|
Name |
Accession |
Description |
Interval |
E-value |
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
23-264 |
4.59e-127 |
|
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: 360.45 E-value: 4.59e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 23 RKAVIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLDELR 102
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 103 SDIGFLFQGSALYDSMTVRENLEFPLRRHKEKlgTPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILK 182
Cdd:COG1127 82 RRIGMLFQGGALFDSLTVFENVAFPLREHTDL--SEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 183 PKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEGSYTELSQSTDPKVEA 262
Cdd:COG1127 160 PEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASDDPWVRQ 239
|
..
gi 1234390149 263 FF 264
Cdd:COG1127 240 FL 241
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
27-263 |
3.87e-107 |
|
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: 309.82 E-value: 3.87e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLDELRSDIG 106
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 107 FLFQGSALYDSMTVRENLEFPLRRHKEKlgTPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKII 186
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTRL--SEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1234390149 187 LYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEGSYTELSQSTDPKVEAF 263
Cdd:cd03261 159 LYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASDDPLVRQF 235
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
26-241 |
6.19e-70 |
|
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: 215.06 E-value: 6.19e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 26 VIRIRDVRKSF----GDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLDEL 101
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 102 RSDIGFLFQ--GSALYDSMTVRENLEFPLRRHKeKLGTPSDTTALVMEALENVGLGRTI-DLMPAELSGGMKRRIALART 178
Cdd:cd03257 81 RKEIQMVFQdpMSSLNPRMTIGEQIAEPLRIHG-KLSKKEARKEAVLLLLVGVGLPEEVlNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1234390149 179 LILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAG 222
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
24-241 |
2.31e-69 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 213.37 E-value: 2.31e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 24 KAVIRIRDVRKSFGDN----HVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLD 99
Cdd:COG1136 2 SPLLELRNLTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 100 ELRSD-IGFLFQGSALYDSMTVRENLEFPLRRHKEKlgtPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALART 178
Cdd:COG1136 82 RLRRRhIGFVFQFFNLLPELTALENVALPLLLAGVS---RKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1234390149 179 LILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARvIADRMVLLVDG 241
Cdd:COG1136 159 LVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAA-RADRVIRLRDG 220
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
26-241 |
7.03e-67 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 207.54 E-value: 7.03e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 26 VIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIaTLDRHTLDELRSDI 105
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINKLRRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 106 GFLFQGSALYDSMTVRENLEFPLRRHKEKlgTPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKI 185
Cdd:COG1126 80 GMVFQQFNLFPHLTVLENVTLAPIKVKKM--SKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1234390149 186 ILYDEPTSGLDPITAKEIIELMRNIQiKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:COG1126 158 MLFDEPTSALDPELVGEVLDVMRDLA-KEGMTMVVVTHEMGFAREVADRVVFMDGG 212
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
10-241 |
2.31e-66 |
|
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: 214.38 E-value: 2.31e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 10 HKDQEGVADRPLERKAVIRIRDVRKSF-----GDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIE 84
Cdd:COG1123 244 GAARGRAAPAAAAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSIL 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 85 VMGKEIATLDRHTLDELRSDIGFLFQG--SALYDSMTVRENLEFPLRRHKekLGTPSDTTALVMEALENVGLGRT-IDLM 161
Cdd:COG1123 324 FDGKDLTKLSRRSLRELRRRVQMVFQDpySSLNPRMTVGDIIAEPLRLHG--LLSRAERRERVAELLERVGLPPDlADRY 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 162 PAELSGGMKRRIALARTLILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:COG1123 402 PHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDG 481
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
27-241 |
2.39e-63 |
|
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: 197.75 E-value: 2.39e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIaTLDRHTLDELRSDIG 106
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TDDKKNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 107 FLFQGSALYDSMTVRENLEFPLRRHKEKlgTPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKII 186
Cdd:cd03262 80 MVFQQFNLFPHLTVLENITLAPIKVKGM--SKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1234390149 187 LYDEPTSGLDPITAKEIIELMRNIQiKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:cd03262 158 LFDEPTSALDPELVGEVLDVMKDLA-EEGMTMVVVTHEMGFAREVADRVIFMDDG 211
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
27-241 |
5.17e-63 |
|
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: 196.94 E-value: 5.17e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDN----HVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLDELR 102
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 103 SD-IGFLFQGSALYDSMTVRENLEFPLRRHKEKlgtPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLIL 181
Cdd:cd03255 81 RRhIGFVFQSFNLLPDLTALENVELPLLLAGVP---KKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 182 KPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARvIADRMVLLVDG 241
Cdd:cd03255 158 DPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDG 216
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
23-238 |
1.57e-61 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 194.54 E-value: 1.57e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 23 RKAVIRIRDVRKSF----GDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRhtl 98
Cdd:COG1116 4 AAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 99 delrsDIGFLFQGSALYDSMTVRENLEFPLRRHKEKlgtPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALART 178
Cdd:COG1116 81 -----DRGVVFQEPALLPWLTVLDNVALGLELRGVP---KAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 179 LILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLL 238
Cdd:COG1116 153 LANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
27-256 |
2.68e-60 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 190.66 E-value: 2.68e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRhtldELRSDIG 106
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPA----EVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 107 FLFQGSALYDSMTVRENLEF--PLRRHKEKlgtpsDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPK 184
Cdd:COG1131 77 YVPQEPALYPDLTVRENLRFfaRLYGLPRK-----EARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1234390149 185 IILYDEPTSGLDPITAKEIIELMRNIQiKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEGSYTELSQST 256
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELA-AEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
27-238 |
1.64e-59 |
|
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: 188.06 E-value: 1.64e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDN----HVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIAtldrhtldELR 102
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT--------GPG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 103 SDIGFLFQGSALYDSMTVRENLEFPLRRHKEKlgtPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILK 182
Cdd:cd03293 73 PDRGYVFQQDALLPWLTVLDNVALGLELQGVP---KAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVD 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1234390149 183 PKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLL 238
Cdd:cd03293 150 PDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
27-241 |
6.24e-59 |
|
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: 186.19 E-value: 6.24e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHtldelRSDIG 106
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE-----RRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 107 FLFQGSALYDSMTVRENLEFPLRRHKEKLGtpsDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKII 186
Cdd:cd03259 76 MVFQDYALFPHLTVAENIAFGLKLRGVPKA---EIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1234390149 187 LYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:cd03259 153 LLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEG 207
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
26-252 |
8.53e-59 |
|
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: 186.63 E-value: 8.53e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 26 VIRIRDVRKSFGDN----HVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLDEL 101
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 102 RSDIGFLFQGSALYDSMTVRENLEFPLRRHKEKlgtPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLIL 181
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVP---KAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1234390149 182 KPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEGSYTEL 252
Cdd:cd03258 158 NPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
27-241 |
7.96e-58 |
|
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: 182.39 E-value: 7.96e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLdELRSDIG 106
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELP-PLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 107 FLFQGSALYDSMTVRENLEFPLrrhkeklgtpsdttalvmealenvglgrtidlmpaelSGGMKRRIALARTLILKPKII 186
Cdd:cd03229 80 MVFQDFALFPHLTVLENIALGL-------------------------------------SGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1234390149 187 LYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
25-241 |
6.30e-57 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 182.56 E-value: 6.30e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 25 AVIRIRDVRKSF-GDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLDELRS 103
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 104 DIGFLFQGSALYDSMTVRENL------EFPLRRHKEKLGTPSDTtALVMEALENVGLGRTIDLMPAELSGGMKRRIALAR 177
Cdd:COG3638 81 RIGMIFQQFNLVPRLSVLTNVlagrlgRTSTWRSLLGLFPPEDR-ERALEALERVGLADKAYQRADQLSGGQQQRVAIAR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1234390149 178 TLILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:COG3638 160 ALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDG 223
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
23-241 |
9.18e-57 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 185.30 E-value: 9.18e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 23 RKAVIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATL---DRhtld 99
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLppeKR---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 100 elrsDIGFLFQGSALYDSMTVRENLEFPLRRHKEKlgtPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTL 179
Cdd:COG3842 78 ----NVGMVFQDYALFPHLTVAENVAFGLRMRGVP---KAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1234390149 180 ILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:COG3842 151 APEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDG 212
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
27-241 |
2.53e-56 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 183.74 E-value: 2.53e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSF----GDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLDELR 102
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 103 SDIGFLFQGSALYDSMTVRENLEFPLRRhkekLGTP-SDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLIL 181
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLEI----AGVPkAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 182 KPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:COG1135 158 NPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENG 217
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
27-241 |
1.82e-55 |
|
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: 177.91 E-value: 1.82e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNH-VLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIatlDRHTLDELRSDI 105
Cdd:COG1122 1 IELENLSFSYPGGTpALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDI---TKKNLRELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 106 GFLFQgsalyD------SMTVRENLEFPLRRhkekLGTPSDT-TALVMEALENVGLGRTIDLMPAELSGGMKRRIALART 178
Cdd:COG1122 78 GLVFQ-----NpddqlfAPTVEEDVAFGPEN----LGLPREEiRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1234390149 179 LILKPKIILYDEPTSGLDPITAKEIIELMRNIQiKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKRLN-KEGKTVIIVTHDLDLVAELADRVIVLDDG 210
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
27-241 |
3.39e-54 |
|
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: 172.97 E-value: 3.39e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRhtldELRSDIG 106
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPE----EVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 107 FLFQGSALYDSMTVRENLefplrrhkeklgtpsdttalvmealenvglgrtidlmpaELSGGMKRRIALARTLILKPKII 186
Cdd:cd03230 77 YLPEEPSLYENLTVRENL---------------------------------------KLSGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1234390149 187 LYDEPTSGLDPITAKEIIELMRNIQiKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRELK-KEGKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
27-241 |
4.81e-54 |
|
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: 174.29 E-value: 4.81e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGL-----MLPDSGYIEVMGKEIATLDRHTLdEL 101
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDVL-EL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 102 RSDIGFLFQGSALYDsMTVRENLEFPLRRHKEKLGTPSDttALVMEALENVGLGRTID--LMPAELSGGMKRRIALARTL 179
Cdd:cd03260 80 RRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELD--ERVEEALRKAALWDEVKdrLHALGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1234390149 180 ILKPKIILYDEPTSGLDPITAKEIIELMRniQIKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIA--ELKKEYTIVIVTHNMQQAARVADRTAFLLNG 216
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
27-241 |
6.84e-54 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 173.46 E-value: 6.84e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHtldELRSDIG 106
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPP---EWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 107 FLFQGSALYDsMTVRENLEFPLRRHKEKlgtPSDTTALvmEALENVGLGRTI-DLMPAELSGGMKRRIALARTLILKPKI 185
Cdd:COG4619 78 YVPQEPALWG-GTVRDNLPFPFQLRERK---FDRERAL--ELLERLGLPPDIlDKPVERLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1234390149 186 ILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
26-241 |
1.03e-53 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 173.31 E-value: 1.03e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 26 VIRIRDVRKSFGDNH-VLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLDELRSD 104
Cdd:COG2884 1 MIRFENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 105 IGFLFQGSALYDSMTVRENLEFPLRRHKEKlgtPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPK 184
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPLRVTGKS---RKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1234390149 185 IILYDEPTSGLDPITAKEIIELMRNIQiKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEIN-RRGTTVLIATHDLELVDRMPKRVLELEDG 213
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
26-236 |
7.39e-53 |
|
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: 174.09 E-value: 7.39e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 26 VIRIRDVRKSF----GDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLP---DSGYIEVMGKEIATLDRHTL 98
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 99 DELR-SDIGFLFQG--SALYDSMTVRENLEFPLRRHKekLGTPSDTTALVMEALENVGL---GRTIDLMPAELSGGMKRR 172
Cdd:COG0444 81 RKIRgREIQMIFQDpmTSLNPVMTVGDQIAEPLRIHG--GLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1234390149 173 IALARTLILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMV 236
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVA 222
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
28-241 |
1.52e-52 |
|
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: 169.96 E-value: 1.52e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 28 RIRDVRKSFGDNH--VLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLdrhTLDELRSDI 105
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKL---SLKELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 106 GFLFQGSalyDSM----TVRENLEFPLrrhkEKLGTP-SDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLI 180
Cdd:cd03225 78 GLVFQNP---DDQffgpTVEEEVAFGL----ENLGLPeEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1234390149 181 LKPKIILYDEPTSGLDPITAKEIIELMRNIQiKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKKLK-AEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
27-241 |
2.01e-52 |
|
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: 170.44 E-value: 2.01e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDN-HVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLDELRSDI 105
Cdd:cd03256 1 IEVENLSKTYPNGkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 106 GFLFQGSALYDSMTVRENL------EFPLRRHKEKLGTPSDTtALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTL 179
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVlsgrlgRRSTWRSLFGLFPKEEK-QRALAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1234390149 180 ILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDG 221
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
25-241 |
1.17e-51 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 171.79 E-value: 1.17e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 25 AVIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATL---DRhtldel 101
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLppkDR------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 102 rsDIGFLFQGSALYDSMTVRENLEFPLRRHKEKlgtPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLIL 181
Cdd:COG3839 76 --NIAMVFQSYALYPHMTVYENIAFPLKLRKVP---KAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1234390149 182 KPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHD-VDcARVIADRMVLLVDG 241
Cdd:COG3839 151 EPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDqVE-AMTLADRIAVMNDG 210
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
30-265 |
3.59e-51 |
|
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: 168.21 E-value: 3.59e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 30 RDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLDELRS-DIGFL 108
Cdd:cd03294 28 EEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRkKISMV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 109 FQGSALYDSMTVRENLEFPLrrhkEKLGTPSDT-TALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKIIL 187
Cdd:cd03294 108 FQSFALLPHRTVLENVAFGL----EVQGVPRAErEERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1234390149 188 YDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEGSYTE-LSQSTDPKVEAFFK 265
Cdd:cd03294 184 MDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEiLTNPANDYVREFFR 262
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
27-241 |
4.19e-51 |
|
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: 167.29 E-value: 4.19e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFG----DNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHtldELR 102
Cdd:COG1124 2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRK---AFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 103 SDIGFLFQ--GSALYDSMTVRENLEFPLRRHKEKlgtpsDTTALVMEALENVGLGRTI-DLMPAELSGGMKRRIALARTL 179
Cdd:COG1124 79 RRVQMVFQdpYASLHPRHTVDRILAEPLRIHGLP-----DREERIAELLEQVGLPPSFlDRYPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1234390149 180 ILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNG 215
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
24-252 |
5.17e-51 |
|
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: 174.32 E-value: 5.17e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 24 KAVIRIRDVRKSF--GDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLmLPD----SGYIEVMGKEIATLdrhT 97
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGL-LPHggriSGEVLLDGRDLLEL---S 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 98 LDELRSDIGFLFQ--GSALyDSMTVRENLEFPLRRHKEklgTPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIAL 175
Cdd:COG1123 78 EALRGRRIGMVFQdpMTQL-NPVTVGDQIAEALENLGL---SRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1234390149 176 ARTLILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEGSYTEL 252
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
26-263 |
2.82e-50 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 166.09 E-value: 2.82e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 26 VIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLDELRSDI 105
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 106 GFLFQGSALYDSMTVRENLEFPLRRHKEKLGTPSDTTalVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKI 185
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHST--VMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1234390149 186 ILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEGSYTELSQSTDPKVEAF 263
Cdd:PRK11831 165 IMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPRVRQF 242
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
26-241 |
1.04e-48 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 160.57 E-value: 1.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 26 VIRIRDVRKSFGDN----HVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLDEL 101
Cdd:TIGR02982 1 VISIRNLNHYYGHGslrkQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 102 RSDIGFLFQGSALYDSMTVRENLEFPLRRHKEKlgTPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLIL 181
Cdd:TIGR02982 81 RRRIGYIFQAHNLLGFLTARQNVQMALELQPNL--SYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVH 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1234390149 182 KPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDvdcARV--IADRMVLLVDG 241
Cdd:TIGR02982 159 HPKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHD---NRIldVADRILQMEDG 217
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
27-241 |
2.03e-48 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 163.39 E-value: 2.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATlDRHTLDelRsDIG 106
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFT-NLPPRE--R-RVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 107 FLFQGSALYDSMTVRENLEFPLRRHKeklGTPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKII 186
Cdd:COG1118 79 FVFQHYALFPHMTVAENIAFGLRVRP---PSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1234390149 187 LYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:COG1118 156 LLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQG 210
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
25-241 |
3.44e-48 |
|
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: 159.52 E-value: 3.44e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 25 AVIRIRDVRKSFGDN----HVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLDE 100
Cdd:COG4181 7 PIIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 101 LRSD-IGFLFQGSALYDSMTVRENLEFPLrrhkEKLGTPsDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTL 179
Cdd:COG4181 87 LRARhVGFVFQSFQLLPTLTALENVMLPL----ELAGRR-DARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1234390149 180 ILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARViADRMVLLVDG 241
Cdd:COG4181 162 ATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAG 222
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
26-264 |
4.26e-48 |
|
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: 159.64 E-value: 4.26e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 26 VIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRhtldELRSDI 105
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR----EARRQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 106 GFLFQGSALYDSMTVRENLEFPLRRHKEKLgtpSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKI 185
Cdd:COG4555 77 GVLPDERGLYDRLTVRENIRYFAELYGLFD---EELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 186 ILYDEPTSGLDPITAKEIIELMRNIqIKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEGSYTELSQST-DPKVEAFF 264
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIgEENLEDAF 232
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
27-241 |
1.60e-47 |
|
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: 157.88 E-value: 1.60e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNHVLNgFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDrhtlDELRsDIG 106
Cdd:cd03299 1 LKVENLSKDWKEFKLKN-VSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLP----PEKR-DIS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 107 FLFQGSALYDSMTVRENLEFPLRRHKEKlgtPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKII 186
Cdd:cd03299 75 YVPQNYALFPHMTVYKNIAYGLKKRKVD---KKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKIL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1234390149 187 LYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:cd03299 152 LLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNG 206
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
26-241 |
2.45e-47 |
|
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: 157.46 E-value: 2.45e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 26 VIRIRDVRKSFGDNH-VLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLDELRSD 104
Cdd:TIGR02315 1 MLEVENLSKVYPNGKqALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 105 IGFLFQGSALYDSMTVRENLEFP-LRRH---KEKLGT-PSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTL 179
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHGrLGYKptwRSLLGRfSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1234390149 180 ILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAG 222
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
27-252 |
4.65e-47 |
|
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: 156.13 E-value: 4.65e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGD--NHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATldrhTLDELRSD 104
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT----DRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 105 IGFLFQGSALYDSMTVRENLEFPLRRHkeklGTPSDTTALVMEA-LENVGLGRTIDLMPAELSGGMKRRIALARTLILKP 183
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLRFYARLK----GLPKSEIKEEVELlLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1234390149 184 KIILYDEPTSGLDPITAKEIIELMRniQIKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEGSYTEL 252
Cdd:cd03263 153 SVLLLDEPTSGLDPASRRAIWDLIL--EVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
20-241 |
1.01e-46 |
|
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: 162.93 E-value: 1.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 20 PLERKAVIRIRDVRKSF-----------GDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLmLPDSGYIEVMGK 88
Cdd:COG4172 269 PPDAPPLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 89 EIATLDRHTLDELRSDIGFLFQG--SALYDSMTVRENLEFPLRRHKEKLgTPSDTTALVMEALENVGL-GRTIDLMPAEL 165
Cdd:COG4172 348 DLDGLSRRALRPLRRRMQVVFQDpfGSLSPRMTVGQIIAEGLRVHGPGL-SAAERRARVAEALEEVGLdPAARHRYPHEF 426
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1234390149 166 SGGMKRRIALARTLILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:COG4172 427 SGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDG 502
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
27-248 |
1.82e-46 |
|
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: 156.05 E-value: 1.82e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNH--VLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGkeIATLDRHTLDELRSD 104
Cdd:TIGR04520 1 IEVENVSFSYPESEkpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENLWEIRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 105 IGFLFQ-------GSalydsmTVRENLEFPLrrhkEKLGTPSDTT-ALVMEALENVGLGRTIDLMPAELSGGMKRRIALA 176
Cdd:TIGR04520 79 VGMVFQnpdnqfvGA------TVEDDVAFGL----ENLGVPREEMrKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1234390149 177 RTLILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCArVIADRMVLLVDGINYAEGS 248
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGT 219
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
26-237 |
2.47e-46 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 154.43 E-value: 2.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 26 VIRIRDVRKSFGDN----HVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLDEL 101
Cdd:TIGR02211 1 LLKCENLGKRYQEGkldtRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 102 RS-DIGFLFQGSALYDSMTVRENLEFPLRRHKEKlgtPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLI 180
Cdd:TIGR02211 81 RNkKLGFIYQFHHLLPDFTALENVAMPLLIGKKS---VKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1234390149 181 LKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVL 237
Cdd:TIGR02211 158 NQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEM 214
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
26-241 |
3.58e-46 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 157.66 E-value: 3.58e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 26 VIRIRDVRKSFGDN----HVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLDEL 101
Cdd:PRK11153 1 MIELKNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 102 RSDIGFLFQGSALYDSMTVRENLEFPLrrhkEKLGTP-SDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLI 180
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVALPL----ELAGTPkAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1234390149 181 LKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:PRK11153 157 SNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAG 217
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
23-242 |
4.49e-46 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 154.96 E-value: 4.49e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 23 RKAVIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIAT---------- 92
Cdd:COG4598 5 APPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLkpdrdgelvp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 93 LDRHTLDELRSDIGFLFQGSALYDSMTVRENL-EFPLRrhkeKLGTP-SDTTALVMEALENVGLGRTIDLMPAELSGGMK 170
Cdd:COG4598 85 ADRRQLQRIRTRLGMVFQSFNLWSHMTVLENViEAPVH----VLGRPkAEAIERAEALLAKVGLADKRDAYPAHLSGGQQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1234390149 171 RRIALARTLILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTsSLIITHDVDCARVIADRMVLLVDGI 242
Cdd:COG4598 161 QRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRT-MLVVTHEMGFARDVSSHVVFLHQGR 231
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
27-241 |
5.57e-46 |
|
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: 153.93 E-value: 5.57e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHtldelRSDIG 106
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH-----KRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 107 FLFQGSALYDSMTVRENLEFPLRRHKEKlgtPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKII 186
Cdd:cd03300 76 TVFQNYALFPHLTVFENIAFGLRLKKLP---KAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1234390149 187 LYDEPTSGLDPITAKEI-IELMRnIQIKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:cd03300 153 LLDEPLGALDLKLRKDMqLELKR-LQKELGITFVFVTHDQEEALTMSDRIAVMNKG 207
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
26-248 |
1.59e-45 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 153.28 E-value: 1.59e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 26 VIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHtldELRSDI 105
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRR---ELARRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 106 GFLFQGSALYDSMTVRENLEFPLRRHKEKLGTPSDT-TALVMEALENVGL----GRTIDlmpaELSGGMKRRIALARTLI 180
Cdd:COG1120 78 AYVPQEPPAPFGLTVRELVALGRYPHLGLFGRPSAEdREAVEEALERTGLehlaDRPVD----ELSGGERQRVLIARALA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1234390149 181 LKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEGS 248
Cdd:COG1120 154 QEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
13-254 |
1.68e-45 |
|
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: 160.32 E-value: 1.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 13 QEGVADRPLERKAVIRIRDVRKSFGDNH--VLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEI 90
Cdd:COG4987 320 TEPAEPAPAPGGPSLELEDVSFRYPGAGrpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 91 ATLDRhtlDELRSDIGFLFQGSALYDSmTVRENLefplrrhkeKLGTPSDTTALVMEALENVGLGRTIDLMP-------- 162
Cdd:COG4987 400 RDLDE---DDLRRRIAVVPQRPHLFDT-TLRENL---------RLARPDATDEELWAALERVGLGDWLAALPdgldtwlg 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 163 ---AELSGGMKRRIALARTLILKPKIILYDEPTSGLDPITAKEIIELMRNIQIkyNTSSLIITHDVDCARvIADRMVLLV 239
Cdd:COG4987 467 eggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLE-RMDRILVLE 543
|
250
....*....|....*
gi 1234390149 240 DGINYAEGSYTELSQ 254
Cdd:COG4987 544 DGRIVEQGTHEELLA 558
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
27-263 |
2.32e-45 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 152.26 E-value: 2.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHtldelRSDIG 106
Cdd:TIGR00968 1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHAR-----DRKIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 107 FLFQGSALYDSMTVRENLEFPL--RRHkeklgTPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPK 184
Cdd:TIGR00968 76 FVFQHYALFKHLTVRDNIAFGLeiRKH-----PKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 185 IILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEGSYTELSQS-TDPKVEAF 263
Cdd:TIGR00968 151 VLLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHpANPFVMSF 230
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
27-241 |
7.26e-45 |
|
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: 151.34 E-value: 7.26e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHtldelRSDIG 106
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ-----ERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 107 FLFQGSALYDSMTVRENLEFPLRRHKEKLGTPSDTT-ALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKI 185
Cdd:cd03296 78 FVFQHYALFRHMTVFDNVAFGLRVKPRSERPPEAEIrAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1234390149 186 ILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKG 213
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
27-254 |
1.05e-44 |
|
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: 160.00 E-value: 1.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNH--VLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDrhtLDELRSD 104
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID---PASLRRQ 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 105 IGFLFQGSALYdSMTVRENLefplrrhkeKLGTPSDTTALVMEALENVGLGRTIDLMP-----------AELSGGMKRRI 173
Cdd:COG2274 551 IGVVLQDVFLF-SGTIRENI---------TLGDPDATDEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRL 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 174 ALARTLILKPKIILYDEPTSGLDPITAKEIIELMRniQIKYNTSSLIITHDVDCARvIADRMVLLVDGINYAEGSYTELS 253
Cdd:COG2274 621 AIARALLRNPRILILDEATSALDAETEAIILENLR--RLLKGRTVIIIAHRLSTIR-LADRIIVLDKGRIVEDGTHEELL 697
|
.
gi 1234390149 254 Q 254
Cdd:COG2274 698 A 698
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
22-236 |
1.77e-44 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 152.58 E-value: 1.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 22 ERKAVIRIRDVRKSF---------GDNHV--LNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEI 90
Cdd:COG4608 3 MAEPLLEVRDLKKHFpvrgglfgrTVGVVkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 91 ATLDRHTLDELRSDIGFLFQGSalYDS----MTVRENLEFPLRRHKekLGTPSDTTALVMEALENVGLGRT-IDLMPAEL 165
Cdd:COG4608 83 TGLSGRELRPLRRRMQMVFQDP--YASlnprMTVGDIIAEPLRIHG--LASKAERRERVAELLELVGLRPEhADRYPHEF 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1234390149 166 SGGMKRRIALARTLILKPKIILYDEPTSGLD-PITAkEIIELMRNIQIKYNTSSLIITHDVDCARVIADR-MV 236
Cdd:COG4608 159 SGGQRQRIGIARALALNPKLIVCDEPVSALDvSIQA-QVLNLLEDLQDELGLTYLFISHDLSVVRHISDRvAV 230
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
27-260 |
2.63e-44 |
|
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: 149.51 E-value: 2.63e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLDELRsdIG 106
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLG--IG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 107 FLFQGSALYDSMTVRENLEFPLRRHKEK-------LGTPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTL 179
Cdd:cd03219 79 RTFQIPRLFPELTVLENVMVAAQARTGSglllaraRREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 180 ILKPKIILYDEPTSGLDPITAKEIIELMRNIQiKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEGSYTELsqSTDPK 259
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNPEETEELAELIRELR-ERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEV--RNNPR 235
|
.
