIVADG 220
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
15-226 |
2.89e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.52 E-value: 2.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 15 VVHAEGLRVRAGRHLAVDGLDLSLGTG--VhGLLGPNGAGKTTLMRALATVVKPAGGTLTlLGHPVHnradlhtlrrsLG 92
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGdrI-GLIGPNGAGKSTLLKLLAGELEPDSGTVK-LGETVK-----------IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 93 YLPQHF-GFYPRFTVREFVEYLAwlkhlPKATIpdavQHAIDRVGL----TAKADTRMKTLSGGMLRRAGIAQAIVNNPA 167
Cdd:COG0488 382 YFDQHQeELDPDKTVLDELRDGA-----PGGTE----QEVRGYLGRflfsGDDAFKPVGVLSGGEKARLALAKLLLSPPN 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2683828925 168 VLLLDEPTVGLDpeqrLDFRELLRDL-----GTdsCVLVS--THLVEDVavaCTDVILINDGQLVH 226
Cdd:COG0488 453 VLLLDEPTNHLD----IETLEALEEAlddfpGT--VLLVShdRYFLDRV---ATRILEFEDGGVRE 509
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
11-232 |
3.73e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 95.09 E-value: 3.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 11 THPWVVHAEGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRADLHTLRR 89
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGeIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 90 SLGYLPQHFGFYPRFTVREFV----EYLAWLKhLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNN 165
Cdd:COG3845 81 GIGMVHQHFMLVPNLTVAENIvlglEPTKGGR-LDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2683828925 166 PAVLLLDEPTVGLDPEQRLDFRELLRDLGTDSC-VLVSTHLVEDVAVACTDVILINDGQLVHQGTTDD 232
Cdd:COG3845 160 ARILILDEPTAVLTPQEADELFEILRRLAAEGKsIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAE 227
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
18-204 |
4.36e-22 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 90.70 E-value: 4.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 18 AEGLRVRAGRHLAVDGLDLSLGTGVHGLL-GPNGAGKTTLMRALATVVKPAGGTLTLLGHPvhnrADLHTLRRSLGYLPQ 96
Cdd:PRK13539 5 GEDLACVRGGRVLFSGLSFTLAAGEALVLtGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD----IDDPDVAEACHYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 97 HFGFYPRFTVREFVEYLAWLKhlpkATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTV 176
Cdd:PRK13539 81 RNAMKPALTVAENLEFWAAFL----GGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTA 156
|
170 180 190
....*....|....*....|....*....|
gi 2683828925 177 GLDPE-QRLdFRELLRD-LGTDSCVLVSTH 204
Cdd:PRK13539 157 ALDAAaVAL-FAELIRAhLAQGGIVIAATH 185
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
30-229 |
5.27e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 92.42 E-value: 5.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 30 AVDGLDLSLGTGVH-GLLGPNGAGKTTLMRALATVVKPAGGTLTLLG-HPVHNRADLHTLRRSLGYLPQhfgfYPRF--- 104
Cdd:PRK13637 22 ALDNVNIEIEDGEFvGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvDITDKKVKLSDIRKKVGLVFQ----YPEYqlf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 105 --TVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAK--ADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDP 180
Cdd:PRK13637 98 eeTIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEdyKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2683828925 181 EQRLDFRELLRDLGTD---SCVLVStHLVEDVAVACTDVILINDGQLVHQGT 229
Cdd:PRK13637 178 KGRDEILNKIKELHKEynmTIILVS-HSMEDVAKLADRIIVMNKGKCELQGT 228
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
19-212 |
5.78e-22 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 90.62 E-value: 5.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 19 EGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKP---AGGTLTLLGHPVHnraDLHTLRRSLGYL 94
Cdd:COG4136 5 ENLTITLGGRPLLAPLSLTVAPGeILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLT---ALPAEQRRIGIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 95 PQHFGFYPRFTVRE---FveylAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLL 171
Cdd:COG4136 82 FQDDLLFPHLSVGEnlaF----ALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2683828925 172 DEPTVGLDPEQRLDFREL----LRDLGTdSCVLVsTHLVEDVAVA 212
Cdd:COG4136 158 DEPFSKLDAALRAQFREFvfeqIRQRGI-PALLV-THDEEDAPAA 200
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
16-225 |
5.86e-22 |
|
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: 90.96 E-value: 5.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 16 VHAEGLRVRAGRH-LAV-DGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHN-----RADLhtL 87
Cdd:COG4181 11 LRGLTKTVGTGAGeLTIlKGISLEVEAGeSVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAldedaRARL--R 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 88 RRSLGYLPQHFGFYPRFTVREFVEYLAWLKHLPKATipDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPA 167
Cdd:COG4181 89 ARHVGFVFQSFQLLPTLTALENVMLPLELAGRRDAR--ARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2683828925 168 VLLLDEPTVGLDPEQRLDFRELLRDL----GTdSCVLVsTHlveDVAVA--CTDVILINDGQLV 225
Cdd:COG4181 167 ILFADEPTGNLDAATGEQIIDLLFELnrerGT-TLVLV-TH---DPALAarCDRVLRLRAGRLV 225
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
15-233 |
5.89e-22 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 91.75 E-value: 5.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 15 VVHAEGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGH--PVHNRADLHTLRRSL 91
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGkITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEniPAMSRSRLYTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 92 GYLPQHFGFYPRFTVREFVEY-LAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLL 170
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVAYpLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIM 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2683828925 171 LDEPTVGLDP------EQRLDfrELLRDLGTdSCVLVStHLVEDVAVACTDVILINDGQLVHQGTTDDL 233
Cdd:PRK11831 167 FDEPFVGQDPitmgvlVKLIS--ELNSALGV-TCVVVS-HDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
16-228 |
8.31e-22 |
|
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: 90.28 E-value: 8.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 16 VHAEGLRVRAGRHLAVDGLDLSLGTGVH-GLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVhnrADLhtlrrSLGYl 94
Cdd:cd03220 23 LGILGRKGEVGEFWALKDVSFEVPRGERiGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS---SLL-----GLGG- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 95 pqhfGFYPRFTVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEP 174
Cdd:cd03220 94 ----GFNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEV 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2683828925 175 T-VGlDPE------QRldFRELLRDLGTdscVLVSTHLVEDVAVACTDVILINDGQLVHQG 228
Cdd:cd03220 170 LaVG-DAAfqekcqRR--LRELLKQGKT---VILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-236 |
8.35e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 91.13 E-value: 8.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 15 VVHAEGLRVRAGRHLAVDGLDLSL-GTGVHGLLGPNGAGKTTLMRALATVVK-----PAGGTLTLLGHPVHnRADLHTLR 88
Cdd:PRK14247 3 KIEIRDLKVSFGQVEVLDGVNLEIpDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIF-KMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 89 RSLGYLPQHFGFYPRFTVREFVEYLAWLKHL--PKATIPDAVQHAIDRVGLTAKADTRMKT----LSGGMLRRAGIAQAI 162
Cdd:PRK14247 82 RRVQMVFQIPNPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLWDEVKDRLDApagkLSGGQQQRLCIARAL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2683828925 163 VNNPAVLLLDEPTVGLDPEQRLDFRELLRDLGTDSCVLVSTHLVEDVAVACTDVILINDGQLVHQGTTDDLITH 236
Cdd:PRK14247 162 AFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTN 235
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
18-204 |
1.49e-21 |
|
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: 88.95 E-value: 1.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 18 AEGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRADLHTlrRSLGYLPQ 96
Cdd:TIGR01189 3 ARNLACSRGERMLFEGLSFTLNAGeALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPH--ENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 97 HFGFYPRFTVREFVEYLAWLKHLPKATIPDAvqhaIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTV 176
Cdd:TIGR01189 81 LPGLKPELSALENLHFWAAIHGGAQRTIEDA----LAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180
....*....|....*....|....*....
gi 2683828925 177 GLDPEQRLDFRELLRD-LGTDSCVLVSTH 204
Cdd:TIGR01189 157 ALDKAGVALLAGLLRAhLARGGIVLLTTH 185
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-230 |
3.15e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 89.52 E-value: 3.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 16 VHAEGLRVRAGRHLAVDGLDLSL-GTGVHGLLGPNGAGKTTLMRALATVVK-----PAGGTLTLLGHPVHN-RADLHTLR 88
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIpQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSpDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 89 RSLGYLPQHFGFYPRFTVREFVEYLAWLKHL--PKATIPDAVQHAIDRVGLTAKADTRMK----TLSGGMLRRAGIAQAI 162
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALWDEVKDRLNdypsNLSGGQRQRLVIARAL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2683828925 163 VNNPAVLLLDEPTVGLDPEQRLDFRELLRDLGTDSCVLVSTHLVEDVAVACTDVILINDGQLVHQGTT 230
Cdd:PRK14267 165 AMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPT 232
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
26-236 |
3.86e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 91.44 E-value: 3.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 26 GRHlAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVhnrADLHTLRRSLGYLPQHFGFYPRF 104
Cdd:PRK11607 31 GQH-AVDDVSLTIYKGeIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL---SHVPPYQRPINMMFQSYALFPHM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 105 TVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQR- 183
Cdd:PRK11607 107 TVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRd 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2683828925 184 ---LDFRELLRDLGTdSCVLVsTHLVEDVAVACTDVILINDGQLVHQGTTDDLITH 236
Cdd:PRK11607 187 rmqLEVVDILERVGV-TCVMV-THDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEH 240
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-242 |
5.08e-21 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 88.94 E-value: 5.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 1 MDTAAAIAPTthpwVVHAEGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRAL---------ATVVkpagGT 70
Cdd:COG1117 1 MTAPASTLEP----KIEVRNLNVYYGDKQALKDINLDIPENkVTALIGPSGCGKSTLLRCLnrmndlipgARVE----GE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 71 LTLLGHPVHNR-ADLHTLRRSLGYLPQH---FgfyPrFTVREFVEYLAWLKHL-PKATIPDAVQHAIDRVGLTAKADTRM 145
Cdd:COG1117 73 ILLDGEDIYDPdVDVVELRRRVGMVFQKpnpF---P-KSIYDNVAYGLRLHGIkSKSELDEIVEESLRKAALWDEVKDRL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 146 KT----LSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLRDLGTDSCVLVSTHLVEDVA-VAcTDVILIN 220
Cdd:COG1117 149 KKsalgLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAArVS-DYTAFFY 227
|
250 260
....*....|....*....|..
gi 2683828925 221 DGQLVHQGTTDDLITHggPDDP 242
Cdd:COG1117 228 LGELVEFGPTEQIFTN--PKDK 247
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
45-237 |
6.04e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 89.31 E-value: 6.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 45 LLGPNGAGKTTLMRALATVVKPAGGTLTLLGH---PVHNRADLHTLRRSLGYL---PQH------------FGfyPR-FT 105
Cdd:PRK13634 38 IIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERvitAGKKNKKLKPLRKKVGIVfqfPEHqlfeetvekdicFG--PMnFG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 106 VREfveylawlkhlpkatiPDAVQHA---IDRVGLTAKADTRMK-TLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPE 181
Cdd:PRK13634 116 VSE----------------EDAKQKAremIELVGLPEELLARSPfELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 182 QRLD----FRELLRDLGTdSCVLVsTHLVEDVAVACTDVILINDGQLVHQGTTDDLITHG 237
Cdd:PRK13634 180 GRKEmmemFYKLHKEKGL-TTVLV-THSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
42-235 |
6.62e-21 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 88.36 E-value: 6.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 42 VHgLLGPNGAGKTTLMRALATVVkPAGGTLTLLGHPVhNRADLHTLRRSLGYLPQHfgFYPRFTVREFvEYLAWlkHLPK 121
Cdd:COG4138 25 IH-LIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPL-SDWSAAELARHRAYLSQQ--QSPPFAMPVF-QYLAL--HQPA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 122 ATIPDAVQHAI----DRVGLTAKADTRMKTLSGGMLRRAGIAQAIV-----NNP--AVLLLDEPTVGLDPEQRLDFRELL 190
Cdd:COG4138 97 GASSEAVEQLLaqlaEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptINPegQLLLLDEPMNSLDVAQQAALDRLL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2683828925 191 R---DLGTdsCVLVSTHLVEDVAVACTDVILINDGQLVHQGTTDDLIT 235
Cdd:COG4138 177 RelcQQGI--TVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMT 222
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
29-228 |
1.01e-20 |
|
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: 86.21 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 29 LAVDGLDLSLGTGVH-GLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRADlhTLRRSLGYLPQHfgfyprftvr 107
Cdd:cd03247 16 QVLKNLSLELKQGEKiALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK--ALSSLISVLNQR---------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 108 efveylawlKHLPKATIpdavqhaIDRVGltakadtrmKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFR 187
Cdd:cd03247 84 ---------PYLFDTTL-------RNNLG---------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLL 138
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2683828925 188 ELLRDLGTDSCVLVSTHLVEDVAVAcTDVILINDGQLVHQG 228
Cdd:cd03247 139 SLIFEVLKDKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
15-224 |
1.34e-20 |
|
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: 85.95 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 15 VVHAEGLRVRAgrhlAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRADLHTLRRSLGY 93
Cdd:cd03215 4 VLEVRGLSVKG----AVRDVSFEVRAGeIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 94 LP---QHFGFYPRFTVREfveylawlkhlpKATIPDavqhaidrvgltakadtrmkTLSGGMLRRAGIAQAIVNNPAVLL 170
Cdd:cd03215 80 VPedrKREGLVLDLSVAE------------NIALSS--------------------LLSGGNQQKVVLARWLARDPRVLI 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2683828925 171 LDEPTVGLDPEQRLDFRELLRDL---GTdSCVLVSTHLVEdvAVACTDVIL-INDGQL 224
Cdd:cd03215 128 LDEPTRGVDVGAKAEIYRLIRELadaGK-AVLLISSELDE--LLGLCDRILvMYEGRI 182
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
18-205 |
1.44e-20 |
|
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: 86.39 E-value: 1.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 18 AEGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRADlhTLRRSLGYLPQ 96
Cdd:cd03231 3 ADELTCERDGRALFSGLSFTLAAGeALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD--SIARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 97 HFGFYPRFTVREFVEYLAWLKHlpkatiPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTV 176
Cdd:cd03231 81 APGIKTTLSVLENLRFWHADHS------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170 180 190
....*....|....*....|....*....|
gi 2683828925 177 GLDPEQRLDFRELLRD-LGTDSCVLVSTHL 205
Cdd:cd03231 155 ALDKAGVARFAEAMAGhCARGGMVVLTTHQ 184
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
41-235 |
1.71e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 88.23 E-value: 1.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 41 GVHGLLGPNGAGKTTLMRALATVV-KPAG----GTLTLLGHPVHNRADLHTLRRSLGYLPQHFGFYPRFTVREFVEYLAW 115
Cdd:PRK14271 48 AVTSLMGPTGSGKTTFLRTLNRMNdKVSGyrysGDVLLGGRSIFNYRDVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 116 LKHLPKATIPDAVQHAIDRVGLTAKADTRMKT----LSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLR 191
Cdd:PRK14271 128 HKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIR 207
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2683828925 192 DLGTDSCVLVSTHLVEDVAVACTDVILINDGQLVHQGTTDDLIT 235
Cdd:PRK14271 208 SLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
29-237 |
3.43e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 87.38 E-value: 3.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 29 LAVDGLDLSLGTGVH-GLLGPNGAGKTTLMRALATVVKPAGGTLTLlGHPVHNRADLHTLRRSLGYLPQHfgfyP--RF- 104
Cdd:PRK13635 21 YALKDVSFSVYEGEWvAIVGHNGSGKSTLAKLLNGLLLPEAGTITV-GGMVLSEETVWDVRRQVGMVFQN----PdnQFv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 105 --TVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQ 182
Cdd:PRK13635 96 gaTVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2683828925 183 RLDFRELLRDLG--TDSCVLVSTHLVEDVAVAcTDVILINDGQLVHQGTTDDLITHG 237
Cdd:PRK13635 176 RREVLETVRQLKeqKGITVLSITHDLDEAAQA-DRVIVMNKGEILEEGTPEEIFKSG 231
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
16-238 |
3.86e-20 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 88.25 E-value: 3.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 16 VHAEGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTlmRAL-ATVVKPAGGTltllgHPVHNR---ADLHTLRRS 90
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGtVLGVLGP*GAA**R--GALpAHV*GPDAGR-----RPWRF*twcANRRALRRT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 91 LG-YLPQHFGFYPRFTVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVL 169
Cdd:NF000106 87 IG*HRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 170 LLDEPTVGLDPEQRLDFRELLRDLGTD-SCVLVSTHLVEDVAVACTDVILINDGQLVHQGTTDDLITHGG 238
Cdd:NF000106 167 YLDEPTTGLDPRTRNEVWDEVRSMVRDgATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG 236
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
9-232 |
5.19e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 85.94 E-value: 5.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 9 PTTHPWVVHAEGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLT-----LLGHPVHNRA 82
Cdd:COG4674 4 DTMHGPILYVEDLTVSFDGFKALNDLSLYVDPGeLRVIIGPNGAGKTTLMDVITGKTRPDSGSVLfggtdLTGLDEHEIA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 83 dlhtlRRSLGYLPQHFGFYPRFTVREFVEyLA-------W--LKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLS-G-- 150
Cdd:COG4674 84 -----RLGIGRKFQKPTVFEELTVFENLE-LAlkgdrgvFasLFARLTAEERDRIEEVLETIGLTDKADRLAGLLShGqk 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 151 -----GMLrragIAQaivnNPAVLLLDEPTVGLDPEQRLDFRELLRDLGTDSCVLVSTHLVEDV-AVACTdVILINDGQL 224
Cdd:COG4674 158 qwleiGML----LAQ----DPKLLLLDEPVAGMTDAETERTAELLKSLAGKHSVVVVEHDMEFVrQIARK-VTVLHQGSV 228
|
....*...
