|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
3-198 |
2.73e-52 |
|
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: 166.90 E-value: 2.73e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADGPLLFH---DLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMRW--------- 70
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQalkGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLsekelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 71 ------IFQNPHGVAQRTAIDHVSLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPS 144
Cdd:cd03255 81 rrhigfVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1447648657 145 LMLVDEPTAQLDMHTAATVSESLSRIARND--TIVVVsTHDPNTRDACTDIIDLKN 198
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAgtTIVVV-THDPELAEYADRIIELRD 215
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-198 |
2.77e-52 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 167.14 E-value: 2.77e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADGPLLFH---DLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGID----------SMR 69
Cdd:COG1136 5 LELRNLTKSYGTGEGEVTalrGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDisslserelaRLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 70 -----WIFQNPHGVAQRTAIDHVSLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPS 144
Cdd:COG1136 85 rrhigFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1447648657 145 LMLVDEPTAQLDMHTAATVSESLSRIARND--TIVVVsTHDPNTRDACTDIIDLKN 198
Cdd:COG1136 165 LILADEPTGNLDSKTGEEVLELLRELNRELgtTIVMV-THDPELAARADRVIRLRD 219
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
3-183 |
1.99e-45 |
|
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: 149.54 E-value: 1.99e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADGP---LLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTR-----QGIDSMR-WIFQ 73
Cdd:cd03293 1 LEVRNVSKTYGGGGgavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVdgepvTGPGPDRgYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 74 NPHGVAQRTAIDHVSLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTA 153
Cdd:cd03293 81 QDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFS 160
|
170 180 190
....*....|....*....|....*....|..
gi 1447648657 154 QLDMHTAATVSESLSRIARND--TIVVVsTHD 183
Cdd:cd03293 161 ALDALTREQLQEELLDIWRETgkTVLLV-THD 191
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-183 |
2.77e-44 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 147.93 E-value: 2.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 1 MRVDLDHVGHRY--ADGPLL-FHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGID------SMRWI 71
Cdd:COG1116 6 PALELRGVSKRFptGGGGVTaLDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPvtgpgpDRGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 72 FQNPHGVAQRTAIDHVSLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEP 151
Cdd:COG1116 86 FQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEP 165
|
170 180 190
....*....|....*....|....*....|....
gi 1447648657 152 TAQLDMHTAATVSESLSRIARND--TIVVVsTHD 183
Cdd:COG1116 166 FGALDALTRERLQDELLRLWQETgkTVLFV-THD 198
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
3-185 |
5.34e-43 |
|
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: 143.63 E-value: 5.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMRW-----------I 71
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKnlrelrrkvglV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 72 FQNPHgvAQ---RTAIDHVSLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLV 148
Cdd:COG1122 81 FQNPD--DQlfaPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVL 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 1447648657 149 DEPTAQLDMHTAATVSESLSRIARNDTIVVVSTHDPN 185
Cdd:COG1122 159 DEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLD 195
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-185 |
1.07e-42 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 142.50 E-value: 1.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGID--SMRW---------- 70
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlsRLKRreipylrrri 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 71 --IFQNPHGVAQRTAIDHVSLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLV 148
Cdd:COG2884 82 gvVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 1447648657 149 DEPTAQLDMHTAATVSESLSRIARNDTIVVVSTHDPN 185
Cdd:COG2884 162 DEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLE 198
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-194 |
2.90e-42 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 142.15 E-value: 2.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADGPLLfHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDsmrwIFQNPHGVA--- 79
Cdd:COG1121 7 IELENLTVSYGGRPVL-EDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP----PRRARRRIGyvp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 80 QRTAIDH---------VSLPLLAK----GLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLM 146
Cdd:COG1121 82 QRAEVDWdfpitvrdvVLMGRYGRrglfRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1447648657 147 LVDEPTAQLDMHTAATVSESLSRIARNDTIVVVSTHDPNT-RDACTDII 194
Cdd:COG1121 162 LLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAvREYFDRVL 210
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-183 |
1.48e-41 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 140.20 E-value: 1.48e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADGPLLfHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMR----------WIF 72
Cdd:COG1131 1 IEVRGLTKRYGDKTAL-DGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARdpaevrrrigYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 73 QNPHGVAQRTAIDHVSLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPT 152
Cdd:COG1131 80 QEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPT 159
|
170 180 190
....*....|....*....|....*....|.
gi 1447648657 153 AQLDMHTAATVSESLSRIARNDTIVVVSTHD 183
Cdd:COG1131 160 SGLDPEARRELWELLRELAAEGKTVLLSTHY 190
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-199 |
2.10e-41 |
|
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: 138.77 E-value: 2.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 1 MRVDLDHVGHRYaDGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGID----------SMRW 70
Cdd:COG4133 1 MMLEAENLSCRR-GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPirdaredyrrRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 71 IFQNPHGVAQRTAIDHVSLplLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDE 150
Cdd:COG4133 80 LGHADGLKPELTVRENLRF--WAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1447648657 151 PTAQLDMHTAATVSESLSRIARNDTIVVVSTHDPNTRDACtDIIDLKNY 199
Cdd:COG4133 158 PFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELAAA-RVLDLGDF 205
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
3-190 |
8.01e-41 |
|
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: 138.34 E-value: 8.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRY--ADGPL-LFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGID------------- 66
Cdd:COG4181 9 IELRGLTKTVgtGAGELtILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDlfaldedararlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 67 --SMRWIFQNPHGVAQRTAIDHVSLPLLAKGlpRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPS 144
Cdd:COG4181 89 arHVGFVFQSFQLLPTLTALENVMLPLELAG--RRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1447648657 145 LMLVDEPTAQLDMHTAATVSESLSRIARND--TIVVVsTHDPNTRDAC 190
Cdd:COG4181 167 ILFADEPTGNLDAATGEQIIDLLFELNRERgtTLVLV-THDPALAARC 213
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-198 |
2.63e-40 |
|
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: 137.30 E-value: 2.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 5 LDHVGHRYADGPLLfHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMR----------WIFQN 74
Cdd:COG4555 4 VENLSKKYGKVPAL-KDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKeprearrqigVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 75 PHGVAQRTAIDHVSLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQ 154
Cdd:COG4555 83 RGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1447648657 155 LDMHTAATVSESLSRIARNDTIVVVSTHDPNTRDA-CTDIIDLKN 198
Cdd:COG4555 163 LDVMARRLLREILRALKKEGKTVLFSSHIMQEVEAlCDRVVILHK 207
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
3-185 |
3.52e-40 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 136.11 E-value: 3.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADGPLLfHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMRW---------IFQ 73
Cdd:cd03259 1 LELKGLSKTYGSVRAL-DDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVpperrnigmVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 74 N----PHgvaqRTAIDHVSLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVD 149
Cdd:cd03259 80 DyalfPH----LTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 1447648657 150 EPTAQLDMHTAATVSESLSRIARN-DTIVVVSTHDPN 185
Cdd:cd03259 156 EPLSALDAKLREELREELKELQRElGITTIYVTHDQE 192
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-198 |
6.45e-40 |
|
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: 142.59 E-value: 6.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGID-----------SMRWI 71
Cdd:COG4988 337 IELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDlsdldpaswrrQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 72 FQNPH----------GVAQRTAIDHvslpLLAKGLPRREAEEQARTLMDRFNlTRVTDRRFAeLSGGEAQRLMLARAFAA 141
Cdd:COG4988 417 PQNPYlfagtirenlRLGRPDASDE----ELEAALEAAGLDEFVAALPDGLD-TPLGEGGRG-LSGGQAQRLALARALLR 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1447648657 142 QPSLMLVDEPTAQLDMHTAATVSESLSRIARNDTIVVVsTHDPNTRDACTDIIDLKN 198
Cdd:COG4988 491 DAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILI-THRLALLAQADRILVLDD 546
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
3-184 |
7.43e-40 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 135.07 E-value: 7.43e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMRW------------ 70
Cdd:TIGR02673 2 IEFHNVSKAYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLrgrqlpllrrri 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 71 --IFQNPHGVAQRTAIDHVSLPLLAKGLPRREAEEQARTLMDRFNLTrvtDRRFA---ELSGGEAQRLMLARAFAAQPSL 145
Cdd:TIGR02673 82 gvVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLE---HKADAfpeQLSGGEQQRVAIARAIVNSPPL 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 1447648657 146 MLVDEPTAQLDMHTAATVSESLSRIARNDTIVVVSTHDP 184
Cdd:TIGR02673 159 LLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDL 197
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-185 |
1.99e-39 |
|
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: 133.75 E-value: 1.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 5 LDHVGHRYADG-PLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMRW-----------IF 72
Cdd:cd03225 2 LKNLSFSYPDGaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLslkelrrkvglVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 73 QNP-HGVAQRTAIDHVSLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEP 151
Cdd:cd03225 82 QNPdDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEP 161
|
170 180 190
....*....|....*....|....*....|....
gi 1447648657 152 TAQLDMHTAATVSESLSRIARNDTIVVVSTHDPN 185
Cdd:cd03225 162 TAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLD 195
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
2-185 |
1.57e-38 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 132.86 E-value: 1.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 2 RVDLDHVGHRYADGPLLfHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQG--IDSMR---------W 70
Cdd:COG1120 1 MLEAENLSVGYGGRPVL-DDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrdLASLSrrelarriaY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 71 IFQNPHGVAQRTAIDHVSL---PLL-AKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLM 146
Cdd:COG1120 80 VPQEPPAPFGLTVRELVALgryPHLgLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1447648657 147 LVDEPTAQLDMHTAATVSESLSRIARN-DTIVVVSTHDPN 185
Cdd:COG1120 160 LLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLN 199
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
4-198 |
1.64e-38 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 130.63 E-value: 1.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 4 DLDHVGHRYADGPLLfHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMRWifqNPHGVAQRTA 83
Cdd:cd03214 1 EVENLSVGYGGRTVL-DDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASL---SPKELARKIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 84 IdhvslpllakgLPrreaeeQArtlMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATV 163
Cdd:cd03214 77 Y-----------VP------QA---LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIEL 136
|
170 180 190
....*....|....*....|....*....|....*..
gi 1447648657 164 SESLSRIAR-NDTIVVVSTHDPN-TRDACTDIIDLKN 198
Cdd:cd03214 137 LELLRRLAReRGKTVVMVLHDLNlAARYADRVILLKD 173
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-200 |
1.46e-37 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 129.17 E-value: 1.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 5 LDHVGHRYADGPLLfHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVT-----RQGIDSMRW------IFQ 73
Cdd:COG4619 3 LEGLSFRVGGKPIL-SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYldgkpLSAMPPPEWrrqvayVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 74 NPHGVAQrTAIDHVSLPLLAKGlpRREAEEQARTLMDRFNLT-RVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPT 152
Cdd:COG4619 82 EPALWGG-TVRDNLPFPFQLRE--RKFDRERALELLERLGLPpDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1447648657 153 AQLDMHTAATVSESLSRIARND--TIVVVsTHDPN-TRDACTDIIDLKNYQ 200
Cdd:COG4619 159 SALDPENTRRVEELLREYLAEEgrAVLWV-SHDPEqIERVADRVLTLEAGR 208
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-153 |
4.53e-37 |
|
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: 125.84 E-value: 4.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 19 FHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDS-----------MRWIFQNPHGVAQRTAIDHV 87
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLtdderkslrkeIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 88 SLPLLAKGLPRREAEEQARTLMDRFNLT----RVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTA 153
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGdladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-200 |
1.08e-36 |
|
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: 125.43 E-value: 1.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 5 LDHVGHRYADGPLLfHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMRWIFqnphgvaqRTAI 84
Cdd:cd00267 2 IENLSFRYGGRTAL-DNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPL--------EELR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 85 DHVSLpllakgLPrreaeeqartlmdrfnltrvtdrrfaELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVS 164
Cdd:cd00267 73 RRIGY------VP--------------------------QLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLL 120
|
170 180 190
....*....|....*....|....*....|....*..
gi 1447648657 165 ESLSRIARNDTIVVVSTHDPNT-RDACTDIIDLKNYQ 200
Cdd:cd00267 121 ELLRELAEEGRTVIIVTHDPELaELAADRVIVLKDGK 157
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-198 |
1.80e-36 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 127.30 E-value: 1.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 5 LDHVGHRYADGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGID----------SMR----W 70
Cdd:cd03256 3 VENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDinklkgkalrQLRrqigM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 71 IFQNPHGVAQRTAIDHVSLPLLAK--------GLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQ 142
Cdd:cd03256 83 IFQQFNLIERLSVLENVLSGRLGRrstwrslfGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQ 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1447648657 143 PSLMLVDEPTAQLDMHTAATVSESLSRIARNDTI-VVVSTHDPN-TRDACTDIIDLKN 198
Cdd:cd03256 163 PKLILADEPVASLDPASSRQVMDLLKRINREEGItVIVSLHQVDlAREYADRIVGLKD 220
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
3-184 |
2.46e-36 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 129.83 E-value: 2.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADGPLLfHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGID---------SMRWIFQ 73
Cdd:COG3842 6 LELENVSKRYGDVTAL-DDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDvtglppekrNVGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 74 N----PHgvaqRTAIDHVSLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVD 149
Cdd:COG3842 85 DyalfPH----LTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLD 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 1447648657 150 EPTAQLDMHTAATVSESLSRI--ARNDTIVVVsTHDP 184
Cdd:COG3842 161 EPLSALDAKLREEMREELRRLqrELGITFIYV-THDQ 196
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-198 |
5.86e-36 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 124.95 E-value: 5.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 5 LDHVGHRYaDGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMR---WIfqnphG-VAQ 80
Cdd:cd03235 2 VEDLTVSY-GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKerkRI-----GyVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 81 RTAIDH---------VSLPLLAK----GLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLML 147
Cdd:cd03235 76 RRSIDRdfpisvrdvVLMGLYGHkglfRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1447648657 148 VDEPTAQLDMHTAATVSESLSRIARNDTIVVVSTHDPNT-RDACTDIIDLKN 198
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLvLEYFDRVLLLNR 207
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3-198 |
6.21e-35 |
|
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: 122.30 E-value: 6.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADGPLLfHDLTASLMPGhVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMR----------WIF 72
Cdd:cd03264 1 LQLENLTKRYGKKRAL-DGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKqpqklrrrigYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 73 QNPHGVAQRTAIDHVSLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPT 152
Cdd:cd03264 79 QEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1447648657 153 AQLDMHTAATVSESLSRIARnDTIVVVSTHD-PNTRDACTDIIDLKN 198
Cdd:cd03264 159 AGLDPEERIRFRNLLSELGE-DRIVILSTHIvEDVESLCNQVAVLNK 204
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-191 |
9.59e-35 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 122.69 E-value: 9.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADGPLLFH---DLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGID------------- 66
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTalkDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDltllsgkelrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 67 -SMRWIFQNPHGVAQRTAIDHVSLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSL 145
Cdd:cd03258 82 rRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1447648657 146 MLVDEPTAQLDMHTAATVSESLSRIAR--NDTIVVVsTHDPNT-RDACT 191
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRelGLTIVLI-THEMEVvKRICD 209
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
3-198 |
1.86e-34 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 119.80 E-value: 1.86e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADGP-LLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGID-------SMR----W 70
Cdd:cd03228 1 IEFKNVSFSYPGRPkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDlrdldleSLRkniaY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 71 IFQNPHgvaqrtaidhvslpLLAkglprreaeeqaRTLmdRFNLtrvtdrrfaeLSGGEAQRLMLARAFAAQPSLMLVDE 150
Cdd:cd03228 81 VPQDPF--------------LFS------------GTI--RENI----------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1447648657 151 PTAQLDMHTAATVSESLSRIARNDTIVVVsTHDPNTRDACTDIIDLKN 198
Cdd:cd03228 123 ATSALDPETEALILEALRALAKGKTVIVI-AHRLSTIRDADRIIVLDD 169
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-184 |
4.30e-34 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 121.06 E-value: 4.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADGPL---LFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGID-----------SM 68
Cdd:COG1124 2 LEVRNLSVSYGQGGRrvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPvtrrrrkafrrRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 69 RWIFQNPHGVA--QRTAIDHVSLPLLAKGLPRREaeEQARTLMDRFNLT-RVTDRRFAELSGGEAQRLMLARAFAAQPSL 145
Cdd:COG1124 82 QMVFQDPYASLhpRHTVDRILAEPLRIHGLPDRE--ERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1447648657 146 MLVDEPTAQLDMHTAATVSESLSRI--ARNDTIVVVStHDP 184
Cdd:COG1124 160 LLLDEPTSALDVSVQAEILNLLKDLreERGLTYLFVS-HDL 199
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
18-196 |
6.04e-34 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 119.64 E-value: 6.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 18 LFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMR---------------WIFQNPHGVAQRT 82
Cdd:TIGR03608 13 ILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPlnskkaskfrreklgYLFQNFALIENET 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 83 AIDHVSLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAAT 162
Cdd:TIGR03608 93 VEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDPKNRDE 172
|
170 180 190
....*....|....*....|....*....|....