gi 1234390149 260 V 260
Cdd:cd03219 236 V 236
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
42-242 |
3.65e-44 |
|
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: 148.60 E-value: 3.65e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 42 LNGFDMDL---YEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGK---------EIATLDRHtldelrsdIGFLF 109
Cdd:cd03297 10 LPDFTLKIdfdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsrkkiNLPPQQRK--------IGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 110 QGSALYDSMTVRENLEFPLRRHKeklgtPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKIILYD 189
Cdd:cd03297 82 QQYALFPHLNVRENLAFGLKRKR-----NREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1234390149 190 EPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDGI 242
Cdd:cd03297 157 EPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGR 209
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
26-265 |
3.70e-44 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 149.47 E-value: 3.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 26 VIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGkeIATLDRHTLD-ELRSD 104
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG--LKVNDPKVDErLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 105 IGFLFQGSALYDSMTVRENLEF-PLR-RHKEKlgtpSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILK 182
Cdd:PRK09493 79 AGMVFQQFYLFPHLTALENVMFgPLRvRGASK----EEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 183 PKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTsSLIITHDVDCARVIADRMVLLVDGINYAEGSYTEL-SQSTDPKVE 261
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMT-MVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLiKNPPSQRLQ 233
|
....
gi 1234390149 262 AFFK 265
Cdd:PRK09493 234 EFLQ 237
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
25-231 |
5.30e-44 |
|
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: 148.01 E-value: 5.30e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 25 AVIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDrhtlDELRSD 104
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR----EDYRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 105 IGFLFQGSALYDSMTVRENLEFPLRRHKeklgtPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPK 184
Cdd:COG4133 77 LAYLGHADGLKPELTVRENLRFWAALYG-----LRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1234390149 185 IILYDEPTSGLDPITAKEIIELMRNiQIKYNTSSLIITHD---VDCARVI 231
Cdd:COG4133 152 LWLLDEPFTALDAAGVALLAELIAA-HLARGGAVLLTTHQpleLAAARVL 200
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
13-255 |
1.02e-43 |
|
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: 155.69 E-value: 1.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 13 QEGVADRPLERKAVIRIRDVRKSFGDNH-VLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIA 91
Cdd:COG4988 323 PAGTAPLPAAGPPSIELEDVSFSYPGGRpALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLS 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 92 TLDrhtLDELRSDIGFLFQGSALYdSMTVRENLefplrrhkeKLGTPSDTTALVMEALENVGLGRTIDLMP--------- 162
Cdd:COG4988 403 DLD---PASWRRQIAWVPQNPYLF-AGTIRENL---------RLGRPDASDEELEAALEAAGLDEFVAALPdgldtplge 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 163 --AELSGGMKRRIALARTLILKPKIILYDEPTSGLDPITAKEIIELMRniQIKYNTSSLIITHDVDcARVIADRMVLLVD 240
Cdd:COG4988 470 ggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALR--RLAKGRTVILITHRLA-LLAQADRILVLDD 546
|
250
....*....|....*
gi 1234390149 241 GINYAEGSYTELSQS 255
Cdd:COG4988 547 GRIVEQGTHEELLAK 561
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
27-242 |
1.15e-43 |
|
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: 147.40 E-value: 1.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATL---DRhtldelrs 103
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLppkDR-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 104 DIGFLFQGSALYDSMTVRENLEFPLRRHKEKlgtPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKP 183
Cdd:cd03301 73 DIAMVFQNYALYPHMTVYDNIAFGLKLRKVP---KDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1234390149 184 KIILYDEPTSGLDpitAKEIIEL---MRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDGI 242
Cdd:cd03301 150 KVFLMDEPLSNLD---AKLRVQMraeLKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQ 208
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
25-248 |
2.29e-43 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 147.54 E-value: 2.29e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 25 AVIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIAtldrhtldELRSD 104
Cdd:COG1121 5 PAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR--------RARRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 105 IGFLFQGSALYDS--MTVRENLEFPLRRHKEKLGTPSDTT-ALVMEALENVGL----GRTIDlmpaELSGGMKRRIALAR 177
Cdd:COG1121 77 IGYVPQRAEVDWDfpITVRDVVLMGRYGRRGLFRRPSRADrEAVDEALERVGLedlaDRPIG----ELSGGQQQRVLLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1234390149 178 TLILKPKIILYDEPTSGLDPITAKEIIELMRNIQiKYNTSSLIITHDVDCARVIADRMVLLVDGInYAEGS 248
Cdd:COG1121 153 ALAQDPDLLLLDEPFAGVDAATEEALYELLRELR-REGKTILVVTHDLGAVREYFDRVLLLNRGL-VAHGP 221
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
28-241 |
2.90e-43 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 144.31 E-value: 2.90e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 28 RIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHtldELRSDIGF 107
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLE---ELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 108 LFQgsalydsmtvrenlefplrrhkeklgtpsdttalvmealenvglgrtidlmpaeLSGGMKRRIALARTLILKPKIIL 187
Cdd:cd00267 78 VPQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1234390149 188 YDEPTSGLDPITAKEIIELMRNIQIKyNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
27-241 |
6.34e-43 |
|
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: 146.29 E-value: 6.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNH-VLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDrhtLDELRSDI 105
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQD---PVELRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 106 GFLFQGSALYDSMTVREN-------LEFPLRRHKEKlgtpsdttalVMEALENVGLGRT--IDLMPAELSGGMKRRIALA 176
Cdd:cd03295 78 GYVIQQIGLFPHMTVEENialvpklLKWPKEKIRER----------ADELLALVGLDPAefADRYPHELSGGQQQRVGVA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1234390149 177 RTLILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:cd03295 148 RALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNG 212
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
27-241 |
1.19e-42 |
|
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: 144.86 E-value: 1.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNHV-LNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLDELRSDI 105
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 106 GFLFQGSALYDSMTVRENLEFPLRRHKEKlgtPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKI 185
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVP---PREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1234390149 186 ILYDEPTSGLDPITAKEIIELMRNIQiKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKIN-KAGTTVVVATHAKELVDTTRHRVIALERG 212
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
27-241 |
4.26e-42 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 147.15 E-value: 4.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATL---DRHtldelrs 103
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLharDRK------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 104 dIGFLFQGSALYDSMTVRENLEFPLR---RHKEklgtPSdTTAL---VMEALENVGLGRTIDLMPAELSGGMKRRIALAR 177
Cdd:PRK10851 76 -VGFVFQHYALFRHMTVFDNIAFGLTvlpRRER----PN-AAAIkakVTQLLEMVQLAHLADRYPAQLSGGQKQRVALAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1234390149 178 TLILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:PRK10851 150 ALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQG 213
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
27-263 |
4.45e-42 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 144.00 E-value: 4.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEI---ATLDRHTLDELRS 103
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 104 DIGFLFQGSALYDSMTVRENL-EFPLRrhkeKLG-TPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLIL 181
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENLiEAPCK----VLGlSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 182 KPKIILYDEPTSGLDP-ITAkEIIELMRNIQIKYNTsSLIITHDVDCARVIADRMVLLVDGINYAEGSYTELSQstdPKV 260
Cdd:COG4161 159 EPQVLLFDEPTAALDPeITA-QVVEIIRELSQTGIT-QVIVTHEVEFARKVASQVVYMEKGRIIEQGDASHFTQ---PQT 233
|
...
gi 1234390149 261 EAF 263
Cdd:COG4161 234 EAF 236
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
27-241 |
6.40e-42 |
|
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: 141.37 E-value: 6.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNH--VLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHtldELRSD 104
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLE---SLRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 105 IGFLFQGSALYdSMTVRENLefplrrhkeklgtpsdttalvmealenvglgrtidlmpaeLSGGMKRRIALARTLILKPK 184
Cdd:cd03228 78 IAYVPQDPFLF-SGTIRENI----------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1234390149 185 IILYDEPTSGLDPITAKEIIELMRNIQIkyNTSSLIITHDVDCARvIADRMVLLVDG 241
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIR-DADRIIVLDDG 170
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
25-266 |
7.53e-42 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 143.74 E-value: 7.53e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 25 AVIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATlDRH------TL 98
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDT-ARSlsqqkgLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 99 DELRSDIGFLFQGSALYDSMTVREN-LEFPLRRHKEKLGtpsDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALAR 177
Cdd:PRK11264 81 RQLRQHVGFVFQNFNLFPHRTVLENiIEGPVIVKGEPKE---EATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 178 TLILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTsSLIITHDVDCARVIADRMVLLVDGINYAEGSYTEL-SQST 256
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRT-MVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALfADPQ 236
|
250
....*....|
gi 1234390149 257 DPKVEAFFKK 266
Cdd:PRK11264 237 QPRTRQFLEK 246
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
27-263 |
1.77e-41 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 142.46 E-value: 1.77e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNHVLngFDMDLY--EGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEI---ATLDRHTLDEL 101
Cdd:PRK11124 3 IQLNGINCFYGAHQAL--FDITLDcpQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 102 RSDIGFLFQGSALYDSMTVRENL-EFPLRrhkeKLG-TPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTL 179
Cdd:PRK11124 81 RRNVGMVFQQYNLWPHLTVQQNLiEAPCR----VLGlSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 180 ILKPKIILYDEPTSGLDP-ITAkEIIELMRNIQiKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEGSYTELSQstdP 258
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDPeITA-QIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASCFTQ---P 231
|
....*
gi 1234390149 259 KVEAF 263
Cdd:PRK11124 232 QTEAF 236
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
24-241 |
1.96e-41 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 146.40 E-value: 1.96e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 24 KAVIRIRDVRKSFGDN----------------------HVL--NGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPD 79
Cdd:COG4175 1 MPKIEVRNLYKIFGKRperalklldqgkskdeilektgQTVgvNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 80 SGYIEVMGKEIATLDRHTLDELR-SDIGFLFQGSALYDSMTVRENLEFPLrrhkEKLGTPSDT-TALVMEALENVGLGRT 157
Cdd:COG4175 81 AGEVLIDGEDITKLSKKELRELRrKKMSMVFQHFALLPHRTVLENVAFGL----EIQGVPKAErRERAREALELVGLAGW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 158 IDLMPAELSGGMKRRIALARTLILKPKIILYDEPTSGLDPITAKEII-ELMRnIQIKYNTSSLIITHDVDCARVIADRMV 236
Cdd:COG4175 157 EDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQdELLE-LQAKLKKTIVFITHDLDEALRLGDRIA 235
|
....*
gi 1234390149 237 LLVDG 241
Cdd:COG4175 236 IMKDG 240
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
27-238 |
4.85e-41 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 144.41 E-value: 4.85e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDrhtlDELRsDIG 106
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLP----PQKR-DYG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 107 FLFQGSALYDSMTVRENLEFPLrrHKEKLGTpSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKII 186
Cdd:TIGR03265 80 IVFQSYALFPNLTVADNIAYGL--KNRGMGR-AEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1234390149 187 LYDEPTSGLDpitAKEIIEL---MRNIQIKYNTSSLIITHDVDCARVIADRMVLL 238
Cdd:TIGR03265 157 LLDEPLSALD---ARVREHLrteIRQLQRRLGVTTIMVTHDQEEALSMADRIVVM 208
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
34-266 |
7.30e-41 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes 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 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. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 144.22 E-value: 7.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 34 KSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLDEL-RSDIGFLFQGS 112
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELREVrRKKIGMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 113 ALYDSMTVRENLEFPLrrhkEKLGTPSDT-TALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKIILYDEP 191
Cdd:TIGR01186 81 ALFPHMTILQNTSLGP----ELLGWPEQErKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1234390149 192 TSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEGSYTE-LSQSTDPKVEAFFKK 266
Cdd:TIGR01186 157 FSALDPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEiLRNPANEYVEEFIGK 232
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
20-241 |
1.53e-40 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 143.55 E-value: 1.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 20 PLERKAVIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIAtldrHTLD 99
Cdd:PRK09452 8 PSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT----HVPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 100 ELRsDIGFLFQGSALYDSMTVRENLEFPLRRHKeklgTPSD-TTALVMEALENVGLGRTIDLMPAELSGGMKRRIALART 178
Cdd:PRK09452 84 ENR-HVNTVFQSYALFPHMTVFENVAFGLRMQK----TPAAeITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1234390149 179 LILKPKIILYDEPTSGLDPITAKEI-IELmRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDYKLRKQMqNEL-KALQRKLGITFVFVTHDQEEALTMSDRIVVMRDG 221
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
42-193 |
1.69e-40 |
|
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: 137.01 E-value: 1.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 42 LNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHtldELRSDIGFLFQGSALYDSMTVR 121
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERK---SLRKEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1234390149 122 ENLEFPLRRHKEKLGTPSDTTALVMEALENVGL-GRTIDLMPAELSGGMKRRIALARTLILKPKIILYDEPTS 193
Cdd:pfam00005 78 ENLRLGLLLKGLSKREKDARAEEALEKLGLGDLaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
20-248 |
5.86e-40 |
|
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: 139.51 E-value: 5.86e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 20 PLERKAvirirdvrksfgdnhvLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLD 99
Cdd:TIGR04521 15 PFEKKA----------------LDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 100 ELRSDIGFLFQGSA--LYdSMTVRENLEFPLRRhkekLG-TPSDTTALVMEALENVGLGRTI-DLMPAELSGGMKRRIAL 175
Cdd:TIGR04521 79 DLRKKVGLVFQFPEhqLF-EETVYKDIAFGPKN----LGlSEEEAEERVKEALELVGLDEEYlERSPFELSGGQMRRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1234390149 176 ARTLILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEGS 248
Cdd:TIGR04521 154 AGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGT 226
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
23-241 |
3.51e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 137.43 E-value: 3.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 23 RKAVIRIRDVRKSFGDNH--VLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIatlDRHTLDE 100
Cdd:PRK13632 4 KSVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI---SKENLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 101 LRSDIGFLFQ-------GSalydsmTVRENLEFPLrrhKEKLGTPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRI 173
Cdd:PRK13632 81 IRKKIGIIFQnpdnqfiGA------TVEDDIAFGL---ENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1234390149 174 ALARTLILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCArVIADRMVLLVDG 241
Cdd:PRK13632 152 AIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEG 218
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
27-241 |
4.05e-39 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 138.30 E-value: 4.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNHV-LNGFDMDLYEGENLVVMGKSGSGKSV---MIKCLVGlmlPDSGYIEVMGKEIATLDrhtLDELR 102
Cdd:COG1125 2 IEFENVTKRYPDGTVaVDDLSLTIPAGEFTVLVGPSGCGKTTtlrMINRLIE---PTSGRILIDGEDIRDLD---PVELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 103 SDIGFLFQGSALYDSMTVRENLEFPLRRhkekLGTPSDTT-ALVMEALENVGLGRTI--DLMPAELSGGMKRRIALARTL 179
Cdd:COG1125 76 RRIGYVIQQIGLFPHMTVAENIATVPRL----LGWDKERIrARVDELLELVGLDPEEyrDRYPHELSGGQQQRVGVARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1234390149 180 ILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:COG1125 152 AADPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREG 213
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
28-238 |
4.50e-39 |
|
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: 135.35 E-value: 4.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 28 RIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIAtldrhtldELRSDIGF 107
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE--------KERKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 108 LFQ-GSALYDS-MTVRENLEFPLRRHKEKLGTPSDTT-ALVMEALENVGLG----RTIDlmpaELSGGMKRRIALARTLI 180
Cdd:cd03235 73 VPQrRSIDRDFpISVRDVVLMGLYGHKGLFRRLSKADkAKVDEALERVGLSeladRQIG----ELSGGQQQRVLLARALV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1234390149 181 LKPKIILYDEPTSGLDPITAKEIIELMRNIQiKYNTSSLIITHDVDCARVIADRMVLL 238
Cdd:cd03235 149 QDPDLLLLDEPFAGVDPKTQEDIYELLRELR-REGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
27-252 |
2.23e-38 |
|
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: 133.65 E-value: 2.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIatldRHTLDELRSDIG 106
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV----VREPREVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 107 FLFQGSALYDSMTVRENLEFplrrHKEKLGTPSDT-TALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKI 185
Cdd:cd03265 77 IVFQDLSVDDELTGWENLYI----HARLYGVPGAErRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1234390149 186 ILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEGSYTEL 252
Cdd:cd03265 153 LFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
24-247 |
3.49e-38 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 135.14 E-value: 3.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 24 KAVIRIRDVRKSFGDN--HVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKeiaTLDRHTLDEL 101
Cdd:PRK13635 3 EEIIRVEHISFRYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEETVWDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 102 RSDIGFLFQ-------GSalydsmTVRENLEFPLrrhkEKLGTPSDT-TALVMEALENVGLGRTIDLMPAELSGGMKRRI 173
Cdd:PRK13635 80 RRQVGMVFQnpdnqfvGA------TVQDDVAFGL----ENIGVPREEmVERVDQALRQVGMEDFLNREPHRLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1234390149 174 ALARTLILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCArVIADRMVLLVDGINYAEG 247
Cdd:PRK13635 150 AIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEEG 222
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
27-241 |
3.62e-38 |
|
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: 132.73 E-value: 3.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIAtldrhTLDELRSDIG 106
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ-----KNIEALRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 107 FLFQGSALYDSMTVRENlefpLRRHKEKLGTPSdttALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKII 186
Cdd:cd03268 76 ALIEAPGFYPNLTAREN----LRLLARLLGIRK---KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1234390149 187 LYDEPTSGLDPITAKEIIELMRNIQiKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:cd03268 149 ILDEPTNGLDPDGIKELRELILSLR-DQGITVLISSHLLSEIQKVADRIGIINKG 202
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
29-241 |
4.22e-38 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 134.03 E-value: 4.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 29 IRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGyiEVMGkeiatlDRHTLDELRSDIGFL 108
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG--ELLA------GTAPLAEAREDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 109 FQGSALYDSMTVRENLefplrrhkeKLGTPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKIILY 188
Cdd:PRK11247 87 FQDARLLPWKKVIDNV---------GLGLKGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1234390149 189 DEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:PRK11247 158 DEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEG 210
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
42-241 |
4.42e-38 |
|
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: 133.36 E-value: 4.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 42 LNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIatldrhtlDELRSDIGFLFQGSALYDSMTVR 121
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI--------TEPGPDRMVVFQNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 122 ENLEFPLRRHKEKLGTPsDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKIILYDEPTSGLDPITAK 201
Cdd:TIGR01184 73 ENIALAVDRVLPDLSKS-ERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1234390149 202 EIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-224 |
2.96e-37 |
|
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: 137.49 E-value: 2.96e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 2 TDDPTTYKHKDQEGVADRPLErKAVIRIRDVRKSF-GDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDS 80
Cdd:TIGR02868 311 LDAAGPVAEGSAPAAGAVGLG-KPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 81 GYIEVMGKEIATLDRhtlDELRSDIGFLFQGSALYDSmTVRENLefplrrhkeKLGTPSDTTALVMEALENVGLGRTIDL 160
Cdd:TIGR02868 390 GEVTLDGVPVSSLDQ---DEVRRRVSVCAQDAHLFDT-TVRENL---------RLARPDATDEELWAALERVGLADWLRA 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1234390149 161 MP-----------AELSGGMKRRIALARTLILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTssLIITHD 224
Cdd:TIGR02868 457 LPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTV--VLITHH 529
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
28-247 |
8.26e-37 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 128.32 E-value: 8.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 28 RIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHtldELRSDIGF 107
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPK---ELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 108 LFQgsalydsmtvrenlefplrrhkeklgtpsdttalvmeALENVGL----GRTIDlmpaELSGGMKRRIALARTLILKP 183
Cdd:cd03214 78 VPQ-------------------------------------ALELLGLahlaDRPFN----ELSGGERQRVLLARALAQEP 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1234390149 184 KIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEG 247
Cdd:cd03214 117 PILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
27-259 |
2.76e-36 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 128.72 E-value: 2.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNHvLNgFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHtldelRSDIG 106
Cdd:COG3840 2 LRLDDLTYRYGDFP-LR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA-----ERPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 107 FLFQGSALYDSMTVRENLEFPLRRhKEKLgTPSDTTAlVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKII 186
Cdd:COG3840 75 MLFQENNLFPHLTVAQNIGLGLRP-GLKL-TAEQRAQ-VEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPIL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1234390149 187 LYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEGSYTELSQSTDPK 259
Cdd:COG3840 152 LLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPP 224
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
27-252 |
4.93e-36 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 127.55 E-value: 4.93e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLdeLRSDIG 106
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHER--ARAGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 107 FLFQGSALYDSMTVRENLE---FPLRRHKEKlgtpsdttalvmEALENVglgrtIDLMPA----------ELSGGMKRRI 173
Cdd:cd03224 79 YVPEGRRIFPELTVEENLLlgaYARRRAKRK------------ARLERV-----YELFPRlkerrkqlagTLSGGEQQML 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1234390149 174 ALARTLILKPKIILYDEPTSGLDPITAKEIIELMRNIQiKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEGSYTEL 252
Cdd:cd03224 142 AIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELR-DEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
25-238 |
4.95e-36 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 128.83 E-value: 4.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 25 AVIRIRDVRKSFGDN----HVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDrhtlde 100
Cdd:COG4525 2 SMLTVRHVSVRYPGGgqpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 101 lrSDIGFLFQGSALYDSMTVRENLEFPLRRHKEKlgtPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLI 180
Cdd:COG4525 76 --ADRGVVFQKDALLPWLNVLDNVAFGLRLRGVP---KAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1234390149 181 LKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLL 238
Cdd:COG4525 151 ADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
27-252 |
7.16e-36 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 134.14 E-value: 7.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVrkSF---GDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDrhtLDELRS 103
Cdd:COG1132 340 IEFENV--SFsypGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLT---LESLRR 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 104 DIGFLFQGSALYdSMTVRENLefplrrhkeKLGTPSDTTALVMEALENVGLGRTIDLMP-----------AELSGGMKRR 172
Cdd:COG1132 415 QIGVVPQDTFLF-SGTIRENI---------RYGRPDATDEEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQR 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 173 IALARTLILKPKIILYDEPTSGLDPITAKEIIE----LMRniqikyNTSSLIITHDVDCARvIADRMVLLVDGINYAEGS 248
Cdd:COG1132 485 IAIARALLKDPPILILDEATSALDTETEALIQEalerLMK------GRTTIVIAHRLSTIR-NADRILVLDDGRIVEQGT 557
|
....
gi 1234390149 249 YTEL 252
Cdd:COG1132 558 HEEL 561
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
27-241 |
2.26e-35 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 132.52 E-value: 2.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLmLPDSGYIEVMGKEIATLDRHTLDELRSDIG 106
Cdd:PRK15134 287 IRKGILKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRL-INSQGEIWFDGQPLHNLNRRQLLPVRHRIQ 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 107 FLFQ--GSALYDSMTVRENLEFPLRRHKEKLgTPSDTTALVMEALENVGLG-RTIDLMPAELSGGMKRRIALARTLILKP 183
Cdd:PRK15134 366 VVFQdpNSSLNPRLNVLQIIEEGLRVHQPTL-SAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKP 444
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1234390149 184 KIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:PRK15134 445 SLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQG 502
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
24-241 |
2.32e-35 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 127.08 E-value: 2.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 24 KAVIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGL--MLPD---SGYIEVMGKEIatLDRHT- 97
Cdd:COG1117 9 EPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGarvEGEILLDGEDI--YDPDVd 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 98 LDELRSDIGFLFQGSALYdSMTVRENLEFPLRRHKEKlgTPSDTTALVMEALENVGL-----GRtIDLMPAELSGGMKRR 172
Cdd:COG1117 87 VVELRRRVGMVFQKPNPF-PKSIYDNVAYGLRLHGIK--SKSELDEIVEESLRKAALwdevkDR-LKKSALGLSGGQQQR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1234390149 173 IALARTLILKPKIILYDEPTSGLDPITAKEIIELMRniQIKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:COG1117 163 LCIARALAVEPEVLLMDEPTSALDPISTAKIEELIL--ELKKDYTIVIVTHNMQQAARVSDYTAFFYLG 229
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
41-241 |
2.46e-35 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 127.11 E-value: 2.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 41 VLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLDELRSDIGFLFQGS--ALYDSM 118
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRDIQMVFQDSisAVNPRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 119 TVRENLEFPLRrHKEKLgTPSDTTALVMEALENVGLGRTI-DLMPAELSGGMKRRIALARTLILKPKIILYDEPTSGLDP 197
Cdd:PRK10419 107 TVREIIREPLR-HLLSL-DKAERLARASEMLRAVDLDDSVlDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1234390149 198 ITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:PRK10419 185 VLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNG 228
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
26-241 |
3.30e-35 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 126.05 E-value: 3.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 26 VIRIRDVRKSFGDNH----VLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLDEL 101
Cdd:PRK10584 6 IVEVHHLKKSVGQGEhelsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 102 RS-DIGFLFQGSALYDSMTVRENLEFP--LRRHKEKlgtpsDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALART 178
Cdd:PRK10584 86 RAkHVGFVFQSFMLIPTLNALENVELPalLRGESSR-----QSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1234390149 179 LILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCArVIADRMVLLVDG 241
Cdd:PRK10584 161 FNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLA-ARCDRRLRLVNG 222
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
31-257 |
3.30e-35 |
|
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: 129.07 E-value: 3.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 31 DVRKSFGDnhvlngFDMD----LYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKeiaTL--DRHTLD---EL 101
Cdd:COG4148 6 DFRLRRGG------FTLDvdftLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGE---VLqdSARGIFlppHR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 102 RSdIGFLFQGSALYDSMTVRENLEFPLRRhkeklGTPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLIL 181
Cdd:COG4148 77 RR-IGYVFQEARLFPHLSVRGNLLYGRKR-----APRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLS 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1234390149 182 KPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEGSYTELSQSTD 257
Cdd:COG4148 151 SPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPD 226
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
43-259 |
4.77e-35 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 128.29 E-value: 4.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 43 NGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLDELRSDIGFLFQG--SALYDSMTV 120
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQDplASLNPRMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 121 RENLEFPLRRHKEKLgTPSDTTALVMEALENVGL-GRTIDLMPAELSGGMKRRIALARTLILKPKIILYDEPTSGLDPIT 199
Cdd:PRK15079 118 GEIIAEPLRTYHPKL-SRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSI 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1234390149 200 AKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDGiNYAE-GSYTELSQstDPK 259
Cdd:PRK15079 197 QAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLG-HAVElGTYDEVYH--NPL 254
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
27-265 |
6.10e-35 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 125.85 E-value: 6.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATL----------DRH 96
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvaDKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 97 TLDELRSDIGFLFQGSALYDSMTVREN-LEFPLrrhkEKLG-TPSDTTALVMEALENVGL-GRTIDLMPAELSGGMKRRI 173
Cdd:PRK10619 86 QLRLLRTRLTMVFQHFNLWSHMTVLENvMEAPI----QVLGlSKQEARERAVKYLAKVGIdERAQGKYPVHLSGGQQQRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 174 ALARTLILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTsSLIITHDVDCARVIADRMVLLVDGINYAEGSYTEL- 252
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKT-MVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLf 240
|
250
....*....|...