gi 2683828925 225 VHQGTTDD 232
Cdd:COG4674 229 LAEGSLDE 236
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
34-233 |
7.04e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 87.45 E-value: 7.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 34 LDLSLGTGVhGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVhnrADLHTLRRSLGYLPQHFGFYPRFTVREFVEYl 113
Cdd:PRK10851 23 LDIPSGQMV-ALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV---SRLHARDRKVGFVFQHYALFRHMTVFDNIAF- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 114 aWLKHLPKATIPDA------VQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFR 187
Cdd:PRK10851 98 -GLTVLPRRERPNAaaikakVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2683828925 188 ELLRDLGTD---SCVLVsTHLVEDVAVACTDVILINDGQLVHQGTTDDL 233
Cdd:PRK10851 177 RWLRQLHEElkfTSVFV-THDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
31-228 |
8.04e-20 |
|
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: 85.21 E-value: 8.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 31 VDGLDLSLGTGVH-GLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRADlhtlRRSLGYlpQHFGFYPRFTVREF 109
Cdd:TIGR01184 1 LKGVNLTIQQGEFiSLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP----DRMVVF--QNYSLLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 110 VeYLA---WLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDF 186
Cdd:TIGR01184 75 I-ALAvdrVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2683828925 187 RELLRDLGTDS---CVLVsTHLVEDVAVACTDVILINDGQLVHQG 228
Cdd:TIGR01184 154 QEELMQIWEEHrvtVLMV-THDVDEALLLSDRVVMLTNGPAANIG 197
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
45-238 |
1.01e-19 |
|
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: 84.97 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 45 LLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNrADLHTLRRSLGYLPQHfgfYPRF--TVREFVEYLAwlkhlPKA 122
Cdd:cd03253 32 IVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIRE-VTLDSLRRAIGVVPQD---TVLFndTIGYNIRYGR-----PDA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 123 T---IPDAVQHA-IDR--VGLTAKADT----RMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLRD 192
Cdd:cd03253 103 TdeeVIEAAKAAqIHDkiMRFPDGYDTivgeRGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2683828925 193 LGTDSCVLVSTHLVEDVaVACTDVILINDGQLVHQGTTDDLITHGG 238
Cdd:cd03253 183 VSKGRTTIVIAHRLSTI-VNADKIIVLKDGRIVERGTHEELLAKGG 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
15-233 |
1.16e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 87.77 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 15 VVHAEGLRVRAGrhlaVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRADLHTLRRSLGY 93
Cdd:COG1129 256 VLEVEGLSVGGV----VRDVSFSVRAGeILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAGIAY 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 94 LP---QHFGFYPRFTVREFVeYLAWLKHLPKATIPD------AVQHAIDRVGL-TAKADTRMKTLSGGMLRRAGIAQAIV 163
Cdd:COG1129 332 VPedrKGEGLVLDLSIRENI-TLASLDRLSRGGLLDrrreraLAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLA 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2683828925 164 NNPAVLLLDEPTVGLDPEQRLDFRELLRDL---GTdSCVLVSTHLVEDVAVActDVILI-NDGQLVHQGTTDDL 233
Cdd:COG1129 411 TDPKVLILDEPTRGIDVGAKAEIYRLIRELaaeGK-AVIVISSELPELLGLS--DRILVmREGRIVGELDREEA 481
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
34-234 |
1.77e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 84.84 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 34 LDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVhNRADLHTLRRSLGYLPQHFGFYPRFTVREFVEY 112
Cdd:PRK10575 30 LSLTFPAGkVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPL-ESWSSKAFARKVAYLPQQLPAAEGMTVRELVAI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 113 --LAWLKHLPKATIPD--AVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRE 188
Cdd:PRK10575 109 grYPWHGALGRFGAADreKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLA 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2683828925 189 LLRDLGTDS--CVLVSTHLVEDVAVACTDVILINDGQLVHQGTTDDLI 234
Cdd:PRK10575 189 LVHRLSQERglTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELM 236
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
45-225 |
2.59e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 84.88 E-value: 2.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 45 LLGPNGAGKTTLMRALATVVKPAGGTLTLLGH---PVHNRADLHTLRRSLGYLPQhFGFYPRF--TVREFVEYLawlkhl 119
Cdd:PRK13641 38 LVGHTGSGKSTLMQHFNALLKPSSGTITIAGYhitPETGNKNLKKLRKKVSLVFQ-FPEAQLFenTVLKDVEFG------ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 120 PK---ATIPDAVQHA---IDRVGLTAK-ADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLRD 192
Cdd:PRK13641 111 PKnfgFSEDEAKEKAlkwLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKD 190
|
170 180 190
....*....|....*....|....*....|....
gi 2683828925 193 LGTDS-CVLVSTHLVEDVAVACTDVILINDGQLV 225
Cdd:PRK13641 191 YQKAGhTVILVTHNMDDVAEYADDVLVLEHGKLI 224
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
9-236 |
3.99e-19 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 83.70 E-value: 3.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 9 PTTHPWVVHAEGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVH-------- 79
Cdd:COG4598 2 TDTAPPALEVRDLHKSFGDLEVLKGVSLTARKGdVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdrdge 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 80 ----NRADLHTLRRSLGYLPQHFGFYPRFTVREFV-EYLAWLKHLPKAtipDAVQHA---IDRVGLTAKADTRMKTLSGG 151
Cdd:COG4598 82 lvpaDRRQLQRIRTRLGMVFQSFNLWSHMTVLENViEAPVHVLGRPKA---EAIERAealLAKVGLADKRDAYPAHLSGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 152 MLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLRDLGTDS-CVLVSTH---LVEDVAvacTDVILINDGQLVHQ 227
Cdd:COG4598 159 QQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGrTMLVVTHemgFARDVS---SHVVFLHQGRIEEQ 235
|
....*....
gi 2683828925 228 GTTDDLITH 236
Cdd:COG4598 236 GPPAEVFGN 244
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
39-256 |
5.64e-19 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 83.78 E-value: 5.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 39 GTGVHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVhNRAdlhtLRRSL-GYLPQHFGFYPRFTVreFVE------ 111
Cdd:PRK15056 32 GGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT-RQA----LQKNLvAYVPQSEEVDWSFPV--LVEdvvmmg 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 112 ---YLAWLKhLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRE 188
Cdd:PRK15056 105 rygHMGWLR-RAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIIS 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2683828925 189 LLRDLGTDSC-VLVSTHLVEDVAVACTDVILINdGQLVHQGTTDDLITHGGpddpgdspAERGYSALLR 256
Cdd:PRK15056 184 LLRELRDEGKtMLVSTHNLGSVTEFCDYTVMVK-GTVLASGPTETTFTAEN--------LELAFSGVLR 243
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
26-225 |
8.46e-19 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 82.23 E-value: 8.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 26 GRHlAVDGLDLSLGTGVHGLL-GPNGAGKTTLMRALATVVKPAGGTLTLLGHPVH--NRADLHTLRRSLGYLPQHFGFYP 102
Cdd:PRK10908 14 GRQ-ALQGVTFHMRPGEMAFLtGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlKNREVPFLRRQIGMIFQDHHLLM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 103 RFTVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQ 182
Cdd:PRK10908 93 DRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2683828925 183 RLDFRELLRDLG-TDSCVLVSTHLVEDVAVACTDVILINDGQLV 225
Cdd:PRK10908 173 SEGILRLFEEFNrVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
34-233 |
9.54e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 83.63 E-value: 9.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 34 LDLSLGTGVH-GLLGPNGAGKTTLMRALATVVKPAGGTL---TLLGHPVHNRADLHTLRRSLGYLPQhfgfYPRF----- 104
Cdd:PRK13643 25 IDLEVKKGSYtALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgDIVVSSTSKQKEIKPVRKKVGVVFQ----FPESqlfee 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 105 TVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKA-DTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQR 183
Cdd:PRK13643 101 TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKAR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2683828925 184 LDFRELLRDL-GTDSCVLVSTHLVEDVAVACTDVILINDGQLVHQGTTDDL 233
Cdd:PRK13643 181 IEMMQLFESIhQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDV 231
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
26-238 |
1.00e-18 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 85.22 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 26 GRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVhNRADLHTLRRSLGYLPQHFGFYPRf 104
Cdd:COG1132 351 GDRPVLKDISLTIPPGeTVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDI-RDLTLESLRRQIGVVPQDTFLFSG- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 105 TVREFVEYLAwlkhlPKATiPDAVQHAIDRVG-------LTAKADT----RMKTLSGGMLRRAGIAQAIVNNPAVLLLDE 173
Cdd:COG1132 429 TIRENIRYGR-----PDAT-DEEVEEAAKAAQahefieaLPDGYDTvvgeRGVNLSGGQRQRIAIARALLKDPPILILDE 502
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2683828925 174 PTVGLDP--EQRLdfRELLRDLGTDSCVLVSTH---LVEDVavactDVIL-INDGQLVHQGTTDDLITHGG 238
Cdd:COG1132 503 ATSALDTetEALI--QEALERLMKGRTTIVIAHrlsTIRNA-----DRILvLDDGRIVEQGTHEELLARGG 566
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
21-235 |
1.08e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 82.32 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 21 LRVRAGRHLAVdgldlslgtgvhglLGPNGAGKTTLMRALATVVKPAGGTLTLlghpvhNRADlHTL----RRSLGYLPQ 96
Cdd:PRK10771 20 LTVERGERVAI--------------LGPSGAGKSTLLNLIAGFLTPASGSLTL------NGQD-HTTtppsRRPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 97 HFGFYPRFTVREFVEyLAW-----LKHLPKATipdaVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLL 171
Cdd:PRK10771 79 ENNLFSHLTVAQNIG-LGLnpglkLNAAQREK----LHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2683828925 172 DEPTVGLDPEQRLDFRELLRDLGTDS--CVLVSTHLVEDVAVACTDVILINDGQLVHQGTTDDLIT 235
Cdd:PRK10771 154 DEPFSALDPALRQEMLTLVSQVCQERqlTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
9-238 |
1.53e-18 |
|
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: 81.89 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 9 PTTHPWVVHAEGLRVRAGRHLAvdgldlslgtgvhgLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNrADLHTLR 88
Cdd:cd03251 11 PGDGPPVLRDISLDIPAGETVA--------------LVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRD-YTLASLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 89 RSLGYLPQH-FGFYPrfTVREFVEYLAwlkhlpkatiPDAVQHAIDRVGLTAKA-----------DT----RMKTLSGGM 152
Cdd:cd03251 76 RQIGLVSQDvFLFND--TVAENIAYGR----------PGATREEVEEAARAANAhefimelpegyDTvigeRGVKLSGGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 153 LRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLRDLGTDSCVLVSTHLVEDVAVAcTDVILINDGQLVHQGTTDD 232
Cdd:cd03251 144 RQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENA-DRIVVLEDGKIVERGTHEE 222
|
....*.
gi 2683828925 233 LITHGG 238
Cdd:cd03251 223 LLAQGG 228
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
15-204 |
2.50e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 80.62 E-value: 2.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 15 VVHAEGLRVRAGRHLAVDGLDLSLGTG--VHgLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVH-NRADLHtlrRSL 91
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGelVQ-IEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRrQRDEYH---QDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 92 GYLPQHFGFYPRFTVrefVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLL 171
Cdd:PRK13538 77 LYLGHQPGIKTELTA---LENLRFYQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWIL 153
|
170 180 190
....*....|....*....|....*....|....
gi 2683828925 172 DEPTVGLDPEQRLDFRELLRD-LGTDSCVLVSTH 204
Cdd:PRK13538 154 DEPFTAIDKQGVARLEALLAQhAEQGGMVILTTH 187
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
27-235 |
5.62e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 80.36 E-value: 5.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 27 RHLAVDGLDLSL------GTGVHgLLGPNGAGKTTLMRALATVVkPAGGTLTLLGHPVhNRADLHTLRRSLGYLPQHFGf 100
Cdd:PRK03695 4 NDVAVSTRLGPLsaevraGEILH-LVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPL-EAWSAAELARHRAYLSQQQT- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 101 yPRFTVREFvEYLAWlkHLPKATIPDAVQHAIDRV----GLTAKADTRMKTLSGGMLRRAGIAQAI-----VNNPA--VL 169
Cdd:PRK03695 80 -PPFAMPVF-QYLTL--HQPDKTRTEAVASALNEVaealGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPAgqLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2683828925 170 LLDEPTVGLDPEQRLDFRELLRDLgtdsC-----VLVSTHLVEDVAVACTDVILINDGQLVHQGTTDDLIT 235
Cdd:PRK03695 156 LLDEPMNSLDVAQQAALDRLLSEL----CqqgiaVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLT 222
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
18-232 |
6.29e-18 |
|
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: 82.87 E-value: 6.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 18 AEGLRVRA--GRHLAVDGLDLSL--GTGVhGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVH--NRADLHtlrRSL 91
Cdd:COG4618 333 VENLTVVPpgSKRPILRGVSFSLepGEVL-GVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSqwDREELG---RHI 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 92 GYLPQHFGFYPRfTVRE----FveylawlkhlPKATiPDAVQHAIDRVG-------LTAKADTRM----KTLSGGMLRRA 156
Cdd:COG4618 409 GYLPQDVELFDG-TIAEniarF----------GDAD-PEKVVAAAKLAGvhemilrLPDGYDTRIgeggARLSGGQRQRI 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 157 GIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLRDL----GTdscVLVSTHLVEdvAVACTDVILI-NDGQLVHQGTTD 231
Cdd:COG4618 477 GLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkargAT---VVVITHRPS--LLAAVDKLLVlRDGRVQAFGPRD 551
|
.
gi 2683828925 232 D 232
Cdd:COG4618 552 E 552
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
42-235 |
6.33e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 80.48 E-value: 6.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 42 VHGLLGPNGAGKTTLMRALATVVK------PAGGTLTLLGHPVHnRADLHTLRRSLGYLPQHFGFYPRFTVREFVEY-LA 114
Cdd:PRK14246 38 IFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIF-QIDAIKLRKEVGMVFQQPNPFPHLSIYDNIAYpLK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 115 WLKHLPKATIPDAVQHAIDRVGLTAKADTRMKT----LSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELL 190
Cdd:PRK14246 117 SHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSpasqLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLI 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2683828925 191 RDLGTDSCVLVSTHLVEDVAVACTDVILINDGQLVHQGTTDDLIT 235
Cdd:PRK14246 197 TELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFT 241
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
28-222 |
7.44e-18 |
|
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: 7.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 28 HLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPV--HNRADLHTLRRSLGYLPQHFGFyprf 104
Cdd:cd03248 27 TLVLQDVSFTLHPGeVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIsqYEHKYLHSKVSLVGQEPVLFAR---- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 105 TVREFVEYlaWLKHLPKATIPDAVQ--HAIDRV-----GLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVG 177
Cdd:cd03248 103 SLQDNIAY--GLQSCSFECVKEAAQkaHAHSFIselasGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2683828925 178 LDPEQRLDFRELLRDLGTDSCVLVSTHLVEDVAVActDVILINDG 222
Cdd:cd03248 181 LDAESEQQVQQALYDWPERRTVLVIAHRLSTVERA--DQILVLDG 223
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
19-224 |
7.97e-18 |
|
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: 78.41 E-value: 7.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 19 EGLRVRAG--RHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVhNRADLHTLRRSLGYLP 95
Cdd:cd03246 4 ENVSFRYPgaEPPVLRNVSFSIEPGeSLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADI-SQWDPNELGDHVGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 96 QHfgfyprftvrefVEYLAwlkhlpkATIPDAVqhaidrvgltakadtrmktLSGGMLRRAGIAQAIVNNPAVLLLDEPT 175
Cdd:cd03246 83 QD------------DELFS-------GSIAENI-------------------LSGGQRQRLGLARALYGNPRILVLDEPN 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2683828925 176 VGLDPEQRLDFRELLRDL-GTDSCVLVSTHLVEDVAvACTDVILINDGQL 224
Cdd:cd03246 125 SHLDVEGERALNQAIAALkAAGATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
28-238 |
8.71e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 82.57 E-value: 8.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 28 HLAVDGLDLSLGTGVH-GLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRADlHTLRRSLGYLPQ--HFgfyprF 104
Cdd:PRK11160 353 QPVLKGLSLQIKAGEKvALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSE-AALRQAISVVSQrvHL-----F 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 105 --TVREFVEyLAwlkhLPKATiPDAVQHAIDRVGLTAKADTRM----------KTLSGGMLRRAGIAQAIVNNPAVLLLD 172
Cdd:PRK11160 427 saTLRDNLL-LA----APNAS-DEALIEVLQQVGLEKLLEDDKglnawlgeggRQLSGGEQRRLGIARALLHDAPLLLLD 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2683828925 173 EPTVGLDPEQRLDFRELLRDLGTDSCVLVSTHLVedVAVACTDVI-LINDGQLVHQGTTDDLITHGG 238
Cdd:PRK11160 501 EPTEGLDAETERQILELLAEHAQNKTVLMITHRL--TGLEQFDRIcVMDNGQIIEQGTHQELLAQQG 565
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
45-235 |
8.90e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 80.42 E-value: 8.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 45 LLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVhNRADLHTLRRSLGYLPQHfgfyP--RF---TVREFVEYLAWLKHL 119
Cdd:PRK13632 40 ILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI-SKENLKEIRKKIGIIFQN----PdnQFigaTVEDDIAFGLENKKV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 120 PKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLRDL--GTDS 197
Cdd:PRK13632 115 PPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLrkTRKK 194
|
170 180 190
....*....|....*....|....*....|....*...