gi 1447648657 163 VSESLSRIARNDTIVVVSTHDPNTRDACTDIIDL 196
Cdd:TIGR03608 173 VLDLLLELNDEGKTIIIVTHDPEVAKQADRVIEL 206
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
3-183 |
1.26e-33 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 119.17 E-value: 1.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADGPLLfHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVT---------RQGIDSMR---- 69
Cdd:cd03262 1 IEIKNLHKSFGDFHVL-KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIidglkltddKKNINELRqkvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 70 WIFQN----PHgvaqRTAIDHVSL-PLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPS 144
Cdd:cd03262 80 MVFQQfnlfPH----LTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 1447648657 145 LMLVDEPTAQLDMHTAATVSESLSRIARNDTIVVVSTHD 183
Cdd:cd03262 156 VMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHE 194
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-196 |
2.03e-33 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 117.72 E-value: 2.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 11 RYADGPLLfHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSmrwifqnPHGVAQRTAIDHvSLP 90
Cdd:NF040873 1 GYGGRPVL-HGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGAR-------VAYVPQRSEVPD-SLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 91 LLAKGL--------------PRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLD 156
Cdd:NF040873 72 LTVRDLvamgrwarrglwrrLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1447648657 157 MHTAATVSESLSRIARNDTIVVVSTHDPNTRDACTDIIDL 196
Cdd:NF040873 152 AESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-196 |
3.11e-33 |
|
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: 123.94 E-value: 3.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 2 RVDLDHVGHRYADGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGI-----------DSMRW 70
Cdd:TIGR02857 321 SLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVpladadadswrDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 71 IFQNPHGVAQrTAIDHVslpLLAKGLPRREAEEQA--RTLMDRF------NLTRVTDRRFAELSGGEAQRLMLARAFAAQ 142
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENI---RLARPDASDAEIREAleRAGLDEFvaalpqGLDTPIGEGGAGLSGGQAQRLALARAFLRD 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1447648657 143 PSLMLVDEPTAQLDMHTAATVSESLSRIARNDTIVVVsTHDPNTRDACTDIIDL 196
Cdd:TIGR02857 477 APLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLV-THRLALAALADRIVVL 529
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
4-198 |
3.40e-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: 117.74 E-value: 3.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 4 DLDHVGHRYADGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMRWI-FQNPHGVAQRT 82
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKErRKSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 83 A----IDHVSLPLL--AKGLPrrEAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLD 156
Cdd:cd03226 81 DyqlfTDSVREELLlgLKELD--AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1447648657 157 MHTAATVSESLSRIARNDTIVVVSTHDPN-TRDACTDIIDLKN 198
Cdd:cd03226 159 YKNMERVGELIRELAAQGKAVIVITHDYEfLAKVCDRVLLLAN 201
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
11-183 |
3.44e-33 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 118.76 E-value: 3.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 11 RYADGPLL---FHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQG--IDSMR-------------WIF 72
Cdd:PRK11629 14 RYQEGSVQtdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpMSKLSsaakaelrnqklgFIY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 73 QNPHGVAQRTAIDHVSLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPT 152
Cdd:PRK11629 94 QFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPT 173
|
170 180 190
....*....|....*....|....*....|..
gi 1447648657 153 AQLDMHTAATVSESLSRI-ARNDTIVVVSTHD 183
Cdd:PRK11629 174 GNLDARNADSIFQLLGELnRLQGTAFLVVTHD 205
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
8-183 |
4.26e-33 |
|
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: 117.89 E-value: 4.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 8 VGHRYADGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGID--------------SMRWIFQ 73
Cdd:cd03292 6 VTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDvsdlrgraipylrrKIGVVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 74 NPHGVAQRTAIDHVSLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTA 153
Cdd:cd03292 86 DFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTG 165
|
170 180 190
....*....|....*....|....*....|
gi 1447648657 154 QLDMHTAATVSESLSRIARNDTIVVVSTHD 183
Cdd:cd03292 166 NLDPDTTWEIMNLLKKINKAGTTVVVATHA 195
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
19-197 |
8.87e-33 |
|
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: 117.15 E-value: 8.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 19 FHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVT----RQGID----------SMR-----WIFQNPHGVA 79
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILvrhdGGWVDlaqaspreilALRrrtigYVSQFLRVIP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 80 QRTAIDHVSLPLLAKGLPRREAEEQARTLMDRFNLtrvtDRRFAEL-----SGGEAQRLMLARAFAAQPSLMLVDEPTAQ 154
Cdd:COG4778 107 RVSALDVVAEPLLERGVDREEARARARELLARLNL----PERLWDLppatfSGGEQQRVNIARGFIADPPLLLLDEPTAS 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1447648657 155 LDMHTAATVSESLSRIARNDTIVVVSTHDPNTRDA-CTDIIDLK 197
Cdd:COG4778 183 LDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAvADRVVDVT 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-183 |
1.10e-32 |
|
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: 122.32 E-value: 1.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADGP----LLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGID-------SMRW- 70
Cdd:COG1123 261 LEVRNLSKRYPVRGkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDltklsrrSLREl 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 71 ------IFQNPHG--VAQRTAIDHVSLPL-LAKGLPRREAEEQARTLMDRFNL-TRVTDRRFAELSGGEAQRLMLARAFA 140
Cdd:COG1123 341 rrrvqmVFQDPYSslNPRMTVGDIIAEPLrLHGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1447648657 141 AQPSLMLVDEPTAQLDMHTAATVSESLSRIAR--NDTIVVVsTHD 183
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRelGLTYLFI-SHD 464
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-183 |
3.50e-32 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 115.86 E-value: 3.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADGPLLfHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVT---------RQGIDSMR---- 69
Cdd:COG1126 2 IEIENLHKSFGDLEVL-KGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITvdgedltdsKKDINKLRrkvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 70 WIFQN----PHgvaqRTAIDHVSL-PLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPS 144
Cdd:COG1126 81 MVFQQfnlfPH----LTVLENVTLaPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1447648657 145 LMLVDEPTAQLD--MhtaatVSESLS---RIARND-TIVVVsTHD 183
Cdd:COG1126 157 VMLFDEPTSALDpeL-----VGEVLDvmrDLAKEGmTMVVV-THE 195
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-182 |
8.63e-32 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 115.18 E-value: 8.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADGPLLfHDLTASLMPG-HVyALTGPSGAGKSTLLGIIAGWTTPAEGQV-----TRQGIDSMRWIfqnph 76
Cdd:COG1119 4 LELRNVTVRRGGKTIL-DDISWTVKPGeHW-AILGPNGAGKSTLLSLITGDLPPTYGNDvrlfgERRGGEDVWEL----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 77 gvaqRTAIDHVSLPLLAK-------------------GLPRR---EAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLM 134
Cdd:COG1119 77 ----RKRIGLVSPALQLRfprdetvldvvlsgffdsiGLYREptdEQRERARELLELLGLAHLADRPFGTLSQGEQRRVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1447648657 135 LARAFAAQPSLMLVDEPTAQLDMHTAATVSESLSRIARND--TIVVVSTH 182
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGapTLVLVTHH 202
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-198 |
1.34e-31 |
|
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: 120.32 E-value: 1.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 2 RVDLDHVGHRYA-DGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGID----SMRWIFQNPH 76
Cdd:COG2274 473 DIELENVSFRYPgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDlrqiDPASLRRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 77 GVAQ------RTAIDHVSLpllakGLPR------REAEEQA------RTLMDRFNlTRVTDRRfAELSGGEAQRLMLARA 138
Cdd:COG2274 553 VVLQdvflfsGTIRENITL-----GDPDatdeeiIEAARLAglhdfiEALPMGYD-TVVGEGG-SNLSGGQRQRLAIARA 625
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 139 FAAQPSLMLVDEPTAQLDMHTAATVSESLSRIARNDTIVVVsTHDPNTRDACTDIIDLKN 198
Cdd:COG2274 626 LLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIII-AHRLSTIRLADRIIVLDK 684
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
3-183 |
1.64e-31 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 114.26 E-value: 1.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADGPLLfHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGID---------SMRWIFQ 73
Cdd:cd03300 1 IELENVSKFYGGFVAL-DGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDitnlpphkrPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 74 N----PHgvaqRTAIDHVSLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVD 149
Cdd:cd03300 80 NyalfPH----LTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 1447648657 150 EPTAQLDMHTAATVSESLSRIARN--DTIVVVsTHD 183
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKElgITFVFV-THD 190
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3-198 |
1.70e-31 |
|
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: 112.49 E-value: 1.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADGPLLfHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDsmrwIFQNPHGVAQRT 82
Cdd:cd03230 1 IEVRNLSKRYGKKTAL-DDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKD----IKKEPEEVKRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 83 AIdhvslpllakgLPrreaeeQARTLMDRFnltrvTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAAT 162
Cdd:cd03230 76 GY-----------LP------EEPSLYENL-----TVRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRRE 133
|
170 180 190
....*....|....*....|....*....|....*....
gi 1447648657 163 VSESLSRIARNDTIVVVSTHdpNTRDA---CTDIIDLKN 198
Cdd:cd03230 134 FWELLRELKKEGKTILLSSH--ILEEAerlCDRVAILNN 170
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-183 |
4.42e-31 |
|
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: 112.98 E-value: 4.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADGPLLFH---DLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGID------------- 66
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKaldDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDllklsrrlrkirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 67 -SMRWIFQNPHGV--AQRTAIDHVSLPLLAKGLPRREAEEQARTLMDRFNL---TRVTDRRFAELSGGEAQRLMLARAFA 140
Cdd:cd03257 82 kEIQMVFQDPMSSlnPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1447648657 141 AQPSLMLVDEPTAQLDMHTAATVSESLSRIA--RNDTIVVVsTHD 183
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQeeLGLTLLFI-THD 205
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-183 |
4.48e-31 |
|
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: 118.08 E-value: 4.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADGPL-LFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPA---EGQVTRQGIDSMRW-------- 70
Cdd:COG1123 5 LEVRDLSVRYPGGDVpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELsealrgrr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 71 ---IFQNP-HGVAQRTAIDHVSLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLM 146
Cdd:COG1123 85 igmVFQDPmTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLL 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 1447648657 147 LVDEPTAQLDMHTAATVSESLSRIARN-DTIVVVSTHD 183
Cdd:COG1123 165 IADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHD 202
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
3-184 |
2.83e-30 |
|
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: 110.73 E-value: 2.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADGPLLfHDLTASLMPGHVYALTGPSGAGKSTLLGIIAG-----WTTPAEGQVTRQGIDSMRW------- 70
Cdd:cd03260 1 IELRDLNVYYGDKHAL-KDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDIYDLdvdvlel 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 71 ------IFQNPHgVAQRTAIDHVSLPLLAKG-LPRREAEEQARTLMDRFNLT-RVTDRRFA-ELSGGEAQRLMLARAFAA 141
Cdd:cd03260 80 rrrvgmVFQKPN-PFPGSIYDNVAYGLRLHGiKLKEELDERVEEALRKAALWdEVKDRLHAlGLSGGQQQRLCLARALAN 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1447648657 142 QPSLMLVDEPTAQLDMHTAATVSESLSRIARNDTIVVVsTHDP 184
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIV-THNM 200
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-184 |
6.14e-30 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 112.55 E-value: 6.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 1 MRVDLDHVGHRYADGPLLfHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMRWI--------- 71
Cdd:COG1118 1 MSIEVRNISKRFGSFTLL-DDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLpprerrvgf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 72 -FQN----PHgvaqRTAIDHVSLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLM 146
Cdd:COG1118 80 vFQHyalfPH----MTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVL 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 1447648657 147 LVDEPTAQLDMHTAATVSESLSRIARNDTIVVV-STHDP 184
Cdd:COG1118 156 LLDEPFGALDAKVRKELRRWLRRLHDELGGTTVfVTHDQ 194
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-183 |
9.79e-30 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 109.80 E-value: 9.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADGPLLfHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGID------SMRWI----- 71
Cdd:PRK09493 2 IEFKNVSKHFGPTQVL-HNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKvndpkvDERLIrqeag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 72 --FQNPHGVAQRTAIDHVSL-PLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLV 148
Cdd:PRK09493 81 mvFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 1447648657 149 DEPTAQLD---MHTAATVSESLsriARNDTIVVVSTHD 183
Cdd:PRK09493 161 DEPTSALDpelRHEVLKVMQDL---AEEGMTMVIVTHE 195
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
3-193 |
1.21e-29 |
|
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: 109.13 E-value: 1.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADGPllFH---DLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDsmrwIFQNPHGVA 79
Cdd:cd03263 1 LQIRNLTKTYKKGT--KPavdDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYS----IRTDRKAAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 80 QR--------------TAIDHVSLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSL 145
Cdd:cd03263 75 QSlgycpqfdalfdelTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1447648657 146 MLVDEPTAQLDMHTAATVSESLSRIARNDTIvVVSTHDPNTRDA-CTDI 193
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEVRKGRSI-ILTTHSMDEAEAlCDRI 202
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-196 |
1.26e-29 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 114.01 E-value: 1.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 5 LDHVGHRYAdGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMRWIFQNPHGVAQRTAI 84
Cdd:COG0488 1 LENLSKSFG-GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 85 DHV--SLPLLAKGLPRRE------------------------------AEEQARTLMDRFNLTRVT-DRRFAELSGGEAQ 131
Cdd:COG0488 80 DTVldGDAELRALEAELEeleaklaepdedlerlaelqeefealggweAEARAEEILSGLGFPEEDlDRPVSELSGGWRR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1447648657 132 RLMLARAFAAQPSLMLVDEPTAQLDMHTAATVSESLSRiaRNDTIVVVStHDpntRD----ACTDIIDL 196
Cdd:COG0488 160 RVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKN--YPGTVLVVS-HD---RYfldrVATRILEL 222
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
17-184 |
1.55e-29 |
|
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: 108.54 E-value: 1.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 17 LLFHDLTASL-MPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQV---------TRQGID------SMRWIFQN----PH 76
Cdd:cd03297 10 LPDFTLKIDFdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngtvlfdSRKKINlppqqrKIGLVFQQyalfPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 77 -GVAQrtaidhvSLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQL 155
Cdd:cd03297 90 lNVRE-------NLAFGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSAL 162
|
170 180 190
....*....|....*....|....*....|
gi 1447648657 156 DMHTAATVSESLSRIARNDTIVVV-STHDP 184
Cdd:cd03297 163 DRALRLQLLPELKQIKKNLNIPVIfVTHDL 192
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
28-190 |
2.73e-29 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 108.33 E-value: 2.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 28 PGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMR---------------WIFQNPHGVAQRTAIDHVSLPLL 92
Cdd:PRK10584 35 RGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmdeearaklrakhvgFVFQSFMLIPTLNALENVELPAL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 93 AKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVSESLSRIAR 172
Cdd:PRK10584 115 LRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNR 194
|
170
....*....|....*....
gi 1447648657 173 N-DTIVVVSTHDPNTRDAC 190
Cdd:PRK10584 195 EhGTTLILVTHDLQLAARC 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
2-184 |
5.58e-29 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 110.16 E-value: 5.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 2 RVDLDHVGHRYADGPLLfHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGID-----------SMrw 70
Cdd:COG3839 3 SLELENVSKSYGGVEAL-KDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDvtdlppkdrniAM-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 71 IFQN----PHgvaqRTAIDHVSLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLM 146
Cdd:COG3839 80 VFQSyalyPH----MTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVF 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 1447648657 147 LVDEPTAQLDMHTAATVSESLSRI-ARNDTIVVVSTHDP 184
Cdd:COG3839 156 LLDEPLSNLDAKLRVEMRAEIKRLhRRLGTTTIYVTHDQ 194
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
5-183 |
7.37e-29 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 107.86 E-value: 7.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 5 LDHVGHRYADGPLLfHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGI-----DSMRWI-FQNPHGV 78
Cdd:PRK11248 4 ISHLYADYGGKPAL-EDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKpvegpGAERGVvFQNEGLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 79 AQRTAIDHVSLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMH 158
Cdd:PRK11248 83 PWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAF 162
|
170 180
....*....|....*....|....*.