gi 1234390149 253 SQSTDPKVEAFFK 265
Cdd:PRK10619 241 GNPQSPRLQQFLK 253
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
29-241 |
1.47e-34 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 127.14 E-value: 1.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 29 IRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIAtldrHTLDELRsDIGFL 108
Cdd:PRK11432 9 LKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT----HRSIQQR-DICMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 109 FQGSALYDSMTVRENLEFPLRrhkeKLGTPSDTTA-LVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKIIL 187
Cdd:PRK11432 84 FQSYALFPHMSLGENVGYGLK----MLGVPKEERKqRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1234390149 188 YDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:PRK11432 160 FDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKG 213
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
27-241 |
1.59e-34 |
|
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: 123.54 E-value: 1.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHtldelrsDIG 106
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARN-------RIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 107 FLFQGSALYDSMTVRENLEFPLRRHKEKlgtPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKII 186
Cdd:cd03269 74 YLPEERGLYPKMKVIDQLVYLAQLKGLK---KEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1234390149 187 LYDEPTSGLDPITAKEIIELMRNIQIKyNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:cd03269 151 ILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
26-252 |
1.94e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 125.19 E-value: 1.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 26 VIRIRDVRKSFGDN-HVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIaTLDRHTLDELRSD 104
Cdd:PRK13639 1 ILETRDLKYSYPDGtEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 105 IGFLFQGSAlyDSM---TVRENLEF-PLrrhkeKLGTPSDTTA-LVMEALENVGLGRTIDLMPAELSGGMKRRIALARTL 179
Cdd:PRK13639 80 VGIVFQNPD--DQLfapTVEEDVAFgPL-----NLGLSKEEVEkRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGIL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1234390149 180 ILKPKIILYDEPTSGLDPITAKEIIELMRNIQiKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEGSYTEL 252
Cdd:PRK13639 153 AMKPEIIVLDEPTSGLDPMGASQIMKLLYDLN-KEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
34-252 |
1.97e-34 |
|
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: 125.97 E-value: 1.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 34 KSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATldrhTLDELRSDIGFLFQGSA 113
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVR----EPRKVRRSIGIVPQYAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 114 LYDSMTVRENLEFplrrHKEKLGTPSDTT-ALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKIILYDEPT 192
Cdd:TIGR01188 77 VDEDLTGRENLEM----MGRLYGLPKDEAeERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPT 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 193 SGLDPITAKEIIELMRNIQiKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEGSYTEL 252
Cdd:TIGR01188 153 TGLDPRTRRAIWDYIRALK-EEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
27-241 |
3.73e-34 |
|
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: 122.69 E-value: 3.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNHVLNGFDMDLYEGEnLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIatldRHTLDELRSDIG 106
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV----LKQPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 107 FLFQGSALYDSMTVRENLEFPLRRHKEklgTPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKII 186
Cdd:cd03264 76 YLPQEFGVYPNFTVREFLDYIAWLKGI---PSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1234390149 187 LYDEPTSGLDPitaKEIIELmRNI--QIKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:cd03264 153 IVDEPTAGLDP---EERIRF-RNLlsELGEDRIVILSTHIVEDVESLCNQVAVLNKG 205
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
37-228 |
3.98e-34 |
|
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: 121.76 E-value: 3.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 37 GDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIAtLDRHTLDELRSDIGFLFQG--SAL 114
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLD-YSRKGLLERRQRVGLVFQDpdDQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 115 YdSMTVRENLEFPLRrhkeKLGTPSD-TTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKIILYDEPTS 193
Cdd:TIGR01166 82 F-AADVDQDVAFGPL----NLGLSEAeVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTA 156
|
170 180 190
....*....|....*....|....*....|....*
gi 1234390149 194 GLDPITAKEIIELMRNIQIKYNTsSLIITHDVDCA 228
Cdd:TIGR01166 157 GLDPAGREQMLAILRRLRAEGMT-VVISTHDVDLA 190
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
24-241 |
4.16e-34 |
|
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: 123.79 E-value: 4.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 24 KAVIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLDE--- 100
Cdd:TIGR02323 1 KPLLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLSEaer 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 101 ---LRSDIGFLFQGSALYDSMTVR------ENLEFPLRRHKEKLgtpsdtTALVMEALENVGLGRT-IDLMPAELSGGMK 170
Cdd:TIGR02323 81 rrlMRTEWGFVHQNPRDGLRMRVSaganigERLMAIGARHYGNI------RATAQDWLEEVEIDPTrIDDLPRAFSGGMQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1234390149 171 RRIALARTLILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:TIGR02323 155 QRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQG 225
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-247 |
2.21e-33 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 123.79 E-value: 2.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 4 DPTTYKHKDQ---EGVADRPLERKAV-IRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPD 79
Cdd:PRK13536 15 ELSPIERKHQgisEAKASIPGSMSTVaIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 80 SGYIEVMGKEIATLDRHTldelRSDIGFLFQGSALYDSMTVRENLEFPLRRHKEKlgtPSDTTALVMEALENVGLGRTID 159
Cdd:PRK13536 95 AGKITVLGVPVPARARLA----RARIGVVPQFDNLDLEFTVRENLLVFGRYFGMS---TREIEAVIPSLLEFARLESKAD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 160 LMPAELSGGMKRRIALARTLILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTsSLIITHDVDCARVIADRMVLLV 239
Cdd:PRK13536 168 ARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKT-ILLTTHFMEEAERLCDRLCVLE 246
|
....*...
gi 1234390149 240 DGINYAEG 247
Cdd:PRK13536 247 AGRKIAEG 254
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
16-241 |
2.81e-33 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 121.57 E-value: 2.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 16 VADRPLerkavIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDR 95
Cdd:PRK11701 1 MMDQPL-----LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 96 HTLDE------LRSDIGFLFQGSALYDSMTVR------ENLEFPLRRHkekLGTPSDTTALVMEALEnVGLGRtIDLMPA 163
Cdd:PRK11701 76 YALSEaerrrlLRTEWGFVHQHPRDGLRMQVSaggnigERLMAVGARH---YGDIRATAGDWLERVE-IDAAR-IDDLPT 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1234390149 164 ELSGGMKRRIALARTLILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:PRK11701 151 TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQG 228
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
24-241 |
3.67e-33 |
|
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: 126.34 E-value: 3.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 24 KAVIRIRDVRKSFGDN----HVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLmLPD-----SGYIEVMGKEIATLD 94
Cdd:COG4172 4 MPLLSVEDLSVAFGQGggtvEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRL-LPDpaahpSGSILFDGQDLLGLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 95 RHTLDELR-SDIGFLFQ--GSALYDSMTVRENLEFPLRRHKeKLgTPSDTTALVMEALENVGL---GRTIDLMPAELSGG 168
Cdd:COG4172 83 ERELRRIRgNRIAMIFQepMTSLNPLHTIGKQIAEVLRLHR-GL-SGAAARARALELLERVGIpdpERRLDAYPHQLSGG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1234390149 169 MKRRIALARTLILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:COG4172 161 QRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQG 233
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
28-241 |
4.56e-33 |
|
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: 119.67 E-value: 4.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 28 RIRDVRKSFGDNH-VLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRhtldelRSDIG 106
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKER------RKSIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 107 FLFQ--GSALYdSMTVRENLEFPLRRhkeklgtPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPK 184
Cdd:cd03226 75 YVMQdvDYQLF-TDSVREELLLGLKE-------LDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1234390149 185 IILYDEPTSGLDPITAKEIIELMRNIQiKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELIRELA-AQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
24-248 |
6.20e-33 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 120.89 E-value: 6.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 24 KAVIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDS---GYIEVMGKEIATLDRHTLD- 99
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELLGRTVQREGRLARDi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 100 -ELRSDIGFLFQGSALYDSMTVRENL------EFPLRRHKEKLGTPSDTTAlVMEALENVGLGRTIDLMPAELSGGMKRR 172
Cdd:PRK09984 82 rKSRANTGYIFQQFNLVNRLSVLENVligalgSTPFWRTCFSWFTREQKQR-ALQALTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1234390149 173 IALARTLILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEGS 248
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
27-247 |
7.65e-33 |
|
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: 119.39 E-value: 7.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDN----HVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRhtldELR 102
Cdd:cd03266 2 ITADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPA----EAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 103 SDIGFLFQGSALYDSMTVRENLEFPLRRHKEKlgtPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILK 182
Cdd:cd03266 78 RRLGFVSDSTGLYDRLTARENLEYFAGLYGLK---GDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1234390149 183 PKIILYDEPTSGLDPITAKEIIELMRNiQIKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEG 247
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQ-LRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
25-255 |
1.05e-32 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 121.45 E-value: 1.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 25 AVIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTldelRSD 104
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA----RQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 105 IGFLFQGSALYDSMTVRENLEFPLRRhkekLGTPSDTT-ALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKP 183
Cdd:PRK13537 82 VGVVPQFDNLDPDFTVRENLLVFGRY----FGLSAAAArALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1234390149 184 KIILYDEPTSGLDPITAKEIIELMRNIQIKYNTsSLIITHDVDCARVIADRMVLLVDGINYAEGSYTELSQS 255
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLRSLLARGKT-ILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
25-238 |
1.28e-32 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 122.26 E-value: 1.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 25 AVIRIRDVRKSF-GDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATL---DRhtlde 100
Cdd:PRK11650 2 AGLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELepaDR----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 101 lrsDIGFLFQGSALYDSMTVRENLEFPLR-RhkeklGTPSDT-TALVMEALENVGLGRTIDLMPAELSGGMKRRIALART 178
Cdd:PRK11650 77 ---DIAMVFQNYALYPHMSVRENMAYGLKiR-----GMPKAEiEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1234390149 179 LILKPKIILYDEPTSGLDpitAK-------EIIELMRNIqikyNTSSLIITHDVDCARVIADRMVLL 238
Cdd:PRK11650 149 IVREPAVFLFDEPLSNLD---AKlrvqmrlEIQRLHRRL----KTTSLYVTHDQVEAMTLADRVVVM 208
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
59-257 |
1.47e-32 |
|
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: 122.14 E-value: 1.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 59 GKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIA-TLDRHTLDELRSDIGFLFQGSALYDSMTVRENLEFPLRRhkeklGT 137
Cdd:TIGR02142 30 GRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFdSRKGIFLPPEKRRIGYVFQEARLFPHLSVRGNLRYGMKR-----AR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 138 PSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTS 217
Cdd:TIGR02142 105 PSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEFGIP 184
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1234390149 218 SLIITHDVDCARVIADRMVLLVDGINYAEGSYTELSQSTD 257
Cdd:TIGR02142 185 ILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPD 224
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
15-238 |
4.35e-32 |
|
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: 123.17 E-value: 4.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 15 GVADRPLERKAVIRIRDVRKSFGD-NHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATL 93
Cdd:TIGR02857 310 GKAPVTAAPASSLEFSGVSVAYPGrRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADA 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 94 DRHTLdelRSDIGFLFQGSALYDSmTVRENLefplrrhkeKLGTPSDTTALVMEALENVGLGRTIDLMP----------- 162
Cdd:TIGR02857 390 DADSW---RDQIAWVPQHPFLFAG-TIAENI---------RLARPDASDAEIREALERAGLDEFVAALPqgldtpigegg 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1234390149 163 AELSGGMKRRIALARTLILKPKIILYDEPTSGLDPITAKEIIELMRniQIKYNTSSLIITHDVDCARViADRMVLL 238
Cdd:TIGR02857 457 AGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALR--ALAQGRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
28-226 |
4.80e-32 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 117.20 E-value: 4.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 28 RIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPD---SGYIEVMGKEIATL---DRHtldel 101
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALpaeQRR----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 102 rsdIGFLFQGSALYDSMTVRENLEFplrrhkeklGTPSDTT-----ALVMEALENVGLGRTIDLMPAELSGGMKRRIALA 176
Cdd:COG4136 78 ---IGILFQDDLLFPHLSVGENLAF---------ALPPTIGraqrrARVEQALEEAGLAGFADRDPATLSGGQRARVALL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1234390149 177 RTLILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVD 226
Cdd:COG4136 146 RALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEE 195
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
27-241 |
7.53e-32 |
|
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: 115.22 E-value: 7.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHtlDELRSDIG 106
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPR--DARRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 107 FLFQgsalydsmtvrenlefplrrhkeklgtpsdttalvmealenvglgrtidlmpaeLSGGMKRRIALARTLILKPKII 186
Cdd:cd03216 79 MVYQ------------------------------------------------------LSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1234390149 187 LYDEPTSGLDPITAKEIIELMRNIQiKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRRLR-AQGVAVIFISHRLDEVFEIADRVTVLRDG 158
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
41-241 |
1.20e-31 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 116.84 E-value: 1.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 41 VLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLDELRS-DIGFLFQGSALYDSMT 119
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNqKLGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 120 VRENLEFPLRRHKEKlgtPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKIILYDEPTSGLDPIT 199
Cdd:PRK11629 104 ALENVAMPLLIGKKK---PAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1234390149 200 AKEIIELMRNIQIKYNTSSLIITHDVDCARVIaDRMVLLVDG 241
Cdd:PRK11629 181 ADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDG 221
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
26-252 |
1.85e-31 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 116.22 E-value: 1.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 26 VIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHtlDELRSDI 105
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMH--ERARLGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 106 GFLFQGSALYDSMTVRENLEFPLRrHKEKLgTPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKI 185
Cdd:TIGR04406 79 GYLPQEASIFRKLTVEENIMAVLE-IRKDL-DRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKF 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1234390149 186 ILYDEPTSGLDPITA---KEIIELM--RNIQIkyntssLIITHDVDCARVIADRMVLLVDGINYAEGSYTEL 252
Cdd:TIGR04406 157 ILLDEPFAGVDPIAVgdiKKIIKHLkeRGIGV------LITDHNVRETLDICDRAYIISDGKVLAEGTPAEI 222
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
26-252 |
4.57e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 116.44 E-value: 4.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 26 VIRIRDVRKSFGDNH--VLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDS---GYIEVMGkeiATLDRHTLDE 100
Cdd:PRK13640 5 IVEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDG---ITLTAKTVWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 101 LRSDIGFLFQG-SALYDSMTVRENLEFPLrrhkEKLGTP-SDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALART 178
Cdd:PRK13640 82 IREKVGIVFQNpDNQFVGATVGDDVAFGL----ENRAVPrPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1234390149 179 LILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCArVIADRMVLLVDGINYAEGSYTEL 252
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEI 230
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
45-252 |
7.55e-31 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 114.68 E-value: 7.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 45 FDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKeiatlDRHTLDELRSDIGFLFQGSALYDSMTVRENL 124
Cdd:PRK10771 18 FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ-----DHTTTPPSRRPVSMLFQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 125 EFPLRrhkEKLGTPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKIILYDEPTSGLDPITAKEII 204
Cdd:PRK10771 93 GLGLN---PGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEML 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1234390149 205 ELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEGSYTEL 252
Cdd:PRK10771 170 TLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
51-265 |
7.95e-31 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 118.21 E-value: 7.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 51 EGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLDELR-SDIGFLFQGSALYDSMTVRENLEFPLr 129
Cdd:PRK10070 53 EGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRrKKIAMVFQSFALMPHMTVLDNTAFGM- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 130 rhkEKLGTPS-DTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKIILYDEPTSGLDPITAKEIIELMR 208
Cdd:PRK10070 132 ---ELAGINAeERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELV 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1234390149 209 NIQIKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEGSYTE-LSQSTDPKVEAFFK 265
Cdd:PRK10070 209 KLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEiLNNPANDYVRTFFR 266
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
27-247 |
8.55e-31 |
|
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: 113.74 E-value: 8.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGdnHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGkeiatLDRHTLDELRSDIG 106
Cdd:cd03298 1 VRLDKIRFSYG--EQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING-----VDVTAAPPADRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 107 FLFQGSALYDSMTVRENLEFPlRRHKEKLgTPSDTTAlVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKII 186
Cdd:cd03298 74 MLFQENNLFAHLTVEQNVGLG-LSPGLKL-TAEDRQA-IEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1234390149 187 LYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEG 247
Cdd:cd03298 151 LLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
24-241 |
8.74e-31 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 114.87 E-value: 8.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 24 KAVIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCL--VGLMLPD---SGYIEVMGKEIATLDRHTL 98
Cdd:PRK14239 3 EPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIYSPRTDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 99 dELRSDIGFLFQGSALYdSMTVRENLEFPLRRHKEKlgtpsdTTALVMEALENVGLGRTI-----DLMPAE---LSGGMK 170
Cdd:PRK14239 83 -DLRKEIGMVFQQPNPF-PMSIYENVVYGLRLKGIK------DKQVLDEAVEKSLKGASIwdevkDRLHDSalgLSGGQQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1234390149 171 RRIALARTLILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYntSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDG 223
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
25-264 |
1.34e-30 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 113.92 E-value: 1.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 25 AVIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLdeLRSD 104
Cdd:COG0410 2 PMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRI--ARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 105 IGFLFQGSALYDSMTVRENLEFPLRRHKEKLGTPSDttalvmealenvgLGRTIDLMP--AE--------LSGGMKRRIA 174
Cdd:COG0410 80 IGYVPEGRRIFPSLTVEENLLLGAYARRDRAEVRAD-------------LERVYELFPrlKErrrqragtLSGGEQQMLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 175 LARTLILKPKIILYDEPTSGLDPITAKEIIELMRNIQiKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEGSYTELSQ 254
Cdd:COG0410 147 IGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLN-REGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLA 225
|
250
....*....|
gi 1234390149 255 stDPKVEAFF 264
Cdd:COG0410 226 --DPEVREAY 233
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-241 |
2.06e-30 |
|
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: 118.75 E-value: 2.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 1 MTDDPTTYKHKDQEGVADRPLER-----KAVIRIRDVRKSF-----GDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIK 70
Cdd:TIGR03269 249 EEGTPDEVVAVFMEGVSEVEKECevevgEPIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSK 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 71 CLVGLMLPDSGYIEV-MGKE-IATLDRHTLDELRSD--IGFLFQGSALYDSMTVRENL------EFPlrrhkEKLGTPSD 140
Cdd:TIGR03269 329 IIAGVLEPTSGEVNVrVGDEwVDMTKPGPDGRGRAKryIGILHQEYDLYPHRTVLDNLteaiglELP-----DELARMKA 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 141 TTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLI 220
Cdd:TIGR03269 404 VITLKMVGFDEEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFII 483
|
250 260
....*....|....*....|.
gi 1234390149 221 ITHDVDCARVIADRMVLLVDG 241
Cdd:TIGR03269 484 VSHDMDFVLDVCDRAALMRDG 504
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
27-260 |
2.82e-30 |
|
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: 113.02 E-value: 2.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTldELRSDIG 106
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK--RARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 107 FLFQGSALYDSMTVRENLEFPLRRHKEklgTPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKII 186
Cdd:cd03218 79 YLPQEASIFRKLTVEENILAVLEIRGL---SKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1234390149 187 LYDEPTSGLDPITAKEIIELMRNIQIKyNTSSLIITHDVDCARVIADRMVLLVDGINYAEGSYTELSQstDPKV 260
Cdd:cd03218 156 LLDEPFAGVDPIAVQDIQKIIKILKDR-GIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAA--NELV 226
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
41-252 |
3.30e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 114.03 E-value: 3.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 41 VLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGkeIATLDRHTLDELRSDIGFLFQGSalyDSMTV 120
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEENLWDIRNKAGMVFQNP---DNQIV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 121 RENLEFPLRRHKEKLGT-PSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKIILYDEPTSGLDPIT 199
Cdd:PRK13633 100 ATIVEEDVAFGPENLGIpPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSG 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1234390149 200 AKEIIELMRNIQIKYNTSSLIITHDVDCArVIADRMVLLVDGINYAEGSYTEL 252
Cdd:PRK13633 180 RREVVNTIKELNKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGTPKEI 231
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
25-241 |
5.06e-30 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 118.29 E-value: 5.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 25 AVIRIRDVRKSF----GDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLDE 100
Cdd:PRK10535 3 ALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 101 LRSD-IGFLFQGSALYDSMTVRENLEFP-----LRRHKEKlgtpsdttALVMEALENVGLGRTIDLMPAELSGGMKRRIA 174
Cdd:PRK10535 83 LRREhFGFIFQRYHLLSHLTAAQNVEVPavyagLERKQRL--------LRAQELLQRLGLEDRVEYQPSQLSGGQQQRVS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1234390149 175 LARTLILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTsSLIITHDVDCARViADRMVLLVDG 241
Cdd:PRK10535 155 IARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHT-VIIVTHDPQVAAQ-AERVIEIRDG 219
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
27-223 |
6.16e-30 |
|
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: 110.48 E-value: 6.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDN--HVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDrhtlDELRSD 104
Cdd:cd03247 1 LSINNVSFSYPEQeqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE----KALSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 105 IGFLFQGSALYDSmTVRENLefplrrhkeklgtpsdttalvmealenvglGRtidlmpaELSGGMKRRIALARTLILKPK 184
Cdd:cd03247 77 ISVLNQRPYLFDT-TLRNNL------------------------------GR-------RFSGGERQRLALARILLQDAP 118
|
170 180 190
....*....|....*....|....*....|....*....
gi 1234390149 185 IILYDEPTSGLDPITAKEIIELMrnIQIKYNTSSLIITH 223
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLI--FEVLKDKTLIWITH 155
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
25-248 |
6.44e-30 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 112.94 E-value: 6.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 25 AVIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLDELRsd 104
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 105 iGFLFQGSALYDSMTVRENLEF---PLRRHKEKlgtpsdTTALVMEALENVGL----GRTIdlmpAELSGGMKRRIALAR 177
Cdd:PRK13548 79 -AVLPQHSSLSFPFTVEEVVAMgraPHGLSRAE------DDALVAAALAQVDLahlaGRDY----PQLSGGEQQRVQLAR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1234390149 178 TLI------LKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEGS 248
Cdd:PRK13548 148 VLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGT 224
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
27-233 |
7.91e-30 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 111.53 E-value: 7.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGD--NHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRhtlDELRSD 104
Cdd:cd03245 3 IEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDP---ADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 105 IGFLFQGSALYdSMTVRENLEfplrrhkekLGTPSDTTALVMEALENVGLG-------RTIDLMPAE----LSGGMKRRI 173
Cdd:cd03245 80 IGYVPQDVTLF-YGTLRDNIT---------LGAPLADDERILRAAELAGVTdfvnkhpNGLDLQIGErgrgLSGGQRQAV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1234390149 174 ALARTLILKPKIILYDEPTSGLDPITAKEIIELMRniQIKYNTSSLIITHD------------VDCARVIAD 233
Cdd:cd03245 150 ALARALLNDPPILLLDEPTSAMDMNSEERLKERLR--QLLGDKTLIIITHRpslldlvdriivMDSGRIVAD 219
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
42-241 |
1.24e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 112.83 E-value: 1.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 42 LNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIaTLDRHTLDELRSDIGFLFQ--GSALYDSmT 119
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDI-TDKKVKLSDIRKKVGLVFQypEYQLFEE-T 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 120 VRENLEFPLRRhkekLG-TPSDTTALVMEALENVGLGRTI--DLMPAELSGGMKRRIALARTLILKPKIILYDEPTSGLD 196
Cdd:PRK13637 101 IEKDIAFGPIN----LGlSEEEIENRVKRAMNIVGLDYEDykDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1234390149 197 PITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:PRK13637 177 PKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKG 221
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
24-241 |
1.51e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 115.89 E-value: 1.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 24 KAVIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIAtlDRHTLDELRS 103
Cdd:COG1129 2 EPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVR--FRSPRDAQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 104 DIGFLFQGSALYDSMTVRENLeFpLRRHKEKLGT--PSDTTALVMEALENVGLgrTIDL-MP-AELSGGMKRRIALARTL 179
Cdd:COG1129 80 GIAIIHQELNLVPNLSVAENI-F-LGREPRRGGLidWRAMRRRARELLARLGL--DIDPdTPvGDLSVAQQQLVEIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1234390149 180 ILKPKIILYDEPTSGLdpiTAKEI---IELMRNIQIKyNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:COG1129 156 SRDARVLILDEPTASL---TEREVerlFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDG 216
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
25-264 |
1.57e-29 |
|
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: 111.33 E-value: 1.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 25 AVIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGY-IEVMGKEiatLDRHTLDELRS 103
Cdd:COG1119 2 PLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGER---RGGEDVWELRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 104 DIGFL-------FQG---------SALYDSMTVRENLefplrrhkeklgTPSDTtALVMEALENVGLGRTIDLMPAELSG 167
Cdd:COG1119 79 RIGLVspalqlrFPRdetvldvvlSGFFDSIGLYREP------------TDEQR-ERARELLELLGLAHLADRPFGTLSQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 168 GMKRRIALARTLILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDV-DCARVIaDRMVLLVDGINYAE 246
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVeEIPPGI-THVLLLKDGRVVAA 224
|
250
....*....|....*...