gi 2683828925 198 CVLVSTHLVEDvAVACTDVILINDGQLVHQGTTDDLIT 235
Cdd:PRK13632 195 TLISITHDMDE-AILADKVIVFSEGKLIAQGKPKEILN 231
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
45-237 |
9.46e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 80.18 E-value: 9.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 45 LLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRaDLHTLRRSLGYLPQH-----FGFYPRFTVREFVEYLAwlkhL 119
Cdd:PRK13648 40 IVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDD-NFEKLRKHIGIVFQNpdnqfVGSIVKYDVAFGLENHA----V 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 120 PKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLRDLGTDSCV 199
Cdd:PRK13648 115 PYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNI 194
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2683828925 200 -LVS-TH-LVEdvAVACTDVILINDGQLVHQGTTDDLITHG 237
Cdd:PRK13648 195 tIISiTHdLSE--AMEADHVIVMNKGTVYKEGTPTEIFDHA 233
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
45-228 |
1.26e-17 |
|
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: 78.69 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 45 LLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVhnrADLHTLRRSLGYLPQHFGFYPRFTVREFVEylawLKHLPKATI 124
Cdd:cd03298 29 IVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV---TAAPPADRPVSMLFQENNLFAHLTVEQNVG----LGLSPGLKL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 125 PDAVQHAID----RVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLRDL--GTDSC 198
Cdd:cd03298 102 TAEDRQAIEvalaRVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLhaETKMT 181
|
170 180 190
....*....|....*....|....*....|
gi 2683828925 199 VLVSTHLVEDVAVACTDVILINDGQLVHQG 228
Cdd:cd03298 182 VLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
33-238 |
1.38e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 82.08 E-value: 1.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 33 GLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPV--HNRADLHTLRRSLGYLPQHFGFyprfTVREF 109
Cdd:TIGR00958 499 GLTFTLHPGeVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLvqYDHHYLHRQVALVGQEPVLFSG----SVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 110 VEYlaWLKHLPKATIPDAVQ--HAIDRV-GLTAKADTRM----KTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQ 182
Cdd:TIGR00958 575 IAY--GLTDTPDEEIMAAAKaaNAHDFImEFPNGYDTEVgekgSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAEC 652
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2683828925 183 RLDFRElLRDLGTDSCVLVSTHL--VEDvavaCTDVILINDGQLVHQGTTDDLITHGG 238
Cdd:TIGR00958 653 EQLLQE-SRSRASRTVLLIAHRLstVER----ADQILVLKKGSVVEMGTHKQLMEDQG 705
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-204 |
1.42e-17 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 81.64 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 4 AAAIAPTTHPWVVhAEGLRVR-AGRHLAVDGLDLSLGTGVH-GLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNr 81
Cdd:TIGR02868 324 AAGAVGLGKPTLE-LRDLSAGyPGAPPVLDGVSLDLPPGERvAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSS- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 82 ADLHTLRRSLGYLPQHFGFYPRfTVREFVEYLAwlkhlPKATiPDAVQHAIDRVGL-------TAKADTRM----KTLSG 150
Cdd:TIGR02868 402 LDQDEVRRRVSVCAQDAHLFDT-TVRENLRLAR-----PDAT-DEELWAALERVGLadwlralPDGLDTVLgeggARLSG 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2683828925 151 GMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLRDLGTDSCVLVSTH 204
Cdd:TIGR02868 475 GERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITH 528
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
28-233 |
2.04e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 79.82 E-value: 2.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 28 HLAVDGLDLSLGTGVH-GLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRAD---LHTLRRSLGYLPQhfgfYPR 103
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYyAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyIRPVRKRIGMVFQ----FPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 104 FTVREFV---EYLAWLKHLpKATIPDAVQHAIDR-VGLTAKADTRMKT---LSGGMLRRAGIAQAIVNNPAVLLLDEPTV 176
Cdd:PRK13646 96 SQLFEDTverEIIFGPKNF-KMNLDEVKNYAHRLlMDLGFSRDVMSQSpfqMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 177 GLDPEQRLDFRELLRDLGTD---SCVLVsTHLVEDVAVACTDVILINDGQLVHQGTTDDL 233
Cdd:PRK13646 175 GLDPQSKRQVMRLLKSLQTDenkTIILV-SHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
30-234 |
2.86e-17 |
|
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: 81.00 E-value: 2.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 30 AVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTL-----------TLLGHPVHNRAdlhtlRRSLGYLPQH 97
Cdd:TIGR03269 299 AVDNVSLEVKEGeIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdewvdmTKPGPDGRGRA-----KRYIGILHQE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 98 FGFYPRFTVrefveylawLKHLPKAT---IPD------AVqHAIDRVGLTAKA-----DTRMKTLSGGMLRRAGIAQAIV 163
Cdd:TIGR03269 374 YDLYPHRTV---------LDNLTEAIgleLPDelarmkAV-ITLKMVGFDEEKaeeilDKYPDELSEGERHRVALAQVLI 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2683828925 164 NNPAVLLLDEPTVGLDPEQRLDFRELL---RDLGTDSCVLVStHLVEDVAVACTDVILINDGQLVHQGTTDDLI 234
Cdd:TIGR03269 444 KEPRIVILDEPTGTMDPITKVDVTHSIlkaREEMEQTFIIVS-HDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
28-238 |
3.48e-17 |
|
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: 78.04 E-value: 3.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 28 HLAVDGLDLSLGTGVH-GLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRaDLHTLRRSLGYLPQHFGFYPRfTV 106
Cdd:cd03254 16 KPVLKDINFSIKPGETvAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDI-SRKSLRSMIGVVLQDTFLFSG-TI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 107 REFVEY-------LAWLKHLPKATIPDAVQHAIDrvGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLD 179
Cdd:cd03254 94 MENIRLgrpnatdEEVIEAAKEAGAHDFIMKLPN--GYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNID 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2683828925 180 PEQRLDFRELLRDLGTDSCVLVSTHLVEDVAVAcTDVILINDGQLVHQGTTDDLITHGG 238
Cdd:cd03254 172 TETEKLIQEALEKLMKGRTSIIIAHRLSTIKNA-DKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
24-240 |
4.88e-17 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 79.69 E-value: 4.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 24 RAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVH--NRADLHTLRRS-LGYLPQHFG 99
Cdd:PRK10070 37 KTGLSLGVKDASLAIEEGeIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkiSDAELREVRRKkIAMVFQSFA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 100 FYPRFTVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLD 179
Cdd:PRK10070 117 LMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2683828925 180 PEQRLDFRELLRDLGTD---SCVLVSTHLVEDVAVAcTDVILINDGQLVHQGTTDDLITHGGPD 240
Cdd:PRK10070 197 PLIRTEMQDELVKLQAKhqrTIVFISHDLDEAMRIG-DRIAIMQNGEVVQVGTPDEILNNPAND 259
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
45-229 |
5.09e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 77.55 E-value: 5.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 45 LLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVH-----NRADLHTlrRSLGYLPQHFGFYPRFTVREFVEYLAWLKHL 119
Cdd:PRK11629 40 IVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSklssaAKAELRN--QKLGFIYQFHHLLPDFTALENVAMPLLIGKK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 120 PKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLRDL----GT 195
Cdd:PRK11629 118 KPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELnrlqGT 197
|
170 180 190
....*....|....*....|....*....|....
gi 2683828925 196 dsCVLVSTHLVEdVAVACTDVILINDGQLVHQGT 229
Cdd:PRK11629 198 --AFLVVTHDLQ-LAKRMSRQLEMRDGRLTAELS 228
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
28-238 |
5.37e-17 |
|
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: 77.58 E-value: 5.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 28 HLAVDGLDLSLGTGVH-GLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNrADLHTLRRSLGYLPQHFGFYPRfTV 106
Cdd:cd03249 16 VPILKGLSLTIPPGKTvALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRD-LNLRWLRSQIGLVSQEPVLFDG-TI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 107 REFVEYlawlkHLPKATIPDAVQHA----IDR--VGLTAKADTRM----KTLSGGMLRRAGIAQAIVNNPAVLLLDEPTV 176
Cdd:cd03249 94 AENIRY-----GKPDATDEEVEEAAkkanIHDfiMSLPDGYDTLVgergSQLSGGQKQRIAIARALLRNPKILLLDEATS 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2683828925 177 GLDPEQRLDFRELLRDLGTDSCVLVSTHLVEDVAVActDVIL-INDGQLVHQGTTDDLITHGG 238
Cdd:cd03249 169 ALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNA--DLIAvLQNGQVVEQGTHDELMAQKG 229
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
30-234 |
6.02e-17 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 77.41 E-value: 6.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 30 AVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKP----AGGTLTLLGHPVhnrADLHTLRRSLGYLPQH--FGFYP 102
Cdd:TIGR02770 1 LVQDLNLSLKRGeVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPL---LPLSIRGRHIATIMQNprTAFNP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 103 RFTVRE-FVEYLAwLKHLPKATIPDAVQHAIDRVGLtAKADTRMKT----LSGGMLRRAGIAQAIVNNPAVLLLDEPTVG 177
Cdd:TIGR02770 78 LFTMGNhAIETLR-SLGKLSKQARALILEALEAVGL-PDPEEVLKKypfqLSGGMLQRVMIALALLLEPPFLIADEPTTD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2683828925 178 LDPEQRLDFRELLRDLGTD--SCVLVSTHLVEDVAVACTDVILINDGQLVHQGTTDDLI 234
Cdd:TIGR02770 156 LDVVNQARVLKLLRELRQLfgTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIF 214
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
20-179 |
6.02e-17 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 79.01 E-value: 6.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 20 GLRVRAGRHL-AVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVH--NRADLHTLRRSLGYLP 95
Cdd:COG4608 22 GLFGRTVGVVkAVDGVSFDIRRGeTLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITglSGRELRPLRRRMQMVF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 96 QH-FG-FYPRFTVREFVEYlAWLKH--LPKATIPDAVQHAIDRVGLTAKADTRM-KTLSGGMLRRAGIAQAIVNNPAVLL 170
Cdd:COG4608 102 QDpYAsLNPRMTVGDIIAE-PLRIHglASKAERRERVAELLELVGLRPEHADRYpHEFSGGQRQRIGIARALALNPKLIV 180
|
....*....
gi 2683828925 171 LDEPTVGLD 179
Cdd:COG4608 181 CDEPVSALD 189
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
16-223 |
6.40e-17 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 75.18 E-value: 6.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 16 VHAEGLRVRAGRHLAVDGLDLSLGTGVH-GLLGPNGAGKTTLMRALATVVKPAGGTLTLLGhpvhnradlhtlRRSLGYL 94
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRiGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS------------TVKIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 95 PQhfgfyprftvrefveylawlkhlpkatipdavqhaidrvgltakadtrmktLSGGMLRRAGIAQAIVNNPAVLLLDEP 174
Cdd:cd03221 69 EQ---------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEP 97
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2683828925 175 TVGLDPEQRLDFRELLRDLgtDSCVLVSTH---LVEDVavaCTDVILINDGQ 223
Cdd:cd03221 98 TNHLDLESIEALEEALKEY--PGTVILVSHdryFLDQV---ATKIIELEDGK 144
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
32-226 |
9.49e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 79.38 E-value: 9.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 32 DGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVH--NRADLHTLRRslgylpQHFGF-------Y 101
Cdd:PRK10535 25 KGISLDIYAGeMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVAtlDADALAQLRR------EHFGFifqryhlL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 102 PRFTVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDP- 180
Cdd:PRK10535 99 SHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSh 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2683828925 181 --EQRLDFRELLRDLGtdSCVLVSTHlVEDVAVACTDVILINDGQLVH 226
Cdd:PRK10535 179 sgEEVMAILHQLRDRG--HTVIIVTH-DPQVAAQAERVIEIRDGEIVR 223
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-184 |
1.65e-16 |
|
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: 76.68 E-value: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 28 HLAVDGLDLSLGTgVHGLLGPNGAGKTTLMRALATVVKPAGGtltllghpvhnraDLHTLRRSLGYLPQHFGfyPRFTVR 107
Cdd:cd03237 14 TLEVEGGSISESE-VIGILGPNGIGKTTFIKMLAGVLKPDEG-------------DIEIELDTVSYKPQYIK--ADYEGT 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2683828925 108 efVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRL 184
Cdd:cd03237 78 --VRDLLSSITKDFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRL 152
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
30-238 |
1.66e-16 |
|
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: 78.60 E-value: 1.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 30 AVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRAdLHTLRRSLGYLPQHFGFYPRfTVRE 108
Cdd:TIGR02203 347 ALDSISLVIEPGeTVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT-LASLRRQVALVSQDVVLFND-TIAN 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 109 FVEYLAwLKHLPKATIPDAVQHA-----IDRV--GLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPE 181
Cdd:TIGR02203 425 NIAYGR-TEQADRAEIERALAAAyaqdfVDKLplGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNE 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2683828925 182 QRLDFRELLRDLGTDSCVLVSTHLVEDVAVAcTDVILINDGQLVHQGTTDDLITHGG 238
Cdd:TIGR02203 504 SERLVQAALERLMQGRTTLVIAHRLSTIEKA-DRIVVMDDGRIVERGTHNELLARNG 559
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
9-239 |
2.19e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 78.35 E-value: 2.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 9 PTTHPWVVHAEGLRVragrhLAVDG------LDLSLGTGVH-GLLGPNGAGKTTLMRALATVVkPAGGTLTLLGHPVHNr 81
Cdd:PRK11174 343 ASNDPVTIEAEDLEI-----LSPDGktlagpLNFTLPAGQRiALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRE- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 82 ADLHTLRRSLGYLPQHfgfyPrftvrefveylawlkHLPKATI--------PDAVQHAIDRVGLTAKA-----------D 142
Cdd:PRK11174 416 LDPESWRKHLSWVGQN----P---------------QLPHGTLrdnvllgnPDASDEQLQQALENAWVseflpllpqglD 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 143 T----RMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLD--PEQRLdfRELLRDLGTDSCVLVSTHLVEDvaVACTDV 216
Cdd:PRK11174 477 TpigdQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDahSEQLV--MQALNAASRRQTTLMVTHQLED--LAQWDQ 552
|
250 260
....*....|....*....|....
gi 2683828925 217 ILI-NDGQLVHQGTTDDLITHGGP 239
Cdd:PRK11174 553 IWVmQDGQIVQQGDYAELSQAGGL 576
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
45-179 |
3.38e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 78.00 E-value: 3.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 45 LLGPNGAGKTTLMRALATVVKPAGGTLTLLghpVHNRADLHTLRRSLGYLPQHFGFYPRFTVREFVEYLAWLKhLPKATI 124
Cdd:PLN03211 99 VLGPSGSGKSTLLNALAGRIQGNNFTGTIL---ANNRKPTKQILKRTGFVTQDDILYPHLTVRETLVFCSLLR-LPKSLT 174
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2683828925 125 PD----AVQHAIDRVGLTAKADT-----RMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLD 179
Cdd:PLN03211 175 KQekilVAESVISELGLTKCENTiignsFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
30-228 |
3.46e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 75.93 E-value: 3.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 30 AVDGLDLSLGTGVH-GLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRADlHTLRRSLGYL-----PQHFGFypr 103
Cdd:PRK13647 20 ALKGLSLSIPEGSKtALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENE-KWVRSKVGLVfqdpdDQVFSS--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 104 fTVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQR 183
Cdd:PRK13647 96 -TVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2683828925 184 LDFRELLRDLGTD-SCVLVSTHLVEDVAVACTDVILINDGQLVHQG 228
Cdd:PRK13647 175 ETLMEILDRLHNQgKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
22-238 |
5.23e-16 |
|
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: 74.83 E-value: 5.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 22 RVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVhNRADLHTLRRSLGYLPQHFGF 100
Cdd:cd03252 9 RYKPDGPVILDNISLRIKPGeVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDL-ALADPAWLRRQVGVVLQENVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 101 YPRfTVREFVeylawlkhlpKATIPDAVQHAIDRVGLTAKA-----------DT----RMKTLSGGMLRRAGIAQAIVNN 165
Cdd:cd03252 88 FNR-SIRDNI----------ALADPGMSMERVIEAAKLAGAhdfiselpegyDTivgeQGAGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2683828925 166 PAVLLLDEPTVGLDPEQRLDFRELLRDLGTDSCVLVSTHLVEdvAVACTDVILIND-GQLVHQGTTDDLITHGG 238
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLS--TVKNADRIIVMEkGRIVEQGSHDELLAENG 228
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
45-238 |
6.34e-16 |
|
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: 77.09 E-value: 6.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 45 LLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNrADLHTLRRSLGYLPQhfgfyprftvREFVEYLAWLKHLPKATI 124
Cdd:TIGR01193 505 IVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKD-IDRHTLRQFINYLPQ----------EPYIFSGSILENLLLGAK 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 125 PDAVQHAIDRVGLTAKADTRMK---------------TLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLD--PEQRLdfR 187
Cdd:TIGR01193 574 ENVSQDEIWAACEIAEIKDDIEnmplgyqtelseegsSISGGQKQRIALARALLTDSKVLILDESTSNLDtiTEKKI--V 651
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2683828925 188 ELLRDLGTDSCVLVSTHLveDVAVACTDVILINDGQLVHQGTTDDLITHGG 238
Cdd:TIGR01193 652 NNLLNLQDKTIIFVAHRL--SVAKQSDKIIVLDHGKIIEQGSHDELLDRNG 700
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
25-204 |
1.60e-15 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 75.26 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 25 AGRHLAVDGLDLSLGTG---VhgLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNR--ADlhtlrRSLGYLPQHFG 99
Cdd:PRK11650 14 DGKTQVIKGIDLDVADGefiV--LVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELepAD-----RDIAMVFQNYA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 100 FYPRFTVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLD 179
Cdd:PRK11650 87 LYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
170 180
....*....|....*....|....*....