gi 1447648657 159 TAATVSESLSRI-ARNDTIVVVSTHD 183
Cdd:PRK11248 163 TREQMQTLLLKLwQETGKQVLLITHD 188
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-183 |
1.99e-28 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 106.87 E-value: 1.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 1 MRVDLDHVGHRYADG---PLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTR-----QGIDSMRWI- 71
Cdd:COG4525 2 SMLTVRHVSVRYPGGgqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLdgvpvTGPGADRGVv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 72 FQNPHGVAQRTAIDHVSLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEP 151
Cdd:COG4525 82 FQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEP 161
|
170 180 190
....*....|....*....|....*....|...
gi 1447648657 152 TAQLDMHTAATVSESLSRI-ARNDTIVVVSTHD 183
Cdd:COG4525 162 FGALDALTREQMQELLLDVwQRTGKGVFLITHS 194
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-200 |
3.00e-28 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 110.63 E-value: 3.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 2 RVDLDHVGHRYADGP-LLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMRWIFQNPHG--- 77
Cdd:COG4987 333 SLELEDVSFRYPGAGrPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRria 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 78 -VAQRTAIDHVSLP---LLAKGlprrEA-EEQARTLMDRFNL------------TRV--TDRRfaeLSGGEAQRLMLARA 138
Cdd:COG4987 413 vVPQRPHLFDTTLRenlRLARP----DAtDEELWAALERVGLgdwlaalpdgldTWLgeGGRR---LSGGERRRLALARA 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1447648657 139 FAAQPSLMLVDEPTAQLDMHTAATVSESLSRIARNDTIVVVsTHDPNTRDACTDIIDLKNYQ 200
Cdd:COG4987 486 LLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLI-THRLAGLERMDRILVLEDGR 546
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
20-183 |
8.91e-28 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 105.12 E-value: 8.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 20 HDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGID----SMRWI--------FQNPHGVAQRTAIDHV 87
Cdd:COG0411 21 DDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDitglPPHRIarlgiartFQNPRLFPELTVLENV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 88 SLPLLAK----------GLPR-----REAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPT 152
Cdd:COG0411 101 LVAAHARlgrgllaallRLPRarreeREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPA 180
|
170 180 190
....*....|....*....|....*....|...
gi 1447648657 153 AQLDMHTAATVSESLSRIARND--TIVVVStHD 183
Cdd:COG0411 181 AGLNPEETEELAELIRRLRDERgiTILLIE-HD 212
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-185 |
1.07e-27 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 104.81 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 6 DHVGHRYADGPLLfHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMRWifqNPHGVAQR---- 81
Cdd:COG4559 5 ENLSVRLGGRTLL-DDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAW---SPWELARRravl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 82 ----------TAIDHVSLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFA-------AQPS 144
Cdd:COG4559 81 pqhsslafpfTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1447648657 145 LMLVDEPTAQLDMHTAATVSESLSRIARNDTIVVVSTHDPN 185
Cdd:COG4559 161 WLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLN 201
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
5-196 |
1.25e-27 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 104.03 E-value: 1.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 5 LDHVGHRYADGPLLfHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGID-----------SMRWIFQ 73
Cdd:PRK10247 10 LQNVGYLAGDAKIL-NNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDistlkpeiyrqQVSYCAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 74 NPhGVAQRTAIDHVSLPLLAkglpRREAEEQARTLMD--RFNLTRVT-DRRFAELSGGEAQRLMLARAFAAQPSLMLVDE 150
Cdd:PRK10247 89 TP-TLFGDTVYDNLIFPWQI----RNQQPDPAIFLDDleRFALPDTIlTKNIAELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1447648657 151 PTAQLDMHTAATVSESLSRIARNDTIVVV-STHDPNTRDACTDIIDL 196
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYVREQNIAVLwVTHDKDEINHADKVITL 210
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
3-192 |
1.61e-27 |
|
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: 103.74 E-value: 1.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADGPLLfHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQG--IDSM----------RW 70
Cdd:cd03261 1 IELRGLTKSFGGRTVL-KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGedISGLseaelyrlrrRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 71 --IFQNPHGVAQRTAIDHVSLPLLAKG-LPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLML 147
Cdd:cd03261 80 gmLFQSGALFDSLTVFENVAFPLREHTrLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1447648657 148 VDEPTAQLDMHTAATVSESLSRIAR--NDTIVVVsTHDPNTRDACTD 192
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRSLKKelGLTSIMV-THDLDTAFAIAD 205
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
3-183 |
1.66e-27 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 103.92 E-value: 1.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMRW-----------I 71
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQdpvelrrkigyV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 72 FQN----PHgvaqRTAIDHVSLPLLAKGLPRREAEEQARTLMDRFNLTRVT--DRRFAELSGGEAQRLMLARAFAAQPSL 145
Cdd:cd03295 81 IQQiglfPH----MTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEfaDRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1447648657 146 MLVDEPTAQLDMHTAATVSESLSRIAR--NDTIVVVsTHD 183
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFV-THD 195
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-198 |
1.74e-27 |
|
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: 101.91 E-value: 1.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 5 LDHVGHRYADG-PLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMRWiFQNPHGvaqrta 83
Cdd:cd03246 3 VENVSFRYPGAePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQW-DPNELG------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 84 iDHV-SLPllakglprREAEEQARTLMDrfNLtrvtdrrfaeLSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAAT 162
Cdd:cd03246 76 -DHVgYLP--------QDDELFSGSIAE--NI----------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERA 134
|
170 180 190
....*....|....*....|....*....|....*..
gi 1447648657 163 VSESLSRI-ARNDTIVVVsTHDPNTRDACTDIIDLKN 198
Cdd:cd03246 135 LNQAIAALkAAGATRIVI-AHRPETLASADRILVLED 170
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
21-183 |
2.02e-27 |
|
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: 103.67 E-value: 2.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 21 DLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMRWI------------FQNPHGVAQRTAIDHVS 88
Cdd:cd03219 18 DVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPpheiarlgigrtFQIPRLFPELTVLENVM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 89 LPLLAKGLP----------RREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMH 158
Cdd:cd03219 98 VAAQARTGSglllararreEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPE 177
|
170 180
....*....|....*....|....*
gi 1447648657 159 TAATVSESLSRIARNDTIVVVSTHD 183
Cdd:cd03219 178 ETEELAELIRELRERGITVLLVEHD 202
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
28-183 |
4.59e-27 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 104.77 E-value: 4.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 28 PGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVT-----------------RQGIdSMrwIFQNPHGVAQRTAIDHVSLP 90
Cdd:COG1135 30 KGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLvdgvdltalserelraaRRKI-GM--IFQHFNLLSSRTVAENVALP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 91 LLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVSESLSRI 170
Cdd:COG1135 107 LEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDI 186
|
170
....*....|....*..
gi 1447648657 171 arND----TIVVVsTHD 183
Cdd:COG1135 187 --NRelglTIVLI-THE 200
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
3-183 |
1.39e-26 |
|
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: 99.95 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADGPLLfHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMRWIFQNPhgvAQRT 82
Cdd:cd03229 1 LELKNVSKRYGQKTVL-NDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELP---PLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 83 AIDHVSlpllakglprreaeeQARTLMdrFNLTRVTDRRFAeLSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAAT 162
Cdd:cd03229 77 RIGMVF---------------QDFALF--PHLTVLENIALG-LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRRE 138
|
170 180
....*....|....*....|..
gi 1447648657 163 VSESLSRIARNDTI-VVVSTHD 183
Cdd:cd03229 139 VRALLKSLQAQLGItVVLVTHD 160
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
19-183 |
1.55e-26 |
|
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: 101.21 E-value: 1.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 19 FHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVT-----------------RQGI----------DSMRwI 71
Cdd:COG1127 21 LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILvdgqditglsekelyelRRRIgmlfqggalfDSLT-V 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 72 FQNphgvaqrtaidhVSLPLLA-KGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDE 150
Cdd:COG1127 100 FEN------------VAFPLREhTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDE 167
|
170 180 190
....*....|....*....|....*....|....*
gi 1447648657 151 PTAQLDMHTAATVSESLSRI--ARNDTIVVVsTHD 183
Cdd:COG1127 168 PTAGLDPITSAVIDELIRELrdELGLTSVVV-THD 201
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
3-183 |
2.97e-26 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 100.02 E-value: 2.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADGPLLfHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMRW---------IFQ 73
Cdd:cd03301 1 VELENVTKRFGNVTAL-DDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLppkdrdiamVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 74 N----PHgvaqRTAIDHVSLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVD 149
Cdd:cd03301 80 NyalyPH----MTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190
....*....|....*....|....*....|....*
gi 1447648657 150 EPTAQLDMHTAATVSESLSRIARN-DTIVVVSTHD 183
Cdd:cd03301 156 EPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHD 190
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-183 |
3.69e-26 |
|
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: 100.23 E-value: 3.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 21 DLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEG-------QVTRQGIDSMRwIFQNPHGVAQRTAIDHVSLPL-- 91
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGgvilegkQITEPGPDRMV-VFQNYSLLPWLTVRENIALAVdr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 92 LAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVSESLSRIA 171
Cdd:TIGR01184 82 VLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQIW 161
|
170
....*....|...
gi 1447648657 172 R-NDTIVVVSTHD 183
Cdd:TIGR01184 162 EeHRVTVLMVTHD 174
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
5-189 |
4.44e-26 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 99.83 E-value: 4.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 5 LDHVGHRYADGPLLFhDLTASlmPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGID-----------SMrwIFQ 73
Cdd:COG3840 4 LDDLTYRYGDFPLRF-DLTIA--AGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDltalppaerpvSM--LFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 74 N----PH-GVAQRTAIDhvslplLAKGLpRREAEEQAR--TLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLM 146
Cdd:COG3840 79 EnnlfPHlTVAQNIGLG------LRPGL-KLTAEQRAQveQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPIL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1447648657 147 LVDEPTAQLDmhtAATVSESLSRIA-----RNDTIVVVsTHDPntRDA 189
Cdd:COG3840 152 LLDEPFSALD---PALRQEMLDLVDelcreRGLTVLMV-THDP--EDA 193
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
14-200 |
4.85e-26 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 99.48 E-value: 4.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 14 DGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTP---AEGQVTRQG--IDSM----RWI---FQ----NPH- 76
Cdd:COG4136 12 GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGrrLTALpaeqRRIgilFQddllFPHl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 77 GVAQRTAIDhvslplLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLD 156
Cdd:COG4136 92 SVGENLAFA------LPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1447648657 157 MHTAATVSE-SLSRIARNDTIVVVSTHDPNTRDACTDIIDLKNYQ 200
Cdd:COG4136 166 AALRAQFREfVFEQIRQRGIPALLVTHDEEDAPAAGRVLDLGNWQ 210
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
21-195 |
5.54e-26 |
|
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: 99.37 E-value: 5.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 21 DLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMR----------WIFQNPHGVAQRTAIDHVSLP 90
Cdd:cd03265 18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVReprevrrrigIVFQDLSVDDELTGWENLYIH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 91 LLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVSESLSRI 170
Cdd:cd03265 98 ARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKL 177
|
170 180
....*....|....*....|....*....
gi 1447648657 171 -ARNDTIVVVSTHDPNTRDACTD---IID 195
Cdd:cd03265 178 kEEFGMTILLTTHYMEEAEQLCDrvaIID 206
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
21-198 |
1.32e-25 |
|
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: 98.12 E-value: 1.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 21 DLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGidsmrwifqNPHGVAQRTAIDHV------------- 87
Cdd:cd03269 18 DISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG---------KPLDIAARNRIGYLpeerglypkmkvi 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 88 -SLPLLA--KGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVS 164
Cdd:cd03269 89 dQLVYLAqlKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLK 168
|
170 180 190
....*....|....*....|....*....|....*
gi 1447648657 165 ESLSRIARNDTIVVVSTHDPNT-RDACTDIIDLKN 198
Cdd:cd03269 169 DVIRELARAGKTVILSTHQMELvEELCDRVLLLNK 203
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-183 |
1.41e-25 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 98.95 E-value: 1.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 1 MRVDLDHVGHRYADGPLLfHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMR---------WI 71
Cdd:cd03296 1 MSIEVRNVSKRFGDFVAL-DDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDvpvqernvgFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 72 FQNPHGVAQRTAIDHVSLPLLAKGLPRR--EAEEQART--LMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLML 147
Cdd:cd03296 80 FQHYALFRHMTVFDNVAFGLRVKPRSERppEAEIRAKVheLLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1447648657 148 VDEPTAQLDmhtaATVSESLSRIAR--NDTIVVVS---THD 183
Cdd:cd03296 160 LDEPFGALD----AKVRKELRRWLRrlHDELHVTTvfvTHD 196
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
7-182 |
2.19e-25 |
|
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: 97.67 E-value: 2.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 7 HVGHRYADGPLLfHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDsmrwiFQNPHGVAQR----- 81
Cdd:cd03268 5 DLTKTYGKKRVL-DDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKS-----YQKNIEALRRigali 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 82 ---------TAIDHVSLPLLAKGLPRREAEEqartLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPT 152
Cdd:cd03268 79 eapgfypnlTARENLRLLARLLGIRKKRIDE----VLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180 190
....*....|....*....|....*....|
gi 1447648657 153 AQLDMHTAATVSESLSRIARNDTIVVVSTH 182
Cdd:cd03268 155 NGLDPDGIKELRELILSLRDQGITVLISSH 184
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-198 |
2.41e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 102.07 E-value: 2.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYaDGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTR----------QGIDSMRwif 72
Cdd:COG0488 316 LELEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLgetvkigyfdQHQEELD--- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 73 qnphgvAQRTAIDHVSlpllakGLPRREAEEQARTLMDRFNLTRvtDRRF---AELSGGEAQRLMLARAFAAQPSLMLVD 149
Cdd:COG0488 392 ------PDKTVLDELR------DGAPGGTEQEVRGYLGRFLFSG--DDAFkpvGVLSGGEKARLALAKLLLSPPNVLLLD 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1447648657 150 EPTAQLDMHTAATVSESLsriarND---TIVVVStHDpntRDA----CTDIIDLKN 198
Cdd:COG0488 458 EPTNHLDIETLEALEEAL-----DDfpgTVLLVS-HD---RYFldrvATRILEFED 504
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-180 |
2.63e-25 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 102.17 E-value: 2.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 2 RVDLDHVGHRYADGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGID-------SMR----W 70
Cdd:COG1132 339 EIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDirdltleSLRrqigV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 71 IFQNPHgVAQRTAIDHVSLpllakGLPR------REAEEQA------RTLMDRFNlTRVTDRrFAELSGGEAQRLMLARA 138
Cdd:COG1132 419 VPQDTF-LFSGTIRENIRY-----GRPDatdeevEEAAKAAqahefiEALPDGYD-TVVGER-GVNLSGGQRQRIAIARA 490
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1447648657 139 FAAQPSLMLVDEPTAQLDMHTAATVSESLSRIARNDTIVVVS 180
Cdd:COG1132 491 LLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIA 532
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
25-183 |
3.25e-25 |
|
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: 97.79 E-value: 3.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 25 SLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGID------SMR---WIFQN----PHgvaqRTAIDHVSLPL 91
Cdd:cd03299 21 EVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDitnlppEKRdisYVPQNyalfPH----MTVYKNIAYGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 92 LAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVSESLSRIA 171
Cdd:cd03299 97 KKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIR 176
|
170
....*....|...
gi 1447648657 172 RN-DTIVVVSTHD 183
Cdd:cd03299 177 KEfGVTVLHVTHD 189
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
3-200 |
3.67e-25 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 97.25 E-value: 3.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMR------------- 69
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRlknrevpflrrqi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 70 -WIFQNPHGVAQRTAIDHVSLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLV 148
Cdd:PRK10908 82 gMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1447648657 149 DEPTAQLDMHTAATVSESLSRIARNDTIVVVSTHDpntrdacTDIIDLKNYQ 200
Cdd:PRK10908 162 DEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHD-------IGLISRRSYR 206
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
15-183 |
5.70e-25 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 97.51 E-value: 5.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 15 GPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVtRQG---IDSMR-----------------WIFQN 74
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTI-RVGditIDTARslsqqkglirqlrqhvgFVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 75 ----PHgvaqRTAIDHV-SLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVD 149
Cdd:PRK11264 94 fnlfPH----RTVLENIiEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFD 169
|
170 180 190
....*....|....*....|....*....|....