gi 1234390149 247 GSYTELsqSTDPKVEAFF 264
Cdd:COG1119 225 GPKEEV--LTSENLSEAF 240
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
25-238 |
1.66e-29 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 113.97 E-value: 1.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 25 AVIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGK---EIATLDRhtldel 101
Cdd:PRK11000 2 ASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmnDVPPAER------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 102 rsDIGFLFQGSALYDSMTVRENLEFPLRRHKEKlgtPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLIL 181
Cdd:PRK11000 76 --GVGMVFQSYALYPHLSVAENMSFGLKLAGAK---KEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1234390149 182 KPKIILYDEPTSGLDPITAKEI-IELMRnIQIKYNTSSLIITHDVDCARVIADRMVLL 238
Cdd:PRK11000 151 EPSVFLLDEPLSNLDAALRVQMrIEISR-LHKRLGRTMIYVTHDQVEAMTLADKIVVL 207
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
26-252 |
1.87e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 112.51 E-value: 1.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 26 VIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTldelrsdI 105
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRR-------I 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 106 GFLFQGSALYDSMTVRENLEFPLRRHkeklG-TPSDTTALVMEALENVGLG----RTIDlmpaELSGGMKRRIALARTLI 180
Cdd:COG4152 74 GYLPEERGLYPKMKVGEQLVYLARLK----GlSKAEAKRRADEWLERLGLGdranKKVE----ELSKGNQQKVQLIAALL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1234390149 181 LKPKIILYDEPTSGLDPITA----KEIIELMRNiqikyNTSSLIITHDVDCARVIADRMVLLVDGINYAEGSYTEL 252
Cdd:COG4152 146 HDPELLILDEPFSGLDPVNVellkDVIRELAAK-----GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
27-251 |
5.31e-29 |
|
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: 109.41 E-value: 5.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHtldelrsDIG 106
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKDLH-------KIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 107 FLFQGSALYDSMTVRENLEFplrrHKEKLGTPSDTtalVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKII 186
Cdd:TIGR03740 74 SLIESPPLYENLTARENLKV----HTTLLGLPDSR---IDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1234390149 187 LYDEPTSGLDPITAKEIIELMRNIQiKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEGSYTE 251
Cdd:TIGR03740 147 ILDEPTNGLDPIGIQELRELIRSFP-EQGITVILSSHILSEVQQLADHIGIISEGVLGYQGKINK 210
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
27-241 |
5.67e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 110.56 E-value: 5.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFG-----DNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTldel 101
Cdd:COG1101 2 LELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYK---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 102 RS-DIGFLFQ----GSAlyDSMTVRENLEFPLRRHKE---KLGTPSDTTALVMEALENVGLG---RTIDLMpAELSGGMK 170
Cdd:COG1101 78 RAkYIGRVFQdpmmGTA--PSMTIEENLALAYRRGKRrglRRGLTKKRRELFRELLATLGLGlenRLDTKV-GLLSGGQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1234390149 171 RRIALARTLILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:COG1101 155 QALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEG 225
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
38-241 |
8.48e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 110.21 E-value: 8.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 38 DNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEiatLDRHTLDELRSDIGFLFQG-SALYD 116
Cdd:PRK13650 19 EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDL---LTEENVWDIRHKIGMVFQNpDNQFV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 117 SMTVRENLEFPLrrhkEKLGTP-SDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKIILYDEPTSGL 195
Cdd:PRK13650 96 GATVEDDVAFGL----ENKGIPhEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSML 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1234390149 196 DPITAKEIIELMRNIQIKYNTSSLIITHDVDcARVIADRMVLLVDG 241
Cdd:PRK13650 172 DPEGRLELIKTIKGIRDDYQMTVISITHDLD-EVALSDRVLVMKNG 216
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
30-231 |
3.21e-28 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 106.88 E-value: 3.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 30 RDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIatldrhTLDELRSDIGFLF 109
Cdd:PRK13539 6 EDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI------DDPDVAEACHYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 110 QGSALYDSMTVRENLEFplrrHKEKLGTPsdtTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKIILYD 189
Cdd:PRK13539 80 HRNAMKPALTVAENLEF----WAAFLGGE---ELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1234390149 190 EPTSGLDPITAKEIIELMRnIQIKYNTSSLIITH---DVDCARVI 231
Cdd:PRK13539 153 EPTAALDAAAVALFAELIR-AHLAQGGIVIAATHiplGLPGAREL 196
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
27-252 |
3.22e-28 |
|
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: 107.70 E-value: 3.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNH-VLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLdrhTLDELRSDI 105
Cdd:cd03253 1 IEFENVTFAYDPGRpVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREV---TLDSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 106 GFLFQGSALYDSmTVRENLEFplrrhkeklGTPSDTTALVMEALENVGLGRTIDLMP-----------AELSGGMKRRIA 174
Cdd:cd03253 78 GVVPQDTVLFND-TIGYNIRY---------GRPDATDEEVIEAAKAAQIHDKIMRFPdgydtivgergLKLSGGEKQRVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 175 LARTLILKPKIILYDEPTSGLDPITAKEIIELMRniQIKYNTSSLIITHDVdcaRVI--ADRMVLLVDGINYAEGSYTEL 252
Cdd:cd03253 148 IARAILKNPPILLLDEATSALDTHTEREIQAALR--DVSKGRTTIVIAHRL---STIvnADKIIVLKDGRIVERGTHEEL 222
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
26-241 |
5.89e-28 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 109.92 E-value: 5.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 26 VIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIAtldrHTLDELRSdI 105
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS----HVPPYQRP-I 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 106 GFLFQGSALYDSMTVRENLEFPLRRHKEKLGtpsDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKI 185
Cdd:PRK11607 94 NMMFQSYALFPHMTVEQNIAFGLKQDKLPKA---EIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 186 ILYDEPTSGLDpitaKEIIELMR----NIQIKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:PRK11607 171 LLLDEPMGALD----KKLRDRMQlevvDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRG 226
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
45-248 |
7.61e-28 |
|
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: 112.41 E-value: 7.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 45 FDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATldrhTLDELRSDIGFLFQGSALYDSMTVRENL 124
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET----NLDAVRQSLGMCPQHNILFHHLTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 125 EFplrrHKEKLGTPSDTTALVMEA-LENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKIILYDEPTSGLDPITAKEI 203
Cdd:TIGR01257 1025 LF----YAQLKGRSWEEAQLEMEAmLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSI 1100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1234390149 204 IELMrniqIKYNTSSLII--THDVDCARVIADRMVLLVDGINYAEGS 248
Cdd:TIGR01257 1101 WDLL----LKYRSGRTIImsTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
27-252 |
8.77e-28 |
|
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: 106.47 E-value: 8.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSF---GDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDrhtLDELRS 103
Cdd:cd03249 1 IEFKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLN---LRWLRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 104 DIGFLFQGSALYDsMTVRENLefplrrhkeKLGTPSDTTALVMEALENVGLGRTIDLMP-----------AELSGGMKRR 172
Cdd:cd03249 78 QIGLVSQEPVLFD-GTIAENI---------RYGKPDATDEEVEEAAKKANIHDFIMSLPdgydtlvgergSQLSGGQKQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 173 IALARTLILKPKIILYDEPTSGLDPITAKEIIELMRNiqIKYNTSSLIITHDVDCARViADRMVLLVDGINYAEGSYTEL 252
Cdd:cd03249 148 IAIARALLRNPKILLLDEATSALDAESEKLVQEALDR--AMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDEL 224
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
57-252 |
1.04e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 107.14 E-value: 1.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 57 VMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIatlDRHTLDELRSDIGFLFQ-------GSAL-YDSMTVRENLEFPL 128
Cdd:PRK13648 40 IVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAI---TDDNFEKLRKHIGIVFQnpdnqfvGSIVkYDVAFGLENHAVPY 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 129 RRHKEKlgtpsdttalVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKIILYDEPTSGLDPITAKEIIELMR 208
Cdd:PRK13648 117 DEMHRR----------VSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVR 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1234390149 209 NIQIKYNTSSLIITHDVDCArVIADRMVLLVDGINYAEGSYTEL 252
Cdd:PRK13648 187 KVKSEHNITIISITHDLSEA-MEADHVIVMNKGTVYKEGTPTEI 229
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
26-252 |
2.11e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 106.86 E-value: 2.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 26 VIRIRDVRKSFGD-NHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIaTLDRHTLDELRSD 104
Cdd:PRK13636 5 ILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 105 IGFLFQG--SALYdSMTVRENLEF-PLrrhkeKLGTPSDTT-ALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLI 180
Cdd:PRK13636 84 VGMVFQDpdNQLF-SASVYQDVSFgAV-----NLKLPEDEVrKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1234390149 181 LKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEGSYTEL 252
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
27-252 |
3.19e-27 |
|
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: 105.00 E-value: 3.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSF-GDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLdelRSDI 105
Cdd:cd03254 3 IEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSL---RSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 106 GFLFQGSALYdSMTVRENLefplrrhkeKLGTPSDTTALVMEALENVGLGRTIDLMP-----------AELSGGMKRRIA 174
Cdd:cd03254 80 GVVLQDTFLF-SGTIMENI---------RLGRPNATDEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1234390149 175 LARTLILKPKIILYDEPTSGLDPITAKEIIELMRNIQikYNTSSLIITHDVDCARViADRMVLLVDGINYAEGSYTEL 252
Cdd:cd03254 150 IARAMLRDPKILILDEATSNIDTETEKLIQEALEKLM--KGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDEL 224
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
24-260 |
3.25e-27 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 105.46 E-value: 3.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 24 KAVIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLdeLRS 103
Cdd:PRK11300 3 QPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQI--ARM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 104 DIGFLFQGSALYDSMTVRENLEFPLRRHKEK------LGTP----SDTTALVMEA--LENVGLGRTIDLMPAELSGGMKR 171
Cdd:PRK11300 81 GVVRTFQHVRLFREMTVIENLLVAQHQQLKTglfsglLKTPafrrAESEALDRAAtwLERVGLLEHANRQAGNLAYGQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 172 RIALARTLILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEGSYTE 251
Cdd:PRK11300 161 RLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEE 240
|
....*....
gi 1234390149 252 LSQstDPKV 260
Cdd:PRK11300 241 IRN--NPDV 247
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
26-247 |
3.71e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 105.97 E-value: 3.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 26 VIRIRDVRKSFGD-NHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIatlDRHTLDELRSD 104
Cdd:PRK13647 4 IIEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREV---NAENEKWVRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 105 IGFLFQG--SALYdSMTVRENLEF-PLrrhkeKLG-TPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLI 180
Cdd:PRK13647 81 VGLVFQDpdDQVF-SSTVWDDVAFgPV-----NMGlDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1234390149 181 LKPKIILYDEPTSGLDPITAKEIIELMRNIQiKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEG 247
Cdd:PRK13647 155 MDPDVIVLDEPMAYLDPRGQETLMEILDRLH-NQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
42-237 |
4.30e-27 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 106.97 E-value: 4.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 42 LNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLDELRSDIGFLFQGSalYDSM--- 118
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKIQIVFQNP--YGSLnpr 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 119 -TVRENLEFPLRRHKEKlgTPSDTTALVMEALENVGLgRT--IDLMPAELSGGMKRRIALARTLILKPKIILYDEPTSGL 195
Cdd:PRK11308 109 kKVGQILEEPLLINTSL--SAAERREKALAMMAKVGL-RPehYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSAL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1234390149 196 DPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADR-MVL 237
Cdd:PRK11308 186 DVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEvMVM 228
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
25-236 |
4.99e-27 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 104.44 E-value: 4.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 25 AVIRIRDVRKSFgDNH--------VLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKE----IAT 92
Cdd:COG4778 3 TLLEVENLSKTF-TLHlqggkrlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdLAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 93 LDRHTLDELRSD-IGFLFQ-------GSALyDsmTVREnlefPLRRhkekLGTPSDTT-ALVMEALENVGLGRTI-DLMP 162
Cdd:COG4778 82 ASPREILALRRRtIGYVSQflrviprVSAL-D--VVAE----PLLE----RGVDREEArARARELLARLNLPERLwDLPP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1234390149 163 AELSGGMKRRIALARTLILKPKIILYDEPTSGLDPITAKEIIELMRniQIKYNTSSLI-ITHDVDCARVIADRMV 236
Cdd:COG4778 151 ATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIE--EAKARGTAIIgIFHDEEVREAVADRVV 223
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
23-241 |
5.18e-27 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 106.73 E-value: 5.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 23 RKAVIRIRDVRKSF----GDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPD---SGYIEVMGKEIATLDR 95
Cdd:PRK09473 9 ADALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 96 HTLDELRSD-IGFLFQG--SALYDSMTVRENLEFPLRRHKEKLGTPSDTTALVMeaLENVGLG---RTIDLMPAELSGGM 169
Cdd:PRK09473 89 KELNKLRAEqISMIFQDpmTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRM--LDAVKMPearKRMKMYPHEFSGGM 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1234390149 170 KRRIALARTLILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:PRK09473 167 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAG 238
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
20-257 |
1.01e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 105.10 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 20 PLERKAvirIRDVRKSFGdnhvlngfdmdlyEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEI-ATLDRHTL 98
Cdd:PRK13634 17 PFERRA---LYDVNVSIP-------------SGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItAGKKNKKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 99 DELRSDIGFLFQ--GSALYDSmTVRENLEF-PLrrhkeKLGTP-SDTTALVMEALENVGLGRTI-DLMPAELSGGMKRRI 173
Cdd:PRK13634 81 KPLRKKVGIVFQfpEHQLFEE-TVEKDICFgPM-----NFGVSeEDAKQKAREMIELVGLPEELlARSPFELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 174 ALARTLILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEGSYTELS 253
Cdd:PRK13634 155 AIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIF 234
|
....
gi 1234390149 254 QSTD 257
Cdd:PRK13634 235 ADPD 238
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
27-253 |
1.23e-26 |
|
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: 107.97 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGL---------------MLPDSGYIEVMGK--- 88
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqyeptsgriiyhvaLCEKCGYVERPSKvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 89 ---------EIATLDRHTLDE-----LRSDIGFLFQGS-ALYDSMTVRENLEFPLrrhkEKLGTPS-DTTALVMEALENV 152
Cdd:TIGR03269 81 pcpvcggtlEPEEVDFWNLSDklrrrIRKRIAIMLQRTfALYGDDTVLDNVLEAL----EEIGYEGkEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 153 GLGRTIDLMPAELSGGMKRRIALARTLILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIA 232
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLS 236
|
250 260
....*....|....*....|.
gi 1234390149 233 DRMVLLVDGINYAEGSYTELS 253
Cdd:TIGR03269 237 DKAIWLENGEIKEEGTPDEVV 257
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
26-241 |
1.25e-26 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 103.42 E-value: 1.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 26 VIRIRDVRKSF-GDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLDELRSD 104
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 105 IGFLFQGSALYDSMTVRENLEFPLRRHKeklGTPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPK 184
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIAG---ASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1234390149 185 IILYDEPTSGLDPITAKEIIELMRNIQiKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGILRLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
27-254 |
1.58e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 107.99 E-value: 1.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVrkSFG----DNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRhtlDELR 102
Cdd:PRK11160 339 LTLNNV--SFTypdqPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSE---AALR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 103 SDIGFLFQGSALYdSMTVRENLefplrrhkeKLGTPSDTTALVMEALENVGLGRTIDLMPA----------ELSGGMKRR 172
Cdd:PRK11160 414 QAISVVSQRVHLF-SATLRDNL---------LLAAPNASDEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRR 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 173 IALARTLILKPKIILYDEPTSGLDPITAKEIIELMRniQIKYNTSSLIITHdvdcaRVIA----DRMVLLVDGINYAEGS 248
Cdd:PRK11160 484 LGIARALLHDAPLLLLDEPTEGLDAETERQILELLA--EHAQNKTVLMITH-----RLTGleqfDRICVMDNGQIIEQGT 556
|
....*.
gi 1234390149 249 YTELSQ 254
Cdd:PRK11160 557 HQELLA 562
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
26-252 |
2.42e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 103.73 E-value: 2.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 26 VIRIRDVRKSF-GDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIAtldRHTLDELRSD 104
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPIT---KENIREVRKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 105 IGFLFQGSalyD----SMTVRENLEF-PLrrhkeKLGTPSDTTA-LVMEALENVGLGRTIDLMPAELSGGMKRRIALART 178
Cdd:PRK13652 80 VGLVFQNP---DdqifSPTVEQDIAFgPI-----NLGLDEETVAhRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1234390149 179 LILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEGSYTEL 252
Cdd:PRK13652 152 IAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
27-241 |
2.60e-26 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 101.14 E-value: 2.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNH--VLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRhtlDELRSD 104
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDP---NELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 105 IGFLFQGSALYDSmTVRENLefplrrhkeklgtpsdttalvmealenvglgrtidlmpaeLSGGMKRRIALARTLILKPK 184
Cdd:cd03246 78 VGYLPQDDELFSG-SIAENI----------------------------------------LSGGQRQRLGLARALYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1234390149 185 IILYDEPTSGLDPITAKEIIELMRNIQIKYNTsSLIITHDVDCARvIADRMVLLVDG 241
Cdd:cd03246 117 ILVLDEPNSHLDVEGERALNQAIAALKAAGAT-RIVIAHRPETLA-SADRILVLEDG 171
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
41-252 |
3.26e-26 |
|
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: 102.56 E-value: 3.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 41 VLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDrhtLDELRSDIGFLFQGSALYdSMTV 120
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALAD---PAWLRRQVGVVLQENVLF-NRSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 121 RENL----EFPLRRHKEKLGTPSDTTALVMEALEnvGLGRTIDLMPAELSGGMKRRIALARTLILKPKIILYDEPTSGLD 196
Cdd:cd03252 93 RDNIaladPGMSMERVIEAAKLAGAHDFISELPE--GYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1234390149 197 PITAKEIIELMRNIQIkyNTSSLIITHDVDCARViADRMVLLVDGINYAEGSYTEL 252
Cdd:cd03252 171 YESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDEL 223
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
35-238 |
3.31e-26 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 101.16 E-value: 3.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 35 SFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKeiatldrhtldelrSDIGFLFQGSAL 114
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG--------------ARVAYVPQRSEV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 115 YDSM--TVRENLEFPLRRHKEKLGTPS-DTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKIILYDEP 191
Cdd:NF040873 67 PDSLplTVRDLVAMGRWARRGLWRRLTrDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEP 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1234390149 192 TSGLDPITAKEIIELMRNIQIKyNTSSLIITHDVDCARViADRMVLL 238
Cdd:NF040873 147 TTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRR-ADPCVLL 191
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
44-241 |
3.55e-26 |
|
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: 102.06 E-value: 3.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 44 GFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPD----SGYIEVMGKEIATLdrhtldELRS-DIGFLFQG--SALYD 116
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGltqtSGEILLDGRPLLPL------SIRGrHIATIMQNprTAFNP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 117 SMTVRENLEFPLRRHkekLGTPSDTTALVMEALENVGL---GRTIDLMPAELSGGMKRRIALARTLILKPKIILYDEPTS 193
Cdd:TIGR02770 78 LFTMGNHAIETLRSL---GKLSKQARALILEALEAVGLpdpEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1234390149 194 GLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:TIGR02770 155 DLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDG 202
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-261 |
4.41e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 102.68 E-value: 4.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 24 KAVIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGL--MLPD---SGYIEVMGKEIATLDrhtL 98
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEarvSGEVYLDGQDIFKMD---V 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 99 DELRSDIGFLFQGSALYDSMTVRENLEFPLRRHKeKLGTPSDTTALVMEALENVGLGRTI----DLMPAELSGGMKRRIA 174
Cdd:PRK14247 78 IELRRRVQMVFQIPNPIPNLSIFENVALGLKLNR-LVKSKKELQERVRWALEKAQLWDEVkdrlDAPAGKLSGGQQQRLC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 175 LARTLILKPKIILYDEPTSGLDPITAKEIIELMrnIQIKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEGSYTELsq 254
Cdd:PRK14247 157 IARALAFQPEVLLADEPTANLDPENTAKIESLF--LELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREV-- 232
|
....*..
gi 1234390149 255 STDPKVE 261
Cdd:PRK14247 233 FTNPRHE 239
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
40-241 |
6.65e-26 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 106.48 E-value: 6.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 40 HVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLDELRSDIGFLFQG--SALYDS 117
Cdd:PRK10261 338 HAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQDpyASLDPR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 118 MTVRENLEFPLRRHKekLGTPSDTTALVMEALENVGLGRTIDL-MPAELSGGMKRRIALARTLILKPKIILYDEPTSGLD 196
Cdd:PRK10261 418 QTVGDSIMEPLRVHG--LLPGKAAAARVAWLLERVGLLPEHAWrYPHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1234390149 197 PITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:PRK10261 496 VSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLG 540
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
22-226 |
7.46e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 101.33 E-value: 7.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 22 ERKAVIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLdrhTLDEL 101
Cdd:PRK10247 3 ENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTL---KPEIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 102 RSDIGFLFQGSALYDSmTVRENLEFPLR-RHKeklgTPsDTTALVmEALENVGLGRTIDLMP-AELSGGMKRRIALARTL 179
Cdd:PRK10247 80 RQQVSYCAQTPTLFGD-TVYDNLIFPWQiRNQ----QP-DPAIFL-DDLERFALPDTILTKNiAELSGGEKQRISLIRNL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1234390149 180 ILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVD 226
Cdd:PRK10247 153 QFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKD 199
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
27-253 |
8.24e-26 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 105.64 E-value: 8.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLDELrsDIG 106
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL--GIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 107 FLFQGSALYDSMTVRENLEFPLRRHKEKLGTP----SDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILK 182
Cdd:PRK09700 84 IIYQELSVIDELTVLENLYIGRHLTKKVCGVNiidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1234390149 183 PKIILYDEPTSGLdpiTAKEIIEL---MRNIQiKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEGSYTELS 253
Cdd:PRK09700 164 AKVIIMDEPTSSL---TNKEVDYLfliMNQLR-KEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVS 233
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
27-252 |
8.79e-26 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 101.15 E-value: 8.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGD--NHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLdrhTLDELRSD 104
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDY---TLASLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 105 IGFLFQGSALYDSmTVRENLEFplrrhkeklGTPSDTTALVMEALENVGLGRTIDLMP-----------AELSGGMKRRI 173
Cdd:cd03251 78 IGLVSQDVFLFND-TVAENIAY---------GRPGATREEVEEAARAANAHEFIMELPegydtvigergVKLSGGQRQRI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1234390149 174 ALARTLILKPKIILYDEPTSGLDPITAKEIIELMRNIQIkyNTSSLIITHDVDCARViADRMVLLVDGINYAEGSYTEL 252
Cdd:cd03251 148 AIARALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEEL 223
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
27-241 |
8.93e-26 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 104.54 E-value: 8.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLDELrsdIG 106
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR---VA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 107 FLFQGSALYDSMTVRENLEFPLRRHKEKLG--TPSDTTAlVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPK 184
Cdd:PRK09536 81 SVPQDTSLSFEFDVRQVVEMGRTPHRSRFDtwTETDRAA-VERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1234390149 185 IILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIItHDVDCARVIADRMVLLVDG 241
Cdd:PRK09536 160 VLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADG 215
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
27-241 |
9.10e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 102.86 E-value: 9.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDN-----HVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLDE- 100
Cdd:PRK13651 3 IKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 101 --------------------LRSDIGFLFQGS--ALYDSmTVRENLEFPLRrhkeKLGTP-SDTTALVMEALENVGLGRT 157
Cdd:PRK13651 83 vleklviqktrfkkikkikeIRRRVGVVFQFAeyQLFEQ-TIEKDIIFGPV----SMGVSkEEAKKRAAKYIELVGLDES 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 158 -IDLMPAELSGGMKRRIALARTLILKPKIILYDEPTSGLDPITAKEIIELMRNIQiKYNTSSLIITHDVDCARVIADRMV 236
Cdd:PRK13651 158 yLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLN-KQGKTIILVTHDLDNVLEWTKRTI 236
|
....*
gi 1234390149 237 LLVDG 241
Cdd:PRK13651 237 FFKDG 241
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
42-252 |
1.34e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 102.17 E-value: 1.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 42 LNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIA--TLDRHtLDELRSDIGFLFQ--GSALYDS 117
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThkTKDKY-IRPVRKRIGMVFQfpESQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 118 MTVRE------NLEFPLRRHKEKlgtpsdTTALVMEalenVGLGRTI-DLMPAELSGGMKRRIALARTLILKPKIILYDE 190
Cdd:PRK13646 102 TVEREiifgpkNFKMNLDEVKNY------AHRLLMD----LGFSRDVmSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1234390149 191 PTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEGSYTEL 252
Cdd:PRK13646 172 PTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
25-260 |
1.63e-25 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 100.49 E-value: 1.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 25 AVIRIRDVRKSFGDNHVLNGFDMDLYEGEnlVV--MGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHtldeLR 102
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGE--IVglLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMH----KR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 103 SD--IGFLFQGSALYDSMTVRENLEFPLRRHKEklgTPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLI 180
Cdd:COG1137 76 ARlgIGYLPQEASIFRKLTVEDNILAVLELRKL---SKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 181 LKPKIILYDEPTSGLDPITAKEIIELM-----RNIQIkyntssLIITHDVDCARVIADRMVLLVDGINYAEGSYTELSQs 255
Cdd:COG1137 153 TNPKFILLDEPFAGVDPIAVADIQKIIrhlkeRGIGV------LITDHNVRETLGICDRAYIISEGKVLAEGTPEEILN- 225
|
....*
gi 1234390149 256 tDPKV 260
Cdd:COG1137 226 -NPLV 229
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
16-241 |
3.83e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 101.47 E-value: 3.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 16 VADRPLERKAVIRIRDVRKSFGDNH-----VLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEV----- 85
Cdd:PRK13631 11 KVPNPLSDDIILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyi 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 86 ---MGKEIATLDRHT-----LDELRSDIGFLFQ--GSALYDSmTVRENLEF-PLrrhkeKLGTP-SDTTALVMEALENVG 153
Cdd:PRK13631 91 gdkKNNHELITNPYSkkiknFKELRRRVSMVFQfpEYQLFKD-TIEKDIMFgPV-----ALGVKkSEAKKLAKFYLNKMG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 154 LGRT-IDLMPAELSGGMKRRIALARTLILKPKIILYDEPTSGLDPITAKEIIELMRNIQiKYNTSSLIITHDVDCARVIA 232
Cdd:PRK13631 165 LDDSyLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAK-ANNKTVFVITHTMEHVLEVA 243
|
....*....
gi 1234390149 233 DRMVLLVDG 241
Cdd:PRK13631 244 DEVIVMDKG 252
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
42-241 |
5.30e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 100.29 E-value: 5.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 42 LNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEI-ATLDRHTLDELRSDIGFLFQ--GSALYDSm 118
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItPETGNKNLKKLRKKVSLVFQfpEAQLFEN- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 119 TVRENLEF-PLrrhkeKLG-TPSDTTALVMEALENVGLGRT-IDLMPAELSGGMKRRIALARTLILKPKIILYDEPTSGL 195
Cdd:PRK13641 102 TVLKDVEFgPK-----NFGfSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1234390149 196 DPITAKEIIELMRNIQiKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:PRK13641 177 DPEGRKEMMQLFKDYQ-KAGHTVILVTHNMDDVAEYADDVLVLEHG 221
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
27-241 |
9.38e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 99.15 E-value: 9.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPD-----SGYIEVMGKEIATLDRHTLdEL 101
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDPI-EV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 102 RSDIGFLFQGSALYDSMTVRENLEFPLRRHKekLGTPSDTTALVME-ALENVGL-----GRTIDlMPAELSGGMKRRIAL 175
Cdd:PRK14267 84 RREVGMVFQYPNPFPHLTIYDNVAIGVKLNG--LVKSKKELDERVEwALKKAALwdevkDRLND-YPSNLSGGQRQRLVI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1234390149 176 ARTLILKPKIILYDEPTSGLDPITAKEIIELMrnIQIKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELL--FELKKEYTIVLVTHSPAQAARVSDYVAFLYLG 224
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
38-261 |
1.68e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 99.01 E-value: 1.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 38 DNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATldrHTLDELRSDIGFLFQG-SALYD 116
Cdd:PRK13642 19 DVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTA---ENVWNLRRKIGMVFQNpDNQFV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 117 SMTVRENLEFPLrrhkEKLGTP-SDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKIILYDEPTSGL 195
Cdd:PRK13642 96 GATVEDDVAFGM----ENQGIPrEEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSML 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1234390149 196 DPITAKEIIELMRNIQIKYNTSSLIITHDVDCArVIADRMVLLVDGINYAEGSYTELSQSTDPKVE 261
Cdd:PRK13642 172 DPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEIIKEAAPSELFATSEDMVE 236
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
27-233 |
1.79e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 98.57 E-value: 1.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDS-----GYIEVMGKEIATlDRHTLDEL 101
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYE-RRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 102 RSDIGFLFQGSALYdSMTVRENLEFPLR----RHKEKLgtpsdtTALVMEALENVGL----GRTIDLMPAELSGGMKRRI 173
Cdd:PRK14258 87 RRQVSMVHPKPNLF-PMSVYDNVAYGVKivgwRPKLEI------DDIVESALKDADLwdeiKHKIHKSALDLSGGQQQRL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 174 ALARTLILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIAD 233
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
21-208 |
2.57e-24 |
|
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: 96.27 E-value: 2.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 21 LERKAVIRIRDVRKSFGdnhvlnGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATldrhTLDE 100
Cdd:TIGR01189 1 LAARNLACSRGERMLFE------GLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAE----QRDE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 101 LRSDIGFLFQGSALYDSMTVRENLEFPLRRHkeklgtpSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLI 180
Cdd:TIGR01189 71 PHENILYLGHLPGLKPELSALENLHFWAAIH-------GGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWL 143
|
170 180
....*....|....*....|....*...