gi 2683828925 180 P----EQRLDFRELLRDLGTDScvLVSTH 204
Cdd:PRK11650 167 AklrvQMRLEIQRLHRRLKTTS--LYVTH 193
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
33-233 |
2.51e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.09 E-value: 2.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 33 GLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRADLHTLRRSLGYLPQHFGFYPRFTVREFVe 111
Cdd:PRK15439 29 GIDFTLHAGeVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYLVPQEPLLFPNLSVKENI- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 112 ylawLKHLPKATIPDA-VQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDP-EQRLDFREL 189
Cdd:PRK15439 108 ----LFGLPKRQASMQkMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPaETERLFSRI 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2683828925 190 --LRDLGTdSCVLVSTHLVEDVAVACTdVILINDGQLVHQGTTDDL 233
Cdd:PRK15439 184 reLLAQGV-GIVFISHKLPEIRQLADR-ISVMRDGTIALSGKTADL 227
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
34-228 |
3.20e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 73.50 E-value: 3.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 34 LDLSLgTGVHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPV-HNRADLHTLRRSLGYL---PQHFGFYP------R 103
Cdd:PRK13638 22 LDFSL-SPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdYSKRGLLALRQQVATVfqdPEQQIFYTdidsdiA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 104 FTVREFveylawlkHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQR 183
Cdd:PRK13638 101 FSLRNL--------GVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGR 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2683828925 184 LDFRELLRDL-GTDSCVLVSTHLVEDVAVACTDVILINDGQLVHQG 228
Cdd:PRK13638 173 TQMIAIIRRIvAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHG 218
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
45-242 |
4.38e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 73.23 E-value: 4.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 45 LLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVhNRADLHTLRRSLGYLPQHfgfyP--RF---TVREFVEYLAWLKHL 119
Cdd:PRK13650 38 IIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLL-TEENVWDIRHKIGMVFQN----PdnQFvgaTVEDDVAFGLENKGI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 120 PKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLRDLGTDS-- 197
Cdd:PRK13650 113 PHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYqm 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2683828925 198 CVLVSTHLVEDVAVAcTDVILINDGQLVHQGTTDDLITHG------GPDDP 242
Cdd:PRK13650 193 TVISITHDLDEVALS-DRVLVMKNGQVESTSTPRELFSRGndllqlGLDIP 242
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
28-229 |
5.91e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 72.02 E-value: 5.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 28 HLAVD------GLDLSLGTG-VHGLLGPNGAGKTTLMRALA--TVVKPAGGTLTLLGH-----PVHNRAdlhtlRRSLGY 93
Cdd:COG0396 7 HVSVEgkeilkGVNLTIKPGeVHAIMGPNGSGKSTLAKVLMghPKYEVTSGSILLDGEdilelSPDERA-----RAGIFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 94 lpqhfGF-YP-RF---TVREFVEYLAWLKHLPKATIPDA---VQHAIDRVGLTAKADTRM--KTLSGGMLRRAGIAQAIV 163
Cdd:COG0396 82 -----AFqYPvEIpgvSVSNFLRTALNARRGEELSAREFlklLKEKMKELGLDEDFLDRYvnEGFSGGEKKRNEILQMLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2683828925 164 NNPAVLLLDEPTVGLDpeqrLD-FR---ELLRDL-GTDSCVLVSTH---LVEDVAVacTDVILINDGQLVHQGT 229
Cdd:COG0396 157 LEPKLAILDETDSGLD----IDaLRivaEGVNKLrSPDRGILIITHyqrILDYIKP--DFVHVLVDGRIVKSGG 224
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
16-204 |
7.20e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 73.69 E-value: 7.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 16 VHAEGLRVR--AGRHLaVDGLDLSLGTGVHGLL-GPNGAGKTTLMRALA--------TVVKPAGGTLTLLghPVHNRADL 84
Cdd:COG4178 363 LALEDLTLRtpDGRPL-LEDLSLSLKPGERLLItGPSGSGKSTLLRAIAglwpygsgRIARPAGARVLFL--PQRPYLPL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 85 HTLRRSLGYlPQhfgfyprftvrefveylawlkhlPKATIPDA-VQHAIDRVGLTAKADtRM-------KTLSGGMLRRA 156
Cdd:COG4178 440 GTLREALLY-PA-----------------------TAEAFSDAeLREALEAVGLGHLAE-RLdeeadwdQVLSLGEQQRL 494
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2683828925 157 GIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLRDLGTDSCVLVSTH 204
Cdd:COG4178 495 AFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGH 542
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
15-204 |
7.83e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 72.12 E-value: 7.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 15 VVHAEGLRVRAGRHLAVDGLDLSL-GTGVHGLLGPNGAGKTTLMRA---LATVVKP--AGGTLTLLGHPVHN-RADLHTL 87
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIpKNQITAFIGPSGCGKSTILRCfnrLNDLIPGfrVEGKVTFHGKNLYApDVDPVEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 88 RRSLGYLPQHFGFYPR-------FTVR---------EFVEylawlKHLPKATIPDAVQHAIDRVGLTakadtrmktLSGG 151
Cdd:PRK14243 90 RRRIGMVFQKPNPFPKsiydniaYGARingykgdmdELVE-----RSLRQAALWDEVKDKLKQSGLS---------LSGG 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2683828925 152 MLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLRDLGTDSCVLVSTH 204
Cdd:PRK14243 156 QQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTH 208
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
15-233 |
1.29e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 71.35 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 15 VVHAEGLRVRAGRHLAVDGLDLSL-GTGVHGLLGPNGAGKTTLMRAL---------ATVVkpagGTLTLLGHPVHN-RAD 83
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFyPNEITALIGPSGSGKSTLLRSInrmndlnpeVTIT----GSIVYNGHNIYSpRTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 84 LHTLRRSLGYLPQHFGFYPrFTVREFVEYLAWLKHLP-KATIPDAVQHAIDRVGLTAKADTRMKT----LSGGMLRRAGI 158
Cdd:PRK14239 81 TVDLRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKdKQVLDEAVEKSLKGASIWDEVKDRLHDsalgLSGGQQQRVCI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2683828925 159 AQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLRDLGTDSCVLVSTHLVEDVAVACTDVILINDGQLVHQGTTDDL 233
Cdd:PRK14239 160 ARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
30-225 |
1.64e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 72.64 E-value: 1.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 30 AVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRADLHTLRRSLGYLPQHFGFYPRFTVRE 108
Cdd:PRK11288 19 ALDDISFDCRAGqVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGVAIIYQELHLVPEMTVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 109 FVeylaWLKHLP-------KATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLD-P 180
Cdd:PRK11288 99 NL----YLGQLPhkggivnRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSaR 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2683828925 181 EQRLDFR--ELLRDLGTdsCVLVSTHLVEDVAVACTDVILINDGQLV 225
Cdd:PRK11288 175 EIEQLFRviRELRAEGR--VILYVSHRMEEIFALCDAITVFKDGRYV 219
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
19-224 |
1.77e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 70.86 E-value: 1.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 19 EGLRVRAGRHLAVDGLDLSLGTGVH-GLLGPNGAGKTTLMRALATVVKPAGGTLtLLGhpvhnRADLHTLRRSLGYLPQH 97
Cdd:PRK11247 16 NAVSKRYGERTVLNQLDLHIPAGQFvAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAG-----TAPLAEAREDTRLMFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 98 FGFYPRFTVREFVEYlawlkHLPKATIPDAVQhAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVG 177
Cdd:PRK11247 90 ARLLPWKKVIDNVGL-----GLKGQWRDAALQ-ALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2683828925 178 LDPEQRLDFRELLRDLGTDS--CVLVSTHLVEDvAVACTD-VILINDGQL 224
Cdd:PRK11247 164 LDALTRIEMQDLIESLWQQHgfTVLLVTHDVSE-AVAMADrVLLIEEGKI 212
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
30-236 |
2.08e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 71.31 E-value: 2.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 30 AVDGLDLSLGTGVH-GLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRA---DLHTLRRSLGYLPQhfgfYPRFT 105
Cdd:PRK13649 22 ALFDVNLTIEDGSYtAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkDIKQIRKKVGLVFQ----FPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 106 VreFVEYLawLKHL---PK---ATIPDAVQHAIDRVGLTAKADTRMKT----LSGGMLRRAGIAQAIVNNPAVLLLDEPT 175
Cdd:PRK13649 98 L--FEETV--LKDVafgPQnfgVSQEEAEALAREKLALVGISESLFEKnpfeLSGGQMRRVAIAGILAMEPKILVLDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2683828925 176 VGLDPEQRLDFRELLRDLGTD--SCVLVsTHLVEDVAVACTDVILINDGQLVHQGTTDDLITH 236
Cdd:PRK13649 174 AGLDPKGRKELMTLFKKLHQSgmTIVLV-THLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
45-193 |
2.27e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 72.83 E-value: 2.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 45 LLGPNGAGKTTLMRALATVVkpAGGTLTLLGHPVHNRADLHTLRRSLGYLPQHFGFYPRFTVREFVEYLAWL---KHLPK 121
Cdd:TIGR00956 794 LMGASGAGKTTLLNVLAERV--TTGVITGGDRLVNGRPLDSSFQRSIGYVQQQDLHLPTSTVRESLRFSAYLrqpKSVSK 871
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2683828925 122 ATIPDAVQHAIDRVGLTAKADTRMKTLSGGM----LRRAGIAQAIVNNPAVLL-LDEPTVGLDPEQRLDFRELLRDL 193
Cdd:TIGR00956 872 SEKMEYVEEVIKLLEMESYADAVVGVPGEGLnveqRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL 948
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
18-242 |
2.45e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 70.73 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 18 AEGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRaDLHTL----RRSL- 91
Cdd:PRK11701 9 VRGLTKLYGPRKGCRDVSFDLYPGeVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLR-DLYALseaeRRRLl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 92 ----GYLPQHfgfyPRFTVREFV-------EYLAWLKHLPKATIPDAVQHAIDRVGL-TAKADTRMKTLSGGMLRRAGIA 159
Cdd:PRK11701 88 rtewGFVHQH----PRDGLRMQVsaggnigERLMAVGARHYGDIRATAGDWLERVEIdAARIDDLPTTFSGGMQQRLQIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 160 QAIVNNPAVLLLDEPTVGLD---PEQRLDF-RELLRDLGTdsCVLVSTHlveDVAVA---CTDVILINDGQLVHQGTTDD 232
Cdd:PRK11701 164 RNLVTHPRLVFMDEPTGGLDvsvQARLLDLlRGLVRELGL--AVVIVTH---DLAVArllAHRLLVMKQGRVVESGLTDQ 238
|
250
....*....|
gi 2683828925 233 LIthggpDDP 242
Cdd:PRK11701 239 VL-----DDP 243
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
45-228 |
2.82e-14 |
|
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: 69.60 E-value: 2.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 45 LLGPNGAGKTTLMRALATVVKPAG---GTLTLLGHPVHNRADLHtlRRSLGYLPQHFGFYPRFTVREFVEYlawlkhlpk 121
Cdd:cd03233 38 VLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEFAEKY--PGEIIYVSEEDVHFPTLTVRETLDF--------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 122 atipdavqhaidrvGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLRDLG--TDSCV 199
Cdd:cd03233 107 --------------ALRCKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMAdvLKTTT 172
|
170 180 190
....*....|....*....|....*....|
gi 2683828925 200 LVSTHLVEDVAVACTD-VILINDGQLVHQG 228
Cdd:cd03233 173 FVSLYQASDEIYDLFDkVLVLYEGRQIYYG 202
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
30-229 |
3.61e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 71.03 E-value: 3.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 30 AVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLlgHPVHNRADLHTLRRSLGYLPQHFGFYPRF---- 104
Cdd:PRK13631 41 ALNNISYTFEKNkIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQV--GDIYIGDKKNNHELITNPYSKKIKNFKELrrrv 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 105 -TVREFVEYlawlkHLPKATI-------PDAV-QHAIDRVGLTAKADTRMK-----------TLSGGMLRRAGIAQAIVN 164
Cdd:PRK13631 119 sMVFQFPEY-----QLFKDTIekdimfgPVALgVKKSEAKKLAKFYLNKMGlddsylerspfGLSGGQKRRVAIAGILAI 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2683828925 165 NPAVLLLDEPTVGLDPEQRLDFRELLRDL-GTDSCVLVSTHLVEDVAVACTDVILINDGQLVHQGT 229
Cdd:PRK13631 194 QPEILIFDEPTAGLDPKGEHEMMQLILDAkANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGT 259
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
45-193 |
4.05e-14 |
|
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: 68.81 E-value: 4.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 45 LLGPNGAGKTTLMRALATVvKPAG---GTLTLLGHPVHNradlhTLRRSLGYLPQHFGFYPRFTVREFVEYLAWLKHLpk 121
Cdd:cd03232 38 LMGESGAGKTTLLDVLAGR-KTAGvitGEILINGRPLDK-----NFQRSTGYVEQQDVHSPNLTVREALRFSALLRGL-- 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2683828925 122 atipdAVQHAidrvgltakadtrmktlsggmlRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLRDL 193
Cdd:cd03232 110 -----SVEQR----------------------KRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKL 154
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
16-224 |
4.38e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 69.42 E-value: 4.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 16 VHAEGLRVRAGRHlavdglDLSLGTGVH---------GLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHN-----R 81
Cdd:PRK10584 9 VHHLKKSVGQGEH------ELSILTGVElvvkrgetiALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmdeeaR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 82 ADLHTlrRSLGYLPQHFGFYPRFTVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQA 161
Cdd:PRK10584 83 AKLRA--KHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2683828925 162 IVNNPAVLLLDEPTVGLDPEQRLDFRELL----RDLGTdSCVLVsTHLVEdVAVACTDVILINDGQL 224
Cdd:PRK10584 161 FNGRPDVLFADEPTGNLDRQTGDKIADLLfslnREHGT-TLILV-THDLQ-LAARCDRRLRLVNGQL 224
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
45-233 |
5.27e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 70.21 E-value: 5.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 45 LLGPNGAGKTTLMRALATVVKP---AGGTLTLLGHPVhNRADLHTLRRSLGYLPQHfgfyP--RF---TVREFVEYLAWL 116
Cdd:PRK13640 38 LIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITL-TAKTVWDIREKVGIVFQN----PdnQFvgaTVGDDVAFGLEN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 117 KHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLRDLGTD 196
Cdd:PRK13640 113 RAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKK 192
|
170 180 190
....*....|....*....|....*....|....*....
gi 2683828925 197 S--CVLVSTHLVEDVAVAcTDVILINDGQLVHQGTTDDL 233
Cdd:PRK13640 193 NnlTVISITHDIDEANMA-DQVLVLDDGKLLAQGSPVEI 230
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
30-235 |
5.60e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.11 E-value: 5.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 30 AVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVkPAG---GTLTLLGHPVHNRADLHTLRRSLGYLPQHFGFYPRFT 105
Cdd:PRK13549 20 ALDNVSLKVRAGeIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEGEELQASNIRDTERAGIAIIHQELALVKELS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 106 VREFVeylaWLKH--LPKATIPDAVQHA-----IDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGL 178
Cdd:PRK13549 99 VLENI----FLGNeiTPGGIMDYDAMYLraqklLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2683828925 179 ---DPEQRLDFRELLRDLGTdSCVLVStHLVEDVAVACTDVILINDGQlvHQGT-------TDDLIT 235
Cdd:PRK13549 175 tesETAVLLDIIRDLKAHGI-ACIYIS-HKLNEVKAISDTICVIRDGR--HIGTrpaagmtEDDIIT 237
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
42-245 |
6.88e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 69.68 E-value: 6.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 42 VHGLLGPNGAGKTTLMRALATVVKPAG-----GTLTLLGHPVHNR-ADLHTLRRSLGYLPQHFGFYPrFTVREFVEY--- 112
Cdd:PRK14258 35 VTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERrVNLNRLRRQVSMVHPKPNLFP-MSVYDNVAYgvk 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 113 -LAWLkhlPKATIPDAVQHAIDRVGLTAKADTRMKT----LSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFR 187
Cdd:PRK14258 114 iVGWR---PKLEIDDIVESALKDADLWDEIKHKIHKsaldLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVE 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2683828925 188 ELLRDLGTDS--CVLVSTHLVEDVAVAC--TDVILIND---GQLVHQGTTDDLIThggpdDPGDS 245
Cdd:PRK14258 191 SLIQSLRLRSelTMVIVSHNLHQVSRLSdfTAFFKGNEnriGQLVEFGLTKKIFN-----SPHDS 250
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
42-242 |
7.89e-14 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK 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 complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 69.09 E-value: 7.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 42 VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRaDLHTL----RRSL-----GYLPQHfgfyPRFTVREFVEY 112
Cdd:TIGR02323 31 VLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAEL-ELYQLseaeRRRLmrtewGFVHQN----PRDGLRMRVSA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 113 LAWLKHLPKAT-------IPDAVQHAIDRVGL-TAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRL 184
Cdd:TIGR02323 106 GANIGERLMAIgarhygnIRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQA 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2683828925 185 DFRELLRDLGTDS--CVLVSTHlveDVAVA---CTDVILINDGQLVHQGTTDDLIthggpDDP 242
Cdd:TIGR02323 186 RLLDLLRGLVRDLglAVIIVTH---DLGVArllAQRLLVMQQGRVVESGLTDQVL-----DDP 240
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
42-184 |
1.03e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 70.61 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 42 VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLlghpvhnradlhTLRRSlgYLPQHFGFYPRFTVREFVEYLA------W 115
Cdd:PRK13409 367 VIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP------------ELKIS--YKPQYIKPDYDGTVEDLLRSITddlgssY 432
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2683828925 116 LKHlpkatipdavqHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRL 184
Cdd:PRK13409 433 YKS-----------EIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRL 490
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
21-236 |
1.10e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.12 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 21 LRVRAGRHLAVDGLDLSLGTGVH-GLLGPNGAGKTTLMRALATVVkPAGGTLTLLGHPVH--NRADLHTLRRSLGYLPQ- 96
Cdd:PRK15134 292 LKRTVDHNVVVKNISFTLRPGETlGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHnlNRRQLLPVRHRIQVVFQd 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 97 -HFGFYPRFTVREFVE--YLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKT-LSGGMLRRAGIAQAIVNNPAVLLLD 172
Cdd:PRK15134 371 pNSSLNPRLNVLQIIEegLRVHQPTLSAAQREQQVIAVMEEVGLDPETRHRYPAeFSGGQRQRIAIARALILKPSLIILD 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2683828925 173 EPTVGLDPEQRLDFRELLRDLGTD---SCVLVStHLVEDVAVACTDVILINDGQLVHQGTTDDLITH 236
Cdd:PRK15134 451 EPTSSLDKTVQAQILALLKSLQQKhqlAYLFIS-HDLHVVRALCHQVIVLRQGEVVEQGDCERVFAA 516
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
30-231 |
1.56e-13 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 69.85 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 30 AVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATvVKPAG---GTLTLLGHPVHNRADLHTLRRSLGYLPQHFGFYPRFT 105
Cdd:TIGR02633 16 ALDGIDLEVRPGeCVGLCGENGAGKSTLMKILSG-VYPHGtwdGEIYWSGSPLKASNIRDTERAGIVIIHQELTLVPELS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 106 VREFVeYLAWLKHLPKATIPDAV-----QHAIDRVGLTAKADTR-MKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLD 179
Cdd:TIGR02633 95 VAENI-FLGNEITLPGGRMAYNAmylraKNLLRELQLDADNVTRpVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2683828925 180 PEQRLDFRELLRDLGTD--SCVLVStHLVEDVAVACTDVILINDGQlvHQGTTD 231
Cdd:TIGR02633 174 EKETEILLDIIRDLKAHgvACVYIS-HKLNEVKAVCDTICVIRDGQ--HVATKD 224
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
15-236 |
1.63e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.22 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 15 VVHAEGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLtllghpvhnradLHTLRRSLGY 93
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGkILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------------KRNGKLRIGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 94 LPQHFGFYPR--FTVREFVEylawlkhLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLL 171
Cdd:PRK09544 72 VPQKLYLDTTlpLTVNRFLR-------LRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2683828925 172 DEPTVGLDPEQRLDFRELLRDLGT--DSCVLVSTHLVEDVaVACTDVILINDGQLVHQGTTDDLITH 236
Cdd:PRK09544 145 DEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLV-MAKTDEVLCLNHHICCSGTPEVVSLH 210
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-236 |
1.69e-13 |
|
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: 69.71 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 19 EGLRVR----AGRHLAVDGLDLSLGTG-VHGLLGPNGAGKT----TLMRALATVVKPAGGTLTLLGHPVhNRADLHTLRR 89
Cdd:COG4172 10 EDLSVAfgqgGGTVEAVKGVSFDIAAGeTLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDL-LGLSERELRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 90 ---------------SLGylpqhfgfyPRFTV-REFVEYLAWLKHLPKAtipDAVQHAI---DRVGLTAkADTRMKT--- 147
Cdd:COG4172 89 irgnriamifqepmtSLN---------PLHTIgKQIAEVLRLHRGLSGA---AARARALellERVGIPD-PERRLDAyph 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 148 -LSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDP---EQRLDF-RELLRDLGTdsCVLVSTH---LVEDVAvacTDVILI 219
Cdd:COG4172 156 qLSGGQRQRVMIAMALANEPDLLIADEPTTALDVtvqAQILDLlKDLQRELGM--ALLLITHdlgVVRRFA---DRVAVM 230
|
250
....*....|....*..