gi 1447648657 150 EPTAQLDMHTAATVSESLSRIARNDTIVVVSTHD 183
Cdd:PRK11264 170 EPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHE 203
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
18-184 |
8.69e-25 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 95.70 E-value: 8.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 18 LFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPA--EGQVTRQGIDSMRWIFQNPHG-VAQRtaiDHVslpllak 94
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPLDKRSFRKIIGyVPQD---DIL------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 95 gLPRREAEEqarTLMDRFNLTRvtdrrfaeLSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVSESLSRIARND 174
Cdd:cd03213 94 -HPTLTVRE---TLMFAAKLRG--------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTG 161
|
170
....*....|
gi 1447648657 175 TIVVVSTHDP 184
Cdd:cd03213 162 RTIICSIHQP 171
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
17-184 |
1.26e-24 |
|
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: 96.19 E-value: 1.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 17 LLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAG---WTTPAEGQVTRQGIDSMRWIFQN--PHGVAQRTAIDHV---- 87
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQPRKPDQFQKcvAYVRQDDILLPGLtvre 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 88 SLPLLAK-GLPRREAEEQ-----ARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAA 161
Cdd:cd03234 101 TLTYTAIlRLPRKSSDAIrkkrvEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTAL 180
|
170 180
....*....|....*....|...
gi 1447648657 162 TVSESLSRIARNDTIVVVSTHDP 184
Cdd:cd03234 181 NLVSTLSQLARRNRIVILTIHQP 203
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
18-185 |
1.75e-24 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 96.38 E-value: 1.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 18 LFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMRWifqNPHGVAQRTAI----DHVSLPLLA 93
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADW---SPAELARRRAVlpqhSSLSFPFTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 94 K------GLPRREAEEQARTL----MDRFNLTRVTDRRFAELSGGEAQRLMLARAFA------AQPSLMLVDEPTAQLDM 157
Cdd:PRK13548 94 EevvamgRAPHGLSRAEDDALvaaaLAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDL 173
|
170 180 190
....*....|....*....|....*....|....
gi 1447648657 158 -HtaatvSESLSRIARNDTI-----VVVSTHDPN 185
Cdd:PRK13548 174 aH-----QHHVLRLARQLAHerglaVIVVLHDLN 202
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-183 |
2.02e-24 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 97.85 E-value: 2.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 1 MRVDLDHVGHRYADGPLLfHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMR---------WI 71
Cdd:PRK10851 1 MSIEIANIKKSFGRTQVL-NDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRlhardrkvgFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 72 FQNPHGVAQRTAIDHVSLPLlaKGLPRRE------AEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSL 145
Cdd:PRK10851 80 FQHYALFRHMTVFDNIAFGL--TVLPRRErpnaaaIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1447648657 146 MLVDEPTAQLDmhtaATVSESLSRIARN------DTIVVVsTHD 183
Cdd:PRK10851 158 LLLDEPFGALD----AQVRKELRRWLRQlheelkFTSVFV-THD 196
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
21-185 |
2.66e-24 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 98.38 E-value: 2.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 21 DLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGID----SMRWIFQNPHGVAQ----------RTAIDH 86
Cdd:PRK09536 21 GVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDvealSARAASRRVASVPQdtslsfefdvRQVVEM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 87 VSLPLLAKGLPRREAEEQA-RTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVSE 165
Cdd:PRK09536 101 GRTPHRSRFDTWTETDRAAvERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLE 180
|
170 180
....*....|....*....|
gi 1447648657 166 SLSRIARNDTIVVVSTHDPN 185
Cdd:PRK09536 181 LVRRLVDDGKTAVAAIHDLD 200
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
20-185 |
3.96e-24 |
|
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: 95.79 E-value: 3.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 20 HDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGID---------------SMRWIFQN----PHgvaq 80
Cdd:cd03294 41 NDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDiaamsrkelrelrrkKISMVFQSfallPH---- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 81 RTAIDHVSLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTA 160
Cdd:cd03294 117 RTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIR 196
|
170 180
....*....|....*....|....*..
gi 1447648657 161 ATVSESLSRIARN--DTIVVVsTHDPN 185
Cdd:cd03294 197 REMQDELLRLQAElqKTIVFI-THDLD 222
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
3-198 |
8.57e-24 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 91.74 E-value: 8.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADGPLlFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRqgidsmrwifqnphgvAQRT 82
Cdd:cd03221 1 IELENLSKTYGGKLL-LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW----------------GSTV 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 83 AIDHvslpllakglprreaeeqartlmdrfnltrvtdrrFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAAT 162
Cdd:cd03221 64 KIGY-----------------------------------FEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEA 108
|
170 180 190
....*....|....*....|....*....|....*..
gi 1447648657 163 VSESLSRIarNDTIVVVStHDPNTRDA-CTDIIDLKN 198
Cdd:cd03221 109 LEEALKEY--PGTVILVS-HDRYFLDQvATKIIELED 142
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-183 |
1.03e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 95.18 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADGPLLfHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGidsmrwifqNPHGVAQR- 81
Cdd:COG4152 2 LELKGLTKRFGDKTAV-DDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG---------EPLDPEDRr 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 82 ---------------TAIDHvsLPLLA--KGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPS 144
Cdd:COG4152 72 rigylpeerglypkmKVGEQ--LVYLArlKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPE 149
|
170 180 190
....*....|....*....|....*....|....*....
gi 1447648657 145 LMLVDEPTAQLDMHTAATVSESLSRIARNDTIVVVSTHD 183
Cdd:COG4152 150 LLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQ 188
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
20-182 |
1.52e-23 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 95.64 E-value: 1.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 20 HDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGID--------------SMRWIFQNPHGVAQRTAID 85
Cdd:PRK11153 22 NNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDltalsekelrkarrQIGMIFQHFNLLSSRTVFD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 86 HVSLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVSE 165
Cdd:PRK11153 102 NVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILE 181
|
170
....*....|....*....
gi 1447648657 166 SLSRIAR--NDTIVVVsTH 182
Cdd:PRK11153 182 LLKDINRelGLTIVLI-TH 199
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
3-185 |
1.79e-23 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 93.61 E-value: 1.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADGPLLfHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMRWifqNPHGVAQRT 82
Cdd:COG4604 2 IEIKNVSKRYGGKVVL-DDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATT---PSRELAKRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 83 AI----DHVSL-----PLLA-------KGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLM 146
Cdd:COG4604 78 AIlrqeNHINSrltvrELVAfgrfpysKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1447648657 147 LVDEPTAQLDMHTAATVSESLSRIAR--NDTIVVVsTHDPN 185
Cdd:COG4604 158 LLDEPLNNLDMKHSVQMMKLLRRLADelGKTVVIV-LHDIN 197
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
12-183 |
2.68e-23 |
|
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: 91.72 E-value: 2.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 12 YADGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQG--IDSMR-----------WIFQNPHGV 78
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGepLDYSRkgllerrqrvgLVFQDPDDQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 79 AQRTAIDH-VSLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDM 157
Cdd:TIGR01166 81 LFAADVDQdVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDP 160
|
170 180
....*....|....*....|....*.
gi 1447648657 158 HTAATVSESLSRIARNDTIVVVSTHD 183
Cdd:TIGR01166 161 AGREQMLAILRRLRAEGMTVVISTHD 186
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
21-198 |
3.64e-23 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 96.33 E-value: 3.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 21 DLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEG--QVTRQGIDSMR-------------WIFQNPHGVAQRTAID 85
Cdd:PRK10535 26 GISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGtyRVAGQDVATLDadalaqlrrehfgFIFQRYHLLSHLTAAQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 86 HVSLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVSE 165
Cdd:PRK10535 106 NVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMA 185
|
170 180 190
....*....|....*....|....*....|...
gi 1447648657 166 SLSRIARNDTIVVVSTHDPNTRDACTDIIDLKN 198
Cdd:PRK10535 186 ILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRD 218
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-183 |
6.66e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 92.77 E-value: 6.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRY--ADGPLLfHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGI---DSMRW------- 70
Cdd:PRK13635 6 IRVEHISFRYpdAATYAL-KDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMvlsEETVWdvrrqvg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 71 -IFQNP-HGVAQRTAIDHVSLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLV 148
Cdd:PRK13635 85 mVFQNPdNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIIL 164
|
170 180 190
....*....|....*....|....*....|....*.
gi 1447648657 149 DEPTAQLDMHTAATVSESLSRIARNDTIVVVS-THD 183
Cdd:PRK13635 165 DEATSMLDPRGRREVLETVRQLKEQKGITVLSiTHD 200
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-182 |
1.91e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 94.14 E-value: 1.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 5 LDHVGHRYAdGPLLFHdltasLMPGHVYALTGPSGAGKSTLLGIIAGWTtPAEGQVTRQGID-------SMR----WIFQ 73
Cdd:PRK11174 358 LSPDGKTLA-GPLNFT-----LPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIElreldpeSWRkhlsWVGQ 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 74 NPHGVAQrTAIDHVslpLLAKGlprREAEEQARTLMDRFNLTRVTDR-----------RFAELSGGEAQRLMLARAFAAQ 142
Cdd:PRK11174 431 NPQLPHG-TLRDNV---LLGNP---DASDEQLQQALENAWVSEFLPLlpqgldtpigdQAAGLSVGQAQRLALARALLQP 503
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1447648657 143 PSLMLVDEPTAQLDMHTAATVSESLSRIARNDTIVVVsTH 182
Cdd:PRK11174 504 CQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMV-TH 542
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
5-184 |
2.66e-22 |
|
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: 93.58 E-value: 2.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 5 LDHVGHRYADGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDS-----------MRWIFQ 73
Cdd:TIGR02868 337 LRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVssldqdevrrrVSVCAQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 74 NPHGVAQ------RTAIDHVSLPLLAKGLPRREAEEQARTLMDRFNlTRVTDRRfAELSGGEAQRLMLARAFAAQPSLML 147
Cdd:TIGR02868 417 DAHLFDTtvrenlRLARPDATDEELWAALERVGLADWLRALPDGLD-TVLGEGG-ARLSGGERQRLALARALLADAPILL 494
|
170 180 190
....*....|....*....|....*....|....*..
gi 1447648657 148 VDEPTAQLDMHTAATVSESLSRIARNDTIVVVsTHDP 184
Cdd:TIGR02868 495 LDEPTEHLDAETADELLEDLLAALSGRTVVLI-THHL 530
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-186 |
3.06e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 91.06 E-value: 3.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQV---------TRQGIDSMR---- 69
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIlfdgkpidySRKGLMKLResvg 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 70 WIFQNP-HGVAQRTAIDHVSLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLV 148
Cdd:PRK13636 86 MVFQDPdNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVL 165
|
170 180 190
....*....|....*....|....*....|....*....
gi 1447648657 149 DEPTAQLDMHTAATVSESLSRIARN-DTIVVVSTHDPNT 186
Cdd:PRK13636 166 DEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDI 204
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-183 |
3.10e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 90.07 E-value: 3.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 1 MRVDLDHVGHRYADGPLLFhDLTASLMPGHVYALTGPSGAGKSTLLGI-------------IAGW-------TTPAEGQV 60
Cdd:PRK11124 1 MSIQLNGINCFYGAHQALF-DITLDCPQGETLVLLGPSGAGKSSLLRVlnllemprsgtlnIAGNhfdfsktPSDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 61 TRQGIdSMrwIFQNPHGVAQRTAIDH-VSLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAF 139
Cdd:PRK11124 80 LRRNV-GM--VFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1447648657 140 AAQPSLMLVDEPTAQLDMHTAATVSESLSRIARNDTIVVVSTHD 183
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHE 200
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-182 |
3.15e-22 |
|
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: 89.73 E-value: 3.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADGPLLFH---DLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMrwifQNPHGVA 79
Cdd:cd03266 2 ITADALTKRFRDVKKTVQavdGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV----KEPAEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 80 QRTAIDHVSLPLLAK--------------GLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSL 145
Cdd:cd03266 78 RRLGFVSDSTGLYDRltarenleyfaglyGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPV 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 1447648657 146 MLVDEPTAQLDMHTAATVSESLSRIARNDTIVVVSTH 182
Cdd:cd03266 158 LLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTH 194
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
3-180 |
6.32e-22 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 89.08 E-value: 6.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRY-ADGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGID----SMRWIFQNPHG 77
Cdd:cd03252 1 ITFEHVRFRYkPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDlalaDPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 78 VAQ------RTAIDHVSLPllAKGLPRREAEEQARtLMDRFNLTR--------VTDRRFAELSGGEAQRLMLARAFAAQP 143
Cdd:cd03252 81 VLQenvlfnRSIRDNIALA--DPGMSMERVIEAAK-LAGAHDFISelpegydtIVGEQGAGLSGGQRQRIAIARALIHNP 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 1447648657 144 SLMLVDEPTAQLDMHTAATVSESLSRIARNDTIVVVS 180
Cdd:cd03252 158 RILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIA 194
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-182 |
6.77e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 91.05 E-value: 6.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 1 MRVDLDHVGHRYADGPLLfHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMRWIFQNPHGVAQ 80
Cdd:PRK13536 40 VAIDLAGVSKSYGDKAVV-NGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 81 RTAIDHVSLPLLAK----------GLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDE 150
Cdd:PRK13536 119 VPQFDNLDLEFTVRenllvfgryfGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDE 198
|
170 180 190
....*....|....*....|....*....|...
gi 1447648657 151 PTAQLDMHTAATVSESL-SRIARNDTIvVVSTH 182
Cdd:PRK13536 199 PTTGLDPHARHLIWERLrSLLARGKTI-LLTTH 230
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
22-185 |
1.08e-21 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 88.74 E-value: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 22 LTASLMPGHVYALTGPSGAGKSTLLGIIAGwTTPAEGQVTRQGIDSMRWifqNPHGVAQRTAI--DHVSLP-------LL 92
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGRPLSDW---SAAELARHRAYlsQQQSPPfampvfqYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 93 AKGLPRREAEEQARTLM----DRFNLTRVTDRRFAELSGGEAQRLMLARAFA-------AQPSLMLVDEPTAQLDMHTAA 161
Cdd:COG4138 91 ALHQPAGASSEAVEQLLaqlaEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptinPEGQLLLLDEPMNSLDVAQQA 170
|
170 180
....*....|....*....|....
gi 1447648657 162 TVSESLSRIARNDTIVVVSTHDPN 185
Cdd:COG4138 171 ALDRLLRELCQQGITVVMSSHDLN 194
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-183 |
1.33e-21 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 88.53 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 1 MRVDLDHVGHRYADGPLLFhDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVT--------RQGIDSMR--- 69
Cdd:COG4161 1 MSIQLKNINCFYGSHQALF-DINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNiaghqfdfSQKPSEKAirl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 70 ------WIFQNPHGVAQRTAIDH-VSLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQ 142
Cdd:COG4161 80 lrqkvgMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1447648657 143 PSLMLVDEPTAQLDMHTAATVSESLSRIARNDTIVVVSTHD 183
Cdd:COG4161 160 PQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHE 200
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
25-190 |
1.47e-21 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 87.98 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 25 SLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQV------TRQGIDSMRWIFQNpHGVAQRTAID--HVSLPLLAKGL 96
Cdd:TIGR03771 2 SADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVkvagasPGKGWRHIGYVPQR-HEFAWDFPISvaHTVMSGRTGHI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 97 -----PRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVSESLSRIA 171
Cdd:TIGR03771 81 gwlrrPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFIELA 160
|
170 180
....*....|....*....|
gi 1447648657 172 RNDTIVVVSTHD-PNTRDAC 190
Cdd:TIGR03771 161 GAGTAILMTTHDlAQAMATC 180
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
3-156 |
1.47e-21 |
|
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: 87.55 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADGPLLFhDLTASlmPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGID-----------SMrwI 71
Cdd:cd03298 1 VRLDKIRFSYGEQPMHF-DLTFA--QGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDvtaappadrpvSM--L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 72 FQNPHGVAQRTAIDHVSLPlLAKGLPRREAEEQA-RTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDE 150
Cdd:cd03298 76 FQENNLFAHLTVEQNVGLG-LSPGLKLTAEDRQAiEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDE 154
|
....*.
gi 1447648657 151 PTAQLD 156
Cdd:cd03298 155 PFAALD 160
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
6-183 |
1.91e-21 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 88.59 E-value: 1.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 6 DHVGHRYADGPLL--------FHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGID----------- 66
Cdd:PRK10419 7 SGLSHHYAHGGLSgkhqhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPlaklnraqrka 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 67 ---SMRWIFQNPHGV--AQRTAIDHVSLPLL-AKGLPRREAEEQARTLMDRFNLT-RVTDRRFAELSGGEAQRLMLARAF 139
Cdd:PRK10419 87 frrDIQMVFQDSISAvnPRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1447648657 140 AAQPSLMLVDEPTAQLDMHTAATVSESLSRI-ARNDTIVVVSTHD 183
Cdd:PRK10419 167 AVEPKLLILDEAVSNLDLVLQAGVIRLLKKLqQQFGTACLFITHD 211
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-184 |
2.04e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 88.05 E-value: 2.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 22 LTASLMPGHVYALTGPSGAGKSTLLGI----IAGWTTP-AEGQVTRQGID-----------SMRWIFQNPHGVAQRTAID 85
Cdd:PRK14247 22 VNLEIPDNTITALMGPSGSGKSTLLRVfnrlIELYPEArVSGEVYLDGQDifkmdvielrrRVQMVFQIPNPIPNLSIFE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 86 HVSLPL----LAKGlpRREAEEQARTLMDRFNL-TRVTDRRFA---ELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDM 157
Cdd:PRK14247 102 NVALGLklnrLVKS--KKELQERVRWALEKAQLwDEVKDRLDApagKLSGGQQQRLCIARALAFQPEVLLADEPTANLDP 179
|
170 180
....*....|....*....|....*..