gi 1234390149 181 LKPKIILYDEPTSGLDPITAKEIIELMR 208
Cdd:TIGR01189 144 SRRPLWILDEPTTALDKAGVALLAGLLR 171
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
27-252 |
3.02e-24 |
|
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: 101.74 E-value: 3.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDN-HVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTldeLRSDI 105
Cdd:TIGR01193 474 IVINDVSYSYGYGsNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHT---LRQFI 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 106 GFLFQGSALYDSmTVRENLefpLRRHKEKLgtpsdTTALVMEALENVGLGRTIDLMP-----------AELSGGMKRRIA 174
Cdd:TIGR01193 551 NYLPQEPYIFSG-SILENL---LLGAKENV-----SQDEIWAACEIAEIKDDIENMPlgyqtelseegSSISGGQKQRIA 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1234390149 175 LARTLILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKyntSSLIITHDVDCARViADRMVLLVDGINYAEGSYTEL 252
Cdd:TIGR01193 622 LARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDEL 695
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
27-231 |
3.59e-24 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 96.79 E-value: 3.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNH--VLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLdelRSD 104
Cdd:cd03244 3 IEFKNVSLRYRPNLppVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDL---RSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 105 IG------FLFQGsalydsmTVRENLEfPLRRHkeklgtpSDTTalVMEALENVGLGRTIDLMP-----------AELSG 167
Cdd:cd03244 80 ISiipqdpVLFSG-------TIRSNLD-PFGEY-------SDEE--LWQALERVGLKEFVESLPggldtvveeggENLSV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1234390149 168 GMKRRIALARTLILKPKIILYDEPTSGLDPITAKEIIELMRNiQIKyNTSSLIITHDV----DCARVI 231
Cdd:cd03244 143 GQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIRE-AFK-DCTVLTIAHRLdtiiDSDRIL 208
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
22-241 |
3.64e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 100.87 E-value: 3.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 22 ERKAVIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATldRHTLDEL 101
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRI--RSPRDAI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 102 RSDIGFLFQGSALYDSMTVRENLEFPLRRHKEKLGTPSDTTALVMEALENVGLgrTIDL--MPAELSGGMKRRIALARTL 179
Cdd:COG3845 79 ALGIGMVHQHFMLVPNLTVAENIVLGLEPTKGGRLDRKAARARIRELSERYGL--DVDPdaKVEDLSVGEQQRVEILKAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1234390149 180 ILKPKIILYDEPTSGLDPITAKEIIELMRNIqIKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:COG3845 157 YRGARILILDEPTAVLTPQEADELFEILRRL-AAEGKSIIFITHKLREVMAIADRVTVLRRG 217
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
27-248 |
8.08e-24 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 96.72 E-value: 8.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLDELRsdiG 106
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRR---A 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 107 FLFQGSALYDSMTVRENLEFPLRRHkekLGTPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLI------ 180
Cdd:COG4559 79 VLPQHSSLAFPFTVEEVVALGRAPH---GSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepv 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1234390149 181 -LKPKIILYDEPTSGLDPITAKEIIELMRNIQIKyNTSSLIITHDVDCARVIADRMVLLVDGINYAEGS 248
Cdd:COG4559 156 dGGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGT 223
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
57-261 |
1.93e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 95.50 E-value: 1.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 57 VMGKSGSGKSVMIKCLVGLM-LPDS-----GYIEVMGKEIATLDRhtlDELRSDIGFLFQGSALYDSMTVRENLEFPLRR 130
Cdd:PRK14246 41 IMGPSGSGKSTLLKVLNRLIeIYDSkikvdGKVLYFGKDIFQIDA---IKLRKEVGMVFQQPNPFPHLSIYDNIAYPLKS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 131 H--KEKlgtpSDTTALVMEALENVGLGRTI----DLMPAELSGGMKRRIALARTLILKPKIILYDEPTSGLDPITAKEII 204
Cdd:PRK14246 118 HgiKEK----REIKKIVEECLRKVGLWKEVydrlNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIE 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1234390149 205 ELMrnIQIKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEGSYTELsqSTDPKVE 261
Cdd:PRK14246 194 KLI--TELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI--FTSPKNE 246
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
41-241 |
3.00e-23 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 95.15 E-value: 3.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 41 VLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIevmgkeiaTLDRHTLDELRSDIGFLFQGSALYDSMTV 120
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSI--------TLDGKPVEGPGAERGVVFQNEGLLPWRNV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 121 RENLEFPLrrhkEKLGTP-SDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKIILYDEPTSGLDPIT 199
Cdd:PRK11248 88 QDNVAFGL----QLAGVEkMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1234390149 200 AKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:PRK11248 164 REQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
26-248 |
3.24e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 95.44 E-value: 3.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 26 VIRIRDVRKSFGDNH-VLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGkeIATLDRHTLDELRSD 104
Cdd:PRK13644 1 MIRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--IDTGDFSKLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 105 IGFLFQG-SALYDSMTVRENLEFplrrHKEKLG-TPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILK 182
Cdd:PRK13644 79 VGIVFQNpETQFVGRTVEEDLAF----GPENLClPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTME 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1234390149 183 PKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTsSLIITHDVDCARViADRMVLLVDGINYAEGS 248
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKT-IVYITHNLEELHD-ADRIIVMDRGKIVLEGE 218
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
37-241 |
3.34e-23 |
|
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: 98.28 E-value: 3.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 37 GDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRhtlDELRSDIGFLFQGSALYD 116
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDR---EELGRHIGYLPQDVELFD 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 117 SmTVRENLEfplrrhkeKLGTPSDttALVMEALENVGLGRTIDLMP-----------AELSGGMKRRIALARTLILKPKI 185
Cdd:COG4618 420 G-TIAENIA--------RFGDADP--EKVVAAAKLAGVHEMILRLPdgydtrigeggARLSGGQRQRIGLARALYGDPRL 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1234390149 186 ILYDEPTSGLDP------ITAkeiIELMRniqiKYNTSSLIITHDVdCARVIADRMVLLVDG 241
Cdd:COG4618 489 VVLDEPNSNLDDegeaalAAA---IRALK----ARGATVVVITHRP-SLLAAVDKLLVLRDG 542
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
41-208 |
5.57e-23 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 92.94 E-value: 5.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 41 VLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGkeiaTLDRHTLDELRSDIGFLFQGSALYDSMTV 120
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG----GPLDFQRDSIARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 121 RENLEFPLRRHkeklgtpsdTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKIILYDEPTSGLDPITA 200
Cdd:cd03231 91 LENLRFWHADH---------SDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
....*...
gi 1234390149 201 KEIIELMR 208
Cdd:cd03231 162 ARFAEAMA 169
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
26-251 |
5.73e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.44 E-value: 5.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 26 VIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVmGK--EIATLDRHtLDELRS 103
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GEtvKIGYFDQH-QEELDP 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 104 DigflfqgsalydsMTVRENL--------EFPLRRHKEKLGTPSDttalvmEALENVGlgrtidlmpaELSGGMKRRIAL 175
Cdd:COG0488 393 D-------------KTVLDELrdgapggtEQEVRGYLGRFLFSGD------DAFKPVG----------VLSGGEKARLAL 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1234390149 176 ARTLILKPKIILYDEPTSGLDPITAKEIIELMRNiqikYNTSSLIITHDVDCARVIADRMVLLVDG-INYAEGSYTE 251
Cdd:COG0488 444 AKLLLSPPNVLLLDEPTNHLDIETLEALEEALDD----FPGTVLLVSHDRYFLDRVATRILEFEDGgVREYPGGYDD 516
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
45-257 |
8.88e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 94.42 E-value: 8.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 45 FDMDL--YEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEI-ATLDRHTLDELRSDIGFLFQ--GSALYDSmT 119
Cdd:PRK13643 23 FDIDLevKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVsSTSKQKEIKPVRKKVGVVFQfpESQLFEE-T 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 120 VRENLEFplrrHKEKLG-TPSDTTALVMEALENVGLGRTI-DLMPAELSGGMKRRIALARTLILKPKIILYDEPTSGLDP 197
Cdd:PRK13643 102 VLKDVAF----GPQNFGiPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 198 ITAKEIIELMRNIQiKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEGSYTELSQSTD 257
Cdd:PRK13643 178 KARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVD 236
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
29-196 |
2.35e-22 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 91.40 E-value: 2.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 29 IRDVRKSFgdnhvlNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDrhtlDELRSDIGFL 108
Cdd:PRK13538 10 ERDERILF------SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQR----DEYHQDLLYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 109 FQGSALYDSMTVRENLEFPLRrhkekLGTPSDTTALvMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKIILY 188
Cdd:PRK13538 80 GHQPGIKTELTALENLRFYQR-----LHGPGDDEAL-WEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWIL 153
|
....*...
gi 1234390149 189 DEPTSGLD 196
Cdd:PRK13538 154 DEPFTAID 161
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
29-250 |
5.60e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 94.75 E-value: 5.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 29 IRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEiatldrhtldelrsDIGFL 108
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL--------------RIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 109 FQGSALYDSMTVRENLE------FPLRRHKEKLGTPSDTTALVMEALENV---------------------GLG---RTI 158
Cdd:COG0488 67 PQEPPLDDDLTVLDTVLdgdaelRALEAELEELEAKLAEPDEDLERLAELqeefealggweaearaeeilsGLGfpeEDL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 159 DLMPAELSGGMKRRIALARTLILKPKIILYDEPTSGLDpitaKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLL 238
Cdd:COG0488 147 DRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD----LESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILEL 222
|
250
....*....|...
gi 1234390149 239 VDG-INYAEGSYT 250
Cdd:COG0488 223 DRGkLTLYPGNYS 235
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
27-248 |
9.27e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 90.84 E-value: 9.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLdrhTLDELRSDIG 106
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISML---SSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 107 FLFQGSALYDSMTVRENLEF---PLRRHKEKLGTpsDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKP 183
Cdd:PRK11231 80 LLPQHHLTPEGITVRELVAYgrsPWLSLWGRLSA--EDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1234390149 184 KIILYDEPTSGLDPITAKEIIELMRNIQIKYNTsslIIT--HDVDCARVIADRMVLLVDGINYAEGS 248
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVELMRLMRELNTQGKT---VVTvlHDLNQASRYCDHLVVLANGHVMAQGT 221
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
45-263 |
1.15e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 91.34 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 45 FDMDL--YEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEI-ATLDRHTLDELRSDIGFLFQ--GSALYDSmT 119
Cdd:PRK13649 24 FDVNLtiEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItSTSKNKDIKQIRKKVGLVFQfpESQLFEE-T 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 120 VRENLEFplrrHKEKLG-TPSDTTALVMEALENVGLGRTI-DLMPAELSGGMKRRIALARTLILKPKIILYDEPTSGLDP 197
Cdd:PRK13649 103 VLKDVAF----GPQNFGvSQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1234390149 198 ITAKEIIELMRNIQIKYNTSSLiITHDVDCARVIADRMVLLVDGINYAEGSYTELSQSTD---------PKVEAF 263
Cdd:PRK13649 179 KGRKELMTLFKKLHQSGMTIVL-VTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQDVDfleekqlgvPKITKF 252
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
30-210 |
1.41e-21 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 90.02 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 30 RDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPD---SGYIEVMGKEiatLDRHTLdelRSDIG 106
Cdd:cd03234 11 LKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQP---RKPDQF---QKCVA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 107 FLFQGSALYDSMTVRENLEF----PLRRHKEKlgtPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILK 182
Cdd:cd03234 85 YVRQDDILLPGLTVRETLTYtailRLPRKSSD---AIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWD 161
|
170 180
....*....|....*....|....*...
gi 1234390149 183 PKIILYDEPTSGLDPITAKEIIELMRNI 210
Cdd:cd03234 162 PKVLILDEPTSGLDSFTALNLVSTLSQL 189
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-255 |
3.35e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 90.16 E-value: 3.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 13 QEGVADRPLERKAVIRIrDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGY-----IEVMG 87
Cdd:PRK14271 9 QSGAADVDAAAPAMAAV-NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 88 KEIatLDRHTLDELRSDIGFLFQGSALYdSMTVRENLEFPLRRHKekLGTPSDTTALVMEALENVGLGRTI-DLM---PA 163
Cdd:PRK14271 88 RSI--FNYRDVLEFRRRVGMLFQRPNPF-PMSIMDNVLAGVRAHK--LVPRKEFRGVAQARLTEVGLWDAVkDRLsdsPF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 164 ELSGGMKRRIALARTLILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTssLIITHDVDCARVIADRMVLLVDGIN 243
Cdd:PRK14271 163 RLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTV--IIVTHNLAQAARISDRAALFFDGRL 240
|
250
....*....|..
gi 1234390149 244 YAEGSYTELSQS 255
Cdd:PRK14271 241 VEEGPTEQLFSS 252
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
49-241 |
3.84e-21 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 89.46 E-value: 3.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 49 LYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHtldeLRSD-IGFLFQ--GSALYDSMTVRENLE 125
Cdd:PRK15112 36 LREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS----YRSQrIRMIFQdpSTSLNPRQRISQILD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 126 FPLRRHKEKlgTPSDTTALVMEALENVGLGRT-IDLMPAELSGGMKRRIALARTLILKPKIILYDEPTSGLDPITAKEII 204
Cdd:PRK15112 112 FPLRLNTDL--EPEQREKQIIETLRQVGLLPDhASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLI 189
|
170 180 190
....*....|....*....|....*....|....*..
gi 1234390149 205 ELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:PRK15112 190 NLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQG 226
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
42-252 |
5.69e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 89.68 E-value: 5.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 42 LNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEI-ATLDR-HTLDELRSDIGFLFQ--GSALYDS 117
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpANLKKiKEVKRLRKEIGLVFQfpEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 118 mTVRENLEF-PLRRHKEKlgtpSDTTALVMEALENVGLGRT-IDLMPAELSGGMKRRIALARTLILKPKIILYDEPTSGL 195
Cdd:PRK13645 107 -TIEKDIAFgPVNLGENK----QEAYKKVPELLKLVQLPEDyVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1234390149 196 DPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEGSYTEL 252
Cdd:PRK13645 182 DPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEI 238
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
16-241 |
1.28e-20 |
|
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: 90.65 E-value: 1.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 16 VADRP----LE-RKAVIRIRDVrkSFG---DNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMG 87
Cdd:COG5265 342 VADAPdappLVvGGGEVRFENV--SFGydpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDG 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 88 KEIATLdrhTLDELRSDIGFLFQGSALYDSmTVRENLEFplrrhkeklGTPSDTTALVMEALENVGLGRTIDLMPA---- 163
Cdd:COG5265 420 QDIRDV---TQASLRAAIGIVPQDTVLFND-TIAYNIAY---------GRPDASEEEVEAAARAAQIHDFIESLPDgydt 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 164 -------ELSGGMKRRIALARTLILKPKIILYDEPTSGLDPITAKEIIELMRniQIKYNTSSLIITHdvdcaR----VIA 232
Cdd:COG5265 487 rvgerglKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALR--EVARGRTTLVIAH-----RlstiVDA 559
|
....*....
gi 1234390149 233 DRMVLLVDG 241
Cdd:COG5265 560 DEILVLEAG 568
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
52-255 |
1.81e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 90.29 E-value: 1.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 52 GENLVVMGKSGSGKSVMIKCLVGLmLPDSGYIEVMGKEIATLDrhtLDELRSDIGFLFQGSALYDSmTVRENLefplrrh 131
Cdd:PRK11174 376 GQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELD---PESWRKHLSWVGQNPQLPHG-TLRDNV------- 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 132 keKLGTPSDTTALVMEALENVGLGRTIDLMP-----------AELSGGMKRRIALARTLILKPKIILYDEPTSGLDPITA 200
Cdd:PRK11174 444 --LLGNPDASDEQLQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSE 521
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1234390149 201 KEIIE-LMRNIQikyNTSSLIITH---DVDCarviADRMVLLVDGINYAEGSYTELSQS 255
Cdd:PRK11174 522 QLVMQaLNAASR---RQTTLMVTHqleDLAQ----WDQIWVMQDGQIVQQGDYAELSQA 573
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
52-223 |
2.35e-20 |
|
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: 85.68 E-value: 2.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 52 GENLVVMGKSGSGKSVMIKCLVGL--MLPDSGYIEVMGKEIatldrhTLDELRSDIGFLFQGSALYDSMTVRENLEFP-- 127
Cdd:cd03213 35 GELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPL------DKRSFRKIIGYVPQDDILHPTLTVRETLMFAak 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 128 LRRhkeklgtpsdttalvmealenvglgrtidlmpaeLSGGMKRRIALARTLILKPKIILYDEPTSGLDPITAKEIIELM 207
Cdd:cd03213 109 LRG----------------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLL 154
|
170
....*....|....*.
gi 1234390149 208 RNIQiKYNTSSLIITH 223
Cdd:cd03213 155 RRLA-DTGRTIICSIH 169
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
25-252 |
4.65e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 86.10 E-value: 4.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 25 AVIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTldELRSD 104
Cdd:PRK10895 2 ATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA--RARRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 105 IGFLFQGSALYDSMTVRENLEFPLRRHKEKlgTPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPK 184
Cdd:PRK10895 80 IGYLPQEASIFRRLSVYDNLMAVLQIRDDL--SAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPK 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1234390149 185 IILYDEPTSGLDPITA---KEIIELMRNiqikYNTSSLIITHDVDCARVIADRMVLLVDGINYAEGSYTEL 252
Cdd:PRK10895 158 FILLDEPFAGVDPISVidiKRIIEHLRD----SGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
40-210 |
7.84e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 88.57 E-value: 7.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 40 HVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPD---SGYIEVMGKEIatldrhTLDELRSDIGFLFQGSALYD 116
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPI------DAKEMRAISAYVQQDDLFIP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 117 SMTVRENLEFPLRRHKEKLGTPSDTTALVMEALENVGLGR---TIDLMPAE---LSGGMKRRIALARTLILKPKIILYDE 190
Cdd:TIGR00955 113 TLTVREHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKcanTRIGVPGRvkgLSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180
....*....|....*....|
gi 1234390149 191 PTSGLDPITAKEIIELMRNI 210
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKGL 212
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
20-241 |
9.58e-20 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 84.83 E-value: 9.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 20 PLERKAVIRIRDVRKSF---GDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRH 96
Cdd:cd03248 5 PDHLKGIVKFQNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 97 TLdelRSDIGFLFQGSALYdSMTVRENLEFplrrhkeklGTPSDTTALVMEALENVGLGRTIDLMP-----------AEL 165
Cdd:cd03248 85 YL---HSKVSLVGQEPVLF-ARSLQDNIAY---------GLQSCSFECVKEAAQKAHAHSFISELAsgydtevgekgSQL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1234390149 166 SGGMKRRIALARTLILKPKIILYDEPTSGLDPITAKEIIELMRniQIKYNTSSLIITHDVDCARViADRMVLLVDG 241
Cdd:cd03248 152 SGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALY--DWPERRTVLVIAHRLSTVER-ADQILVLDGG 224
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
19-257 |
1.05e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 88.24 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 19 RPLERKAVIRIRDVRKSF---GDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDR 95
Cdd:TIGR00958 471 APLNLEGLIEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDH 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 96 HTLdelRSDIGFLFQGSALYdSMTVRENLEFPLRRHKEklgtpSDTTALVMEALEN---VGLGRTIDLMPAE----LSGG 168
Cdd:TIGR00958 551 HYL---HRQVALVGQEPVLF-SGSVRENIAYGLTDTPD-----EEIMAAAKAANAHdfiMEFPNGYDTEVGEkgsqLSGG 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 169 MKRRIALARTLILKPKIILYDEPTSGLDpitaKEIIELMRNIQIKYNTSSLIITHDVDCARViADRMVLLVDGINYAEGS 248
Cdd:TIGR00958 622 QKQRIAIARALVRKPRVLILDEATSALD----AECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGT 696
|
....*....
gi 1234390149 249 YTELSQSTD 257
Cdd:TIGR00958 697 HKQLMEDQG 705
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-241 |
1.90e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 87.41 E-value: 1.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 22 ERKAVIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLD---RHTL 98
Cdd:PRK15439 7 TAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpakAHQL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 99 delrsDIGFLFQGSALYDSMTVRENLEFPLRRHKEklgTPSDTTALVMEalenvgLGRTIDL-MPAELSGGMKRRIA-LA 176
Cdd:PRK15439 87 -----GIYLVPQEPLLFPNLSVKENILFGLPKRQA---SMQKMKQLLAA------LGCQLDLdSSAGSLEVADRQIVeIL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1234390149 177 RTLILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKyNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:PRK15439 153 RGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDG 216
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
36-257 |
2.24e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 85.06 E-value: 2.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 36 FGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLdELRSDIGFLFQGSALY 115
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLL-ALRQQVATVFQDPEQQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 116 DSMT-VRENLEFPLRrhkeKLGTPSDTTAL-VMEALENVGlGRTIDLMPAE-LSGGMKRRIALARTLILKPKIILYDEPT 192
Cdd:PRK13638 90 IFYTdIDSDIAFSLR----NLGVPEAEITRrVDEALTLVD-AQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1234390149 193 SGLDPITAKEIIELMRNIQIKYNtSSLIITHDVDCARVIADRMVLLVDGINYAEGSYTELSQSTD 257
Cdd:PRK13638 165 AGLDPAGRTQMIAIIRRIVAQGN-HVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTE 228
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
27-224 |
3.69e-19 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 81.34 E-value: 3.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEiatldrhtldelrsDIG 106
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV--------------KIG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 107 FLFQgsalydsmtvrenlefplrrhkeklgtpsdttalvmealenvglgrtidlmpaeLSGGMKRRIALARTLILKPKII 186
Cdd:cd03221 67 YFEQ------------------------------------------------------LSGGEKMRLALAKLLLENPNLL 92
|
170 180 190
....*....|....*....|....*....|....*...
gi 1234390149 187 LYDEPTSGLDPITAKEIIELMRNiqikYNTSSLIITHD 224
Cdd:cd03221 93 LLDEPTNHLDLESIEALEEALKE----YPGTVILVSHD 126
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
40-231 |
3.74e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 85.14 E-value: 3.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 40 HVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKeIATLDRHtldELRSDIGFLF-QGSALYDSM 118
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGY-VPFKRRK---EFARRIGVVFgQRSQLWWDL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 119 TVRENLEF-------PLRRHKEKLGTpsdttaLVmEALEnvgLGRTIDLMPAELSGG--MKRRIALArtLILKPKIILYD 189
Cdd:COG4586 112 PAIDSFRLlkaiyriPDAEYKKRLDE------LV-ELLD---LGELLDTPVRQLSLGqrMRCELAAA--LLHRPKILFLD 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1234390149 190 EPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVD-----CARVI 231
Cdd:COG4586 180 EPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDdiealCDRVI 226
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
41-241 |
3.97e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 86.30 E-value: 3.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 41 VLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLmLPD------SGYIEVMGKEIATLDRHTLDELRSD-IGFLFQG-- 111
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSVTALSILRL-LPSppvvypSGDIRFHGESLLHASEQTLRGVRGNkIAMIFQEpm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 112 SALYDSMTVRENLEFPLRRHKEKLGTPSDTTALvmEALENVGL----GRTIDLmPAELSGGMKRRIALARTLILKPKIIL 187
Cdd:PRK15134 103 VSLNPLHTLEKQLYEVLSLHRGMRREAARGEIL--NCLDRVGIrqaaKRLTDY-PHQLSGGERQRVMIAMALLTRPELLI 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1234390149 188 YDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:PRK15134 180 ADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNG 233
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
24-241 |
7.19e-19 |
|
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: 81.32 E-value: 7.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 24 KAVIRIRDVRKSfgdnHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATldRHTLDELRS 103
Cdd:cd03215 2 EPVLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTR--RSPRDAIRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 104 DIGFL---FQGSALYDSMTVRENLefplrrhkeklgtpsdttalvmealenvglgrtidLMPAELSGGMKRRIALARTLI 180
Cdd:cd03215 76 GIAYVpedRKREGLVLDLSVAENI-----------------------------------ALSSLLSGGNQQKVVLARWLA 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1234390149 181 LKPKIILYDEPTSGLDPITAKEIIELMRNIQiKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:cd03215 121 RDPRVLILDEPTRGVDVGAKAEIYRLIRELA-DAGKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
16-255 |
8.86e-19 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 85.40 E-value: 8.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 16 VADRP----LER-KAVIRIRDVRKSF-GDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKE 89
Cdd:PRK13657 319 VRDPPgaidLGRvKGAVEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 90 IATLdrhTLDELRSDIGFLFQGSALYDSmTVRENLefplrrhkeKLGTPSDTTALVMEALE-----------------NV 152
Cdd:PRK13657 399 IRTV---TRASLRRNIAVVFQDAGLFNR-SIEDNI---------RVGRPDATDEEMRAAAEraqahdfierkpdgydtVV 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 153 G-LGRtidlmpaELSGGMKRRIALARTLILKPKIILYDEPTSGLDPIT-AK---EIIELMRniqikyNTSSLIITHDVDC 227
Cdd:PRK13657 466 GeRGR-------QLSGGERQRLAIARALLKDPPILILDEATSALDVETeAKvkaALDELMK------GRTTFIIAHRLST 532
|
250 260
....*....|....*....|....*...