gi 2683828925 220 NDGQLVHQGTTDDLITH 236
Cdd:COG4172 231 RQGEIVEQGPTAELFAA 247
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
30-179 |
2.08e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 68.96 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 30 AVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPV--HNRADLHTLRRSLGYLPQH--FGFYPRF 104
Cdd:PRK15079 36 AVDGVTLRLYEGeTLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlgMKDDEWRAVRSDIQMIFQDplASLNPRM 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2683828925 105 TVREFV-EYL-AWLKHLPKATIPDAVQHAIDRVGLTAKADTRM-KTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLD 179
Cdd:PRK15079 116 TIGEIIaEPLrTYHPKLSRQEVKDRVKAMMLKVGLLPNLINRYpHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
42-184 |
2.40e-13 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 69.43 E-value: 2.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 42 VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLlghpvhnradlhTLRRSlgYLPQHF-GFYPRfTVREFVEylawlkhlp 120
Cdd:COG1245 368 VLGIVGPNGIGKTTFAKILAGVLKPDEGEVDE------------DLKIS--YKPQYIsPDYDG-TVEEFLR--------- 423
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 121 kATIPDAVQ------HAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRL 184
Cdd:COG1245 424 -SANTDDFGssyyktEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRL 492
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
15-233 |
2.41e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 69.29 E-value: 2.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 15 VVHAEGLRVRAGR-HLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRADLHTLRRSLG 92
Cdd:COG3845 257 VLEVENLSVRDDRgVPALKDVSLEVRAGeILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 93 YLP---QHFGFYPRFTVRE-----------FVEYLaWLKhlpKATIPDAVQHAIDRVGL-TAKADTRMKTLSGGMLRRAG 157
Cdd:COG3845 337 YIPedrLGRGLVPDMSVAEnlilgryrrppFSRGG-FLD---RKAIRAFAEELIEEFDVrTPGPDTPARSLSGGNQQKVI 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 158 IAQAIVNNPAVLLLDEPTVGLDPE------QRLdfRElLRDLGTdSCVLVSTHLVEDVAVActDVIL-INDGQLVHQGTT 230
Cdd:COG3845 413 LARELSRDPKLLIAAQPTRGLDVGaiefihQRL--LE-LRDAGA-AVLLISEDLDEILALS--DRIAvMYEGRIVGEVPA 486
|
...
gi 2683828925 231 DDL 233
Cdd:COG3845 487 AEA 489
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
27-229 |
2.74e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 68.19 E-value: 2.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 27 RHLAVDGLDLSLGTGVH-GLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRADLHTLRRSLGYLPQHfgfyP--- 102
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFlVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIRNKAGMVFQN----Pdnq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 103 --RFTVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDP 180
Cdd:PRK13633 98 ivATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2683828925 181 EQRLDFRELLRDLGTDS--CVLVSTHLVEDVAVAcTDVILINDGQLVHQGT 229
Cdd:PRK13633 178 SGRREVVNTIKELNKKYgiTIILITHYMEEAVEA-DRIIVMDSGKVVMEGT 227
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
30-246 |
3.04e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 67.70 E-value: 3.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 30 AVDGLDLSLGTGVH-GLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRADLHTLRRSLGYLPQHfgfyP--RFTV 106
Cdd:PRK13644 17 ALENINLVIKKGEYiGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGIVFQN----PetQFVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 107 REFVEYLAWLKH---LPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQR 183
Cdd:PRK13644 93 RTVEEDLAFGPEnlcLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSG 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2683828925 184 LDFRELLRDLGTDSCVLV-STHLVEDVAVAcTDVILINDGQLVHQGTTDDLITHGGPDDPGDSP 246
Cdd:PRK13644 173 IAVLERIKKLHEKGKTIVyITHNLEELHDA-DRIIVMDRGKIVLEGEPENVLSDVSLQTLGLTP 235
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
47-227 |
3.25e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 68.52 E-value: 3.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 47 GPNGAGKTTLMRALATVVKPAGGTLtLLGHPVHNraDLHTLRRSLGYLPQHFGFYPRFTVREFVEYLAWLKHLPKATIPD 126
Cdd:PRK11000 36 GPSGCGKSTLLRMIAGLEDITSGDL-FIGEKRMN--DVPPAERGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 127 AVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFR----ELLRDLGtdSCVLVS 202
Cdd:PRK11000 113 RVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRieisRLHKRLG--RTMIYV 190
|
170 180
....*....|....*....|....*.
gi 2683828925 203 TH-LVEDVAVActDVILINDGQLVHQ 227
Cdd:PRK11000 191 THdQVEAMTLA--DKIVVLDAGRVAQ 214
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
30-235 |
3.32e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 69.04 E-value: 3.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 30 AVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPvHNRADlHTLRRSLGY--LPQHFG------- 99
Cdd:PRK09700 20 ALKSVNLTVYPGeIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNIN-YNKLD-HKLAAQLGIgiIYQELSvideltv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 100 ----FYPRFTVREF--VEYLAWLKHLPKATIpdavqhAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDE 173
Cdd:PRK09700 98 lenlYIGRHLTKKVcgVNIIDWREMRVRAAM------MLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2683828925 174 PTVGLDPEQRLDFRELLRDLGTDSCVLVS-THLVEDVAVACTDVILINDGQLVHQG-----TTDDLIT 235
Cdd:PRK09700 172 PTSSLTNKEVDYLFLIMNQLRKEGTAIVYiSHKLAEIRRICDRYTVMKDGSSVCSGmvsdvSNDDIVR 239
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
42-219 |
3.55e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 68.68 E-value: 3.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 42 VHGLLGPNGAGKTTLMRALATVVKPAggtltlLGHPVHNRADLHTLRRSLG-----YL-------------PQHFGFYPR 103
Cdd:PRK13409 101 VTGILGPNGIGKTTAVKILSGELIPN------LGDYEEEPSWDEVLKRFRGtelqnYFkklyngeikvvhkPQYVDLIPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 104 F---TVREFveylawLKHLPKATIPDAVqhaIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDP 180
Cdd:PRK13409 175 VfkgKVREL------LKKVDERGKLDEV---VERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDI 245
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2683828925 181 EQRLDFRELLRDLGTDSCVLVSTHlveDVAV--ACTDVILI 219
Cdd:PRK13409 246 RQRLNVARLIRELAEGKYVLVVEH---DLAVldYLADNVHI 283
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
30-233 |
4.80e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 67.68 E-value: 4.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 30 AVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPV--HNRADLHTLRRSLGYLPQH-FG-FYPRF 104
Cdd:PRK11308 30 ALDGVSFTLERGkTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkADPEAQKLLRQKIQIVFQNpYGsLNPRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 105 TVREFV-EYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTR---MktLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLD- 179
Cdd:PRK11308 110 KVGQILeEPLLINTSLSAAERREKALAMMAKVGLRPEHYDRyphM--FSGGQRQRIAIARALMLDPDVVVADEPVSALDv 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2683828925 180 --PEQRLD-FRELLRDLGTdSCVLVSTHL--VEDVAvacTDVILINDGQLVHQGTTDDL 233
Cdd:PRK11308 188 svQAQVLNlMMDLQQELGL-SYVFISHDLsvVEHIA---DEVMVMYLGRCVEKGTKEQI 242
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
30-233 |
4.88e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.49 E-value: 4.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 30 AVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRADLHTLRRSLGYLPQHFGFYPRFTV-- 106
Cdd:PRK10762 19 ALSGAALNVYPGrVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGIGIIHQELNLIPQLTIae 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 107 -----REFVEYLA---WLKHLPKAtipDAVqhaIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGL 178
Cdd:PRK10762 99 niflgREFVNRFGridWKKMYAEA---DKL---LARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2683828925 179 -DPEQRLDFReLLRDLGTDSCVLVS-THLVEDVAVACTDVILINDGQLVHQGTTDDL 233
Cdd:PRK10762 173 tDTETESLFR-VIRELKSQGRGIVYiSHRLKEIFEICDDVTVFRDGQFIAEREVADL 228
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
18-235 |
7.18e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 66.77 E-value: 7.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 18 AEGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALA----TVVKPAG----GTLTLLGHPVHnRADLHTLR 88
Cdd:PRK13547 4 ADHLHVARRHRAILRDLSLRIEPGrVTALLGRNGAGKSTLLKALAgdltGGGAPRGarvtGDVTLNGEPLA-AIDAPRLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 89 RSLGYLPQHFGFYPRFTVREFVeYLAWLKHLPKATIP-----DAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIV 163
Cdd:PRK13547 83 RLRAVLPQAAQPAFAFSAREIV-LLGRYPHARRAGALthrdgEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 164 N---------NPAVLLLDEPTVGLDPEQRLDFRELLRDLGTD--SCVLVSTHLVEDVAVACTDVILINDGQLVHQGTTDD 232
Cdd:PRK13547 162 QlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwnLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPAD 241
|
...
gi 2683828925 233 LIT 235
Cdd:PRK13547 242 VLT 244
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
28-195 |
7.58e-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: 64.87 E-value: 7.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 28 HLAVDGLDLSLGTGVHGLL-GPNGAGKTTLMRALATVVKPAGGTLtllghpvhnraDLHTLRRSLgYLPQHfGFYPRFTV 106
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLItGPSGTGKSSLFRALAGLWPWGSGRI-----------GMPEGEDLL-FLPQR-PYLPLGTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 107 REFVEYlAWlkhlpkatipdavqhaidrvgltakadtrMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDF 186
Cdd:cd03223 81 REQLIY-PW-----------------------------DDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRL 130
|
....*....
gi 2683828925 187 RELLRDLGT 195
Cdd:cd03223 131 YQLLKELGI 139
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
13-233 |
1.43e-12 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 65.49 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 13 PWVVHAEGLRVRAGRHLaVDGLDLSLGTG-VHGLLGPNGAGKTtLMRALATVVKPAG-----GTLTLLGHPVHnradLHT 86
Cdd:PRK10418 2 PQQIELRNIALQAAQPL-VHGVSLTLQRGrVLALVGGSGSGKS-LTCAAALGILPAGvrqtaGRVLLDGKPVA----PCA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 87 LR-RSLGYLPQH--FGFYPRFTVREFVeyLAWLKHLPKATIPDAVQHAIDRVGLtAKADTRMKT----LSGGMLRRAGIA 159
Cdd:PRK10418 76 LRgRKIATIMQNprSAFNPLHTMHTHA--RETCLALGKPADDATLTAALEAVGL-ENAARVLKLypfeMSGGMLQRMMIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 160 QAIVNNPAVLLLDEPTVGLDPEQRLDFRELL------RDLGtdscVLVSTHLVEDVAVACTDVILINDGQLVHQGTTDDL 233
Cdd:PRK10418 153 LALLCEAPFIIADEPTTDLDVVAQARILDLLesivqkRALG----MLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
25-238 |
1.55e-12 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 66.91 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 25 AGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVhNRADLHTLRRSLGYLPQHFGFYPR 103
Cdd:PRK13657 345 DNSRQGVEDVSFEAKPGqTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDI-RTVTRASLRRNIAVVFQDAGLFNR 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 104 fTVREFVEYlawlkHLPKAT---IPDAVQHA-----IDR--VGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDE 173
Cdd:PRK13657 424 -SIEDNIRV-----GRPDATdeeMRAAAERAqahdfIERkpDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDE 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2683828925 174 PTVGLDPEQRLDFRELLRDLGTDSCVLVSTHLVEDVAVActDVILIND-GQLVHQGTTDDLITHGG 238
Cdd:PRK13657 498 ATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNA--DRILVFDnGRVVESGSFDELVARGG 561
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
42-211 |
1.66e-12 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 66.73 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 42 VHGLLGPNGAGKTTLMRALATVVKPAggtltlLGHPvHNRAD----LHTLRRS-LG-YL-------------PQHFGFYP 102
Cdd:COG1245 101 VTGILGPNGIGKSTALKILSGELKPN------LGDY-DEEPSwdevLKRFRGTeLQdYFkklangeikvahkPQYVDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 103 RF---TVREFVEylawlkhlpKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLD 179
Cdd:COG1245 174 KVfkgTVRELLE---------KVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
170 180 190
....*....|....*....|....*....|...
gi 2683828925 180 PEQRLDFRELLRDL-GTDSCVLVSTHlveDVAV 211
Cdd:COG1245 245 IYQRLNVARLIRELaEEGKYVLVVEH---DLAI 274
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
20-229 |
1.85e-12 |
|
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: 64.82 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 20 GLRVRAGRHLAVDGLDLSLGTGVH-GLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVhNRADLHTLRRSLGYLPQH- 97
Cdd:cd03244 9 SLRYRPNLPPVLKNISFSIKPGEKvGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDI-SKIGLHDLRSRISIIPQDp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 98 ---FGfyprfTVRE----FVEYlawlkhlpkatiPDA-VQHAIDRVGLTAKADT-----RMKTLSGGMLRRAG------I 158
Cdd:cd03244 88 vlfSG-----TIRSnldpFGEY------------SDEeLWQALERVGLKEFVESlpgglDTVVEEGGENLSVGqrqllcL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2683828925 159 AQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLRDLGTDSCVLVSTHLVEDVaVACTDVILINDGQLVHQGT 229
Cdd:cd03244 151 ARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTI-IDSDRILVLDKGRVVEFDS 220
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
47-204 |
2.23e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 64.48 E-value: 2.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 47 GPNGAGKTTLMRALATVVKPAGGTLTLLGHPVhNRADLHTLRRSLGYLPqhfGFYPRFTVREFVEYLAWLKHLPKATIPD 126
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQIDGKTA-TRGDRSRFMAYLGHLP---GLKADLSTLENLHFLCGLHGRRAKQMPG 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2683828925 127 avqHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQ-RLDFRELLRDLGTDSCVLVSTH 204
Cdd:PRK13543 120 ---SALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGiTLVNRMISAHLRGGGAALVTTH 195
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
30-234 |
2.72e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 65.49 E-value: 2.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 30 AVDGLDLSLGTGVH-GLLGPNGAGKTTLMRALATVVKPAGGTLTLLghpVHNRADLHTLRRSLGYLPQHFGFYPRF---- 104
Cdd:PRK13651 22 ALDNVSVEINQGEFiAIIGQTGSGKTTFIEHLNALLLPDTGTIEWI---FKDEKNKKKTKEKEKVLEKLVIQKTRFkkik 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 105 ----------TVREFVEYlawlkHLPKATI---------------PDAVQHA---IDRVGLTAKADTRMK-TLSGGMLRR 155
Cdd:PRK13651 99 kikeirrrvgVVFQFAEY-----QLFEQTIekdiifgpvsmgvskEEAKKRAakyIELVGLDESYLQRSPfELSGGQKRR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 156 AGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLRDLGTD-SCVLVSTHLVEDVAVACTDVILINDGQLVHQGTTDDLI 234
Cdd:PRK13651 174 VALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDIL 253
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
45-236 |
3.53e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 64.13 E-value: 3.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 45 LLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRADLHTLRRSLGYLPQHFGFYPRFTVREFVEYLAWLKHlpkati 124
Cdd:PRK11614 36 LIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRRVFSRMTVEENLAMGGFFAE------ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 125 PDAVQHAIDRV-----GLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDP---EQRLDFRELLRDLGTd 196
Cdd:PRK11614 110 RDQFQERIKWVyelfpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPiiiQQIFDTIEQLREQGM- 188
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2683828925 197 SCVLVSTHLVEDVAVACTDVILINdGQLVHQGTTDDLITH 236
Cdd:PRK11614 189 TIFLVEQNANQALKLADRGYVLEN-GHVVLEDTGDALLAN 227
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
44-181 |
3.78e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 65.73 E-value: 3.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 44 GLLGPNGAGKTTLMRALATVVKPAGGTLTLlghpvhnradlhTLRRSLGYLPQHFGFYPRFTVREFVEY-LAWLKHL--- 119
Cdd:TIGR03719 35 GVLGLNGAGKSTLLRIMAGVDKDFNGEARP------------QPGIKVGYLPQEPQLDPTKTVRENVEEgVAEIKDAldr 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 120 -----PKATIPDA-----------VQHAID---------RVGLTAKA------DTRMKTLSGGMLRRAGIAQAIVNNPAV 168
Cdd:TIGR03719 103 fneisAKYAEPDAdfdklaaeqaeLQEIIDaadawdldsQLEIAMDAlrcppwDADVTKLSGGERRRVALCRLLLSKPDM 182
|
170
....*....|...