gi 1447648657 158 HTAATVSESLSRIARNDTIVVVsTHDP 184
Cdd:PRK14247 180 ENTAKIESLFLELKKDMTIVLV-THFP 205
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-197 |
2.13e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 91.02 E-value: 2.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 2 RVDLDHVGHRYADGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAG-WTtPAEGQVTRQGIDSMRWIFQNPHgVAQ 80
Cdd:COG4178 362 ALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGlWP-YGSGRIARPAGARVLFLPQRPY-LPL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 81 RTAIDHVSLPllakGLPRREAEEQARTLMDRFNLTRVTDRRFAE------LSGGEAQRLMLARAFAAQPSLMLVDEPTAQ 154
Cdd:COG4178 440 GTLREALLYP----ATAEAFSDAELREALEAVGLGHLAERLDEEadwdqvLSLGEQQRLAFARLLLHKPDWLFLDEATSA 515
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1447648657 155 LDMHTAATVSESLSRIARNDTIVVVStHDPNTRDACTDIIDLK 197
Cdd:COG4178 516 LDEENEAALYQLLREELPGTTVISVG-HRSTLAAFHDRVLELT 557
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-184 |
3.00e-21 |
|
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: 89.39 E-value: 3.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 1 MRVDLDhVGHRYADGPLlfhDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQG---IDSMRWIFQNPHg 77
Cdd:COG4148 1 MMLEVD-FRLRRGGFTL---DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSARGIFLPPH- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 78 vaQRtAIDHV----SL-PLL---------AKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQP 143
Cdd:COG4148 76 --RR-RIGYVfqeaRLfPHLsvrgnllygRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1447648657 144 SLMLVDEPTAQLDMHTAATVSESLSRIARNDTI-VVVSTHDP 184
Cdd:COG4148 153 RLLLMDEPLAALDLARKAEILPYLERLRDELDIpILYVSHSL 194
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
3-179 |
3.86e-21 |
|
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: 87.21 E-value: 3.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADGP--LLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDsMRwiFQNPHGVaq 80
Cdd:cd03249 1 IEFKNVSFRYPSRPdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVD-IR--DLNLRWL-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 81 RTAIDHVSL-PLL---------AKGLPRREAEEQAR------------TLMDRFNlTRVTDRRFaELSGGEAQRLMLARA 138
Cdd:cd03249 76 RSQIGLVSQePVLfdgtiaeniRYGKPDATDEEVEEaakkanihdfimSLPDGYD-TLVGERGS-QLSGGQKQRIAIARA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1447648657 139 FAAQPSLMLVDEPTAQLDMHTAATVSESLSRIARNDTIVVV 179
Cdd:cd03249 154 LLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVI 194
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
25-183 |
4.70e-21 |
|
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: 88.19 E-value: 4.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 25 SLMPGHVYALTGPSGAGKSTL----LGIIAGwTTPAEGQVTRQGID----------SMRW-----IFQNPHG----VaqR 81
Cdd:COG0444 27 DVRRGETLGLVGESGSGKSTLaraiLGLLPP-PGITSGEILFDGEDllklsekelrKIRGreiqmIFQDPMTslnpV--M 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 82 TAIDHVSLPLLA-KGLPRREAEEQARTLMDRFNLTRVTDR--RFA-ELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDM 157
Cdd:COG0444 104 TVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDPERRldRYPhELSGGMRQRVMIARALALEPKLLIADEPTTALDV 183
|
170 180
....*....|....*....|....*...
gi 1447648657 158 HTAATVSESLSRIAR--NDTIVVVsTHD 183
Cdd:COG0444 184 TIQAQILNLLKDLQRelGLAILFI-THD 210
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
14-183 |
7.07e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 88.74 E-value: 7.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 14 DGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGID---------SMRWIFQN----PHgvaq 80
Cdd:PRK11607 30 DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDlshvppyqrPINMMFQSyalfPH---- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 81 RTAIDHVSLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTA 160
Cdd:PRK11607 106 MTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLR 185
|
170 180
....*....|....*....|....
gi 1447648657 161 ATVS-ESLSRIARNDTIVVVSTHD 183
Cdd:PRK11607 186 DRMQlEVVDILERVGVTCVMVTHD 209
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-194 |
9.99e-21 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 85.72 E-value: 9.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 2 RVDLDHVGHRYADGPLL-FHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMRWifqnpHGVAQ 80
Cdd:cd03245 2 RIEFRNVSFSYPNQEIPaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQL-----DPADL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 81 RTAIDHVSL-PLLAKG-------LPRREAEEQArtLMDRFNLTRVT----------DRRFAE----LSGGEAQRLMLARA 138
Cdd:cd03245 77 RRNIGYVPQdVTLFYGtlrdnitLGAPLADDER--ILRAAELAGVTdfvnkhpnglDLQIGErgrgLSGGQRQAVALARA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1447648657 139 FAAQPSLMLVDEPTAQLDMHTAATVSESLSRIARNDTIVVVsTHDPNTRDACTDII 194
Cdd:cd03245 155 LLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIII-THRPSLLDLVDRII 209
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
10-179 |
1.01e-20 |
|
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: 87.86 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 10 HRYADgpllfHDLTASL-MPGH-VYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGI---DSMRWIFQNPHGVA----- 79
Cdd:TIGR02142 7 KRLGD-----FSLDADFtLPGQgVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfDSRKGIFLPPEKRRigyvf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 80 -QRTAIDHVSLPL-LAKGLPR-REAEEQAR--TLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQ 154
Cdd:TIGR02142 82 qEARLFPHLSVRGnLRYGMKRaRPSERRISfeRVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1447648657 155 LDMHTAAT------------------VSESLSRIAR-NDTIVVV 179
Cdd:TIGR02142 162 LDDPRKYEilpylerlhaefgipilyVSHSLQEVLRlADRVVVL 205
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-194 |
1.04e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 86.64 E-value: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 12 YADGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGI------IAGWTTPAEGQVTRQGIDSMR-----------WIFQN 74
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVlnrlieIYDSKIKVDGKVLYFGKDIFQidaiklrkevgMVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 75 PHGVAQRTAIDHVSLPLLAKGLP-RREAEEQARTLMDRFNLTRVTDRRF----AELSGGEAQRLMLARAFAAQPSLMLVD 149
Cdd:PRK14246 99 PNPFPHLSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLWKEVYDRLnspaSQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1447648657 150 EPTAQLDMHTAATVSESLSRIARNDTIVVVStHDPNTRDACTDII 194
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNEIAIVIVS-HNPQQVARVADYV 222
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
3-198 |
1.34e-20 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 85.74 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDsMRWIFQNphgvAQRT 82
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQD-IREVTLD----SLRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 83 AIDHV--SLPL--------LAKGLPR------REAEEQAR------TLMDRFNlTRVTDRRFaELSGGEAQRLMLARAFA 140
Cdd:cd03253 76 AIGVVpqDTVLfndtigynIRYGRPDatdeevIEAAKAAQihdkimRFPDGYD-TIVGERGL-KLSGGEKQRVAIARAIL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1447648657 141 AQPSLMLVDEPTAQLDMHTAATVSESLSRIARNDTIVVVsTHDPNTRDACTDIIDLKN 198
Cdd:cd03253 154 KNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVI-AHRLSTIVNADKIIVLKD 210
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
11-183 |
1.96e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 85.94 E-value: 1.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 11 RYADGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGID----SMRWI-------FQNPHG-V 78
Cdd:PRK13647 13 RYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREvnaeNEKWVrskvglvFQDPDDqV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 79 AQRTAIDHVSLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMH 158
Cdd:PRK13647 93 FSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPR 172
|
170 180
....*....|....*....|....*
gi 1447648657 159 TAATVSESLSRIARNDTIVVVSTHD 183
Cdd:PRK13647 173 GQETLMEILDRLHNQGKTVIVATHD 197
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-156 |
2.48e-20 |
|
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: 84.90 E-value: 2.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 5 LDHVGHRYADGPLLfHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMRWifqNPHGVAQR--- 81
Cdd:cd03218 3 AENLSKRYGKRKVV-NGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKL---PMHKRARLgig 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 82 ------------TAIDHVSLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVD 149
Cdd:cd03218 79 ylpqeasifrklTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLD 158
|
....*..
gi 1447648657 150 EPTAQLD 156
Cdd:cd03218 159 EPFAGVD 165
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
15-199 |
2.73e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 84.16 E-value: 2.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 15 GPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSmrwifQNPHGVAQRTAIDHVSL--PLL 92
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI-----DDPDVAEACHYLGHRNAmkPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 93 A-----------KGLPRREAEEQArtlmDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAA 161
Cdd:PRK13539 89 TvaenlefwaafLGGEELDIAAAL----EAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVA 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 1447648657 162 TVSESLSRIARNDTIVVVSTHDPNTRDACTdIIDLKNY 199
Cdd:PRK13539 165 LFAELIRAHLAQGGIVIAATHIPLGLPGAR-ELDLGPF 201
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
14-184 |
3.81e-20 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 83.70 E-value: 3.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 14 DGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVtrqgidsmRWifqNPHGVAQRTAIDHVSLPLLA 93
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRV--------LL---NGGPLDFQRDSIARGLLYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 94 -----KG-LPRRE---------AEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMH 158
Cdd:cd03231 80 hapgiKTtLSVLEnlrfwhadhSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
170 180
....*....|....*....|....*.
gi 1447648657 159 TAATVSESLSRIARNDTIVVVSTHDP 184
Cdd:cd03231 160 GVARFAEAMAGHCARGGMVVLTTHQD 185
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-194 |
3.82e-20 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 84.20 E-value: 3.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 2 RVDLDHVGHRYADGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGID-------SMR----W 70
Cdd:cd03254 2 EIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDirdisrkSLRsmigV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 71 IFQNPHgVAQRTAIDHVslpLLAKGLPRREAEEQARTL--MDRF--NLTRVTDRRFAE----LSGGEAQRLMLARAFAAQ 142
Cdd:cd03254 82 VLQDTF-LFSGTIMENI---RLGRPNATDEEVIEAAKEagAHDFimKLPNGYDTVLGEnggnLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1447648657 143 PSLMLVDEPTAQLDMHTAATVSESLSRIARNDTIVVVStHDPNT-RDActDII 194
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIA-HRLSTiKNA--DKI 207
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
3-179 |
5.14e-20 |
|
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: 84.20 E-value: 5.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRY-ADGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGID-------SMRWIFQN 74
Cdd:cd03251 1 VEFKNVTFRYpGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDvrdytlaSLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 75 phgVAQRTAIDHVSLPL-LAKGLP---RREAEEQART-----LMDRFNL---TRVTDRRfAELSGGEAQRLMLARAFAAQ 142
Cdd:cd03251 81 ---VSQDVFLFNDTVAEnIAYGRPgatREEVEEAARAanaheFIMELPEgydTVIGERG-VKLSGGQRQRIAIARALLKD 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 1447648657 143 PSLMLVDEPTAQLDMHTAATVSESLSRIARNDTIVVV 179
Cdd:cd03251 157 PPILILDEATSALDTESERLVQAALERLMKNRTTFVI 193
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
25-156 |
1.12e-19 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 84.78 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 25 SLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGID-------SMRW-------IFQNPHGV--AQRTAIDHVS 88
Cdd:COG4608 40 DIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDitglsgrELRPlrrrmqmVFQDPYASlnPRMTVGDIIA 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 89 LPLLAKGL-PRREAEEQARTLMDRFNLTRVTDRRFA-ELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLD 156
Cdd:COG4608 120 EPLRIHGLaSKAERRERVAELLELVGLRPEHADRYPhEFSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
31-184 |
1.57e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 83.35 E-value: 1.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 31 VYALTGPSGAGKSTLLG-----IIAGWTTPAEGQVTRQG-------IDSMR------WIFQNPHGVAQRTAIDHVSLPLL 92
Cdd:PRK14267 32 VFALMGPSGCGKSTLLRtfnrlLELNEEARVEGEVRLFGrniyspdVDPIEvrrevgMVFQYPNPFPHLTIYDNVAIGVK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 93 AKGL--PRREAEEQARTLMDRFNL-TRVTDR---RFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVSES 166
Cdd:PRK14267 112 LNGLvkSKKELDERVEWALKKAALwDEVKDRlndYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEEL 191
|
170
....*....|....*...
gi 1447648657 167 LSRIARNDTIVVVsTHDP 184
Cdd:PRK14267 192 LFELKKEYTIVLV-THSP 208
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
20-179 |
2.12e-19 |
|
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: 82.10 E-value: 2.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 20 HDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQG--IDSMRwifqnPHGVAQRtAIDHV---------- 87
Cdd:cd03224 17 FGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGrdITGLP-----PHERARA-GIGYVpegrrifpel 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 88 ----SLPLLAKGLPRREAEEQARTLMDRF-NLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAAT 162
Cdd:cd03224 91 tveeNLLLGAYARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEE 170
|
170
....*....|....*...
gi 1447648657 163 VSESLSRIARND-TIVVV 179
Cdd:cd03224 171 IFEAIRELRDEGvTILLV 188
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
5-156 |
3.83e-19 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 81.55 E-value: 3.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 5 LDHVGHRYADGPLLFhDLTASlmPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGID-----------SMrwIFQ 73
Cdd:PRK10771 4 LTDITWLYHHLPMRF-DLTVE--RGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDhtttppsrrpvSM--LFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 74 N----PH-GVAQRTAIDhvslplLAKGLprREAEEQARTLMD---RFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSL 145
Cdd:PRK10771 79 EnnlfSHlTVAQNIGLG------LNPGL--KLNAAQREKLHAiarQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPI 150
|
170
....*....|.
gi 1447648657 146 MLVDEPTAQLD 156
Cdd:PRK10771 151 LLLDEPFSALD 161
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
19-181 |
4.94e-19 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 81.98 E-value: 4.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 19 FHDLTASLMPGHVYALTGPSGAGKSTLL----GIIAGWTTPA------------EGQVTRQgIDSMR----WIFQNPHGV 78
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsGLITGDKSAGshiellgrtvqrEGRLARD-IRKSRantgYIFQQFNLV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 79 AQRTAIDHV------SLPLLAKGLP--RREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDE 150
Cdd:PRK09984 99 NRLSVLENVligalgSTPFWRTCFSwfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADE 178
|
170 180 190
....*....|....*....|....*....|.
gi 1447648657 151 PTAQLDMHTAATVSESLSRIARNDTIVVVST 181
Cdd:PRK09984 179 PIASLDPESARIVMDTLRDINQNDGITVVVT 209
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
28-156 |
5.28e-19 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 81.61 E-value: 5.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 28 PGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMRWifqnP-HGVAQR---------------TAIDHVSLPL 91
Cdd:COG1137 28 QGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHL----PmHKRARLgigylpqeasifrklTVEDNILAVL 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1447648657 92 LAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLD 156
Cdd:COG1137 104 ELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVD 168
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
18-189 |
5.30e-19 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 81.16 E-value: 5.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 18 LFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAG--WTTPAEGQVTrqgidsmrwIFQNPHGVaQRTAIDHVSL---PLL 92
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVD---------VPDNQFGR-EASLIDAIGRkgdFKD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 93 AKGLprreaeeqartlmdrfnLTRV--TD-----RRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVSE 165
Cdd:COG2401 115 AVEL-----------------LNAVglSDavlwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVAR 177
|
170 180
....*....|....*....|....*
gi 1447648657 166 SLSRIARNDTI-VVVSTHDPNTRDA 189
Cdd:COG2401 178 NLQKLARRAGItLVVATHHYDVIDD 202
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
12-185 |
1.45e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 80.83 E-value: 1.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 12 YADGPLLfHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGID----SMRWIFQN----------PHG 77
Cdd:PRK11231 12 YGTKRIL-NDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPismlSSRQLARRlallpqhhltPEG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 78 VAQRTAIDHVSLPLLAK-GLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLD 156
Cdd:PRK11231 91 ITVRELVAYGRSPWLSLwGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD 170
|
170 180
....*....|....*....|....*....