gi 1234390149 228 ARViADRMVLLVDGINYAEGSYTELSQS 255
Cdd:PRK13657 533 VRN-ADRILVFDNGRVVESGSFDELVAR 559
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
32-241 |
9.92e-19 |
|
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: 82.38 E-value: 9.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 32 VRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGkEIATLDRhtlDELRSDIGFLF-Q 110
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-LVPWKRR---KKFLRRIGVVFgQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 111 GSALYDSMTVRENLEF-------PLRRHKEKLgtpsdttALVMEALEnvgLGRTIDLMPAELSGGMKRRIALARTLILKP 183
Cdd:cd03267 103 KTQLWWDLPVIDSFYLlaaiydlPPARFKKRL-------DELSELLD---LEELLDTPVRQLSLGQRMRAEIAAALLHEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1234390149 184 KIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:cd03267 173 EILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKG 230
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
9-209 |
1.39e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 85.18 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 9 KHKDQEGVADRPLERKA----VIRIRDVRKSFGD----NHVlngfDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDS 80
Cdd:NF033858 245 KRRGHQPVVIPPRPADDddepAIEARGLTMRFGDftavDHV----SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 81 GYIEVMGKEIATLDRHTldelRSDIGFLFQGSALYDSMTVRENLE-----FPLrrhkeklgTPSDTTALVMEALENVGLG 155
Cdd:NF033858 321 GEAWLFGQPVDAGDIAT----RRRVGYMSQAFSLYGELTVRQNLElharlFHL--------PAAEIAARVAEMLERFDLA 388
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1234390149 156 RTIDLMPAELSGGMKRRIALARTLILKPKIILYDEPTSGLDPItAKE-----IIELMRN 209
Cdd:NF033858 389 DVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPV-ARDmfwrlLIELSRE 446
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
57-255 |
1.85e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 83.39 E-value: 1.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 57 VMGKSGSGKSVMIKCLVGLMLPDSGYIevmgkeiaTLDRHTLDELRSD---------IGFLFQGSALYDSMTVRENLEFP 127
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRI--------VLNGRVLFDAEKGiclppekrrIGYVFQDARLFPHYKVRGNLRYG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 128 LRRhkeklGTPSDTTALVmealENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKIILYDEPTSGLDPITAKEIIELM 207
Cdd:PRK11144 101 MAK-----SMVAQFDKIV----ALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1234390149 208 RNIQIKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEGSYTELSQS 255
Cdd:PRK11144 172 ERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWAS 219
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
28-240 |
3.58e-18 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 80.77 E-value: 3.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 28 RIRDVRKSFG------DNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLML--PDSGYIEVMGKEIatldrhtld 99
Cdd:COG2401 26 RVAIVLEAFGvelrvvERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQF--------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 100 elrsdigflfqgsalYDSMTVRENLefplrrhkeklgTPSDTTALVMEALENVGLGRTIDLM--PAELSGGMKRRIALAR 177
Cdd:COG2401 97 ---------------GREASLIDAI------------GRKGDFKDAVELLNAVGLSDAVLWLrrFKELSTGQKFRFRLAL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1234390149 178 TLILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVD 240
Cdd:COG2401 150 LLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVIDDLQPDLLIFVG 212
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
18-247 |
4.38e-18 |
|
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: 80.27 E-value: 4.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 18 DRPLERKAVIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKeIATLdrht 97
Cdd:cd03220 14 KGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR-VSSL---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 98 ldelrsdIGFlfqGSALYDSMTVRENLEFPLRrhkeKLG-TPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALA 176
Cdd:cd03220 89 -------LGL---GGGFNPELTGRENIYLNGR----LLGlSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1234390149 177 RTLILKPKIILYDEPTSGLDPITAKEIIELMRNiQIKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEG 247
Cdd:cd03220 155 IATALEPDILLIDEVLAVGDAAFQEKCQRRLRE-LLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
27-209 |
7.31e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 82.55 E-value: 7.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNHVL-NGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGyievmgkeiaTLDRHTLDEL---- 101
Cdd:COG4178 363 LALEDLTLRTPDGRPLlEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSG----------RIARPAGARVlflp 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 102 -RSdigFLFQGsalydsmTVRENLEFPlrrhkeklGTPSDTT-ALVMEALENVGLGRTIDLMPAE------LSGGMKRRI 173
Cdd:COG4178 433 qRP---YLPLG-------TLREALLYP--------ATAEAFSdAELREALEAVGLGHLAERLDEEadwdqvLSLGEQQRL 494
|
170 180 190
....*....|....*....|....*....|....*.
gi 1234390149 174 ALARTLILKPKIILYDEPTSGLDPITAKEIIELMRN 209
Cdd:COG4178 495 AFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE 530
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
27-241 |
1.79e-17 |
|
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: 78.34 E-value: 1.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLM--LPDSGYIEVMGKEIATLDRHtlDELRSD 104
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPE--ERARLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 105 IGFLFQGSALYDSMTVrenlefplrrhkeklgtpsdttalvMEALENVGLGrtidlmpaeLSGGMKRRIALARTLILKPK 184
Cdd:cd03217 79 IFLAFQYPPEIPGVKN-------------------------ADFLRYVNEG---------FSGGEKKRNEILQLLLLEPD 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1234390149 185 IILYDEPTSGLDpITAKEIIELMRNIQIKYNTSSLIITHDVDCAR-VIADRMVLLVDG 241
Cdd:cd03217 125 LAILDEPDSGLD-IDALRLVAEVINKLREEGKSVLIITHYQRLLDyIKPDRVHVLYDG 181
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
51-252 |
2.04e-17 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 80.17 E-value: 2.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 51 EGENLVVMGKSGSGKSVMIKCLVGLmlpdsgyIEVMGKEIA---TLDRHTLDELR---------SDIGFLFQG--SALYD 116
Cdd:PRK11022 32 QGEVVGIVGESGSGKSVSSLAIMGL-------IDYPGRVMAeklEFNGQDLQRISekerrnlvgAEVAMIFQDpmTSLNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 117 SMTVRENLEFPLRRHKEklGTPSDTTALVMEALENVGL---GRTIDLMPAELSGGMKRRIALARTLILKPKIILYDEPTS 193
Cdd:PRK11022 105 CYTVGFQIMEAIKVHQG--GNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTT 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1234390149 194 GLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEGSYTEL 252
Cdd:PRK11022 183 ALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
35-238 |
2.29e-17 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 78.35 E-value: 2.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 35 SFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLdelrsdIGFLFQGSAL 114
Cdd:PRK13543 20 SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRF------MAYLGHLPGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 115 YDSMTVRENLEFPLRRH-KEKLGTPSDttalvmeALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKIILYDEPTS 193
Cdd:PRK13543 94 KADLSTLENLHFLCGLHgRRAKQMPGS-------ALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1234390149 194 GLDP--ITakeIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLL 238
Cdd:PRK13543 167 NLDLegIT---LVNRMISAHLRGGGAALVTTHGAYAAPPVRTRMLTL 210
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
26-225 |
3.50e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 78.62 E-value: 3.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 26 VIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKeiatldrhtldeLRsdI 105
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK------------LR--I 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 106 GFLFQGSALYDSMtvrenlefPLRRHKEKLGTPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKI 185
Cdd:PRK09544 70 GYVPQKLYLDTTL--------PLTVNRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1234390149 186 ILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDV 225
Cdd:PRK09544 142 LVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDL 181
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
49-252 |
3.70e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 80.67 E-value: 3.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 49 LYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMG-------KEIATLDRHTLDELR----SDIGFLFQG--SALY 115
Cdd:PRK10261 39 LQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsRQVIELSEQSAAQMRhvrgADMAMIFQEpmTSLN 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 116 DSMTVRENLEFPLRRHKEKLGTPSDTTALVMeaLENVGLGRTIDLM---PAELSGGMKRRIALARTLILKPKIILYDEPT 192
Cdd:PRK10261 119 PVFTVGEQIAESIRLHQGASREEAMVEAKRM--LDQVRIPEAQTILsryPHQLSGGMRQRVMIAMALSCRPAVLIADEPT 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 193 SGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEGSYTEL 252
Cdd:PRK10261 197 TALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
26-233 |
7.98e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 77.90 E-value: 7.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 26 VIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGL--MLPD---SGYIEVMGKEIATLDRHTLdE 100
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGfrvEGKVTFHGKNLYAPDVDPV-E 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 101 LRSDIGFLFQGSALYdSMTVRENLEFPLRrhkeKLGTPSDTTALVMEALENVGLGRTI-DLMPAE---LSGGMKRRIALA 176
Cdd:PRK14243 89 VRRRIGMVFQKPNPF-PKSIYDNIAYGAR----INGYKGDMDELVERSLRQAALWDEVkDKLKQSglsLSGGQQQRLCIA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1234390149 177 RTLILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTssLIITHDVDCARVIAD 233
Cdd:PRK14243 164 RAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTI--IIVTHNMQQAARVSD 218
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
52-241 |
1.04e-16 |
|
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: 79.67 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 52 GENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATldrhTLDELRSDIGFLFQGSALYDSMTVRENLEFPLRRH 131
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT----NISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLR 2040
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 132 keklGTPSDTTALVME-ALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKIILYDEPTSGLDPITAKEIIELMRNI 210
Cdd:TIGR01257 2041 ----GVPAEEIEKVANwSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSI 2116
|
170 180 190
....*....|....*....|....*....|.
gi 1234390149 211 qIKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:TIGR01257 2117 -IREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
41-231 |
1.81e-16 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 75.53 E-value: 1.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 41 VLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDrhtLDELRSDIGFLFQGSALYDSmTV 120
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIP---LEDLRSSLTIIPQDPTLFSG-TI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 121 RENLEfPLRRHKEKLgtpsdttalVMEALENVGLGrtidlmpAELSGGMKRRIALARTLILKPKIILYDEPTSGLDPITA 200
Cdd:cd03369 99 RSNLD-PFDEYSDEE---------IYGALRVSEGG-------LNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATD 161
|
170 180 190
....*....|....*....|....*....|....*
gi 1234390149 201 KEIIELMRniQIKYNTSSLIITHD----VDCARVI 231
Cdd:cd03369 162 ALIQKTIR--EEFTNSTILTIAHRlrtiIDYDKIL 194
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
26-241 |
1.83e-16 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 76.66 E-value: 1.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 26 VIRIRDVRKSfGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPD----SGYIEVMGKEIAtldrhtLDEL 101
Cdd:PRK10418 4 QIELRNIALQ-AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGKPVA------PCAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 102 RS-DIGFLFQG--SALYDSMTVRENLEFPLRrhkeKLGTPSDTtALVMEALENVGLG---RTIDLMPAELSGGMKRRIAL 175
Cdd:PRK10418 77 RGrKIATIMQNprSAFNPLHTMHTHARETCL----ALGKPADD-ATLTAALEAVGLEnaaRVLKLYPFEMSGGMLQRMMI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1234390149 176 ARTLILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:PRK10418 152 ALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHG 217
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
28-216 |
5.30e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 77.23 E-value: 5.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 28 RIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSgyieVMGKEIATlDRHTLDELRSDIGF 107
Cdd:PLN03211 70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNN----FTGTILAN-NRKPTKQILKRTGF 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 108 LFQGSALYDSMTVRENLEF--------PLRRHKEKLGTPSDTTALVMEALENVGLGRTidlMPAELSGGMKRRIALARTL 179
Cdd:PLN03211 145 VTQDDILYPHLTVRETLVFcsllrlpkSLTKQEKILVAESVISELGLTKCENTIIGNS---FIRGISGGERKRVSIAHEM 221
|
170 180 190
....*....|....*....|....*....|....*..
gi 1234390149 180 ILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNT 216
Cdd:PLN03211 222 LINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKT 258
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
42-221 |
7.28e-16 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 73.84 E-value: 7.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 42 LNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMlpdSGYIEVMGKeiATLDRHTLDELRSdigfLFQGSALYDS---- 117
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRT---EGNVSVEGD--IHYNGIPYKEFAE----KYPGEIIYVSeedv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 118 ----MTVRENLEFPLRrhkeklgtpsdttalvMEALENVglgRTIdlmpaelSGGMKRRIALARTLILKPKIILYDEPTS 193
Cdd:cd03233 94 hfptLTVRETLDFALR----------------CKGNEFV---RGI-------SGGERKRVSIAEALVSRASVLCWDNSTR 147
|
170 180
....*....|....*....|....*...
gi 1234390149 194 GLDPITAKEIIELMRNIQIKYNTSSLII 221
Cdd:cd03233 148 GLDSSTALEILKCIRTMADVLKTTTFVS 175
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
26-241 |
1.09e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 74.35 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 26 VIRIRDVRKSF----------------------GDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYI 83
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 84 EVMGKeIATLdrhtldelrsdIGFlfqGSALYDSMTVRENLEFPLRRhkekLG-TPSDTTALVMEALENVGLGRTIDlMP 162
Cdd:COG1134 84 EVNGR-VSAL-----------LEL---GAGFHPELTGRENIYLNGRL----LGlSRKEIDEKFDEIVEFAELGDFID-QP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 163 AE-LSGGMKRRIALARTLILKPKIILYDEPTSGLDPITAKEIIELMRNIqIKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:COG1134 144 VKtYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIREL-RESGRTVIFVSHSMGAVRRLCDRAIWLEKG 222
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
34-208 |
1.55e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 75.83 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 34 KSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATldRHTLDELRSDIGFL----- 108
Cdd:COG1129 260 EGLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRI--RSPRDAIRAGIAYVpedrk 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 109 FQGSALydSMTVRENLEFPLRRHKEKLG--TPSDTTALVMEALENVGLgRT--IDLMPAELSGGMKRRIALARTLILKPK 184
Cdd:COG1129 338 GEGLVL--DLSIRENITLASLDRLSRGGllDRRRERALAEEYIKRLRI-KTpsPEQPVGNLSGGNQQKVVLAKWLATDPK 414
|
170 180
....*....|....*....|....*
gi 1234390149 185 IILYDEPTSGLDpITAK-EIIELMR 208
Cdd:COG1129 415 VLILDEPTRGID-VGAKaEIYRLIR 438
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
27-241 |
1.65e-15 |
|
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: 72.89 E-value: 1.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDV-----RKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKeiatldrhtldel 101
Cdd:cd03250 1 ISVEDAsftwdSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 102 rsdIGFLFQGSALYdSMTVRENLEFPLRRHKEKLgtpsdttalvMEALENVGLGRTIDLMPA-------E----LSGGMK 170
Cdd:cd03250 68 ---IAYVSQEPWIQ-NGTIRENILFGKPFDEERY----------EKVIKACALEPDLEILPDgdlteigEkginLSGGQK 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1234390149 171 RRIALARTLILKPKIILYDEPTSGLDPITAKEIIE-----LMRNiqikyNTSSLIITHDVDcARVIADRMVLLVDG 241
Cdd:cd03250 134 QRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncilgLLLN-----NKTRILVTHQLQ-LLPHADQIVVLDNG 203
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
25-210 |
3.65e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 74.56 E-value: 3.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 25 AVIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATldRHTLDELRSD 104
Cdd:PRK11288 3 PYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRF--ASTTAALAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 105 IGFLFQGSALYDSMTVRENL---EFPLRR---HKEKLgtpsdtTALVMEALENVGlgrtIDLMP----AELSGGMKRRIA 174
Cdd:PRK11288 81 VAIIYQELHLVPEMTVAENLylgQLPHKGgivNRRLL------NYEAREQLEHLG----VDIDPdtplKYLSIGQRQMVE 150
|
170 180 190
....*....|....*....|....*....|....*.
gi 1234390149 175 LARTLILKPKIILYDEPTSGLdpiTAKEIIELMRNI 210
Cdd:PRK11288 151 IAKALARNARVIAFDEPTSSL---SAREIEQLFRVI 183
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
32-224 |
9.24e-15 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 73.43 E-value: 9.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 32 VRKSFGDN-HVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLmlpDSGYI-EVMGKEIATldrhtldelrsdIGFLF 109
Cdd:TIGR03719 10 VSKVVPPKkEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV---DKDFNgEARPQPGIK------------VGYLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 110 QGSALYDSMTVRENLEFPLRRHK----------EKLGTPS-DTTALV--MEALENV-------GLGRTIDL-MPA----- 163
Cdd:TIGR03719 75 QEPQLDPTKTVRENVEEGVAEIKdaldrfneisAKYAEPDaDFDKLAaeQAELQEIidaadawDLDSQLEIaMDAlrcpp 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1234390149 164 ------ELSGGMKRRIALARTLILKPKIILYDEPTSGLDpitAKEIIELMRNIQiKYNTSSLIITHD 224
Cdd:TIGR03719 155 wdadvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD---AESVAWLERHLQ-EYPGTVVAVTHD 217
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
24-252 |
9.74e-15 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 72.85 E-value: 9.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 24 KAVIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSG--KSVMIKCLVGlmlPDSGYIEVMGKEIATLDRhtldEL 101
Cdd:NF000106 11 RNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPWRF*TWCANRR----AL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 102 RSDIGF---LFQGSAlyDSMTVRENLeFPLRRHKEKlgTPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALART 178
Cdd:NF000106 84 RRTIG*hrpVR*GRR--ESFSGRENL-YMIGR*LDL--SRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAAS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1234390149 179 LILKPKIILYDEPTSGLDPITAKEIIELMRNIqIKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEGSYTEL 252
Cdd:NF000106 159 MIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSM-VRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
36-252 |
1.16e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 71.94 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 36 FGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIatlDRHTLDELRSDIGFLFQGSALY 115
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHI---QHYASKEVARRIGLLAQNATTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 116 DSMTVRENL---EFP-----LRRHKEklgtpsDTTAlVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKIIL 187
Cdd:PRK10253 94 GDITVQELVargRYPhqplfTRWRKE------DEEA-VTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1234390149 188 YDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEGSYTEL 252
Cdd:PRK10253 167 LDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
25-238 |
1.26e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 73.06 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 25 AVIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATldRHTLDELRSD 104
Cdd:PRK11147 2 SLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVA--RLQQDPPRNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 105 IGFLFQgsalYDSMTVRENLEFPLRRHK--EKLGT-PSDTT----ALVMEALENVG--------------LGRTIDLMPA 163
Cdd:PRK11147 80 EGTVYD----FVAEGIEEQAEYLKRYHDisHLVETdPSEKNlnelAKLQEQLDHHNlwqlenrinevlaqLGLDPDAALS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1234390149 164 ELSGGMKRRIALARTLILKPKIILYDEPTSGLDpITAkeiIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLL 238
Cdd:PRK11147 156 SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD-IET---IEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDL 226
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
29-241 |
1.79e-14 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 70.87 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 29 IRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLmlPD----SGYIEVMGKEIATLDrhtLDElRSD 104
Cdd:COG0396 3 IKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGH--PKyevtSGSILLDGEDILELS---PDE-RAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 105 IG-FL-FQ------GsalydsMTVRENLEFPLRRHKEKLGTPSDTTALVMEALENVG-----LGRTIDlmpAELSGGMKR 171
Cdd:COG0396 77 AGiFLaFQypveipG------VSVSNFLRTALNARRGEELSAREFLKLLKEKMKELGldedfLDRYVN---EGFSGGEKK 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1234390149 172 RIALARTLILKPKIILYDEPTSGLDpITA----KEIIELMRNiqikYNTSSLIITHDvdcAR----VIADRMVLLVDG 241
Cdd:COG0396 148 RNEILQMLLLEPKLAILDETDSGLD-IDAlrivAEGVNKLRS----PDRGILIITHY---QRildyIKPDFVHVLVDG 217
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
24-241 |
1.96e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 70.68 E-value: 1.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 24 KAVIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIAtlDRHTLDELRS 103
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDIT--DWQTAKIMRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 104 DIGFLFQGSALYDSMTVRENLefplrrhkeKLGTPSDTTALVMEALEnvglgRTIDLMP----------AELSGGMKRRI 173
Cdd:PRK11614 81 AVAIVPEGRRVFSRMTVEENL---------AMGGFFAERDQFQERIK-----WVYELFPrlherriqraGTMSGGEQQML 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1234390149 174 ALARTLILKPKIILYDEPTSGLDPITAKEIIELMRNIQiKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:PRK11614 147 AIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLR-EQGMTIFLVEQNANQALKLADRGYVLENG 213
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
41-248 |
4.53e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 70.24 E-value: 4.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 41 VLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGlMLPDS---------GYIEVMGKEIATLDRHTLDELRSdigFLFQG 111
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG-DLTGGgaprgarvtGDVTLNGEPLAAIDAPRLARLRA---VLPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 112 SALYDSMTVRENLEFPLRRHKEKLGTPS-DTTALVMEALENVG----LGRTIdlmpAELSGGMKRRIALARTL------- 179
Cdd:PRK13547 92 AQPAFAFSAREIVLLGRYPHARRAGALThRDGEIAWQALALAGatalVGRDV----TTLSGGELARVQFARVLaqlwpph 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1234390149 180 --ILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEGS 248
Cdd:PRK13547 168 daAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGA 238
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
11-252 |
6.63e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 70.90 E-value: 6.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 11 KDQEGVADRPLERKAvIRIRDVRKSF-GDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKE 89
Cdd:PRK10790 326 RQQYGNDDRPLQSGR-IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRP 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 90 IATLDRHTLdelRSDIGFLFQGSA-LYDSMTVRENLEFPLRRHKeklgtpsdttalVMEALENVGLGRTIDLMPA----- 163
Cdd:PRK10790 405 LSSLSHSVL---RQGVAMVQQDPVvLADTFLANVTLGRDISEEQ------------VWQALETVQLAELARSLPDglytp 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 164 ------ELSGGMKRRIALARTLILKPKIILYDEPTSGLDPITAKEIIELMRniQIKYNTSSLIITHDVDCArVIADRMVL 237
Cdd:PRK10790 470 lgeqgnNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALA--AVREHTTLVVIAHRLSTI-VEADTILV 546
|
250
....*....|....*
gi 1234390149 238 LVDGINYAEGSYTEL 252
Cdd:PRK10790 547 LHRGQAVEQGTHQQL 561
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
48-242 |
8.90e-14 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 68.97 E-value: 8.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 48 DLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIAtldrHTLDELRSDIgflfqgsalydSMTVRENLEFP 127
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS----YKPQYIKADY-----------EGTVRDLLSSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 128 LRRHkeklGTPSDTTALVMEALenvGLGRTIDLMPAELSGGMKRRIALARTLILKPKIILYDEPTSGLDP---ITAKEII 204
Cdd:cd03237 86 TKDF----YTHPYFKTEIAKPL---QIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVeqrLMASKVI 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 1234390149 205 elmRNIQIKYNTSSLIITHDVDCARVIADRmVLLVDGI 242
Cdd:cd03237 159 ---RRFAENNEKTAFVVEHDIIMIDYLADR-LIVFEGE 192
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
22-223 |
1.54e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 68.51 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 22 ERKAVIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGlmLPD----SGYIEVMGKEIATLDrht 97
Cdd:CHL00131 3 KNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLE--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 98 lDELRSDIG-FL-FQGSALYDSMTvreNLEFpLR-----RHKEKLGTPSDTTA---LVMEALENVG-----LGRTIDlmp 162
Cdd:CHL00131 78 -PEERAHLGiFLaFQYPIEIPGVS---NADF-LRlaynsKRKFQGLPELDPLEfleIINEKLKLVGmdpsfLSRNVN--- 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1234390149 163 AELSGGMKRRIALARTLILKPKIILYDEPTSGLDpITAKEIIELMRNIQIKYNTSSLIITH 223
Cdd:CHL00131 150 EGFSGGEKKRNEILQMALLDSELAILDETDSGLD-IDALKIIAEGINKLMTSENSIILITH 209
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
40-238 |
2.32e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 68.78 E-value: 2.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 40 HVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLmLPDSGYIevmgkeiaTLDRHTLDE--------------LRSDI 105
Cdd:COG4170 21 KAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGI-TKDNWHV--------TADRFRWNGidllklsprerrkiIGREI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 106 GFLFQ--GSALYDSMTVRENLEFPL----------RRHKEKlgtpsdtTALVMEALENVGLGRTIDLM---PAELSGGMK 170
Cdd:COG4170 92 AMIFQepSSCLDPSAKIGDQLIEAIpswtfkgkwwQRFKWR-------KKRAIELLHRVGIKDHKDIMnsyPHELTEGEC 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1234390149 171 RRIALARTLILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLL 238
Cdd:COG4170 165 QKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVL 232
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
32-208 |
3.43e-13 |
|
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: 67.57 E-value: 3.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 32 VRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDsGYIEVMGkeiATLDRHTLDELRSDIGFLFQG 111
Cdd:cd03289 10 AKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDG---VSWNSVPLQKWRKAFGVIPQK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 112 SALYdSMTVRENLEfPLRRHKEKLgtpsdttalVMEALENVGLGRTIDLMPAEL-----------SGGMKRRIALARTLI 180
Cdd:cd03289 86 VFIF-SGTFRKNLD-PYGKWSDEE---------IWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVL 154
|
170 180
....*....|....*....|....*...
gi 1234390149 181 LKPKIILYDEPTSGLDPITAKEIIELMR 208
Cdd:cd03289 155 SKAKILLLDEPSAHLDPITYQVIRKTLK 182
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
36-204 |
3.83e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 66.51 E-value: 3.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 36 FGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATlDRHTLDElrsDIGFLFQGSALY 115
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQK---QLCFVGHRSGIN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 116 DSMTVRENLEFPLRRHKEKLGtpsdttalVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKIILYDEPTSGL 195
Cdd:PRK13540 87 PYLTLRENCLYDIHFSPGAVG--------ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVAL 158
|
....*....
gi 1234390149 196 DPITAKEII 204
Cdd:PRK13540 159 DELSLLTII 167
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-241 |
4.36e-13 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 68.66 E-value: 4.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 3 DDPTTYKHKDQEGVADrPLerkavIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGY 82
Cdd:PRK10636 295 DNPFHFSFRAPESLPN-PL-----LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGE 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 83 IEVM-GKEIATLDRHTLDELRSDigflfqgsalydsmtvrenlEFPLrRHKEKLGtPSDTTALVMEALENVGL-GRTIDL 160
Cdd:PRK10636 369 IGLAkGIKLGYFAQHQLEFLRAD--------------------ESPL-QHLARLA-PQELEQKLRDYLGGFGFqGDKVTE 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 161 MPAELSGGMKRRIALARTLILKPKIILYDEPTSGLDPITAKEIIELMrniqIKYNTSSLIITHDVDCARVIADRMVLLVD 240
Cdd:PRK10636 427 ETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEAL----IDFEGALVVVSHDRHLLRSTTDDLYLVHD 502
|
.
gi 1234390149 241 G 241
Cdd:PRK10636 503 G 503
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
38-266 |
5.64e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 68.46 E-value: 5.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 38 DNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGlmlpdsgyiEVMGKEIATLDrhtldeLRSDIGFLFQGSALYDS 117
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG---------ELSHAETSSVV------IRGSVAYVPQVSWIFNA 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 118 mTVRENLEFPLRRHKEKLGTPSDTTALVMEALENVGLGRT-IDLMPAELSGGMKRRIALARTLILKPKIILYDEPTSGLD 196
Cdd:PLN03232 694 -TVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTeIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 197 PITAKEIIELMRNIQIKYNTSSLiITHDVDCARVIaDRMVLLVDGINYAEGSYTELSQSTDpkveaFFKK 266
Cdd:PLN03232 773 AHVAHQVFDSCMKDELKGKTRVL-VTNQLHFLPLM-DRIILVSEGMIKEEGTFAELSKSGS-----LFKK 835
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
27-208 |
7.03e-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: 7.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNHVL-NGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGyievmgkeiaTLDRHTldelRSDI 105
Cdd:cd03223 1 IELENLSLATPDGRVLlKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSG----------RIGMPE----GEDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 106 GFLFQGSALYDSmTVRENLEFPLRRhkeklgtpsdttalvmealenvglgrtidlmpaELSGGMKRRIALARTLILKPKI 185
Cdd:cd03223 67 LFLPQRPYLPLG-TLREQLIYPWDD---------------------------------VLSGGEQQRLAFARLLLHKPKF 112
|
170 180
....*....|....*....|...
gi 1234390149 186 ILYDEPTSGLDPITAKEIIELMR 208
Cdd:cd03223 113 VFLDEATSALDEESEDRLYQLLK 135
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
26-241 |
7.08e-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: 67.93 E-value: 7.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 26 VIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMlPD---SGYIEVMGKEIATldRHTLDELR 102
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPLKA--SNIRDTER 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 103 SDIGFLFQGSALYDSMTVRENL----EFPLRrhkeklGTPSDTTALVMEAlENVGLGRTIDLMP-----AELSGGMKRRI 173
Cdd:TIGR02633 78 AGIVIIHQELTLVPELSVAENIflgnEITLP------GGRMAYNAMYLRA-KNLLRELQLDADNvtrpvGDYGGGQQQLV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1234390149 174 ALARTLILKPKIILYDEPTSGLdpiTAKEI---IELMRNIQiKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:TIGR02633 151 EIAKALNKQARLLILDEPSSSL---TEKETeilLDIIRDLK-AHGVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
31-210 |
1.23e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 67.44 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 31 DVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMlpDSGYIEvmgKEIATLDRHTLDEL--RSdIGFL 108
Cdd:TIGR00956 768 EVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERV--TTGVIT---GGDRLVNGRPLDSSfqRS-IGYV 841
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 109 FQGSALYDSMTVRENLEFP--LRRHKE-KLGTPSDTTALVMEALENVGLGRTIDLMPAE-LSGGMKRRIALARTLILKPK 184
Cdd:TIGR00956 842 QQQDLHLPTSTVRESLRFSayLRQPKSvSKSEKMEYVEEVIKLLEMESYADAVVGVPGEgLNVEQRKRLTIGVELVAKPK 921
|
170 180
....*....|....*....|....*..