gi 2683828925 169 LLLDEPTVGLDPE 181
Cdd:TIGR03719 183 LLLDEPTNHLDAE 195
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
19-204 |
3.94e-12 |
|
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: 63.31 E-value: 3.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 19 EGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATV--VKPAGGTLTLLGH-----PVHNRAdlhtlRRS 90
Cdd:cd03217 4 KDLHVSVGGKEILKGVNLTIKKGeVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEditdlPPEERA-----RLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 91 LGYLPQHFGFYPRFTVREFVEYLawlkhlpkatipdavqhaidRVGltakadtrmktLSGGMLRRAGIAQAIVNNPAVLL 170
Cdd:cd03217 79 IFLAFQYPPEIPGVKNADFLRYV--------------------NEG-----------FSGGEKKRNEILQLLLLEPDLAI 127
|
170 180 190
....*....|....*....|....*....|....*
gi 2683828925 171 LDEPTVGLDPEQ-RLDFRELLRDLGTDSCVLVSTH 204
Cdd:cd03217 128 LDEPDSGLDIDAlRLVAEVINKLREEGKSVLIITH 162
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
44-233 |
9.96e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 64.30 E-value: 9.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 44 GLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRADLHTLRRSLGYLP---QHFGFYPRFTVREFVEYLA------ 114
Cdd:PRK15439 293 GLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVYLPedrQSSGLYLDAPLAWNVCALThnrrgf 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 115 WLKHLPKATIPDAVQHAIdrvGLT-AKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLRDL 193
Cdd:PRK15439 373 WIKPARENAVLERYRRAL---NIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSI 449
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2683828925 194 GTD--SCVLVSTHLVEDVAVAcTDVILINDGQLVHQGTTDDL 233
Cdd:PRK15439 450 AAQnvAVLFISSDLEEIEQMA-DRVLVMHQGEISGALTGAAI 490
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
30-223 |
1.01e-11 |
|
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: 62.84 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 30 AVDGLDLSLGTGVH-GLLGPNGAGKTTLMRAL---------ATVVKPAGGTLTLLGHPVHnraDLHTLRRS-LGYLPQHF 98
Cdd:COG4778 26 VLDGVSFSVAAGECvALTGPSGAGKSTLLKCIygnylpdsgSILVRHDGGWVDLAQASPR---EILALRRRtIGYVSQFL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 99 GFYPRFTVREFV----------------EYLAWLKHLpkaTIPDAVQHAidrvgltAKAdtrmkTLSGGMLRRAGIAQAI 162
Cdd:COG4778 103 RVIPRVSALDVVaepllergvdreearaRARELLARL---NLPERLWDL-------PPA-----TFSGGEQQRVNIARGF 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2683828925 163 VNNPAVLLLDEPTVGLDPEQRLDFRELLRDLGTDSCVLVS-THLVEDVAVACTDVILINDGQ 223
Cdd:COG4778 168 IADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGiFHDEEVREAVADRVVDVTPFS 229
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
30-180 |
3.34e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 61.64 E-value: 3.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 30 AVDGLDLSLGTG----VhglLGPNGAGKTTLMRALATVVKPAGGTLTLLGH-----PVHNRAdlHTLRR----------- 89
Cdd:COG1101 21 ALDGLNLTIEEGdfvtV---IGSNGAGKSTLLNAIAGSLPPDSGSILIDGKdvtklPEYKRA--KYIGRvfqdpmmgtap 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 90 --------SLGYL-PQHFGFYPRFTVRE---FVEYLAWLKhlpkatipdavqhaidrVGLTAKADTRMKTLSGGmlRRag 157
Cdd:COG1101 96 smtieenlALAYRrGKRRGLRRGLTKKRrelFRELLATLG-----------------LGLENRLDTKVGLLSGG--QR-- 154
|
170 180
....*....|....*....|....*....
gi 2683828925 158 iaQAI------VNNPAVLLLDEPTVGLDP 180
Cdd:COG1101 155 --QALsllmatLTKPKLLLLDEHTAALDP 181
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
15-204 |
3.44e-11 |
|
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: 63.03 E-value: 3.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 15 VVHAEGLRVRAGRHLAVDGLDLSL-GTGVHGLLGPNGAGKTTLMRALATVVKPAGGTLTlLGHPVHnradlhtlrrsLGY 93
Cdd:TIGR03719 322 VIEAENLTKAFGDKLLIDDLSFKLpPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIE-IGETVK-----------LAY 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 94 LPQ-HFGFYPRFTVREFVEYLAWLKHLPKATIPDavQHAIDRVGLT-AKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLL 171
Cdd:TIGR03719 390 VDQsRDALDPNKTVWEEISGGLDIIKLGKREIPS--RAYVGRFNFKgSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLL 467
|
170 180 190
....*....|....*....|....*....|...
gi 2683828925 172 DEPTVGLDPEQRLDFRELLRDLGtdSCVLVSTH 204
Cdd:TIGR03719 468 DEPTNDLDVETLRALEEALLNFA--GCAVVISH 498
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
21-238 |
3.97e-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: 62.53 E-value: 3.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 21 LRVRAGRHLAVdgldlslgtgvhglLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVhnRA-DLHTLRRSLGYLPQHfg 99
Cdd:COG5265 379 FEVPAGKTVAI--------------VGPSGAGKSTLARLLFRFYDVTSGRILIDGQDI--RDvTQASLRAAIGIVPQD-- 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 100 fyprfTV------REFVEYLAwlkhlPKATiPDAVQHAIDR-------VGLTAKADTR-----MKtLSGGMLRRAGIAQA 161
Cdd:COG5265 441 -----TVlfndtiAYNIAYGR-----PDAS-EEEVEAAARAaqihdfiESLPDGYDTRvgergLK-LSGGEKQRVAIART 508
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2683828925 162 IVNNPAVLLLDEPTVGLDPEQRLDFRELLRDLGTDSCVLVSTHLVEDVAVActDVIL-INDGQLVHQGTTDDLITHGG 238
Cdd:COG5265 509 LLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDA--DEILvLEAGRIVERGTHAELLAQGG 584
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
31-237 |
4.60e-11 |
|
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: 62.53 E-value: 4.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 31 VDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPA-GGTLTLLGHPVHNRADLHTLRRSLGYLPQ---HFGFYPRFT 105
Cdd:TIGR02633 276 VDDVSFSLRRGeILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQAIRAGIAMVPEdrkRHGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 106 VREFVEyLAWLKHLPKATIPDA------VQHAIDRVGL-TAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGL 178
Cdd:TIGR02633 356 VGKNIT-LSVLKSFCFKMRIDAaaelqiIGSAIQRLKVkTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGV 434
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2683828925 179 DPEQRLDFRELLRDLGTD--SCVLVSTHLVEDVAVAcTDVILINDGQLvhQGttdDLITHG 237
Cdd:TIGR02633 435 DVGAKYEIYKLINQLAQEgvAIIVVSSELAEVLGLS-DRVLVIGEGKL--KG---DFVNHA 489
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
44-235 |
6.54e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 62.11 E-value: 6.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 44 GLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRADLHTLRRSLGYLPQH---FGFYPRFTVREFVeylAWLKHLP 120
Cdd:PRK09700 293 GFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYITESrrdNGFFPNFSIAQNM---AISRSLK 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 121 KATIPDAV----QHAIDRVGLTAKADTRMKT---------LSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFR 187
Cdd:PRK09700 370 DGGYKGAMglfhEVDEQRTAENQRELLALKChsvnqniteLSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIY 449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2683828925 188 ELLRDLGTDSCV--LVSTHLVEDVAVaCTDVILINDGQLVHQGTTDDLIT 235
Cdd:PRK09700 450 KVMRQLADDGKVilMVSSELPEIITV-CDRIAVFCEGRLTQILTNRDDMS 498
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
47-233 |
6.81e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 61.95 E-value: 6.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 47 GPNGAGKTTLMRALAtvvkpagGTLTLLGHPVHNRADlHTLRRSLGYLPQ-------------------HFGFyprfTVR 107
Cdd:PRK10938 36 GANGSGKSALARALA-------GELPLLSGERQSQFS-HITRLSFEQLQKlvsdewqrnntdmlspgedDTGR----TTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 108 EFVeylawLKHLPKatiPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFR 187
Cdd:PRK10938 104 EII-----QDEVKD---PARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2683828925 188 ELLRDLGTDSCVLVsthLV----EDVAVACTDVILINDGQLVHQGTTDDL 233
Cdd:PRK10938 176 ELLASLHQSGITLV---LVlnrfDEIPDFVQFAGVLADCTLAETGEREEI 222
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
41-211 |
7.55e-11 |
|
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: 60.84 E-value: 7.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 41 GVHGLLGPNGAGKTTLMRALATVVKPAGGTLT-----------LLGHPVHN------RADLHTLRRslgylPQHFGFYPR 103
Cdd:cd03236 27 QVLGLVGPNGIGKSTALKILAGKLKPNLGKFDdppdwdeildeFRGSELQNyftkllEGDVKVIVK-----PQYVDLIPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 104 fTVREFVEYLawlkhLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQR 183
Cdd:cd03236 102 -AVKGKVGEL-----LKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQR 175
|
170 180
....*....|....*....|....*....
gi 2683828925 184 LDFRELLRDLGTDS-CVLVSTHlveDVAV 211
Cdd:cd03236 176 LNAARLIRELAEDDnYVLVVEH---DLAV 201
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
41-237 |
8.06e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.87 E-value: 8.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 41 GVHGLLGpngAGKTTLMRALATVVKPA-GGTLTLLGHPVHNRADLHTLRRSLGYLPQ---HFGFYPRFTVREFVEyLAWL 116
Cdd:PRK13549 292 GIAGLVG---AGRTELVQCLFGAYPGRwEGEIFIDGKPVKIRNPQQAIAQGIAMVPEdrkRDGIVPVMGVGKNIT-LAAL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 117 KHLPKATIPDA------VQHAIDRVGL-TAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFREL 189
Cdd:PRK13549 368 DRFTGGSRIDDaaelktILESIQRLKVkTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKL 447
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2683828925 190 LRDLGTD--SCVLVSTHLVEdvavactdVILINDGQLV-HQGT-TDDLITHG 237
Cdd:PRK13549 448 INQLVQQgvAIIVISSELPE--------VLGLSDRVLVmHEGKlKGDLINHN 491
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
34-234 |
1.50e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 60.97 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 34 LDLSLGTG-VHGLLGPNGAGKTTLMRAL--------------------------------ATVVKPAGGTLTLLGHPVHN 80
Cdd:TIGR03269 19 ISFTIEEGeVLGILGRSGAGKSVLMHVLrgmdqyeptsgriiyhvalcekcgyverpskvGEPCPVCGGTLEPEEVDFWN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 81 RADLHT--LRRSLGYLPQH-FGFYPRFTVREFVeylawLKHLPKATIP--DAVQHAIDRVGLTaKADTRM----KTLSGG 151
Cdd:TIGR03269 99 LSDKLRrrIRKRIAIMLQRtFALYGDDTVLDNV-----LEALEEIGYEgkEAVGRAVDLIEMV-QLSHRIthiaRDLSGG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 152 MLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLRDLGTDS--CVLVSTHLVEDVAVACTDVILINDGQLVHQGT 229
Cdd:TIGR03269 173 EKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPEVIEDLSDKAIWLENGEIKEEGT 252
|
....*
gi 2683828925 230 TDDLI 234
Cdd:TIGR03269 253 PDEVV 257
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
44-181 |
1.62e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.90 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 44 GLLGPNGAGKTTLMRALATVVKPAGGTLTLL-GHPVhnradlhtlrrslGYLPQHFGFYPRFTVREFVE-----YLAWLK 117
Cdd:PRK11819 37 GVLGLNGAGKSTLLRIMAGVDKEFEGEARPApGIKV-------------GYLPQEPQLDPEKTVRENVEegvaeVKAALD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 118 HL----PKATIPDA-----------VQHAID---------RVGLTAKA------DTRMKTLSGGMLRRAGIAQAIVNNPA 167
Cdd:PRK11819 104 RFneiyAAYAEPDAdfdalaaeqgeLQEIIDaadawdldsQLEIAMDAlrcppwDAKVTKLSGGERRRVALCRLLLEKPD 183
|
170
....*....|....
gi 2683828925 168 VLLLDEPTVGLDPE 181
Cdd:PRK11819 184 MLLLDEPTNHLDAE 197
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
30-234 |
3.26e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 59.74 E-value: 3.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 30 AVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRADLHTLRRSLGYLPQHFGFYPRFTVRE 108
Cdd:PRK10982 13 ALDNVNLKVRPHsIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQELNLVLQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 109 FVeylaWLKHLPKATIpdAVQH--------AI-DRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLD 179
Cdd:PRK10982 93 NM----WLGRYPTKGM--FVDQdkmyrdtkAIfDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 180 PEQRLDFRELLRDLGTDSCVLVS-THLVEDVAVACTDVILINDGQLVH----QGTTDDLI 234
Cdd:PRK10982 167 EKEVNHLFTIIRKLKERGCGIVYiSHKMEEIFQLCDEITILRDGQWIAtqplAGLTMDKI 226
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
34-228 |
3.99e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 59.12 E-value: 3.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 34 LDLSL-GTGVHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGH---PVHNRADLHTLRRSLGYLPQHFGFYPRFTVREF 109
Cdd:PRK11144 17 VNLTLpAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEKGICLPPEKRRIGYVFQDARLFPHYKVRGN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 110 VEYlaWLKHLPKATIPDAVQ-----HAIDRVGLtakadtrmkTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLD-PEQr 183
Cdd:PRK11144 97 LRY--GMAKSMVAQFDKIVAllgiePLLDRYPG---------SLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRK- 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2683828925 184 ldfRELLRDLGTDS------CVLVSTHLVEDVAVAcTDVILINDGQLVHQG 228
Cdd:PRK11144 165 ---RELLPYLERLAreinipILYVSHSLDEILRLA-DRVVVLEQGKVKAFG 211
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
41-179 |
4.83e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 59.25 E-value: 4.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 41 GVHGLLGpngAGKTTLMRALATVVKPAGGTLTLLGHPVHNRADLHTLRRSLGYLPQ---HFGFYPRFTVREFVEyLAWLK 117
Cdd:PRK10762 282 GVSGLMG---AGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIVYISEdrkRDGLVLGMSVKENMS-LTALR 357
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2683828925 118 HLPKATIpdAVQHAIDRVGL----------TAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLD 179
Cdd:PRK10762 358 YFSRAGG--SLKHADEQQAVsdfirlfnikTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
16-229 |
5.28e-10 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 57.81 E-value: 5.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 16 VHAEGLRVRAGRHL--AVDGLDLSLGTGVH-GLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVhNRADLHTLRRSLG 92
Cdd:cd03369 7 IEVENLSVRYAPDLppVLKNVSFKVKAGEKiGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDI-STIPLEDLRSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 93 YLPQH---FGFYPRFTVREFVEYlawlkhlpkatiPDAVQHAIDRV---GLtakadtrmkTLSGGMLRRAGIAQAIVNNP 166
Cdd:cd03369 86 IIPQDptlFSGTIRSNLDPFDEY------------SDEEIYGALRVsegGL---------NLSQGQRQLLCLARALLKRP 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2683828925 167 AVLLLDEPTVGLDPEQRLDFRELLRDLGTDSCVLVSTHLVEDVAvACTDVILINDGQLVHQGT 229
Cdd:cd03369 145 RVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTII-DYDKILVMDAGEVKEYDH 206
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
32-213 |
5.70e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 59.26 E-value: 5.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 32 DGLDLSLGTGVH-GLLGPNGAGKTTLMrALATVVKPAG--GTLTLLGHpvhNRADLHTL---RRSLGYLPQ--HFGFYPR 103
Cdd:PRK10938 277 HNLSWQVNPGEHwQIVGPNGAGKSTLL-SLITGDHPQGysNDLTLFGR---RRGSGETIwdiKKHIGYVSSslHLDYRVS 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 104 FTVREFV---------EYLAwlkhlpkatIPDAVQHA----IDRVGLTAK-ADTRMKTLSGGMLRRAGIAQAIVNNPAVL 169
Cdd:PRK10938 353 TSVRNVIlsgffdsigIYQA---------VSDRQQKLaqqwLDILGIDKRtADAPFHSLSWGQQRLALIVRALVKHPTLL 423
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2683828925 170 LLDEPTVGLDPEQRLDFRELLRDLGTDSC--VLVSTHLVEDvAVAC 213
Cdd:PRK10938 424 ILDEPLQGLDPLNRQLVRRFVDVLISEGEtqLLFVSHHAED-APAC 468
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
45-179 |
6.08e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 59.47 E-value: 6.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 45 LLGPNGAGKTTLMRALATVvKPAG---GTLTLLGHPVHNradlHTLRRSLGYLPQHFGFYPRFTVREFVEYLAWLKhLPK 121
Cdd:PLN03140 911 LMGVSGAGKTTLMDVLAGR-KTGGyieGDIRISGFPKKQ----ETFARISGYCEQNDIHSPQVTVRESLIYSAFLR-LPK 984
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2683828925 122 ATIPDAVQHAIDRVGLTAKADTR---------MKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLD 179
Cdd:PLN03140 985 EVSKEEKMMFVDEVMELVELDNLkdaivglpgVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
30-229 |
1.47e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 57.33 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 30 AVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTlTLLGH---PVHNRA--DLHTLRRSLGYLPQhFGFYPR 103
Cdd:PRK13645 26 ALNNTSLTFKKNkVTCVIGTTGSGKSTMIQLTNGLIISETGQ-TIVGDyaiPANLKKikEVKRLRKEIGLVFQ-FPEYQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 104 F--TVREFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMK-TLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDP 180
Cdd:PRK13645 104 FqeTIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPfELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDP 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2683828925 181 EQRLDFRELLRDLGTDSC--VLVSTHLVEDVAVACTDVILINDGQLVHQGT 229
Cdd:PRK13645 184 KGEEDFINLFERLNKEYKkrIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
45-179 |
2.21e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 57.65 E-value: 2.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 45 LLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRadlhtlrrslgyLPQHfgfYPRF---TVREFV--------EYL 113
Cdd:PRK11147 34 LVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVAR------------LQQD---PPRNvegTVYDFVaegieeqaEYL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 114 --------------------------AWLKHLPKATIPDAVQHAIDRVGLTAkaDTRMKTLSGGMLRRAGIAQAIVNNPA 167
Cdd:PRK11147 99 kryhdishlvetdpseknlnelaklqEQLDHHNLWQLENRINEVLAQLGLDP--DAALSSLSGGWLRKAALGRALVSNPD 176
|
170
....*....|..
gi 2683828925 168 VLLLDEPTVGLD 179
Cdd:PRK11147 177 VLLLDEPTNHLD 188
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
148-238 |
4.11e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 56.57 E-value: 4.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 148 LSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLRDLGTDSCVLVSTHLVEDVAVActDVIL-INDGQLVH 226
Cdd:PRK11176 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKA--DEILvVEDGEIVE 558
|
90
....*....|..