gi 1447648657 157 MHTAATVSESLSRIARNDTIVVVSTHDPN 185
Cdd:PRK11231 171 INHQVELMRLMRELNTQGKTVVTVLHDLN 199
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
21-195 |
1.95e-18 |
|
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: 80.01 E-value: 1.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 21 DLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMRWifqNPHGVAQR---------------TAID 85
Cdd:TIGR04406 19 DVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHL---PMHERARLgigylpqeasifrklTVEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 86 HVSLPL-LAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDmhtAATVS 164
Cdd:TIGR04406 96 NIMAVLeIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAGVD---PIAVG 172
|
170 180 190
....*....|....*....|....*....|...
gi 1447648657 165 E--SLSRIARNDTIVVVSThDPNTRDAcTDIID 195
Cdd:TIGR04406 173 DikKIIKHLKERGIGVLIT-DHNVRET-LDICD 203
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
10-183 |
3.50e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 80.12 E-value: 3.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 10 HRYADGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQV----------------TRQ--GIdsmrwI 71
Cdd:PRK13639 9 YSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVlikgepikydkkslleVRKtvGI-----V 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 72 FQNPHG-VAQRTAIDHVSLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDE 150
Cdd:PRK13639 84 FQNPDDqLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDE 163
|
170 180 190
....*....|....*....|....*....|...
gi 1447648657 151 PTAQLDMHTAATVSESLSRIARNDTIVVVSTHD 183
Cdd:PRK13639 164 PTSGLDPMGASQIMKLLYDLNKEGITIIISTHD 196
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
29-183 |
3.86e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 79.63 E-value: 3.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 29 GHVYALTGPSGAGKSTLLGIIAGWTTPAEGQ--VTRQGIDSMR----------------------WIFQNPHGVAQRTAI 84
Cdd:PRK10619 31 GDVISIIGSSGSGKSTFLRCINFLEKPSEGSivVNGQTINLVRdkdgqlkvadknqlrllrtrltMVFQHFNLWSHMTVL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 85 DHV-SLPLLAKGLPRREAEEQARTLMDRFNLT-RVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAAT 162
Cdd:PRK10619 111 ENVmEAPIQVLGLSKQEARERAVKYLAKVGIDeRAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGE 190
|
170 180
....*....|....*....|.
gi 1447648657 163 VSESLSRIARNDTIVVVSTHD 183
Cdd:PRK10619 191 VLRIMQQLAEEGKTMVVVTHE 211
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
29-190 |
5.89e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 81.00 E-value: 5.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 29 GHVYALTGPSGAGKSTLLGIIAGWTTPAEGQV-----------TRQGIDS-------MRWIFQN----PHgvaqRTAIDH 86
Cdd:TIGR03269 310 GEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdewvdmTKPGPDGrgrakryIGILHQEydlyPH----RTVLDN 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 87 VSLPL---LAKGLPRREA----------EEQARTLMDRFnltrvTDrrfaELSGGEAQRLMLARAFAAQPSLMLVDEPTA 153
Cdd:TIGR03269 386 LTEAIgleLPDELARMKAvitlkmvgfdEEKAEEILDKY-----PD----ELSEGERHRVALAQVLIKEPRIVILDEPTG 456
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1447648657 154 QLDMHTAATVSESL--SRIARNDTIVVVStHDPN-TRDAC 190
Cdd:TIGR03269 457 TMDPITKVDVTHSIlkAREEMEQTFIIVS-HDMDfVLDVC 495
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
3-156 |
9.85e-18 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 79.76 E-value: 9.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADGPLLfHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQ-------VTRQGIDSmRWI---F 72
Cdd:PRK11432 7 VVLKNITKRFGSNTVI-DNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQifidgedVTHRSIQQ-RDIcmvF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 73 QN----PHgvaqRTAIDHVSLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLV 148
Cdd:PRK11432 85 QSyalfPH----MSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLF 160
|
....*...
gi 1447648657 149 DEPTAQLD 156
Cdd:PRK11432 161 DEPLSNLD 168
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
3-157 |
1.10e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 78.23 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADGPLLfHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQgiDSMRWIFqnphgVAQRT 82
Cdd:PRK09544 5 VSLENVSVSFGQRRVL-SDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRN--GKLRIGY-----VPQKL 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1447648657 83 AIDhVSLPLLAKGLPR-REAEEQARTL--MDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDM 157
Cdd:PRK09544 77 YLD-TTLPLTVNRFLRlRPGTKKEDILpaLKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDV 153
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
6-194 |
1.10e-17 |
|
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: 78.18 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 6 DHVGHRYADGPLLFHDLtASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQvtRQGIDSMRWIFQNPHGVA-----Q 80
Cdd:cd03236 4 DEPVHRYGPNSFKLHRL-PVPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGK--FDDPPDWDEILDEFRGSElqnyfT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 81 RTAIDHVS----------LPLLAKG-----LPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSL 145
Cdd:cd03236 81 KLLEGDVKvivkpqyvdlIPKAVKGkvgelLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1447648657 146 MLVDEPTAQLDMHTAATVSESLSRIARNDTIVVVSTHDPNTRDACTDII 194
Cdd:cd03236 161 YFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYI 209
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1-182 |
1.24e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 78.52 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 1 MRVDLDHVGHRY-ADGP---LLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVT--------------- 61
Cdd:PRK13634 1 MDITFQKVEHRYqYKTPferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTigervitagkknkkl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 62 ---RQ--GIdsmrwIFQNP-HGVAQRTAIDHVSLPLLAKGLPRREAEEQARTLMDRFNLTR-VTDRRFAELSGGEAQRLM 134
Cdd:PRK13634 81 kplRKkvGI-----VFQFPeHQLFEETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1447648657 135 LARAFAAQPSLMLVDEPTAQLDMHTAATVSESLSRIAR--NDTIVVVsTH 182
Cdd:PRK13634 156 IAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKekGLTTVLV-TH 204
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
22-187 |
2.12e-17 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 79.54 E-value: 2.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 22 LTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPA---------EGQVTRQGIDSMRWIFQN----PHGVAQRTAIdHVS 88
Cdd:PLN03211 87 VTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnftgtilanNRKPTKQILKRTGFVTQDdilyPHLTVRETLV-FCS 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 89 LPLLAKGLPRREAEEQARTLMDRFNLTR-----VTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATV 163
Cdd:PLN03211 166 LLRLPKSLTKQEKILVAESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRL 245
|
170 180
....*....|....*....|....
gi 1447648657 164 SESLSRIARNDTIVVVSTHDPNTR 187
Cdd:PLN03211 246 VLTLGSLAQKGKTIVTSMHQPSSR 269
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-183 |
2.14e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 77.41 E-value: 2.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 5 LDHVGHRYADGPLLfHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVT------RQGIDSMRWIFQNPHGV 78
Cdd:PRK11247 15 LNAVSKRYGERTVL-NQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLagtaplAEAREDTRLMFQDARLL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 79 AQRTAIDHVSLPLlaKGLPRREAEE--QARTLMDRFNltrvtdRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLD 156
Cdd:PRK11247 94 PWKKVIDNVGLGL--KGQWRDAALQalAAVGLADRAN------EWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 1447648657 157 mhtaatvseSLSRIARNDTI----------VVVSTHD 183
Cdd:PRK11247 166 ---------ALTRIEMQDLIeslwqqhgftVLLVTHD 193
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-187 |
2.57e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 79.32 E-value: 2.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 18 LFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPA---EGQVTRQGIDSMRWIFQNPHGVAQR--------TAIDH 86
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRAISAYVQQddlfiptlTVREH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 87 VSLPLLAKgLPRREAEEQAR----TLMDRFNL-----TRV-TDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLD 156
Cdd:TIGR00955 120 LMFQAHLR-MPRRVTKKEKRervdEVLQALGLrkcanTRIgVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
170 180 190
....*....|....*....|....*....|.
gi 1447648657 157 MHTAATVSESLSRIARNDTIVVVSTHDPNTR 187
Cdd:TIGR00955 199 SFMAYSVVQVLKGLAQKGKTIICTIHQPSSE 229
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-189 |
2.88e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 79.23 E-value: 2.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 2 RVDLDHVGHRYADGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGID-------SMRW---- 70
Cdd:PRK13657 334 AVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDirtvtraSLRRniav 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 71 IFQNPhGVAQRTAIDHVSLpllakGLPR------REAEEQARTL------MDRFNlTRVTDRRfAELSGGEAQRLMLARA 138
Cdd:PRK13657 414 VFQDA-GLFNRSIEDNIRV-----GRPDatdeemRAAAERAQAHdfierkPDGYD-TVVGERG-RQLSGGERQRLAIARA 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1447648657 139 FAAQPSLMLVDEPTAQLDMHTAATVSESLSRIARNDTIVVVSTHDPNTRDA 189
Cdd:PRK13657 486 LLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNA 536
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
8-183 |
3.33e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 77.35 E-value: 3.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 8 VGHRYADGPLLfHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQV---------TRQGIDSMRW----IFQN 74
Cdd:PRK13638 7 LWFRYQDEPVL-KGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVlwqgkpldySKRGLLALRQqvatVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 75 PHGVAQRTAIDH-VSLPLLAKGLPRreaEEQARTLMDRfnLTRVTDRRFAE-----LSGGEAQRLMLARAFAAQPSLMLV 148
Cdd:PRK13638 86 PEQQIFYTDIDSdIAFSLRNLGVPE---AEITRRVDEA--LTLVDAQHFRHqpiqcLSHGQKKRVAIAGALVLQARYLLL 160
|
170 180 190
....*....|....*....|....*....|....*
gi 1447648657 149 DEPTAQLDMHTAATVSESLSRIARNDTIVVVSTHD 183
Cdd:PRK13638 161 DEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHD 195
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
20-198 |
3.67e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 76.95 E-value: 3.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 20 HDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMRWIFQNphgVAQRTAI---------DHVSLP 90
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKE---VARRIGLlaqnattpgDITVQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 91 LLAKG-LP--------RREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAA 161
Cdd:PRK10253 101 LVARGrYPhqplftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1447648657 162 TVSESLSRIARNDTIVVVST-HDPNtrDAC---TDIIDLKN 198
Cdd:PRK10253 181 DLLELLSELNREKGYTLAAVlHDLN--QACryaSHLIALRE 219
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
20-179 |
4.24e-17 |
|
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: 76.17 E-value: 4.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 20 HDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQG--IDSMRwifqnPHGVAQRtAIDHVslP------- 90
Cdd:COG0410 20 HGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGedITGLP-----PHRIARL-GIGYV--Pegrrifp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 91 -------LLAKGLPRREAEEQARTL---MDRF-NLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHT 159
Cdd:COG0410 92 sltveenLLLGAYARRDRAEVRADLervYELFpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLI 171
|
170 180
....*....|....*....|.
gi 1447648657 160 AATVSESLSRIARND-TIVVV 179
Cdd:COG0410 172 VEEIFEIIRRLNREGvTILLV 192
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
22-185 |
5.01e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 76.51 E-value: 5.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 22 LTASLMPGHVYALTGPSGAGKSTLLGIIAGwTTPAEGQVTRQGIDSMRWifqNPHGVAQRTA--IDHVSLPL-------L 92
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQPLEAW---SAAELARHRAylSQQQTPPFampvfqyL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 93 AKGLPRREAEEQARTLMD----RFNLTRVTDRRFAELSGGEAQRLMLARAF-----AAQPS--LMLVDEPTAQLDMHTAA 161
Cdd:PRK03695 91 TLHQPDKTRTEAVASALNevaeALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPAgqLLLLDEPMNSLDVAQQA 170
|
170 180
....*....|....*....|....
gi 1447648657 162 TVSESLSRIARNDTIVVVSTHDPN 185
Cdd:PRK03695 171 ALDRLLSELCQQGIAVVMSSHDLN 194
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
21-183 |
7.04e-17 |
|
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: 75.83 E-value: 7.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 21 DLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSmrWIFQNPH----GV--AQRT-------AIDhv 87
Cdd:cd03267 39 GISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVP--WKRRKKFlrriGVvfGQKTqlwwdlpVID-- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 88 SLPLLAK--GLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVSE 165
Cdd:cd03267 115 SFYLLAAiyDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRN 194
|
170
....*....|....*....
gi 1447648657 166 SLSRIARN-DTIVVVSTHD 183
Cdd:cd03267 195 FLKEYNRErGTTVLLTSHY 213
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-183 |
1.25e-16 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 77.28 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADgPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVT-------------RQGIDSMR 69
Cdd:TIGR03719 323 IEAENLTKAFGD-KLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEigetvklayvdqsRDALDPNK 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 70 WIFQNPHGvaqrtAIDHVSLpllakglprREAEEQARTLMDRFNLtRVTD--RRFAELSGGEAQRLMLARAFAAQPSLML 147
Cdd:TIGR03719 402 TVWEEISG-----GLDIIKL---------GKREIPSRAYVGRFNF-KGSDqqKKVGQLSGGERNRVHLAKTLKSGGNVLL 466
|
170 180 190
....*....|....*....|....*....|....*.
gi 1447648657 148 VDEPTAQLDMHTAATVSESLSRIARNdtiVVVSTHD 183
Cdd:TIGR03719 467 LDEPTNDLDVETLRALEEALLNFAGC---AVVISHD 499
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-198 |
1.84e-16 |
|
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: 76.71 E-value: 1.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 2 RVDLDHVGHRY--ADGPLLfHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDsmrwIFQNPHGVA 79
Cdd:COG4618 330 RLSVENLTVVPpgSKRPIL-RGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGAD----LSQWDREEL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 80 QRtaidHVS-LP----LLA----------KGLPRREAEEQART-----LMDRFNL---TRVTDRRFAeLSGGEAQRLMLA 136
Cdd:COG4618 405 GR----HIGyLPqdveLFDgtiaeniarfGDADPEKVVAAAKLagvheMILRLPDgydTRIGEGGAR-LSGGQRQRIGLA 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1447648657 137 RAFAAQPSLMLVDEPTAQLDMHTAATVSESLSRIARNDTIVVVSTHDPNTRDACTDIIDLKN 198
Cdd:COG4618 480 RALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAAVDKLLVLRD 541
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
25-156 |
2.12e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 76.60 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 25 SLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVT---------------RQGIdSMrwIFQNPHGVAQRTAIDHVSL 89
Cdd:COG1129 26 ELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILldgepvrfrsprdaqAAGI-AI--IHQELNLVPNLSVAENIFL 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 90 ---PLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLD 156
Cdd:COG1129 103 grePRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLT 172
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-197 |
2.65e-16 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 76.30 E-value: 2.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 2 RVDLDHVGHRYADGP--LLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDsmrwIFQNPHGVA 79
Cdd:TIGR00958 478 LIEFQDVSFSYPNRPdvPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVP----LVQYDHHYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 80 QRtaidHVSL----PLL---------AKGLPRREAEE-QARTLM---DRF--NLTRVTDRRFAE----LSGGEAQRLMLA 136
Cdd:TIGR00958 554 HR----QVALvgqePVLfsgsvreniAYGLTDTPDEEiMAAAKAanaHDFimEFPNGYDTEVGEkgsqLSGGQKQRIAIA 629
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1447648657 137 RAFAAQPSLMLVDEPTAQLDMHTAATVSESLSRIARndTIVVVsTHDPNTRDACTDIIDLK 197
Cdd:TIGR00958 630 RALVRKPRVLILDEATSALDAECEQLLQESRSRASR--TVLLI-AHRLSTVERADQILVLK 687
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-182 |
3.27e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 74.84 E-value: 3.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADgPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGidsmRWIFQNPHGVAQRT 82
Cdd:PRK13537 8 IDFRNVEKRYGD-KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG----EPVPSRARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 83 AI----DHV--------SLPLLAK--GLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLV 148
Cdd:PRK13537 83 GVvpqfDNLdpdftvreNLLVFGRyfGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190
....*....|....*....|....*....|....*
gi 1447648657 149 DEPTAQLDMHTAATVSESL-SRIARNDTIvVVSTH 182
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLrSLLARGKTI-LLTTH 196
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
19-182 |
3.71e-16 |
|
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: 72.73 E-value: 3.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 19 FHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGI------DSMRWIF----QNPHgvaqrtaidhvs 88
Cdd:cd03247 18 LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVpvsdleKALSSLIsvlnQRPY------------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 89 lpLLAKglprreaeeqarTLMDrfNLtrvtDRRFaelSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVSESLS 168
Cdd:cd03247 86 --LFDT------------TLRN--NL----GRRF---SGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIF 142
|
170
....*....|....