gi 1234390149 185 IILY-DEPTSGLDPITAKEIIELMRNI 210
Cdd:TIGR00956 922 LLLFlDEPTSGLDSQTAWSICKLMRKL 948
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
18-251 |
1.48e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 66.84 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 18 DRPLERKAVIrIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGyiEVMGKEIAtldrht 97
Cdd:PRK15064 312 DKKLHRNALE-VENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSG--TVKWSENA------ 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 98 ldelrsDIGFLFQGSA--------LYDSMTvrenlefplrrhkeKLGTPSDTTALVMEAlenvgLGR------TIDLMPA 163
Cdd:PRK15064 383 ------NIGYYAQDHAydfendltLFDWMS--------------QWRQEGDDEQAVRGT-----LGRllfsqdDIKKSVK 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 164 ELSGGMKRRIALARTLILKPKIILYDEPTSGLDpitaKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMV-LLVDGI 242
Cdd:PRK15064 438 VLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMD----MESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIeITPDGV 513
|
....*....
gi 1234390149 243 NYAEGSYTE 251
Cdd:PRK15064 514 VDFSGTYEE 522
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
22-236 |
1.54e-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: 67.12 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 22 ERKAVIRIRDVRKSFGdnhvlnGFDMD-----LYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEvMGKEIAtldrH 96
Cdd:COG1245 337 EEETLVEYPDLTKSYG------GFSLEveggeIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD-EDLKIS----Y 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 97 TLDELRSDIgflfqgsalydSMTVRENLEfplrrhkEKLGTPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALA 176
Cdd:COG1245 406 KPQYISPDY-----------DGTVEEFLR-------SANTDDFGSSYYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIA 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1234390149 177 RTLILKPKIILYDEPTSGLDP----ITAKEIIELMRNiqikYNTSSLIITHDVDCARVIADRMV 236
Cdd:COG1245 468 ACLSRDADLYLLDEPSAHLDVeqrlAVAKAIRRFAEN----RGKTAMVVDHDIYLIDYISDRLM 527
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
26-251 |
1.69e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 66.88 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 26 VIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVmGK--EIATLD--RHTLDEL 101
Cdd:TIGR03719 322 VIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GEtvKLAYVDqsRDALDPN 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 102 RSdigfLFQG-SALYDSMTVrENLEFPLRRHKEKLG-TPSDTTALVmealenvglgrtidlmpAELSGGMKRRIALARTL 179
Cdd:TIGR03719 401 KT----VWEEiSGGLDIIKL-GKREIPSRAYVGRFNfKGSDQQKKV-----------------GQLSGGERNRVHLAKTL 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 180 ILKPKIILYDEPTSGLDpitakeiIELMRNIQ---IKYNTSSLIITHDvdcaRVIADRM---VLLVDG---INYAEGSYT 250
Cdd:TIGR03719 459 KSGGNVLLLDEPTNDLD-------VETLRALEealLNFAGCAVVISHD----RWFLDRIathILAFEGdshVEWFEGNFS 527
|
.
gi 1234390149 251 E 251
Cdd:TIGR03719 528 E 528
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
26-197 |
1.90e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 66.69 E-value: 1.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 26 VIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIAtlDRHTLDELRSDI 105
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA--DARHRRAVCPRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 106 GFLFQ--GSALYDSMTVRENLEF---------PLRRHKeklgtpsdttalVMEALENVGLGRTIDlMPA-ELSGGMKRRI 173
Cdd:NF033858 79 AYMPQglGKNLYPTLSVFENLDFfgrlfgqdaAERRRR------------IDELLRATGLAPFAD-RPAgKLSGGMKQKL 145
|
170 180
....*....|....*....|....
gi 1234390149 174 ALARTLILKPKIILYDEPTSGLDP 197
Cdd:NF033858 146 GLCCALIHDPDLLILDEPTTGVDP 169
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
41-258 |
1.92e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 67.07 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 41 VLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDrhtLDELRSDIGFLFQGSALYdSMTV 120
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFG---LMDLRKVLGIIPQAPVLF-SGTV 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 121 RENLEfPLRRHKEklgtpsdttALVMEALENVGLGRTIDLMP----AEL-------SGGMKRRIALARTLILKPKIILYD 189
Cdd:PLN03130 1330 RFNLD-PFNEHND---------ADLWESLERAHLKDVIRRNSlgldAEVseagenfSVGQRQLLSLARALLRRSKILVLD 1399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 190 EPTS----GLDPITAKEIIELMRNIQIkyntssLIITHD----VDCARVI---ADRMV-------LLVDGinyaEGSYTE 251
Cdd:PLN03130 1400 EATAavdvRTDALIQKTIREEFKSCTM------LIIAHRlntiIDCDRILvldAGRVVefdtpenLLSNE----GSAFSK 1469
|
....*..
gi 1234390149 252 LSQSTDP 258
Cdd:PLN03130 1470 MVQSTGA 1476
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
48-221 |
1.92e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.57 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 48 DLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATldRHTLDELRSDIGFLFQ---GSALYDSMTVRENL 124
Cdd:PRK10762 274 TLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVT--RSPQDGLANGIVYISEdrkRDGLVLGMSVKENM 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 125 EFPLRRHKEKLGTPSDTTALVMEALENVGLGR----TIDLMPAELSGGMKRRIALARTLILKPKIILYDEPTSGLDPITA 200
Cdd:PRK10762 352 SLTALRYFSRAGGSLKHADEQQAVSDFIRLFNiktpSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAK 431
|
170 180
....*....|....*....|.
gi 1234390149 201 KEIIELMRniQIKYNTSSLII 221
Cdd:PRK10762 432 KEIYQLIN--QFKAEGLSIIL 450
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
41-265 |
2.31e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.92 E-value: 2.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 41 VLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIAtldRHTLDELRSDIGFLFQGSALYdSMTV 120
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVA---KFGLTDLRRVLSIIPQSPVLF-SGTV 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 121 RENLEfPLRRHKEklgtpsdttALVMEALENVGLGRTIDLMPAEL-----------SGGMKRRIALARTLILKPKIILYD 189
Cdd:PLN03232 1327 RFNID-PFSEHND---------ADLWEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLD 1396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 190 EPTSGLDPITAKEIielMRNIQIKYNTSS-LIITHD----VDCarviaDRMVLLVDGINYAEGSYTE-LSQSTdpkvEAF 263
Cdd:PLN03232 1397 EATASVDVRTDSLI---QRTIREEFKSCTmLVIAHRlntiIDC-----DKILVLSSGQVLEYDSPQElLSRDT----SAF 1464
|
..
gi 1234390149 264 FK 265
Cdd:PLN03232 1465 FR 1466
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
19-252 |
7.78e-12 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 65.04 E-value: 7.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 19 RPLER-KAVIRIRDVRKSF--GDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEiatLDR 95
Cdd:PRK11176 333 RVIERaKGDIEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHD---LRD 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 96 HTLDELRSDIGFLFQGSALYDSmTVRENLEFPLRRH--KEKLGTPSdTTALVMEALENV--GLGRTIDLMPAELSGGMKR 171
Cdd:PRK11176 410 YTLASLRNQVALVSQNVHLFND-TIANNIAYARTEQysREQIEEAA-RMAYAMDFINKMdnGLDTVIGENGVLLSGGQRQ 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 172 RIALARTLILKPKIILYDEPTSGLDpiTAKEiielmRNIQ-----IKYNTSSLIITHDVDcarVI--ADRMVLLVDGINY 244
Cdd:PRK11176 488 RIAIARALLRDSPILILDEATSALD--TESE-----RAIQaaldeLQKNRTSLVIAHRLS---TIekADEILVVEDGEIV 557
|
....*...
gi 1234390149 245 AEGSYTEL 252
Cdd:PRK11176 558 ERGTHAEL 565
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
41-258 |
7.90e-12 |
|
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: 65.32 E-value: 7.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 41 VLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKeiatldrhtldelrsdIGFLFQGSALYDSmTV 120
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR----------------ISFSPQTSWIMPG-TI 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 121 RENLEFPLRRHKEKLgtPSDTTALVMEalENVGLGRTIDLMP-----AELSGGMKRRIALARTLILKPKIILYDEPTSGL 195
Cdd:TIGR01271 504 KDNIIFGLSYDEYRY--TSVIKACQLE--EDIALFPEKDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFTHL 579
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1234390149 196 DPITAKEIIELMRnIQIKYNTSSLIITHDVDCARViADRMVLLVDGINYAEGSYTELsQSTDP 258
Cdd:TIGR01271 580 DVVTEKEIFESCL-CKLMSNKTRILVTSKLEHLKK-ADKILLLHEGVCYFYGTFSEL-QAKRP 639
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
37-199 |
8.83e-12 |
|
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: 64.93 E-value: 8.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 37 GDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDsGYIEVMGkeiATLDRHTLDELRSDIGFLFQGSALYd 116
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDG---VSWNSVTLQTWRKAFGVIPQKVFIF- 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 117 SMTVRENLEfPLRRHkeklgtpSDTTalVMEALENVGLGRTIDLMPAEL-----------SGGMKRRIALARTLILKPKI 185
Cdd:TIGR01271 1305 SGTFRKNLD-PYEQW-------SDEE--IWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKI 1374
|
170
....*....|....
gi 1234390149 186 ILYDEPTSGLDPIT 199
Cdd:TIGR01271 1375 LLLDEPSAHLDPVT 1388
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
18-256 |
9.70e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 63.27 E-value: 9.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 18 DRPLERKAVIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHT 97
Cdd:PRK10575 3 EYTNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 98 LDElrsDIGFLFQGSALYDSMTVRENL---EFPLRRHKEKLGtpSDTTALVMEALENVGL----GRTIDlmpaELSGGMK 170
Cdd:PRK10575 83 FAR---KVAYLPQQLPAAEGMTVRELVaigRYPWHGALGRFG--AADREKVEEAISLVGLkplaHRLVD----SLSGGER 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 171 RRIALARTLILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEGSYT 250
Cdd:PRK10575 154 QRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPA 233
|
....*.
gi 1234390149 251 ELSQST 256
Cdd:PRK10575 234 ELMRGE 239
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
57-263 |
1.55e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 62.98 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 57 VMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLdelrsdIGFLFQGSALYDSMTV---------RENLEFP 127
Cdd:PRK15056 38 LVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL------VAYVPQSEEVDWSFPVlvedvvmmgRYGHMGW 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 128 LRRHKEKlgtpsdTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKIILYDEPTSGLDPITAKEIIELM 207
Cdd:PRK15056 112 LRRAKKR------DRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLL 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1234390149 208 RNIQIKYNTsSLIITHDVDCARVIADRMVlLVDGINYAEGSyTELSQSTDPKVEAF 263
Cdd:PRK15056 186 RELRDEGKT-MLVSTHNLGSVTEFCDYTV-MVKGTVLASGP-TETTFTAENLELAF 238
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
30-224 |
1.83e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.60 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 30 RDVRKSFGDN-HVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGyiEVMGKEIATldrhtldelrsdIGFL 108
Cdd:PRK11819 10 NRVSKVVPPKkQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG--EARPAPGIK------------VGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 109 FQGSALYDSMTVRENLEFPLRRHKEKL----------GTP---SDTTALVMEALENV-------GLGRTIDL-MPA---- 163
Cdd:PRK11819 76 PQEPQLDPEKTVRENVEEGVAEVKAALdrfneiyaayAEPdadFDALAAEQGELQEIidaadawDLDSQLEIaMDAlrcp 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1234390149 164 -------ELSGGMKRRIALARTLILKPKIILYDEPTSGLDpitAKEIIELMRNIQiKYNTSSLIITHD 224
Cdd:PRK11819 156 pwdakvtKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD---AESVAWLEQFLH-DYPGTVVAVTHD 219
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
47-241 |
2.26e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 63.53 E-value: 2.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 47 MDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDrhTLDELRSDIGFL---FQGSALYdsmtvren 123
Cdd:PRK15439 284 LEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALS--TAQRLARGLVYLpedRQSSGLY-------- 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 124 LEFPLRRHKEKLgTPSDTTALVMEALENVGLGR-----TIDLMPAE-----LSGGMKRRIALARTLILKPKIILYDEPTS 193
Cdd:PRK15439 354 LDAPLAWNVCAL-THNRRGFWIKPARENAVLERyrralNIKFNHAEqaartLSGGNQQKVLIAKCLEASPQLLIVDEPTR 432
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1234390149 194 GLDPITAKEIIELMRNIQiKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:PRK15439 433 GVDVSARNDIYQLIRSIA-AQNVAVLFISSDLEEIEQMADRVLVMHQG 479
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
30-241 |
2.73e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.02 E-value: 2.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 30 RDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMlPD---SGYIEVMGKEIATldRHTLDELRSDIG 106
Cdd:PRK13549 9 KNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQA--SNIRDTERAGIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 107 FLFQGSALYDSMTVRENLeFplrrhkekLG---TPS---DTTALVMEA---LENVGLGRTIDLMPAELSGGMKRRIALAR 177
Cdd:PRK13549 86 IIHQELALVKELSVLENI-F--------LGneiTPGgimDYDAMYLRAqklLAQLKLDINPATPVGNLGLGQQQLVEIAK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1234390149 178 TLILKPKIILYDEPTSGLdpiTAKEI---IELMRNIQiKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:PRK13549 157 ALNKQARLLILDEPTASL---TESETavlLDIIRDLK-AHGIACIYISHKLNEVKAISDTICVIRDG 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
24-241 |
3.36e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 62.74 E-value: 3.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 24 KAVIRIRDVR-KSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLDELR 102
Cdd:COG3845 255 EVVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLG 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 103 sdIGF-----LFQGSALydSMTVRENLefPLRRHKEKLGTPS---DTTALVMEALENVG----LGRTIDLMPAELSGGMK 170
Cdd:COG3845 335 --VAYipedrLGRGLVP--DMSVAENL--ILGRYRRPPFSRGgflDRKAIRAFAEELIEefdvRTPGPDTPARSLSGGNQ 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1234390149 171 RRIALARTLILKPKIILYDEPTSGLDpITA-----KEIIELMRNiqikyNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:COG3845 409 QKVILARELSRDPKLLIAAQPTRGLD-VGAiefihQRLLELRDA-----GAAVLLISEDLDEILALSDRIAVMYEG 478
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
24-256 |
6.00e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.94 E-value: 6.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 24 KAVIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLDElrS 103
Cdd:PRK10762 2 QALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQE--A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 104 DIGFLFQGSALYDSMTVRENLeFPLRRHKEKLGTpSDTTALVMEA---LENVGLGRTIDLMPAELSGGMKRRIALARTLI 180
Cdd:PRK10762 80 GIGIIHQELNLIPQLTIAENI-FLGREFVNRFGR-IDWKKMYAEAdklLARLNLRFSSDKLVGELSIGEQQMVEIAKVLS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 181 LKPKIILYDEPTsglDPITAKEIIELMRNIQ--------IKYntssliITHDVDCARVIADRMVLLVDGINYAEGSYTEL 252
Cdd:PRK10762 158 FESKVIIMDEPT---DALTDTETESLFRVIRelksqgrgIVY------ISHRLKEIFEICDDVTVFRDGQFIAEREVADL 228
|
....
gi 1234390149 253 SQST 256
Cdd:PRK10762 229 TEDS 232
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
24-224 |
7.48e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.89 E-value: 7.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 24 KAVIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGK-EIATLDRH--TLDE 100
Cdd:PRK11147 317 KIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKlEVAYFDQHraELDP 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 101 LRsdigflfqgsalydsmTVRENL-----EFPL---RRHKekLGTPSDTTALVMEALENVglgrtidlmpAELSGGMKRR 172
Cdd:PRK11147 397 EK----------------TVMDNLaegkqEVMVngrPRHV--LGYLQDFLFHPKRAMTPV----------KALSGGERNR 448
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1234390149 173 IALARtLILKPK--IILyDEPTSGLDpitaKEIIELMRNIQIKYNTSSLIITHD 224
Cdd:PRK11147 449 LLLAR-LFLKPSnlLIL-DEPTNDLD----VETLELLEELLDSYQGTVLLVSHD 496
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
5-229 |
8.53e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.97 E-value: 8.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 5 PTTYKHKDQEGVAD-RPLERKAVIRIRDVRKsfgDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGyi 83
Cdd:PTZ00265 366 PLVENNDDGKKLKDiKKIQFKNVRFHYDTRK---DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEG-- 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 84 evmgkEIATLDRHTLDEL-----RSDIGFLFQGSALYdSMTVRENLEFPLRRHKE------------------------- 133
Cdd:PTZ00265 441 -----DIIINDSHNLKDInlkwwRSKIGVVSQDPLLF-SNSIKNNIKYSLYSLKDlealsnyynedgndsqenknkrnsc 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 134 ---------KLGTPSDTTALV--------MEALENVGLGRTI---DLMPA--------------ELSGGMKRRIALARTL 179
Cdd:PTZ00265 515 rakcagdlnDMSNTTDSNELIemrknyqtIKDSEVVDVSKKVlihDFVSAlpdkyetlvgsnasKLSGGQKQRISIARAI 594
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1234390149 180 ILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCAR 229
Cdd:PTZ00265 595 IRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIR 644
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
41-258 |
9.54e-11 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 60.64 E-value: 9.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 41 VLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKeiatldrhtldelrsdIGFLFQGSALYDSmTV 120
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR----------------ISFSSQFSWIMPG-TI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 121 RENLEFPLR----RHKEKLGT---PSDTTALVMEALENVGLGRTIdlmpaeLSGGMKRRIALARTLILKPKIILYDEPTS 193
Cdd:cd03291 115 KENIIFGVSydeyRYKSVVKAcqlEEDITKFPEKDNTVLGEGGIT------LSGGQRARISLARAVYKDADLYLLDSPFG 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 194 GLDPITAKEIIE-----LMRniqikyNTSSLIITHDVDCARvIADRMVLLVDGINYAEGSYTELsQSTDP 258
Cdd:cd03291 189 YLDVFTEKEIFEscvckLMA------NKTRILVTSKMEHLK-KADKILILHEGSSYFYGTFSEL-QSLRP 250
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
22-236 |
1.31e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 61.36 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 22 ERKAVIRIRDVRKSFGDN--HVLNGFdmdLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVmgkeiatldrhTLD 99
Cdd:PRK13409 336 ERETLVEYPDLTKKLGDFslEVEGGE---IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP-----------ELK 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 100 ------ELRSDigflfqgsalYDsMTVRENLefplRRHKEKLGTPSDTTalvmEALENVGLGRTIDLMPAELSGGMKRRI 173
Cdd:PRK13409 402 isykpqYIKPD----------YD-GTVEDLL----RSITDDLGSSYYKS----EIIKPLQLERLLDKNVKDLSGGELQRV 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1234390149 174 ALARTLILKPKIILYDEPTSGLDP----ITAKEIIELMRNiqikYNTSSLIITHDVDCARVIADR-MV 236
Cdd:PRK13409 463 AIAACLSRDADLYLLDEPSAHLDVeqrlAVAKAIRRIAEE----REATALVVDHDIYMIDYISDRlMV 526
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
27-241 |
1.64e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 60.76 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKSFGDNhvlnGF-----DMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRhtlDEL 101
Cdd:PRK10522 323 LELRNVTFAYQDN----GFsvgpiNLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQP---EDY 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 102 RSDIGFLFQGSALYDSMTVREnlefplrrhkeklGTPSDTtALVMEALENVGLGRTIDL-----MPAELSGGMKRRIALA 176
Cdd:PRK10522 396 RKLFSAVFTDFHLFDQLLGPE-------------GKPANP-ALVEKWLERLKMAHKLELedgriSNLKLSKGQKKRLALL 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1234390149 177 RTLILKPKIILYDEPTSGLDP----ITAKEIIELMRNIQIkyntSSLIITHDvDCARVIADRMVLLVDG 241
Cdd:PRK10522 462 LALAEERDILLLDEWAADQDPhfrrEFYQVLLPLLQEMGK----TIFAISHD-DHYFIHADRLLEMRNG 525
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
57-210 |
1.95e-10 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 58.79 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 57 VMGKSGSGKSVMIKCLVGLmlPDSGYIEvmgKEIaTLDRHTLDE-LRSDIGFLFQGSALYDSMTVRENLEFP--LRrhke 133
Cdd:cd03232 38 LMGESGAGKTTLLDVLAGR--KTAGVIT---GEI-LINGRPLDKnFQRSTGYVEQQDVHSPNLTVREALRFSalLR---- 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1234390149 134 klgtpsdttalvmealenvglgrtidlmpaELSGGMKRRIALARTLILKPKIILYDEPTSGLDPITAKEIIELMRNI 210
Cdd:cd03232 108 ------------------------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKL 154
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
52-220 |
2.53e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.51 E-value: 2.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 52 GENLVVMGKSGSGKSVMIKCL----VGLMLPDSGYIevmgkeiaTLDRHTLDELRSDigflFQGSALYDS--------MT 119
Cdd:TIGR00956 87 GELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVI--------TYDGITPEEIKKH----YRGDVVYNAetdvhfphLT 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 120 VRENLEFPLRrhkekLGTP-------------SDTTALVMEALenvGLGRTIDL-----MPAELSGGMKRRIALARTLIL 181
Cdd:TIGR00956 155 VGETLDFAAR-----CKTPqnrpdgvsreeyaKHIADVYMATY---GLSHTRNTkvgndFVRGVSGGERKRVSIAEASLG 226
|
170 180 190
....*....|....*....|....*....|....*....
gi 1234390149 182 KPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLI 220
Cdd:TIGR00956 227 GAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLV 265
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
37-254 |
2.72e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 60.73 E-value: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 37 GDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKeiatldrhtldelrsdIGFLFQgSALYD 116
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS----------------VAYVPQ-QAWIQ 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 117 SMTVRENLEFPLRRHKEKLGTPSDTTALVMEaLENVGLG-RT-IDLMPAELSGGMKRRIALARTLILKPKIILYDEPTSG 194
Cdd:TIGR00957 712 NDSLRENILFGKALNEKYYQQVLEACALLPD-LEILPSGdRTeIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSA 790
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1234390149 195 LDPITAKEIIE-LMRNIQIKYNTSSLIITHDVDCARVIaDRMVLLVDGINYAEGSYTELSQ 254
Cdd:TIGR00957 791 VDAHVGKHIFEhVIGPEGVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQ 850
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
79-265 |
3.33e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 60.43 E-value: 3.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 79 DSGYIEVMGKEIATldrHTLDELRSDIGFLFQGSALYDsMTVRENLEFplrrhkeklGTPSDTTALVMEALENVGLGRTI 158
Cdd:PTZ00265 1275 NSGKILLDGVDICD---YNLKDLRNLFSIVSQEPMLFN-MSIYENIKF---------GKEDATREDVKRACKFAAIDEFI 1341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 159 DLMPAE-----------LSGGMKRRIALARTLILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDC 227
Cdd:PTZ00265 1342 ESLPNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIAS 1421
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1234390149 228 ARViADRMVLLVD-----GINYAEGSYTELSQSTDPKVEAFFK 265
Cdd:PTZ00265 1422 IKR-SDKIVVFNNpdrtgSFVQAHGTHEELLSVQDGVYKKYVK 1463
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
21-210 |
5.41e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.41 E-value: 5.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 21 LERKAVIRIRDVRKSfgDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATldRHTLDE 100
Cdd:PRK09700 260 LAHETVFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISP--RSPLDA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 101 LRSDIGFLFQG---SALYDSMTVRENL----EFPLRRHKEKLG--TPSDTTALVMEALENVGLG-RTIDLMPAELSGGMK 170
Cdd:PRK09700 336 VKKGMAYITESrrdNGFFPNFSIAQNMaisrSLKDGGYKGAMGlfHEVDEQRTAENQRELLALKcHSVNQNITELSGGNQ 415
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1234390149 171 RRIALARTLILKPKIILYDEPTSGLDPITAKEIIELMRNI 210
Cdd:PRK09700 416 QKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL 455
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
35-255 |
5.95e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 59.37 E-value: 5.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 35 SFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVmgkeiatldrhtldeLRSDIGFLFQGSAL 114
Cdd:PLN03130 626 SKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV---------------IRGTVAYVPQVSWI 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 115 YDSmTVRENLEFplrrhkeklGTPSDTtALVMEALENVGLGRTIDLMPA-----------ELSGGMKRRIALARTLILKP 183
Cdd:PLN03130 691 FNA-TVRDNILF---------GSPFDP-ERYERAIDVTALQHDLDLLPGgdlteigergvNISGGQKQRVSMARAVYSNS 759
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1234390149 184 KIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARViaDRMVLLVDGINYAEGSYTELSQS 255
Cdd:PLN03130 760 DVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQV--DRIILVHEGMIKEEGTYEELSNN 829
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
41-255 |
9.37e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 58.80 E-value: 9.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 41 VLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHtldELRSDIGFLFQGSALYdSMTV 120
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLH---DLRFKITIIPQDPVLF-SGSL 1376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 121 RENLEfPLRRHKEKlgtpsdttaLVMEALENVGLGRTIDLMPAE-----------LSGGMKRRIALARTLILKPKIILYD 189
Cdd:TIGR00957 1377 RMNLD-PFSQYSDE---------EVWWALELAHLKTFVSALPDKldhecaeggenLSVGQRQLVCLARALLRKTKILVLD 1446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1234390149 190 EPTSGLDPITAKEIielMRNIQIKYNTSS-LIITHDVDcarVIAD--RMVLLVDGINYAEGSYTELSQS 255
Cdd:TIGR00957 1447 EATAAVDLETDNLI---QSTIRTQFEDCTvLTIAHRLN---TIMDytRVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
47-241 |
9.44e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 58.28 E-value: 9.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 47 MDLYEGENLVVMGKSGSGKSVMIKCLVGLMlPDSGYIevmgkeiaTLDRHTLDEL--------------RSDIGFLFQ-- 110
Cdd:PRK15093 28 MTLTEGEIRGLVGESGSGKSLIAKAICGVT-KDNWRV--------TADRMRFDDIdllrlsprerrklvGHNVSMIFQep 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 111 GSALYDSMTVRENL---------------EFPLRRHKeklgtpsdttalVMEALENVGLGRTIDLM---PAELSGGMKRR 172
Cdd:PRK15093 99 QSCLDPSERVGRQLmqnipgwtykgrwwqRFGWRKRR------------AIELLHRVGIKDHKDAMrsfPYELTEGECQK 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1234390149 173 IALARTLILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:PRK15093 167 VMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCG 235
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
29-241 |
1.17e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.20 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 29 IRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIatlDRHTLDE-LRSDIGF 107
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI---DFKSSKEaLENGISM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 108 LFQGSALYDSMTVRENL---EFPLR----RHKEKLgtpSDTTALVMEAlenvglgrTIDLMP----AELSGGMKRRIALA 176
Cdd:PRK10982 78 VHQELNLVLQRSVMDNMwlgRYPTKgmfvDQDKMY---RDTKAIFDEL--------DIDIDPrakvATLSVSQMQMIEIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1234390149 177 RTLILKPKIILYDEPTSGLdpiTAKEIIELMRNIQ-IKYNTSSLI-ITHDVDCARVIADRMVLLVDG 241
Cdd:PRK10982 147 KAFSYNAKIVIMDEPTSSL---TEKEVNHLFTIIRkLKERGCGIVyISHKMEEIFQLCDEITILRDG 210
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
57-221 |
4.19e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 54.88 E-value: 4.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 57 VMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLDELRSDIGflfqgsaLYDSMTVRENLEFPLRRHkeklg 136
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIGHNLG-------LKLEMTVFENLKFWSEIY----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 137 tpsDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKPKIILYDEPTSGLDpitaKEIIELMRN-IQIKYN 215
Cdd:PRK13541 99 ---NSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS----KENRDLLNNlIVMKAN 171
|
....*.