gi 2683828925 227 QGTTDDLITHGG 238
Cdd:PRK11176 559 RGTHAELLAQNG 570
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
24-217 |
4.92e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 55.11 E-value: 4.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 24 RAGRHLAVDGLDLSLGTGVHGLL-GPNGAGKTTLMRALATVVKPAGGTLTLLGHPVhnrADL--HTLRRSLGY---LPQH 97
Cdd:PRK10247 16 LAGDAKILNNISFSLRAGEFKLItGPSGCGKSTLLKIVASLISPTSGTLLFEGEDI---STLkpEIYRQQVSYcaqTPTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 98 FGfyprFTVREFVEYLAWLKHlpKATIPDAVQHAIDRVGLTAKA-DTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTV 176
Cdd:PRK10247 93 FG----DTVYDNLIFPWQIRN--QQPDPAIFLDDLERFALPDTIlTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITS 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2683828925 177 GLDPEQRLDFRELLRDLGTDS--CVLVSTHLVEDVAvACTDVI 217
Cdd:PRK10247 167 ALDESNKHNVNEIIHRYVREQniAVLWVTHDKDEIN-HADKVI 208
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
44-219 |
9.76e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 55.30 E-value: 9.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 44 GLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRADLHTLRRSLGYLPQ---HFGFYPRFTVREFVEYLAWLKHLP 120
Cdd:PRK11288 283 GLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMLCPEdrkAEGIIPVHSVADNINISARRHHLR 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 121 KATIPDA------VQHAIDRVGL-TAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLRDL 193
Cdd:PRK11288 363 AGCLINNrweaenADRFIRSLNIkTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYEL 442
|
170 180
....*....|....*....|....*...
gi 2683828925 194 GTDSC--VLVSTHLVEDVAVActDVILI 219
Cdd:PRK11288 443 AAQGVavLFVSSDLPEVLGVA--DRIVV 468
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
20-204 |
1.27e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 53.81 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 20 GLRVRAGRHLAVDGLDLSLGTGVHGLL-GPNGAGKTTLMRALATvvkpaggtlTLLGHPVHNRADLHTLRrslgylpqhf 98
Cdd:COG2401 35 GVELRVVERYVLRDLNLEIEPGEIVLIvGASGSGKSTLLRLLAG---------ALKGTPVAGCVDVPDNQ---------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 99 gFYPRFTVrefveylawLKHLPKATIPDAVQHAIDRVGLtakAD-----TRMKTLSGGMLRRAGIAQAIVNNPAVLLLDE 173
Cdd:COG2401 96 -FGREASL---------IDAIGRKGDFKDAVELLNAVGL---SDavlwlRRFKELSTGQKFRFRLALLLAERPKLLVIDE 162
|
170 180 190
....*....|....*....|....*....|....*
gi 2683828925 174 PTVGLDPE--QRL--DFRELLRDLGTdSCVLVSTH 204
Cdd:COG2401 163 FCSHLDRQtaKRVarNLQKLARRAGI-TLVVATHH 196
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
45-231 |
1.31e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.50 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 45 LLGPNGAGKTTLMRALATVV----KPAGGTLTLLGHPVHNRadLHTLRRSLGYLPQ---HFgfyPRFTVREFVEYLAWLK 117
Cdd:TIGR00956 92 VLGRPGSGCSTLLKTIASNTdgfhIGVEGVITYDGITPEEI--KKHYRGDVVYNAEtdvHF---PHLTVGETLDFAARCK 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 118 hlPKATIPDAV------QHAIDRV----GLTAKADTR-----MKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQ 182
Cdd:TIGR00956 167 --TPQNRPDGVsreeyaKHIADVYmatyGLSHTRNTKvgndfVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSAT 244
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2683828925 183 RLDFRELLRDLG--TDSCVLVSTH-LVEDVAVACTDVILINDGQLVHQGTTD 231
Cdd:TIGR00956 245 ALEFIRALKTSAniLDTTPLVAIYqCSQDAYELFDKVIVLYEGYQIYFGPAD 296
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
45-228 |
2.02e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.48 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 45 LLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRAD--LHTLRRSLGYLPQ--HFGFYPRFTV-REFVEYLAWLKHL 119
Cdd:PRK10261 355 LVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPgkLQALRRDIQFIFQdpYASLDPRQTVgDSIMEPLRVHGLL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 120 PKATIPDAVQHAIDRVGLTAKADTRM-KTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLRDLGTDSC 198
Cdd:PRK10261 435 PGKAAAARVAWLLERVGLLPEHAWRYpHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFG 514
|
170 180 190
....*....|....*....|....*....|..
gi 2683828925 199 V--LVSTHLVEDVAVACTDVILINDGQLVHQG 228
Cdd:PRK10261 515 IayLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
41-179 |
2.29e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.03 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 41 GVHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVhnRADLHTLRRSLGYLPQHFGFYPRFTVREFVEYlawlkHLP 120
Cdd:PRK13540 28 GLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI--KKDLCTYQKQLCFVGHRSGINPYLTLRENCLY-----DIH 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2683828925 121 KATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLD 179
Cdd:PRK13540 101 FSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
26-224 |
2.30e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.41 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 26 GRHLAVDGLDLSLGTGVH-GLLGPNGAGKTTLMRALATVVKPAGGTLTLlghpvhnradlhTLRRSLGYLPQHfgfyprf 104
Cdd:PRK10636 323 GDRIILDSIKLNLVPGSRiGLLGRNGAGKSTLIKLLAGELAPVSGEIGL------------AKGIKLGYFAQH------- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 105 tvreFVEYL----AWLKHLPKATIPDAVQHAIDRVGLTA----KADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTV 176
Cdd:PRK10636 384 ----QLEFLradeSPLQHLARLAPQELEQKLRDYLGGFGfqgdKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTN 459
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2683828925 177 GLDPEQRLDFRELLRDLgtDSCVLVSTHLVEDVAVACTDVILINDGQL 224
Cdd:PRK10636 460 HLDLDMRQALTEALIDF--EGALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
28-223 |
2.89e-08 |
|
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: 52.19 E-value: 2.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 28 HLAVDGLDLSLGTgVHGLLGPNGAGKTTLMRALATVVKPAGGTLTLlghpvhnraDLHTLrrslGYLPQHFgfyprftvr 107
Cdd:cd03222 14 FLLVELGVVKEGE-VIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW---------DGITP----VYKPQYI--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 108 efveylawlkhlpkatipdavqhaidrvgltakadtrmkTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFR 187
Cdd:cd03222 71 ---------------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAA 111
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2683828925 188 ELLRDLGTDS--CVLVSTHlveDVAVA--CTDVILINDGQ 223
Cdd:cd03222 112 RAIRRLSEEGkkTALVVEH---DLAVLdyLSDRIHVFEGE 148
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
30-242 |
3.69e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 53.19 E-value: 3.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 30 AVDGLDLSLGTG-VHGLLGPNGAGKT----TLMRALATVVKpAGGTLTLLGHPVHN--RADLHTLRR---SLGYLPQHFG 99
Cdd:PRK09473 31 AVNDLNFSLRAGeTLGIVGESGSGKSqtafALMGLLAANGR-IGGSATFNGREILNlpEKELNKLRAeqiSMIFQDPMTS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 100 FYPRFTVRE-FVEYLAWLKHLPKATIPDAVQHAIDRVGLtAKADTRMKT----LSGGMLRRAGIAQAIVNNPAVLLLDEP 174
Cdd:PRK09473 110 LNPYMRVGEqLMEVLMLHKGMSKAEAFEESVRMLDAVKM-PEARKRMKMypheFSGGMRQRVMIAMALLCRPKLLIADEP 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 175 TVGLDPEQRLDFRELLRDLGTD--SCVLVSTHLVEDVAVACTDVILINDGQLVHQGTTDDLITHggPDDP 242
Cdd:PRK09473 189 TTALDVTVQAQIMTLLNELKREfnTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQ--PSHP 256
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
129-233 |
5.11e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 52.82 E-value: 5.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 129 QHAID---RVGLTAKA---DTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLRDLGTDSC--VL 200
Cdd:PRK11022 129 QRAIDllnQVGIPDPAsrlDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENmaLV 208
|
90 100 110
....*....|....*....|....*....|...
gi 2683828925 201 VSTHLVEDVAVACTDVILINDGQLVHQGTTDDL 233
Cdd:PRK11022 209 LITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
47-205 |
6.63e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 51.41 E-value: 6.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 47 GPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRADLHtlrrsLGYLPQHFGFYPRFTVREFVEYlaWLKHLPKATIPD 126
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPY-----CTYIGHNLGLKLEMTVFENLKF--WSEIYNSAETLY 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 127 AvqhAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQrldfRELLRDL-----GTDSCVLV 201
Cdd:PRK13541 106 A---AIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKEN----RDLLNNLivmkaNSGGIVLL 178
|
....
gi 2683828925 202 STHL 205
Cdd:PRK13541 179 SSHL 182
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
31-233 |
6.80e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 52.40 E-value: 6.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 31 VDGLDLSLGTGVH-GLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVhNRADLHTLRRSLGYLPQH-FGFYPRFTVRE 108
Cdd:PRK13642 23 LNGVSFSITKGEWvSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELL-TAENVWNLRRKIGMVFQNpDNQFVGATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 109 FVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRE 188
Cdd:PRK13642 102 DVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2683828925 189 LLRDLGTDS--CVLVSTHLVeDVAVACTDVILINDGQLVHQGTTDDL 233
Cdd:PRK13642 182 VIHEIKEKYqlTVLSITHDL-DEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
30-225 |
1.30e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.10 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 30 AVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVkPAG---GTLTLLGHPVHnradLHTLRRS--------------- 90
Cdd:NF040905 16 ALDDVNLSVREGeIHALCGENGAGKSTLMKVLSGVY-PHGsyeGEILFDGEVCR----FKDIRDSealgiviihqelali 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 91 ----------LGYLPQHFGF--YPRfTVREFVEYLAwlkhlpkatipdavqhaidRVGLTAKADTRMKTLSGGMLRRAGI 158
Cdd:NF040905 91 pylsiaenifLGNERAKRGVidWNE-TNRRARELLA-------------------KVGLDESPDTLVTDIGVGKQQLVEI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2683828925 159 AQAIVNNPAVLLLDEPTVGL---DPEQRLDFRELLRDLGTdSCVLVSTHLVEDVAVActDVI-LINDGQLV 225
Cdd:NF040905 151 AKALSKDVKLLILDEPTAALneeDSAALLDLLLELKAQGI-TSIIISHKLNEIRRVA--DSItVLRDGRTI 218
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
15-181 |
2.17e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 51.27 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 15 VVHAEGLRVRAGRHLAVDGLDLSL--GtGVHGLLGPNGAGKTTLMRALATVVKPAGGTLTlLGHPVHnradlhtlrrsLG 92
Cdd:PRK11819 324 VIEAENLSKSFGDRLLIDDLSFSLppG-GIVGIIGPNGAGKSTLFKMITGQEQPDSGTIK-IGETVK-----------LA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 93 YLPQ-HFGFYPRFTVREFV----EYLawlkHLPKATIPdavQHA-IDRVGLTAkAD--TRMKTLSGG---------MLRR 155
Cdd:PRK11819 391 YVDQsRDALDPNKTVWEEIsgglDII----KVGNREIP---SRAyVGRFNFKG-GDqqKKVGVLSGGernrlhlakTLKQ 462
|
170 180
....*....|....*....|....*.
gi 2683828925 156 AGiaqaivNnpaVLLLDEPTVGLDPE 181
Cdd:PRK11819 463 GG------N---VLLLDEPTNDLDVE 479
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
45-235 |
2.51e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.39 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 45 LLGPNGAGKTTLMRALATVVKPA---GGTLTLLGHpvhnRADLHTLRRSLGYLPQ---HFGFyprFTVREFVEYLA---- 114
Cdd:PLN03140 196 LLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGY----RLNEFVPRKTSAYISQndvHVGV---MTVKETLDFSArcqg 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 115 ------WLKHLP------------------KATIPDAVQ------HAIDRVGL-----TAKADTRMKTLSGGMLRRAGIA 159
Cdd:PLN03140 269 vgtrydLLSELArrekdagifpeaevdlfmKATAMEGVKsslitdYTLKILGLdickdTIVGDEMIRGISGGQKKRVTTG 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 160 QAIVNNPAVLLLDEPTVGLDPEQRLDFRELLRDLG--TDSCVLVS-------THLVEDvavactDVILINDGQLVHQGTT 230
Cdd:PLN03140 349 EMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVhlTEATVLMSllqpapeTFDLFD------DIILLSEGQIVYQGPR 422
|
....*
gi 2683828925 231 DDLIT 235
Cdd:PLN03140 423 DHILE 427
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
44-249 |
2.59e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 51.45 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 44 GLLGPNGAGKTTLMRALATVVKpAGGTLTLLGHPvHNRADLHTLRRSLGYLPQhfgfyprftvREFVEYLAWLKHL-PKA 122
Cdd:TIGR01271 1249 GLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVS-WNSVTLQTWRKAFGVIPQ----------KVFIFSGTFRKNLdPYE 1316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 123 TIPDA-VQHAIDRVGLTA-------KADTRMK----TLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELL 190
Cdd:TIGR01271 1317 QWSDEeIWKVAEEVGLKSvieqfpdKLDFVLVdggyVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTL 1396
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2683828925 191 RDLGTDSCVLVSTHLVEDVaVACTDVILINDGQLVHQGTTDDLITHGGPDDPGDSPAER 249
Cdd:TIGR01271 1397 KQSFSNCTVILSEHRVEAL-LECQQFLVIEGSSVKQYDSIQKLLNETSLFKQAMSAADR 1454
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
26-264 |
1.62e-06 |
|
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: 48.31 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 26 GRHLAVDGLDLSLGTGVH-GLLGPNGAGKTTLMRALATVVKpAGGTLTLLGHPvHNRADLHTLRRSLGYLPQHFgFYPRF 104
Cdd:cd03289 15 GGNAVLENISFSISPGQRvGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVS-WNSVPLQKWRKAFGVIPQKV-FIFSG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 105 TVREFVE-YLAWL-KHLPKATIPDAVQHAIDRvgLTAKADTRMK----TLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGL 178
Cdd:cd03289 92 TFRKNLDpYGKWSdEEIWKVAEEVGLKSVIEQ--FPGQLDFVLVdggcVLSHGHKQLMCLARSVLSKAKILLLDEPSAHL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 179 DPEQRLDFRELLRDLGTDSCVLVSTHLVEDVaVACTDVILINDGQLVHQGTTDDLITHGGPDDPGDSPAERgYSALLRRH 258
Cdd:cd03289 170 DPITYQVIRKTLKQAFADCTVILSEHRIEAM-LECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAISPSDR-LKLFPRRN 247
|
....*.
gi 2683828925 259 RTAAGR 264
Cdd:cd03289 248 SSKSKR 253
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
28-236 |
1.77e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 48.73 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 28 HLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALATVVKPAGGTLTLLGhpvhnradlhtlrrSLGYLPQHFGFYPRFTV 106
Cdd:PRK13545 37 HYALNNISFEVPEGeIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG--------------SAALIAISSGLNGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 107 REFVEYLAWLKHLPKATIPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEP-TVGLDP----- 180
Cdd:PRK13545 103 IENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEAlSVGDQTftkkc 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2683828925 181 -EQRLDFREllrdlgTDSCVLVSTHLVEDVAVACTDVILINDGQLVHQGTTDDLITH 236
Cdd:PRK13545 183 lDKMNEFKE------QGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
22-194 |
2.13e-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: 48.59 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 22 RVRAGRHLAVdgldlslgtgvhglLGPNGAGKTTLMRALATVVKPAGGTLTLlghPVHNRadlhtlrrsLGYLPQHfGFY 101
Cdd:TIGR00954 474 EVPSGNNLLI--------------CGPNGCGKSSLFRILGELWPVYGGRLTK---PAKGK---------LFYVPQR-PYM 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 102 PRFTVREFVEYLAWLKHLPKATIPDAV----------QHAIDR-VGLTAKADTrMKTLSGGMLRRAGIAQAIVNNPAVLL 170
Cdd:TIGR00954 527 TLGTLRDQIIYPDSSEDMKRRGLSDKDleqildnvqlTHILEReGGWSAVQDW-MDVLSGGEKQRIAMARLFYHKPQFAI 605
|
170 180
....*....|....*....|....*.