gi 1447648657 169 RIARNDTIVVVSTH 182
Cdd:cd03247 143 EVLKDKTLIWITHH 156
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-182 |
4.03e-16 |
|
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: 72.08 E-value: 4.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADGPLLfHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTrqgIDSMRWIFQNPHGvAQRT 82
Cdd:cd03216 1 LELRGITKRFGGVKAL-DGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEIL---VDGKEVSFASPRD-ARRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 83 AIDHVSlpllakglprreaeeqartlmdrfnltrvtdrrfaELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAAT 162
Cdd:cd03216 76 GIAMVY-----------------------------------QLSVGERQMVEIARALARNARLLILDEPTAALTPAEVER 120
|
170 180
....*....|....*....|
gi 1447648657 163 VSESLSRIARNDTIVVVSTH 182
Cdd:cd03216 121 LFKVIRRLRAQGVAVIFISH 140
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
5-183 |
5.26e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 74.15 E-value: 5.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 5 LDHVGHRYADGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMRWIFQNPHG-VAQRTA 83
Cdd:PRK15056 9 VNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAyVPQSEE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 84 IDHvSLPLLAK-----------GLPRReAEEQARTLMD----RFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLV 148
Cdd:PRK15056 89 VDW-SFPVLVEdvvmmgryghmGWLRR-AKKRDRQIVTaalaRVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILL 166
|
170 180 190
....*....|....*....|....*....|....*
gi 1447648657 149 DEPTAQLDMHTAATVSESLSRIARNDTIVVVSTHD 183
Cdd:PRK15056 167 DEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHN 201
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-196 |
1.11e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 73.30 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADGPL-LFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMR------W----- 70
Cdd:PRK13640 6 VEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITltaktvWdirek 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 71 ---IFQNP-HGVAQRTAIDHVSLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLM 146
Cdd:PRK13640 86 vgiVFQNPdNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKII 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1447648657 147 LVDEPTAQLDMHTAATVSESLSRIARNDTIVVVS-THDPNTRDACTDIIDL 196
Cdd:PRK13640 166 ILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISiTHDIDEANMADQVLVL 216
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
34-183 |
1.13e-15 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 73.83 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 34 LTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGID---------SMRWIFQN----PHgvaqRTAIDHVSLPLLAKGLPRRE 100
Cdd:PRK09452 45 LLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDithvpaenrHVNTVFQSyalfPH----MTVFENVAFGLRMQKTPAAE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 101 AEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVSESLSRIAR--NDTIVV 178
Cdd:PRK09452 121 ITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRklGITFVF 200
|
....*
gi 1447648657 179 VsTHD 183
Cdd:PRK09452 201 V-THD 204
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
22-191 |
1.15e-15 |
|
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: 74.66 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 22 LTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQG---IDSMRWIFQNPHGVAQRTAID-------HVSLPL 91
Cdd:TIGR01257 1958 LCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGksiLTNISDVHQNMGYCPQFDAIDdlltgreHLYLYA 2037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 92 LAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVSESLSRIA 171
Cdd:TIGR01257 2038 RLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSII 2117
|
170 180
....*....|....*....|.
gi 1447648657 172 RNDTIVVVSTHDPNTRDA-CT 191
Cdd:TIGR01257 2118 REGRAVVLTSHSMEECEAlCT 2138
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
20-182 |
1.17e-15 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 72.76 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 20 HDLTASLMPGHVYALTGPSGAGKSTLL-------GIIAGWTTpaEGQVTRQGID---------SMR----WIFQNP---- 75
Cdd:COG1117 28 KDINLDIPENKVTALIGPSGCGKSTLLrclnrmnDLIPGARV--EGEILLDGEDiydpdvdvvELRrrvgMVFQKPnpfp 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 76 -------------HGVAQRTAIDHV---SLpllakglprREA---EEqartlmdrfnltrVTDR--RFA-ELSGGEAQRL 133
Cdd:COG1117 106 ksiydnvayglrlHGIKSKSELDEIveeSL---------RKAalwDE-------------VKDRlkKSAlGLSGGQQQRL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1447648657 134 MLARAFAAQPSLMLVDEPTAQLDMHTAATVSESLSRIARNDTIVVVsTH 182
Cdd:COG1117 164 CIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIV-TH 211
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1-156 |
1.19e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 73.24 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 1 MRVDLDHVGHRYA-----DGPLLFhDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVT-----------RQG 64
Cdd:PRK13649 1 MGINLQNVSYTYQagtpfEGRALF-DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRvddtlitstskNKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 65 IDSMR----WIFQNPHG-VAQRTAIDHVSLPLLAKGLPRREAEEQARtlmDRFNLTRVTDRRFA----ELSGGEAQRLML 135
Cdd:PRK13649 80 IKQIRkkvgLVFQFPESqLFEETVLKDVAFGPQNFGVSQEEAEALAR---EKLALVGISESLFEknpfELSGGQMRRVAI 156
|
170 180
....*....|....*....|.
gi 1447648657 136 ARAFAAQPSLMLVDEPTAQLD 156
Cdd:PRK13649 157 AGILAMEPKILVLDEPTAGLD 177
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
28-182 |
1.69e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 72.02 E-value: 1.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 28 PGHVYALTGPSGAGKSTLLGIIAGwtTPA----EGQVTRQGIDSMRW------------IFQNP---HGVAQ----RTAI 84
Cdd:COG0396 25 PGEVHAIMGPNGSGKSTLAKVLMG--HPKyevtSGSILLDGEDILELspderaragiflAFQYPveiPGVSVsnflRTAL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 85 DHVSLPLLakglPRREAEEQARTLMDRFNLtrvtDRRFAE------LSGGEAQRL----MLARafaaQPSLMLVDEPTAQ 154
Cdd:COG0396 103 NARRGEEL----SAREFLKLLKEKMKELGL----DEDFLDryvnegFSGGEKKRNeilqMLLL----EPKLAILDETDSG 170
|
170 180
....*....|....*....|....*...
gi 1447648657 155 LDMHTAATVSESLSRIARNDTIVVVSTH 182
Cdd:COG0396 171 LDIDALRIVAEGVNKLRSPDRGILIITH 198
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
14-184 |
1.97e-15 |
|
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: 71.24 E-value: 1.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 14 DGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMRwifQNPHGVAQRTAIDHvsLPLLA 93
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAE---QRDEPHENILYLGH--LPGLK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 94 KGLPRRE-----------AEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAAT 162
Cdd:TIGR01189 86 PELSALEnlhfwaaihggAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVAL 165
|
170 180
....*....|....*....|..
gi 1447648657 163 VSESLSRIARNDTIVVVSTHDP 184
Cdd:TIGR01189 166 LAGLLRAHLARGGIVLLTTHQD 187
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
14-182 |
2.47e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 70.99 E-value: 2.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 14 DGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGID----------SMRWIFQNPhGVAQR-T 82
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPirrqrdeyhqDLLYLGHQP-GIKTElT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 83 AIDHVSLPLLAKGLPRREAEEQArtlMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAAT 162
Cdd:PRK13538 91 ALENLRFYQRLHGPGDDEALWEA---LAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVAR 167
|
170 180
....*....|....*....|
gi 1447648657 163 VSESLSRIARNDTIVVVSTH 182
Cdd:PRK13538 168 LEALLAQHAEQGGMVILTTH 187
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
3-183 |
2.55e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 72.33 E-value: 2.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMRW------------ 70
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFsklqgirklvgi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 71 IFQNPHG-VAQRTAIDHVSLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVD 149
Cdd:PRK13644 82 VFQNPETqFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFD 161
|
170 180 190
....*....|....*....|....*....|....
gi 1447648657 150 EPTAQLDMHTAATVSESLSRIARNDTIVVVSTHD 183
Cdd:PRK13644 162 EVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHN 195
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
20-163 |
4.76e-15 |
|
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: 72.41 E-value: 4.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 20 HDLTASLMPGHVYALTGPSGAGKSTL----LGIIagwttPAEGQVTRQGID--------------SMRWIFQNPHG---- 77
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLglalLRLI-----PSEGEIRFDGQDldglsrralrplrrRMQVVFQDPFGslsp 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 78 ---VAQrtaIdhVSLPL--LAKGLPRREAEEQARTLMDRFNLTRVTDRRF-AELSGGEAQRLMLARAFAAQPSLMLVDEP 151
Cdd:COG4172 378 rmtVGQ---I--IAEGLrvHGPGLSAAERRARVAEALEEVGLDPAARHRYpHEFSGGQRQRIAIARALILEPKLLVLDEP 452
|
170
....*....|..
gi 1447648657 152 TAQLDMHTAATV 163
Cdd:COG4172 453 TSALDVSVQAQI 464
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-182 |
4.89e-15 |
|
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: 70.58 E-value: 4.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 2 RVDLDHVGHRYADGP--LLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGidsmRWIFQNPH--- 76
Cdd:cd03248 11 IVKFQNVTFAYPTRPdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDG----KPISQYEHkyl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 77 -----GVAQ------RTAIDHVSLPLLAKGLPRREAEEQ---ARTLMDRFNLTRVTD--RRFAELSGGEAQRLMLARAFA 140
Cdd:cd03248 87 hskvsLVGQepvlfaRSLQDNIAYGLQSCSFECVKEAAQkahAHSFISELASGYDTEvgEKGSQLSGGQKQRVAIARALI 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1447648657 141 AQPSLMLVDEPTAQLDMHTAATVSESLSRIARNDTIVVVSTH 182
Cdd:cd03248 167 RNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHR 208
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
6-183 |
8.95e-15 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 70.34 E-value: 8.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 6 DHVGHRYADGpLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDS----------------MR 69
Cdd:PRK11701 10 RGLTKLYGPR-KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGqlrdlyalseaerrrlLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 70 --WIF--QNP-HGV-AQRTAIDHVSLPLLAKGLPR-REAEEQARTLMDR--FNLTRVTD--RRFaelSGGEAQRLMLARA 138
Cdd:PRK11701 89 teWGFvhQHPrDGLrMQVSAGGNIGERLMAVGARHyGDIRATAGDWLERveIDAARIDDlpTTF---SGGMQQRLQIARN 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1447648657 139 FAAQPSLMLVDEPTAQLDMHTAATVSESLSRIARN-DTIVVVSTHD 183
Cdd:PRK11701 166 LVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHD 211
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-179 |
9.30e-15 |
|
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: 71.77 E-value: 9.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 2 RVDLDHVGHRY-ADGPLLfHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTrqgIDSmrwifQNPHGVAQ 80
Cdd:COG5265 357 EVRFENVSFGYdPERPIL-KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRIL---IDG-----QDIRDVTQ 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 81 ---RTAI-----DHVslpL--------LAKGLP---RREAEEQAR---------TLMDRFNlTRVTDRRFaELSGGEAQR 132
Cdd:COG5265 428 aslRAAIgivpqDTV---LfndtiaynIAYGRPdasEEEVEAAARaaqihdfieSLPDGYD-TRVGERGL-KLSGGEKQR 502
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1447648657 133 LMLARAFAAQPSLMLVDEPTAQLDMHTAATVSESLSRIARNDTIVVV 179
Cdd:COG5265 503 VAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVI 549
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
8-198 |
9.60e-15 |
|
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: 69.87 E-value: 9.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 8 VGHRYAdgpllFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGidSMRWIFQNPHGV-AQRTAIDH 86
Cdd:cd03220 32 VGEFWA-----LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG--RVSSLLGLGGGFnPELTGREN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 87 VSLPLLAKGLPRREAEEqartLMDR---FN-LTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAAT 162
Cdd:cd03220 105 IYLNGRLLGLSRKEIDE----KIDEiieFSeLGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEK 180
|
170 180 190
....*....|....*....|....*....|....*..
gi 1447648657 163 VSESLSRIARNDTIVVVSTHDPNT-RDACTDIIDLKN 198
Cdd:cd03220 181 CQRRLRELLKQGKTVILVSHDPSSiKRLCDRALVLEK 217
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
25-153 |
1.01e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 71.60 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 25 SLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVT---------------RQGIdSMrwIFQNPHGVAQRTAIDHVSL 89
Cdd:COG3845 27 TVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILidgkpvrirsprdaiALGI-GM--VHQHFMLVPNLTVAENIVL 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1447648657 90 ---PLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTA 153
Cdd:COG3845 104 glePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTA 170
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
26-156 |
1.71e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 69.63 E-value: 1.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 26 LMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVT---------------RQGIdsMRwIFQNPHGVAQRTAID----- 85
Cdd:PRK11300 28 VREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILlrgqhieglpghqiaRMGV--VR-TFQHVRLFREMTVIEnllva 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 86 ---HVSLPLLAkGL--------PRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQ 154
Cdd:PRK11300 105 qhqQLKTGLFS-GLlktpafrrAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAG 183
|
..
gi 1447648657 155 LD 156
Cdd:PRK11300 184 LN 185
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
12-183 |
1.72e-14 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 69.73 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 12 YADGPLLfHDLTASLMPGHVYALTGPSGAGKS----TLLGIIAGWTTPAEGQVTRQGI----DSMR-----WIFQNPHGV 78
Cdd:PRK10418 13 QAAQPLV-HGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKpvapCALRgrkiaTIMQNPRSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 79 AQ--RTAIDHVSLPLLAKGLPRREAeeQARTLMDRFNLT---RVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTA 153
Cdd:PRK10418 92 FNplHTMHTHARETCLALGKPADDA--TLTAALEAVGLEnaaRVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190
....*....|....*....|....*....|.
gi 1447648657 154 QLDMHTAATVSESLSRIARNDTI-VVVSTHD 183
Cdd:PRK10418 170 DLDVVAQARILDLLESIVQKRALgMLLVTHD 200
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
5-200 |
2.95e-14 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 70.20 E-value: 2.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 5 LDHVGHRYADGPLLfHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVT-RQGIdSMRWIFQnpHGVAQRTA 83
Cdd:PRK10636 315 MEKVSAGYGDRIIL-DSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGlAKGI-KLGYFAQ--HQLEFLRA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 84 iDHVSLPLLAKGLPRrEAEEQARTLMDRFNLT--RVTD--RRFaelSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHT 159
Cdd:PRK10636 391 -DESPLQHLARLAPQ-ELEQKLRDYLGGFGFQgdKVTEetRRF---SGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDM 465
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1447648657 160 AATVSESLsrIARNDTIVVVStHDPNTRDACTDII-------------DLKNYQ 200
Cdd:PRK10636 466 RQALTEAL--IDFEGALVVVS-HDRHLLRSTTDDLylvhdgkvepfdgDLEDYQ 516
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
20-183 |
3.21e-14 |
|
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: 70.10 E-value: 3.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 20 HDLTASLMPGHVYALTGPSGAGKS----TLLGIIAGWTTPAEGQVTRQGID-----------------SMrwIFQ----- 73
Cdd:COG4172 27 KGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDllglserelrrirgnriAM--IFQepmts 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 74 -NPHgvaqRTAIDHVSLPL-LAKGLPRREAEEQARTLMDRfnlTRVTD--RRFA----ELSGGEAQRLMLARAFAAQPSL 145
Cdd:COG4172 105 lNPL----HTIGKQIAEVLrLHRGLSGAAARARALELLER---VGIPDpeRRLDayphQLSGGQRQRVMIAMALANEPDL 177
|
170 180 190
....*....|....*....|....*....|....*....
gi 1447648657 146 MLVDEPTAQLDMHTAATVSESLSRI-ARNDTIVVVSTHD 183
Cdd:COG4172 178 LIADEPTTALDVTVQAQILDLLKDLqRELGMALLLITHD 216
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
21-183 |
3.42e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 70.06 E-value: 3.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 21 DLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGID---------------SMRWIFQNPHGVAQRTAID 85
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDiakisdaelrevrrkKIAMVFQSFALMPHMTVLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 86 HVSLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVSE 165
Cdd:PRK10070 126 NTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQD 205
|
170
....*....|....*....
gi 1447648657 166 SLSRI-ARNDTIVVVSTHD 183
Cdd:PRK10070 206 ELVKLqAKHQRTIVFISHD 224
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
15-181 |
3.76e-14 |
|
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: 67.46 E-value: 3.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 15 GPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMRWifqNPHGvAQRTAIDHVSlpllak 94
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRR---SPRD-AIRAGIAYVP------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 95 GLPRREAEEQARTLMDRFNLTRVtdrrfaeLSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVSESLSRIARND 174
Cdd:cd03215 82 EDRKREGLVLDLSVAENIALSSL-------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAG 154
|
....*...
gi 1447648657 175 T-IVVVST 181
Cdd:cd03215 155 KaVLLISS 162
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
19-194 |
5.16e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 68.18 E-value: 5.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 19 FHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGidSMRWIFQ-----NPhgvaQRTAIDHVSLPLLA 93
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG--RVSALLElgagfHP----ELTGRENIYLNGRL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 94 KGLPRREAEEqartLMDrfnltRVTDrrFAEL-----------SGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAAT 162
Cdd:COG1134 116 LGLSRKEIDE----KFD-----EIVE--FAELgdfidqpvktySSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKK 184
|
170 180 190
....*....|....*....|....*....|....