gi 1234390149 216 TSSLII 221
Cdd:PRK13541 172 SGGIVL 177
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
14-256 |
6.50e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 56.26 E-value: 6.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 14 EGVADRPLERKAV-IRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIAT 92
Cdd:PRK10789 302 DGSEPVPEGRGELdVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTK 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 93 LdrhTLDELRSDIGFLFQGSALYdSMTVRENLefplrrhkeKLGTPSDTTALVMEA--LENVG-----LGRTIDLMPAE- 164
Cdd:PRK10789 382 L---QLDSWRSRLAVVSQTPFLF-SDTVANNI---------ALGRPDATQQEIEHVarLASVHddilrLPQGYDTEVGEr 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 165 ---LSGGMKRRIALARTLILKPKIILYDEPTSGLDPITAKEIielMRNIQIKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:PRK10789 449 gvmLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQI---LHNLRQWGEGRTVIISAHRLSALTEASEILVMQHG 525
|
250
....*....|....*
gi 1234390149 242 INYAEGSYTELSQST 256
Cdd:PRK10789 526 HIAQRGNHDQLAQQS 540
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
52-248 |
2.42e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 53.40 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 52 GENLVVMGKSGSGKSVMIKCLVGLmLPDSGYIEVMGKEIATLDRHTLDELRsdiGFLFQGSALYDSMTVRENLEfplrRH 131
Cdd:PRK03695 22 GEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHR---AYLSQQQTPPFAMPVFQYLT----LH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 132 KEKLGTPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALA-------RTLILKPKIILYDEPTSGLDpITAK--- 201
Cdd:PRK03695 94 QPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNSLD-VAQQaal 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1234390149 202 -EIIELMRNIQIkyntSSLIITHDVDCARVIADRMVLLVDGINYAEGS 248
Cdd:PRK03695 173 dRLLSELCQQGI----AVVMSSHDLNHTLRHADRVWLLKQGKLLASGR 216
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
41-203 |
2.73e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.40 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 41 VLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATldrHTLDELRSDIGFLFQGSALYDSmTV 120
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGA---YGLRELRRQFSMIPQDPVLFDG-TV 1400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 121 RENLEFPLRRhkeklgtpsdTTALVMEALENVGL-GRT------IDLMPAE----LSGGMKRRIALARTLILK-PKIILY 188
Cdd:PTZ00243 1401 RQNVDPFLEA----------SSAEVWAALELVGLrERVasesegIDSRVLEggsnYSVGQRQLMCMARALLKKgSGFILM 1470
|
170
....*....|....*
gi 1234390149 189 DEPTSGLDPITAKEI 203
Cdd:PTZ00243 1471 DEATANIDPALDRQI 1485
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
57-209 |
4.04e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 54.08 E-value: 4.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 57 VMGKSGSGKSVMIKCLVGLmlPDSGYIE----VMG--KEIATLDRHTldelrsdiGFLFQGSALYDSMTVRENLEFP--L 128
Cdd:PLN03140 911 LMGVSGAGKTTLMDVLAGR--KTGGYIEgdirISGfpKKQETFARIS--------GYCEQNDIHSPQVTVRESLIYSafL 980
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 129 RRHKE-----KLGTPSDttalVMEALENVGLGRTIDLMPA--ELSGGMKRRIALARTLILKPKIILYDEPTSGLDPITAK 201
Cdd:PLN03140 981 RLPKEvskeeKMMFVDE----VMELVELDNLKDAIVGLPGvtGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAA 1056
|
....*...
gi 1234390149 202 EIIELMRN 209
Cdd:PLN03140 1057 IVMRTVRN 1064
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
49-254 |
5.26e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 53.29 E-value: 5.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 49 LYEGENLVVMGKSGSGKSVMIKCLVGlMLPD--SGYIEVMGKEIATldRHTLDELRSDIGFLFQG---SALYDSMTVREN 123
Cdd:TIGR02633 283 LRRGEILGVAGLVGAGRTELVQALFG-AYPGkfEGNVFINGKPVDI--RNPAQAIRAGIAMVPEDrkrHGIVPILGVGKN 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 124 LEFPLRRHKEKLGTPSDTTAL--VMEALENVGLgRTI--DLMPAELSGGMKRRIALARTLILKPKIILYDEPTSGLDPIT 199
Cdd:TIGR02633 360 ITLSVLKSFCFKMRIDAAAELqiIGSAIQRLKV-KTAspFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGA 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1234390149 200 AKEIIELMrNIQIKYNTSSLIITHDVDCARVIADRMVLLVDGINYAEGSYTELSQ 254
Cdd:TIGR02633 439 KYEIYKLI-NQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDFVNHALTQ 492
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
44-196 |
6.63e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.33 E-value: 6.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 44 GFDMDlyegENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGK-EIATLDRHTLDELRsdigfLFQGSALYDSMTVRE 122
Cdd:PLN03073 531 GIDLD----SRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKvRMAVFSQHHVDGLD-----LSSNPLLYMMRCFPG 601
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1234390149 123 NLEFPLRRHkekLGTPSDTTALVMEALENvglgrtidlmpaeLSGGMKRRIALARTLILKPKIILYDEPTSGLD 196
Cdd:PLN03073 602 VPEQKLRAH---LGSFGVTGNLALQPMYT-------------LSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
26-224 |
9.43e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.43 E-value: 9.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 26 VIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVmGK--EIATLD--RHTLDel 101
Cdd:PRK11819 324 VIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GEtvKLAYVDqsRDALD-- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 102 rsdigflfqgsalyDSMTVRENlefplrrhkeklgtpsdttalVMEALENVGLGRTIdlMPA------------------ 163
Cdd:PRK11819 401 --------------PNKTVWEE---------------------ISGGLDIIKVGNRE--IPSrayvgrfnfkggdqqkkv 443
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1234390149 164 -ELSGGMKRRIALARTLILKPKIILYDEPTSGLDpitakeiIELMRNIQ---IKYNTSSLIITHD 224
Cdd:PRK11819 444 gVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD-------VETLRALEealLEFPGCAVVISHD 501
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
42-196 |
1.41e-07 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 50.79 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 42 LNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLDEL-RSDIGFLFQGSALYDSmTV 120
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnRYSVAYAAQKPWLLNA-TV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 121 RENLEF--PLRRHKEKLgtpsdttalVMEAlenVGLGRTIDLMP-----------AELSGGMKRRIALARTLILKPKIIL 187
Cdd:cd03290 96 EENITFgsPFNKQRYKA---------VTDA---CSLQPDIDLLPfgdqteigergINLSGGQRQRICVARALYQNTNIVF 163
|
....*....
gi 1234390149 188 YDEPTSGLD 196
Cdd:cd03290 164 LDDPFSALD 172
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
27-236 |
2.14e-07 |
|
ATP-binding cassette domain I 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: 213237 [Multi-domain] Cd Length: 226 Bit Score: 50.33 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 27 IRIRDVRKsfgdnHVLNGFDMDLYEGENLVVMGKSGSGKSVM--------------------IKCLVGLM-LPDSGYIEV 85
Cdd:cd03270 1 IIVRGARE-----HNLKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryveslsayARQFLGQMdKPDVDSIEG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 86 MGKEIATLDRHTLDELRSDIG-------FLfqgSALYDSMTVRENLEFplrrhkeklgtpsdttalvmeaLENVGLGR-T 157
Cdd:cd03270 76 LSPAIAIDQKTTSRNPRSTVGtvteiydYL---RLLFARVGIRERLGF----------------------LVDVGLGYlT 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 158 IDLMPAELSGGMKRRIALARTLILKPKIILY--DEPTSGLDPITAKEIIELMRNIQIKYNTsSLIITHDVDCARvIADRM 235
Cdd:cd03270 131 LSRSAPTLSGGEAQRIRLATQIGSGLTGVLYvlDEPSIGLHPRDNDRLIETLKRLRDLGNT-VLVVEHDEDTIR-AADHV 208
|
.
gi 1234390149 236 V 236
Cdd:cd03270 209 I 209
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
129-226 |
9.88e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 47.70 E-value: 9.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 129 RRHKEKLGTPSDTTALVMEALE---NVGLGR-TIDLMPAELSGGMKRRIALARTLI--LKPKIILYDEPTSGLDPITAKE 202
Cdd:cd03238 48 ARLISFLPKFSRNKLIFIDQLQfliDVGLGYlTLGQKLSTLSGGELQRVKLASELFsePPGTLFILDEPSTGLHQQDINQ 127
|
90 100
....*....|....*....|....
gi 1234390149 203 IIELMRNIqIKYNTSSLIITHDVD 226
Cdd:cd03238 128 LLEVIKGL-IDLGNTVILIEHNLD 150
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
26-223 |
2.01e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 47.86 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 26 VIRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGL--MLPDSGYIEVMGKEIATLDrhtlDELRS 103
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELS----PEDRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 104 DIG-FL-FQGSALYDSMTVRENLEFPLRRHKEKLGTPS----DTTALVMEALENVGlgrtidlMPAEL---------SGG 168
Cdd:PRK09580 77 GEGiFMaFQYPVEIPGVSNQFFLQTALNAVRSYRGQEPldrfDFQDLMEEKIALLK-------MPEDLltrsvnvgfSGG 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1234390149 169 MKRRIALARTLILKPKIILYDEPTSGLDpITAKEIIELMRNIQIKYNTSSLIITH 223
Cdd:PRK09580 150 EKKRNDILQMAVLEPELCILDESDSGLD-IDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
7-207 |
2.77e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.96 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 7 TYKHKDQEGVADRPLERKAVIRIRDV--RKSFGDNH-VLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYI 83
Cdd:PRK13545 2 NYKVKFEHVTKKYKMYNKPFDKLKDLffRSKDGEYHyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 84 EVMGKeiATLdrhtldelrsdigfLFQGSALYDSMTVRENLEFP-----LRRHKEKLGTPsdttalvmEALENVGLGRTI 158
Cdd:PRK13545 82 DIKGS--AAL--------------IAISSGLNGQLTGIENIELKglmmgLTKEKIKEIIP--------EIIEFADIGKFI 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1234390149 159 DLMPAELSGGMKRRIALARTLILKPKIILYDEPTSGLDPITAKEIIELM 207
Cdd:PRK13545 138 YQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKM 186
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
157-207 |
7.44e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 46.85 E-value: 7.44e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1234390149 157 TIDLMPAELSGGMKRRIALARTLILKPKIILYDEPTSGLDpITAK-EIIELM 207
Cdd:PRK13549 398 SPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID-VGAKyEIYKLI 448
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
48-241 |
9.71e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.26 E-value: 9.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 48 DLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRH---------TLDELRSdigflfqgSALYDSM 118
Cdd:PRK10982 270 DLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANeainhgfalVTEERRS--------TGIYAYL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 119 TVREN-LEFPLRRHKEKLGTPSDT-----TALVMEALENVGLGRTIDLmpAELSGGMKRRIALARTLILKPKIILYDEPT 192
Cdd:PRK10982 342 DIGFNsLISNIRNYKNKVGLLDNSrmksdTQWVIDSMRVKTPGHRTQI--GSLSGGNQQKVIIGRWLLTQPEILMLDEPT 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1234390149 193 SGLDpITAK-EIIELMRNIQiKYNTSSLIITHDVDCARVIADRMVLLVDG 241
Cdd:PRK10982 420 RGID-VGAKfEIYQLIAELA-KKDKGIIIISSEMPELLGITDRILVMSNG 467
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
158-224 |
1.02e-05 |
|
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: 45.29 E-value: 1.02e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1234390149 158 IDLMPAELSGGMKR------RIALARTLILKPKIILYDEPTSGLDPITAKE-IIELMRNIQIKYNTSSLIITHD 224
Cdd:cd03240 109 LLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEEsLAEIIEERKSQKNFQLIVITHD 182
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
52-199 |
1.58e-05 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 45.28 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 52 GENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRHTLdelRSDIGFLFQGSALYdSMTVRENLEfPLRrh 131
Cdd:cd03288 47 GQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTL---RSRLSIILQDPILF-SGSIRFNLD-PEC-- 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1234390149 132 keklgTPSDTTalVMEALENVGLGRTIDLMPAEL-----------SGGMKRRIALARTLILKPKIILYDEPTSGLDPIT 199
Cdd:cd03288 120 -----KCTDDR--LWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT 191
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
87-242 |
1.68e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.98 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 87 GKEIATLDRHTLDELrsdigFLFQGSALYDSMTVRENLEfplrrhkeklGTPSDTTALVMEALENVGLGRTIdlmpAELS 166
Cdd:PRK00635 418 GKTFAEFQQMSLQEL-----FIFLSQLPSKSLSIEEVLQ----------GLKSRLSILIDLGLPYLTPERAL----ATLS 478
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1234390149 167 GGMKRRIALARTLILKPKIILY--DEPTSGLDPITAKEIIELMRNIQIKYNTsSLIITHDvdcarviaDRMVLLVDGI 242
Cdd:PRK00635 479 GGEQERTALAKHLGAELIGITYilDEPSIGLHPQDTHKLINVIKKLRDQGNT-VLLVEHD--------EQMISLADRI 547
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
41-223 |
4.11e-05 |
|
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: 44.35 E-value: 4.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 41 VLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMlpdsgyiEVMGkeiatlDRHTLDElRSDIGFLFQGSalYDSM-T 119
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELW-------PVYG------GRLTKPA-KGKLFYVPQRP--YMTLgT 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 120 VRENLEFPLRRHKEKLGTPSDttALVMEALENVGLGRTI----------DLMPaELSGGMKRRIALARTLILKPKIILYD 189
Cdd:TIGR00954 531 LRDQIIYPDSSEDMKRRGLSD--KDLEQILDNVQLTHILereggwsavqDWMD-VLSGGEKQRIAMARLFYHKPQFAILD 607
|
170 180 190
....*....|....*....|....*....|....
gi 1234390149 190 EPTSGLDPITAKEIIELMRNiqikYNTSSLIITH 223
Cdd:TIGR00954 608 ECTSAVSVDVEGYMYRLCRE----FGITLFSVSH 637
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
56-210 |
4.13e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.84 E-value: 4.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 56 VVMGKSGSGKSVMIKCLVGLMLPDsgyIEVMGKeiATLDRHTLDEL--RSDIGFLFQGSALYDSMTVRENLEFP------ 127
Cdd:PLN03140 195 LLLGPPSSGKTTLLLALAGKLDPS---LKVSGE--ITYNGYRLNEFvpRKTSAYISQNDVHVGVMTVKETLDFSarcqgv 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 128 ----------LRRHKEKLGTPSDTTALVME--ALENVG-----------LGRTI-------DLMPAELSGGMKRRIALAR 177
Cdd:PLN03140 270 gtrydllselARREKDAGIFPEAEVDLFMKatAMEGVKsslitdytlkiLGLDIckdtivgDEMIRGISGGQKKRVTTGE 349
|
170 180 190
....*....|....*....|....*....|...
gi 1234390149 178 TLILKPKIILYDEPTSGLDPITAKEIIELMRNI 210
Cdd:PLN03140 350 MIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQI 382
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
17-244 |
4.82e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 44.24 E-value: 4.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 17 ADRPLERKAV------IRIRDVRKSFGDNHVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGlmlpD--SGY---IEV 85
Cdd:PRK10938 245 PDEPSARHALpaneprIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG----DhpQGYsndLTL 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 86 MGKEIATLDrhTLDELRSDIGFLfqGSALY-D---SMTVRENLefpLRRHKEKLG----TPSDTTALVMEALENVGLGRT 157
Cdd:PRK10938 321 FGRRRGSGE--TIWDIKKHIGYV--SSSLHlDyrvSTSVRNVI---LSGFFDSIGiyqaVSDRQQKLAQQWLDILGIDKR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 158 IDLMP-AELSGGMKRRIALARTLILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITH-DVDCARVIADRM 235
Cdd:PRK10938 394 TADAPfHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHhAEDAPACITHRL 473
|
....*....
gi 1234390149 236 VLLVDGINY 244
Cdd:PRK10938 474 EFVPDGDIY 482
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
43-224 |
7.15e-05 |
|
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: 43.62 E-value: 7.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 43 NGFDmdLY------EGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRhtldelrsdigflFQGSALYD 116
Cdd:COG1245 86 NGFR--LYglpvpkKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPSWDEVLKR-------------FRGTELQD 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 117 SMT-VREN----------LEFPLRRHKeklGTPS------DTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTL 179
Cdd:COG1245 151 YFKkLANGeikvahkpqyVDLIPKVFK---GTVRellekvDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAAL 227
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1234390149 180 ILKPKIILYDEPTSGLDpitAKEIIELMRNIQ--IKYNTSSLIITHD 224
Cdd:COG1245 228 LRDADFYFFDEPSSYLD---IYQRLNVARLIRelAEEGKYVLVVEHD 271
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
164-238 |
7.19e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 42.56 E-value: 7.19e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1234390149 164 ELSGGMKRRIALARTLILKPKIILYDEPTSGLDPITAKEIIELMRNIQIKYNTSSLIITHDVDCARVIADRMVLL 238
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVF 145
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
166-196 |
9.53e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.31 E-value: 9.53e-05
10 20 30
....*....|....*....|....*....|.
gi 1234390149 166 SGGMKRRIALARTLILKPKIILYDEPTSGLD 196
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
51-224 |
1.08e-04 |
|
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: 42.74 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 51 EGENLVVMGKSGSGKSVMIKCLVGLMLPDSGyievmgkeiatldRHTLDELRSDIGFLFQGSALYDSMT----------- 119
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLG-------------KFDDPPDWDEILDEFRGSELQNYFTkllegdvkviv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 120 ---------------VRENLEfplrrHKEKLGTpSDTTALVMEaLENVgLGRTIDlmpaELSGGMKRRIALARTLILKPK 184
Cdd:cd03236 92 kpqyvdlipkavkgkVGELLK-----KKDERGK-LDELVDQLE-LRHV-LDRNID----QLSGGELQRVAIAAALARDAD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1234390149 185 IILYDEPTSGLD---PITAKEII-ELmrniqIKYNTSSLIITHD 224
Cdd:cd03236 160 FYFFDEPSSYLDikqRLNAARLIrEL-----AEDDNYVLVVEHD 198
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
52-206 |
1.21e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 42.98 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 52 GENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATldRHTLDELRSDIGF---------LFQGSalydsmTVRE 122
Cdd:PRK11288 279 GEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDI--RSPRDAIRAGIMLcpedrkaegIIPVH------SVAD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 123 NLEFPLRRHKEKLG------TPSDTTALVMEALENVGLGRTIDLMpaELSGGMKRRIALARTLILKPKIILYDEPTSGLD 196
Cdd:PRK11288 351 NINISARRHHLRAGclinnrWEAENADRFIRSLNIKTPSREQLIM--NLSGGNQQKAILGRWLSEDMKVILLDEPTRGID 428
|
170
....*....|.
gi 1234390149 197 pITAK-EIIEL 206
Cdd:PRK11288 429 -VGAKhEIYNV 438
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
149-257 |
2.43e-04 |
|
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: 42.31 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 149 LENVGLGR-TIDLMPAELSGGMKRRIALARTLILKPKIILY--DEPTSGLDPITAKEIIELMRNIQIKYNTsSLIITHDV 225
Cdd:TIGR00630 472 LIDVGLDYlSLSRAAGTLSGGEAQRIRLATQIGSGLTGVLYvlDEPSIGLHQRDNRRLINTLKRLRDLGNT-LIVVEHDE 550
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1234390149 226 DCARViADRmvlLVD---------GINYAEGSYTELSQSTD 257
Cdd:TIGR00630 551 DTIRA-ADY---VIDigpgagehgGEVVASGTPEEILANPD 587
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
160-224 |
2.79e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.80 E-value: 2.79e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1234390149 160 LMpAELSGGMKRRIALARTLILKPKIILYDEPTSGLDPITakeiIELMRNIQIKYNTSSLIITHD 224
Cdd:PRK15064 152 LM-SEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINT----IRWLEDVLNERNSTMIIISHD 211
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
162-224 |
2.84e-04 |
|
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: 41.61 E-value: 2.84e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1234390149 162 PAELSGGMKRRIALARTLIL---KPKIILYDEPTSGLDPITAKEIIELMRN-----IQIkyntssLIITHD 224
Cdd:pfam13304 234 AFELSDGTKRLLALLAALLSalpKGGLLLIDEPESGLHPKLLRRLLELLKElsrngAQL------ILTTHS 298
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
118-226 |
3.01e-04 |
|
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: 41.92 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 118 MTVRENLEF----PLRRHKeklgtpsdttalvMEALENVGLGrTIDL-MPA-ELSGGMKRRIALARTLILK---PKIILY 188
Cdd:TIGR00630 791 MTVEEAYEFfeavPSISRK-------------LQTLCDVGLG-YIRLgQPAtTLSGGEAQRIKLAKELSKRstgRTLYIL 856
|
90 100 110
....*....|....*....|....*....|....*...
gi 1234390149 189 DEPTSGLDPITAKEIIELMRNIQIKYNTsSLIITHDVD 226
Cdd:TIGR00630 857 DEPTTGLHFDDIKKLLEVLQRLVDKGNT-VVVIEHNLD 893
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
166-236 |
6.21e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.92 E-value: 6.21e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1234390149 166 SGGMKRRIALARTLILKPKIILYDEPTSGLDpitAKEIIELMRNIQiKYNTSSLIITHDVDCARVIADRMV 236
Cdd:PRK10636 151 SGGWRMRLNLAQALICRSDLLLLDEPTNHLD---LDAVIWLEKWLK-SYQGTLILISHDRDFLDPIVDKII 217
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
28-193 |
6.62e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 40.18 E-value: 6.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 28 RIRDVRKSFGDN---HVLNGFDMDLYEGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGkeiatldrhtldelrsD 104
Cdd:PRK13546 23 RMKDALIPKHKNktfFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG----------------E 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 105 IGFLFQGSALYDSMTVRENLEFPLRrhkeKLG-TPSDTTALVMEALENVGLGRTIDLMPAELSGGMKRRIALARTLILKP 183
Cdd:PRK13546 87 VSVIAISAGLSGQLTGIENIEFKML----CMGfKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNP 162
|
170
....*....|
gi 1234390149 184 KIILYDEPTS 193
Cdd:PRK13546 163 DILVIDEALS 172
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
43-224 |
6.72e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 40.56 E-value: 6.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 43 NGFDmdLY------EGENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMGKEIATLDRhtldelrsdigflFQGSALYD 116
Cdd:PRK13409 86 NGFK--LYglpipkEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPSWDEVLKR-------------FRGTELQN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 117 SM--------------------------TVRENLEFPLRRHK-----EKLGtpsdttalvmeaLENVgLGRTIDlmpaEL 165
Cdd:PRK13409 151 YFkklyngeikvvhkpqyvdlipkvfkgKVRELLKKVDERGKldevvERLG------------LENI-LDRDIS----EL 213
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1234390149 166 SGGMKRRIALARTLILKPKIILYDEPTSGLDpI-----TAKEIIELMRNiqiKYntsSLIITHD 224
Cdd:PRK13409 214 SGGELQRVAIAAALLRDADFYFFDEPTSYLD-IrqrlnVARLIRELAEG---KY---VLVVEHD 270
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
165-224 |
1.52e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 38.11 E-value: 1.52e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1234390149 165 LSGGMKRRIALARTLIL-----KPKIILyDEPTSGLDPITAKEIIELMRNIQIKYNTsSLIITHD 224
Cdd:cd03227 78 LSGGEKELSALALILALaslkpRPLYIL-DEIDRGLDPRDGQALAEAILEHLVKGAQ-VIVITHL 140
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
52-225 |
1.62e-03 |
|
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: 38.12 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 52 GENLVVMGKSGSGKSVMIKCLVGLMLPDSGYIEVMgkeiatldrhtldelrsdigflfqgsalydsmtvrenlefplrrh 131
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYI--------------------------------------------- 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 132 keklgTPSDTTALVMEALENVGLGRTidlmPAELSGGMKRRIALARTLILKPKIILYDEPTSGLDPITAKEIIELMR--- 208
Cdd:smart00382 37 -----DGEDILEEVLDQLLLIIVGGK----KASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrl 107
|
170
....*....|....*....
gi 1234390149 209 --NIQIKYNTSSLIITHDV 225
Cdd:smart00382 108 llLLKSEKNLTVILTTNDE 126
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
89-224 |
2.52e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 38.07 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 89 EIATLDRHTLDELRSDIGFLFQGSALYDSMTVRENLEFPLRRHKEKLGTpsdttalvMEALENVGLGRTIDLMPAE-LSG 167
Cdd:COG0419 90 EFAEFLEAKPSERKEALKRLLGLEIYEELKERLKELEEALESALEELAE--------LQKLKQEILAQLSGLDPIEtLSG 161
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1234390149 168 GMKRRIALARTLilkpKIILyDepTSGLDPITAKEIIELMRNIQikyntsslIITHD 224
Cdd:COG0419 162 GERLRLALADLL----SLIL-D--FGSLDEERLERLLDALEELA--------IITHV 203
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
118-195 |
5.06e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.08 E-value: 5.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 118 MTVRENLEF--PLRRHKEKLGTpsdttalvmeaLENVGLGrTIDL-MPA-ELSGGMKRRIALARTLILKPK----IILyD 189
Cdd:COG0178 788 MTVEEALEFfeNIPKIARKLQT-----------LQDVGLG-YIKLgQPAtTLSGGEAQRVKLASELSKRSTgktlYIL-D 854
|
....*.
gi 1234390149 190 EPTSGL 195
Cdd:COG0178 855 EPTTGL 860
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
118-195 |
8.41e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 37.36 E-value: 8.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234390149 118 MTVRENLEF-----PLRRHkeklgtpsdttalvMEALENVGLGrTIDL-MPA-ELSGGMKRRIALA---------RTL-I 180
Cdd:PRK00349 792 MTVEEALEFfeaipKIARK--------------LQTLVDVGLG-YIKLgQPAtTLSGGEAQRVKLAkelskrstgKTLyI 856
|
90
....*....|....*
gi 1234390149 181 LkpkiilyDEPTSGL 195
Cdd:PRK00349 857 L-------DEPTTGL 864
|
|
| |