gi 2683828925 171 LDEPT--VGLDPEQRLdfRELLRDLG 194
Cdd:TIGR00954 606 LDECTsaVSVDVEGYM--YRLCREFG 629
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
34-237 |
2.95e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.20 E-value: 2.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 34 LDLSLGTGVhGLLGPNGAGKTTLMRALATVVKPaggtltllghpvhnRADLH-TLRRSLGYLPQhFGFYPRFTVREFVEY 112
Cdd:PLN03130 638 LDVPVGSLV-AIVGSTGEGKTSLISAMLGELPP--------------RSDASvVIRGTVAYVPQ-VSWIFNATVRDNILF 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 113 LAWLKhlpkatiPDAVQHAIDRVGLTAKADT-----------RMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPE 181
Cdd:PLN03130 702 GSPFD-------PERYERAIDVTALQHDLDLlpggdlteigeRGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAH 774
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 182 -QRLDFRELLRD-LGTDSCVLVST--HLVEDVavacTDVILINDGQLVHQGTTDDLITHG 237
Cdd:PLN03130 775 vGRQVFDKCIKDeLRGKTRVLVTNqlHFLSQV----DRIILVHEGMIKEEGTYEELSNNG 830
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
31-235 |
3.85e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.39 E-value: 3.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 31 VDGLDLSLGTG-VHGLLGPNGAGKT----TLMRALAT--VVKPAGGTL----TLLghpvhnRADLHTLRRSLG------Y 93
Cdd:PRK15134 25 VNDVSLQIEAGeTLALVGESGSGKSvtalSILRLLPSppVVYPSGDIRfhgeSLL------HASEQTLRGVRGnkiamiF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 94 LPQHFGFYPRFTV-REFVEYLAWLKHLPKATIPDAVQHAIDRVGLTaKADTRMK----TLSGGMLRRAGIAQAIVNNPAV 168
Cdd:PRK15134 99 QEPMVSLNPLHTLeKQLYEVLSLHRGMRREAARGEILNCLDRVGIR-QAAKRLTdyphQLSGGERQRVMIAMALLTRPEL 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2683828925 169 LLLDEPTVGLD---PEQRLD-FRELLRDLGTDscVLVSTHLVEDVAVACTDVILINDGQLVHQGTTDDLIT 235
Cdd:PRK15134 178 LIADEPTTALDvsvQAQILQlLRELQQELNMG--LLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFS 246
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
41-219 |
5.34e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.03 E-value: 5.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 41 GVHGLLGpngAGKTTLMRALATVVKPAGGTLTLLGHPVHNRADLHTL----------RRSLG---YLPQHFGFyprfTVR 107
Cdd:PRK10982 278 GIAGLVG---AKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAInhgfalvteeRRSTGiyaYLDIGFNS----LIS 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 108 EFVEYLAWLKHLPKATIPDAVQHAIDRVGL-TAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDF 186
Cdd:PRK10982 351 NIRNYKNKVGLLDNSRMKSDTQWVIDSMRVkTPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEI 430
|
170 180 190
....*....|....*....|....*....|....*
gi 2683828925 187 RELLRDLGTDS--CVLVSTHLVEDVAVacTDVILI 219
Cdd:PRK10982 431 YQLIAELAKKDkgIIIISSEMPELLGI--TDRILV 463
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
44-238 |
5.60e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 47.01 E-value: 5.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 44 GLLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHnRADLHTLRRSLGYLPQhfgfyprfTVREFVEYLAWLKHLPKat 123
Cdd:PRK10789 345 GICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLT-KLQLDSWRSRLAVVSQ--------TPFLFSDTVANNIALGR-- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 124 iPDAVQHAIDRV---------------GLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRE 188
Cdd:PRK10789 414 -PDATQQEIEHVarlasvhddilrlpqGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILH 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2683828925 189 LLRDLGTDSCVLVSTHLVEDVAVAcTDVILINDGQLVHQGTTDDLITHGG 238
Cdd:PRK10789 493 NLRQWGEGRTVIISAHRLSALTEA-SEILVMQHGHIAQRGNHDQLAQQSG 541
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
45-234 |
8.20e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 45.94 E-value: 8.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 45 LLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHnRADLHTLRRSLGYLPQ--HFGFYPRFTVREFVEY-LAWLKHLPK 121
Cdd:PRK15112 44 IIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH-FGDYSYRSQRIRMIFQdpSTSLNPRQRISQILDFpLRLNTDLEP 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 122 ATIPDAVQHAIDRVGLTAK-ADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLRDLGTD---S 197
Cdd:PRK15112 123 EQREKQIIETLRQVGLLPDhASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqgiS 202
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2683828925 198 CVLVSTHL-----VEDvavactDVILINDGQLVHQGTTDDLI 234
Cdd:PRK15112 203 YIYVTQHLgmmkhISD------QVLVMHQGEVVERGSTADVL 238
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
32-200 |
9.64e-06 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 45.39 E-value: 9.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 32 DGLDLSLGTGVHGLLGPNGAGKTTLMRALA--------------------------------------TVVKPAGGTLTL 73
Cdd:COG0419 15 DTETIDFDDGLNLIVGPNGAGKSTILEAIRyalygkarsrsklrsdlinvgseeasvelefehggkryRIERRQGEFAEF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 74 LGHPVHNRADLhtLRRSLGylpqhfgfyprftVREFVEYLAWLKHLpKATIPDAVQHAIDRVGLTAKADTRM------KT 147
Cdd:COG0419 95 LEAKPSERKEA--LKRLLG-------------LEIYEELKERLKEL-EEALESALEELAELQKLKQEILAQLsgldpiET 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2683828925 148 LSGGMLRRAGIAQAIvnnpaVLLLDepTVGLDPEQRLDFRELLRDLGTDSCVL 200
Cdd:COG0419 159 LSGGERLRLALADLL-----SLILD--FGSLDEERLERLLDALEELAIITHVI 204
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
21-238 |
1.12e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.04 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 21 LRVRAGRHLAVdgldlslgtgvhglLGPNGAGKTTLMRALATVVKPAGGTLTLlghpvhnradlhTLRRSLGYLPQHfgf 100
Cdd:PRK15064 340 LLLEAGERLAI--------------IGENGVGKTTLLRTLVGELEPDSGTVKW------------SENANIGYYAQD--- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 101 yprfTVREFVEYLA---WLKHLPKATIPD-AVQHAIDRVgLTAKADTR--MKTLSGGMLRRAGIAQAIVNNPAVLLLDEP 174
Cdd:PRK15064 391 ----HAYDFENDLTlfdWMSQWRQEGDDEqAVRGTLGRL-LFSQDDIKksVKVLSGGEKGRMLFGKLMMQKPNVLVMDEP 465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2683828925 175 TVGLDPE------QRLDFREllrdlGTdsCVLVStHLVEDVAVACTDVILINDGQLVH-QGTTDDLITHGG 238
Cdd:PRK15064 466 TNHMDMEsieslnMALEKYE-----GT--LIFVS-HDREFVSSLATRIIEITPDGVVDfSGTYEEYLRSQG 528
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
131-235 |
1.58e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.18 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 131 AIDRV--GLTAKADTRM----KTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLRDL--GTDSCVLVS 202
Cdd:PTZ00265 1336 AIDEFieSLPNKYDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADKTIITI 1415
|
90 100 110
....*....|....*....|....*....|....*..
gi 2683828925 203 THLVEDVAVACTDVILIN---DGQLVH-QGTTDDLIT 235
Cdd:PTZ00265 1416 AHRIASIKRSDKIVVFNNpdrTGSFVQaHGTHEELLS 1452
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
148-233 |
1.67e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 45.62 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 148 LSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLRDLGTDSC--VLVSTHLVEDVAVACTDVILINDGQLV 225
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
....*...
gi 2683828925 226 HQGTTDDL 233
Cdd:PRK10261 249 ETGSVEQI 256
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
43-179 |
2.19e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.27 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 43 HGLLGPNGAGKTTLMRALATVVKPAGGTLTLlghPVHNRadlhtlrrsLGYLPQ-HFGfYPRFTVREFV----EYLAWLK 117
Cdd:PRK15064 30 YGLIGANGCGKSTFMKILGGDLEPSAGNVSL---DPNER---------LGKLRQdQFA-FEEFTVLDTVimghTELWEVK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 118 H-------LPKATIPDAVQHA--------IDrvGLTAKAdtR------------------MKTLSGGMLRRAGIAQAIVN 164
Cdd:PRK15064 97 QerdriyaLPEMSEEDGMKVAdlevkfaeMD--GYTAEA--RagelllgvgipeeqhyglMSEVAPGWKLRVLLAQALFS 172
|
170
....*....|....*
gi 2683828925 165 NPAVLLLDEPTVGLD 179
Cdd:PRK15064 173 NPDILLLDEPTNNLD 187
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
145-194 |
2.70e-05 |
|
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: 43.47 E-value: 2.70e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2683828925 145 MKTLSGGMLRRAGIAQAIVNNP--AVLLLDEPTVGLDPEQRLDFRELLRDLG 194
Cdd:cd03238 85 LSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVIKGLI 136
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
34-237 |
3.45e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 44.97 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 34 LDLSLGTGVhGLLGPNGAGKTTLMRALatvvkpaggtltlLGHPVHNRADLHTLRRSLGYLPQHFGFYpRFTVREFVEYL 113
Cdd:PLN03232 638 LEIPVGSLV-AIVGGTGEGKTSLISAM-------------LGELSHAETSSVVIRGSVAYVPQVSWIF-NATVRENILFG 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 114 AWLK--HLPKATIPDAVQHAIDrvgLTAKAD-----TRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPE-QRLD 185
Cdd:PLN03232 703 SDFEseRYWRAIDVTALQHDLD---LLPGRDlteigERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHvAHQV 779
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2683828925 186 FRELLRD-LGTDSCVLVSTHLveDVAVACTDVILINDGQLVHQGTTDDLITHG 237
Cdd:PLN03232 780 FDSCMKDeLKGKTRVLVTNQL--HFLPLMDRIILVSEGMIKEEGTFAELSKSG 830
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
19-179 |
1.04e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 42.47 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 19 EGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALA--TVVKPAGGTLTLLG-------------------- 75
Cdd:PRK09580 5 KDLHVSVEDKAILRGLNLEVRPGeVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGkdllelspedragegifmaf 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 76 -HPVH-----NRADLHTlrrSLGYLPQHFGFYP--RFTVREFVEYLAWLKHLPkatiPDAVQHAIDrVGltakadtrmkt 147
Cdd:PRK09580 85 qYPVEipgvsNQFFLQT---ALNAVRSYRGQEPldRFDFQDLMEEKIALLKMP----EDLLTRSVN-VG----------- 145
|
170 180 190
....*....|....*....|....*....|..
gi 2683828925 148 LSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLD 179
Cdd:PRK09580 146 FSGGEKKRNDILQMAVLEPELCILDESDSGLD 177
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
147-223 |
1.58e-04 |
|
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: 41.69 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 147 TLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDP--EQRLdFRELLRDLGTDS--CVLVsTHLVEdVAVACTDVILINDG 222
Cdd:cd03250 127 NLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAhvGRHI-FENCILGLLLNNktRILV-THQLQ-LLPHADQIVVLDNG 203
|
.
gi 2683828925 223 Q 223
Cdd:cd03250 204 R 204
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
19-179 |
1.58e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 41.94 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 19 EGLRVRAGRHLAVDGLDLSLGTG-VHGLLGPNGAGKTTLMRALAtvvkpaggtltllGHPVHN--RADLHTLRRSLGYLP 95
Cdd:CHL00131 11 KNLHASVNENEILKGLNLSINKGeIHAIMGPNGSGKSTLSKVIA-------------GHPAYKilEGDILFKGESILDLE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 96 ----QHFGFY---------PRFTVREFVE--YLAWLKHLPKATIpDAVQ------HAIDRVGLTAKADTRM--KTLSGGM 152
Cdd:CHL00131 78 peerAHLGIFlafqypieiPGVSNADFLRlaYNSKRKFQGLPEL-DPLEfleiinEKLKLVGMDPSFLSRNvnEGFSGGE 156
|
170 180
....*....|....*....|....*..
gi 2683828925 153 LRRAGIAQAIVNNPAVLLLDEPTVGLD 179
Cdd:CHL00131 157 KKRNEILQMALLDSELAILDETDSGLD 183
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
148-220 |
1.97e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 42.71 E-value: 1.97e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2683828925 148 LSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLRDL--GTDSCVLVSTHLVEDVAVACTDVILIN 220
Cdd:PTZ00265 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkgNENRITIIIAHRLSTIRYANTIFVLSN 654
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
44-208 |
3.32e-04 |
|
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: 40.05 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 44 GLLGPNGAGKTTLMRALATVVKPAGGTltllghpvhnradlhtlrrslgylpqhfgfyprftvrefVEYLAwlkhlpkat 123
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELGPPGGG---------------------------------------VIYID--------- 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 124 iPDAVQHAIDRVGLTAKADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLRDL-------GTD 196
Cdd:smart00382 38 -GEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRlllllksEKN 116
|
170
....*....|..
gi 2683828925 197 SCVLVSTHLVED 208
Cdd:smart00382 117 LTVILTTNDEKD 128
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
47-193 |
3.61e-04 |
|
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: 40.67 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 47 GPNGAGKTTLMRAL--ATVvkpagGTLTLLGHPVHNRADLHTLRRSLGYLpqhfgfYPRFTVREFVEYLAWLKhlpkati 124
Cdd:cd03240 29 GQNGAGKTTIIEALkyALT-----GELPPNSKGGAHDPKLIREGEVRAQV------KLAFENANGKKYTITRS------- 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2683828925 125 PDAVQHAI-DRVGLTAKADTRM-KTLSGG------MLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRldfRELLRDL 193
Cdd:cd03240 91 LAILENVIfCHQGESNWPLLDMrGRCSGGekvlasLIIRLALAETFGSNCGILALDEPTTNLDEENI---EESLAEI 164
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
34-204 |
6.75e-04 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 40.37 E-value: 6.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 34 LDLSLGTGVHGLLGPNGAGKTTLMRALA--------------------TVVKPAGGTLTLLGHPVH---NRADLHTLRRS 90
Cdd:COG3950 19 IDFDNPPRLTVLVGENGSGKTTLLEAIAlalsgllsrlddvkfrklliRNGEFGDSAKLILYYGTSrllLDGPLKKLERL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 91 LG-YLPQHFGFYPRFT----VREFVEYLAW----LKHLPKATIP---DAVQHAID---------RVGLTAKADTRMKT-- 147
Cdd:COG3950 99 KEeYFSRLDGYDSLLDedsnLREFLEWLREyledLENKLSDELDeklEAVREALNkllpdfkdiRIDRDPGRLVILDKng 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2683828925 148 -------LSGG----------MLRRAGIA----QAIVNNPAVLLLDEPTVGLDPE-QRLdFRELLRDLGTDSCVLVSTH 204
Cdd:COG3950 179 eelplnqLSDGersllalvgdLARRLAELnpalENPLEGEGIVLIDEIDLHLHPKwQRR-ILPDLRKIFPNIQFIVTTH 256
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
45-179 |
9.65e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.23 E-value: 9.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 45 LLGPNGAGKTTLMRALATVVKPAGGTL------TLLGHPVHNRADLHTLRRSLGYLPQHFGFYPRFTVRefveylawlKH 118
Cdd:PLN03073 540 MVGPNGIGKSTILKLISGELQPSSGTVfrsakvRMAVFSQHHVDGLDLSSNPLLYMMRCFPGVPEQKLR---------AH 610
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2683828925 119 LpkatipdavqhaiDRVGLTAK-ADTRMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLD 179
Cdd:PLN03073 611 L-------------GSFGVTGNlALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
148-204 |
1.00e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 39.68 E-value: 1.00e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2683828925 148 LSGGMLRRAGIAQAI---VNNPAVLLLDEPTVGLDPEQRLDFRELLRDLGTDSC-VLVSTH 204
Cdd:pfam13304 237 LSDGTKRLLALLAALlsaLPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAqLILTTH 297
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
35-238 |
1.11e-03 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 40.09 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 35 DLSLGTGVHG---LLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVHNRAdlH-TLRRSLGYLPQH-----FGFYPRFT 105
Cdd:PRK10790 359 NINLSVPSRGfvaLVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLS--HsVLRQGVAMVQQDpvvlaDTFLANVT 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 106 V-REFVEYLAWlkhlpkaTIPDAVQHAIDRVGLTAKADTRM----KTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDP 180
Cdd:PRK10790 437 LgRDISEEQVW-------QALETVQLAELARSLPDGLYTPLgeqgNNLSVGQKQLLALARVLVQTPQILILDEATANIDS 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2683828925 181 EQRLDFRELLRDLGTDSCVLVSTHLVEDVAVActDVILI-NDGQLVHQGTTDDLITHGG 238
Cdd:PRK10790 510 GTEQAIQQALAAVREHTTLVVIAHRLSTIVEA--DTILVlHRGQAVEQGTHQQLLAAQG 566
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
45-190 |
1.63e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 39.57 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 45 LLGPNGAGKTTLMRALATVVKPAGGTLTLLGHPVH--NRA-----------DLHTLRRSLGylPQHFGFYPrftvrEFVE 111
Cdd:PRK10522 354 LIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTaeQPEdyrklfsavftDFHLFDQLLG--PEGKPANP-----ALVE 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 112 ylAWLKHLpkaTIPDAVQHAIDRVgltakADTRmktLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDF-RELL 190
Cdd:PRK10522 427 --KWLERL---KMAHKLELEDGRI-----SNLK---LSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFyQVLL 493
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
147-212 |
2.06e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.50 E-value: 2.06e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2683828925 147 TLSGG------MLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFREL----LRDLGTDSCVLVSTHLVEDVAVA 212
Cdd:PRK01156 801 SLSGGektavaFALRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIieysLKDSSDIPQVIMISHHRELLSVA 876
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
144-225 |
2.48e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.07 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 144 RMKTLSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDPEQRLDFRELLrdLGTDSCVLVSTHLVEDVAVACTDVILINDGQ 223
Cdd:PLN03073 341 ATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYL--LKWPKTFIVVSHAREFLNTVVTDILHLHGQK 418
|
..
gi 2683828925 224 LV 225
Cdd:PLN03073 419 LV 420
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
134-235 |
2.65e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 38.63 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 134 RVGLTAKADTrMKT----LSGGMLRRAGIAQAIVNNPAVLLLDEPTVGLDP-EQRLDFRELLR-DLGTDSCVLVSTHLVE 207
Cdd:PRK15093 142 RVGIKDHKDA-MRSfpyeLTEGECQKVMIAIALANQPRLLIADEPTNAMEPtTQAQIFRLLTRlNQNNNTTILLISHDLQ 220
|
90 100
....*....|....*....|....*...
gi 2683828925 208 DVAVACTDVILINDGQLVHQGTTDDLIT 235
Cdd:PRK15093 221 MLSQWADKINVLYCGQTVETAPSKELVT 248
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
146-236 |
2.72e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.85 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 146 KTLSGGMLRRAGIAQAI----VNnpaVL-LLDEPTVGLdpEQRlDFREL------LRDLGtdSCVLVsthlVE-Dvavac 213
Cdd:COG0178 484 GTLSGGEAQRIRLATQIgsglVG---VLyVLDEPSIGL--HQR-DNDRLietlkrLRDLG--NTVIV----VEhD----- 546
|
90 100 110
....*....|....*....|....*....|....*.
gi 2683828925 214 TDVILIND-------------GQLVHQGTTDDLITH 236
Cdd:COG0178 547 EDTIRAADyiidigpgagehgGEVVAQGTPEEILKN 582
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
32-60 |
4.23e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 37.48 E-value: 4.23e-03
10 20
....*....|....*....|....*....
gi 2683828925 32 DGLDLSLGTGVHGLLGPNGAGKTTLMRAL 60
Cdd:pfam13476 10 RDQTIDFSKGLTLITGPNGSGKTTILDAI 38
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
41-68 |
6.58e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 34.11 E-value: 6.58e-03
10 20
....*....|....*....|....*...
gi 2683828925 41 GVHGLLGPNGAGKTTLMRALATVVKPAG 68
Cdd:pfam13555 23 GNTLLTGPSGSGKSTLLDAIQTLLVPAK 50
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
42-61 |
6.69e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 37.37 E-value: 6.69e-03
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
147-234 |
7.26e-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: 37.69 E-value: 7.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2683828925 147 TLSGGMLRRAGIA---QAIVNNPAVLLLDEPTVGL---DPEQRLDFRELLRDLGtDSCVLVSTHLveDVaVACTDVIL-- 218
Cdd:TIGR00630 829 TLSGGEAQRIKLAkelSKRSTGRTLYILDEPTTGLhfdDIKKLLEVLQRLVDKG-NTVVVIEHNL--DV-IKTADYIIdl 904
|
90 100
....*....|....*....|.
gi 2683828925 219 -----INDGQLVHQGTTDDLI 234
Cdd:TIGR00630 905 gpeggDGGGTVVASGTPEEVA 925
|
|
| |