gi 1447648657 163 VSESL-SRIARNDTIVVVStHDPNT-RDACTDII 194
Cdd:COG1134 185 CLARIrELRESGRTVIFVS-HSMGAvRRLCDRAI 217
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-180 |
8.46e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 68.98 E-value: 8.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 2 RVDLDHVGHRYADGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEG--------------QVTRQGI-- 65
Cdd:PRK10790 340 RIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGeirldgrplsslshSVLRQGVam 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 66 ---------DSMrwiFQN--------PHGVAQrtAIDHVSLPLLAKGLP---RREAEEQARTlmdrfnltrvtdrrfaeL 125
Cdd:PRK10790 420 vqqdpvvlaDTF---LANvtlgrdisEEQVWQ--ALETVQLAELARSLPdglYTPLGEQGNN-----------------L 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1447648657 126 SGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVSESLSRIARNDTIVVVS 180
Cdd:PRK10790 478 SVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIA 532
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
3-183 |
9.19e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 67.85 E-value: 9.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRY-ADGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQ-------VTRQGIDSMR----W 70
Cdd:PRK13648 8 IVFKNVSFQYqSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEifynnqaITDDNFEKLRkhigI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 71 IFQNPHG--VAQRTAIDhVSLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLV 148
Cdd:PRK13648 88 VFQNPDNqfVGSIVKYD-VAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIIL 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 1447648657 149 DEPTAQLDMHTAATVSESLSRIARNDTIVVVS-THD 183
Cdd:PRK13648 167 DEATSMLDPDARQNLLDLVRKVKSEHNITIISiTHD 202
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-152 |
9.51e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 68.89 E-value: 9.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 19 FHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTrqgIDSMRWIFQNP-----HGVA-------------Q 80
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIR---LDGKPVRIRSPrdairAGIAyvpedrkgeglvlD 344
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1447648657 81 RTAIDHVSLPLLAKG-----LPRREAEEQARTLMDRFNL-TRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPT 152
Cdd:COG1129 345 LSIRENITLASLDRLsrgglLDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
20-180 |
9.88e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 67.49 E-value: 9.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 20 HDLTASLMPGHVYALTGPSGAGKSTLLGII--AGWTTP---AEGQVTRQG--IDSMR-----------WIFQNPHGVAQr 81
Cdd:PRK14239 22 NSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGhnIYSPRtdtvdlrkeigMVFQQPNPFPM- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 82 TAIDHVSLPLLAKGLPRREAEEQA--RTLMDRFNLTRVTDRRFAE---LSGGEAQRLMLARAFAAQPSLMLVDEPTAQLD 156
Cdd:PRK14239 101 SIYENVVYGLRLKGIKDKQVLDEAveKSLKGASIWDEVKDRLHDSalgLSGGQQQRVCIARVLATSPKIILLDEPTSALD 180
|
170 180
....*....|....*....|....
gi 1447648657 157 MHTAATVSESLSRIARNDTIVVVS 180
Cdd:PRK14239 181 PISAGKIEETLLGLKDDYTMLLVT 204
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
18-187 |
1.38e-13 |
|
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: 66.11 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 18 LFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAgwttpaegqvtrqgidsmrwifqnphgvaQRTAIDHVSLPLLAKGLP 97
Cdd:cd03232 22 LLNNISGYVKPGTLTALMGESGAGKTTLLDVLA-----------------------------GRKTAGVITGEILINGRP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 98 RREA-------EEQARTLMDrfNLTRVTDRRFA----ELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVSES 166
Cdd:cd03232 73 LDKNfqrstgyVEQQDVHSP--NLTVREALRFSallrGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRF 150
|
170 180
....*....|....*....|.
gi 1447648657 167 LSRIARNDTIVVVSTHDPNTR 187
Cdd:cd03232 151 LKKLADSGQAILCTIHQPSAS 171
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-183 |
1.43e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 68.30 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 26 LMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQgIDsmrwIFQNPhgvaQRTAIDH---VSLPLlakglprREAE 102
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LK----ISYKP----QYIKPDYdgtVEDLL-------RSIT 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 103 EQART------LMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVSESLSRIARND-- 174
Cdd:PRK13409 426 DDLGSsyykseIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEERea 505
|
....*....
gi 1447648657 175 TIVVVStHD 183
Cdd:PRK13409 506 TALVVD-HD 513
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
21-172 |
1.54e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 67.81 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 21 DLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMR-----W---------IFQNP-HGVAQRTAI- 84
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGmkddeWravrsdiqmIFQDPlASLNPRMTIg 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 85 DHVSLPLLA--KGLPRREAEEQARTLMDRFNL-TRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAA 161
Cdd:PRK15079 119 EIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQA 198
|
170
....*....|.
gi 1447648657 162 TVSESLSRIAR 172
Cdd:PRK15079 199 QVVNLLQQLQR 209
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-189 |
1.91e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 66.65 E-value: 1.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 18 LFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMRW-----------IFQNP-HGVAQRTAI- 84
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLpeykrakyigrVFQDPmMGTAPSMTIe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 85 DHVSLPL-------LAKGLPRREaEEQARTLMDRFNL---TRVTDrRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQ 154
Cdd:COG1101 101 ENLALAYrrgkrrgLRRGLTKKR-RELFRELLATLGLgleNRLDT-KVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAA 178
|
170 180 190
....*....|....*....|....*....|....*...
gi 1447648657 155 LDMHTAATVSESLSRIARND---TIVVvsTHdpNTRDA 189
Cdd:COG1101 179 LDPKTAALVLELTEKIVEENnltTLMV--TH--NMEQA 212
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-183 |
2.04e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 66.94 E-value: 2.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADG-PLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEG-------QVTRQGIDSMR----W 70
Cdd:PRK13632 8 IKVENVSFSYPNSeNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGeikidgiTISKENLKEIRkkigI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 71 IFQNPH----GVaqrTAIDHVSLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLM 146
Cdd:PRK13632 88 IFQNPDnqfiGA---TVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEII 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 1447648657 147 LVDEPTAQLDMHTAATVSESLSRIARNDTIVVVS-THD 183
Cdd:PRK13632 165 IFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISiTHD 202
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-183 |
2.58e-13 |
|
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: 66.28 E-value: 2.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 29 GHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDsmrwIFQNPHGVA--QRTAIDHvslpLLAKGLPRREAEEQAR 106
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT----VSYKPQYIKadYEGTVRD----LLSSITKDFYTHPYFK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 107 T-LMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVSESLSRIARND--TIVVVStHD 183
Cdd:cd03237 97 TeIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNekTAFVVE-HD 175
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-183 |
2.68e-13 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 67.50 E-value: 2.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 28 PGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQG-----IDSMRWI-----FQNphgVAQ---RTA-----IDHVsl 89
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPswdevLKRFRGTelqdyFKK---LANgeiKVAhkpqyVDLI-- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 90 PLLAKGLPR---REAEE--QARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVS 164
Cdd:COG1245 173 PKVFKGTVRellEKVDErgKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVA 252
|
170
....*....|....*....
gi 1447648657 165 ESLSRIARNDTIVVVSTHD 183
Cdd:COG1245 253 RLIRELAEEGKYVLVVEHD 271
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
21-190 |
3.00e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 66.07 E-value: 3.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 21 DLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVT---------------RQGIDsmrWIFQNPHGVAQRTAID 85
Cdd:PRK10895 21 DVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIiddedisllplharaRRGIG---YLPQEASIFRRLSVYD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 86 HVSLPL-LAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVS 164
Cdd:PRK10895 98 NLMAVLqIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIK 177
|
170 180
....*....|....*....|....*..
gi 1447648657 165 ESLSRIARNDTIVVVSTHD-PNTRDAC 190
Cdd:PRK10895 178 RIIEHLRDSGLGVLITDHNvRETLAVC 204
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
21-182 |
3.07e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 66.68 E-value: 3.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 21 DLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQV-----------TRQGIDSMR----WIFQNPHG-VAQRTAI 84
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdivvsstsKQKEIKPVRkkvgVVFQFPESqLFEETVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 85 DHVSLPLLAKGLPRREAEEQARTLMDRFNLTR-VTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATV 163
Cdd:PRK13643 104 KDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEM 183
|
170
....*....|....*....
gi 1447648657 164 SESLSRIARNDTIVVVSTH 182
Cdd:PRK13643 184 MQLFESIHQSGQTVVLVTH 202
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-183 |
3.67e-13 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 67.27 E-value: 3.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 5 LDHVGHRYADGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQ-GIdSMRWIFQNPH------- 76
Cdd:TIGR03719 7 MNRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQpGI-KVGYLPQEPQldptktv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 77 ------GVAQ-RTAIDHVSLPLLAKGLPRRE----AEEQARtLMDR------FNLTRVTDR------------RFAELSG 127
Cdd:TIGR03719 86 renveeGVAEiKDALDRFNEISAKYAEPDADfdklAAEQAE-LQEIidaadaWDLDSQLEIamdalrcppwdaDVTKLSG 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1447648657 128 GEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVSESLSRIArnDTIVVVsTHD 183
Cdd:TIGR03719 165 GERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYP--GTVVAV-THD 217
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
11-180 |
4.48e-13 |
|
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: 65.13 E-value: 4.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 11 RYA-DGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDsmrwIFQNP-HGVAQRTAI---D 85
Cdd:cd03369 15 RYApDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGID----ISTIPlEDLRSSLTIipqD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 86 hvslPLLAKGlprreaeeQARTLMDRFNltRVTDR------RFAE----LSGGEAQRLMLARAFAAQPSLMLVDEPTAQL 155
Cdd:cd03369 91 ----PTLFSG--------TIRSNLDPFD--EYSDEeiygalRVSEgglnLSQGQRQLLCLARALLKRPRVLVLDEATASI 156
|
170 180
....*....|....*....|....*
gi 1447648657 156 DMHTAATVSESLSRIARNDTIVVVS 180
Cdd:cd03369 157 DYATDALIQKTIREEFTNSTILTIA 181
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
14-184 |
4.95e-13 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 66.75 E-value: 4.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 14 DGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTT--PAEGQV------------------------------T 61
Cdd:TIGR03269 11 DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyhvalcekcgyverpskvgepcpvcggtlE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 62 RQGID-----------SMRWI---FQNPHGV-AQRTAIDHVSLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELS 126
Cdd:TIGR03269 91 PEEVDfwnlsdklrrrIRKRIaimLQRTFALyGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRITHIARDLS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1447648657 127 GGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVSESLSRIARNDTI-VVVSTHDP 184
Cdd:TIGR03269 171 GGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGIsMVLTSHWP 229
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
25-163 |
5.05e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 66.14 E-value: 5.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 25 SLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGID--------------SMRWIFQNPHGV--AQRTAIDHVS 88
Cdd:PRK11308 37 TLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDllkadpeaqkllrqKIQIVFQNPYGSlnPRKKVGQILE 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1447648657 89 LPLLAK-GLPRREAEEQARTLMDRFNL-TRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATV 163
Cdd:PRK11308 117 EPLLINtSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQV 193
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-181 |
5.48e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 66.59 E-value: 5.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 2 RVDLDHVGHRYADGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQV-------TRQGIDSMR----- 69
Cdd:COG3845 257 VLEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIrldgediTGLSPRERRrlgva 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 70 WIFQNPHG--------VAQRTAIDHVSLPLLAKG--LPRREAEEQARTLMDRFNL-TRVTDRRFAELSGGEAQRLMLARA 138
Cdd:COG3845 337 YIPEDRLGrglvpdmsVAENLILGRYRRPPFSRGgfLDRKAIRAFAEELIEEFDVrTPGPDTPARSLSGGNQQKVILARE 416
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1447648657 139 FAAQPSLMLVDEPTAQLDMHTAATVSESLsrIARND---TIVVVST 181
Cdd:COG3845 417 LSRDPKLLIAAQPTRGLDVGAIEFIHQRL--LELRDagaAVLLISE 460
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-194 |
5.86e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 66.37 E-value: 5.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 28 PGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQG-----IDSMRW---------IFQNPHGVAQRT-AIDHvsLPLL 92
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPswdevLKRFRGtelqnyfkkLYNGEIKVVHKPqYVDL--IPKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 93 AKG-----LPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVSESL 167
Cdd:PRK13409 176 FKGkvrelLKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLI 255
|
170 180
....*....|....*....|....*..
gi 1447648657 168 SRIARNDTIVVVStHDPNTRDACTDII 194
Cdd:PRK13409 256 RELAEGKYVLVVE-HDLAVLDYLADNV 281
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-180 |
6.12e-13 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 66.66 E-value: 6.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 2 RVDLDHVGHRY-ADGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMRWIFQNphgvaQ 80
Cdd:TIGR02203 330 DVEFRNVTFRYpGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLAS-----L 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 81 RTAIDHVSLPL----------LAKGLPRREAEEQARTLMDRFNLTRVTDR-----------RFAELSGGEAQRLMLARAF 139
Cdd:TIGR02203 405 RRQVALVSQDVvlfndtiannIAYGRTEQADRAEIERALAAAYAQDFVDKlplgldtpigeNGVLLSGGQRQRLAIARAL 484
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1447648657 140 AAQPSLMLVDEPTAQLDMHTAATVSESLSRIARNDTIVVVS 180
Cdd:TIGR02203 485 LKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIA 525
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
30-183 |
7.04e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 65.19 E-value: 7.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 30 HVYALTGPSGAGKSTLL-------GIIAGWTtpAEGQVTRQG-------IDSMR------WIFQNPHGVAqRTAIDHVSL 89
Cdd:PRK14243 37 QITAFIGPSGCGKSTILrcfnrlnDLIPGFR--VEGKVTFHGknlyapdVDPVEvrrrigMVFQKPNPFP-KSIYDNIAY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 90 PLLAKGLPRREAEEQARTLMDRFNLTRVTDR---RFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVSES 166
Cdd:PRK14243 114 GARINGYKGDMDELVERSLRQAALWDEVKDKlkqSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEEL 193
|
170
....*....|....*..
gi 1447648657 167 LSRIARNDTIVVVsTHD 183
Cdd:PRK14243 194 MHELKEQYTIIIV-THN 209
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
21-183 |
8.17e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 65.14 E-value: 8.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 21 DLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQG----IDSMrW--------IFQNP-HGVAQRTAIDHV 87
Cdd:PRK13650 25 DVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGdlltEENV-WdirhkigmVFQNPdNQFVGATVEDDV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 88 SLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVSESL 167
Cdd:PRK13650 104 AFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTI 183
|
170
....*....|....*..
gi 1447648657 168 SRIARNDTIVVVS-THD 183
Cdd:PRK13650 184 KGIRDDYQMTVISiTHD 200
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
8-156 |
1.03e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 65.88 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 8 VGHRYAdgpllFHDLTASLMPGHVYALTGPSGAGKST----LLGIIAgwttpAEGQVTRQGIDSMRW------------- 70
Cdd:PRK15134 296 VDHNVV-----VKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLnrrqllpvrhriq 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 71 -IFQNPHG-------VAQrtaIDHVSLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRF-AELSGGEAQRLMLARAFAA 141
Cdd:PRK15134 366 vVFQDPNSslnprlnVLQ---IIEEGLRVHQPTLSAAQREQQVIAVMEEVGLDPETRHRYpAEFSGGQRQRIAIARALIL 442
|
170
....*....|....*
gi 1447648657 142 QPSLMLVDEPTAQLD 156
Cdd:PRK15134 443 KPSLIILDEPTSSLD 457
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
17-183 |
1.08e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 64.79 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 17 LLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQV----------TRQGI----DSMRWIFQNPHGVAQRT 82
Cdd:PRK11831 21 CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEIlfdgenipamSRSRLytvrKRMSMLFQSGALFTDMN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 83 AIDHVSLPLLAKG-LPrrEAEEQARTLM--DRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHT 159
Cdd:PRK11831 101 VFDNVAYPLREHTqLP--APLLHSTVMMklEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPIT 178
|
170 180
....*....|....*....|....*.
gi 1447648657 160 AATVSESLSRI--ARNDTIVVVStHD 183
Cdd:PRK11831 179 MGVLVKLISELnsALGVTCVVVS-HD 203
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
25-183 |
1.97e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 64.34 E-value: 1.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 25 SLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEG-------QVTRQGIDSMR----WIFQNP-HGVAQRTAIDHVSLPLL 92
Cdd:PRK13642 29 SITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGkvkidgeLLTAENVWNLRrkigMVFQNPdNQFVGATVEDDVAFGME 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 93 AKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVSESLSRIAR 172
Cdd:PRK13642 109 NQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKE 188
|
170
....*....|..
gi 1447648657 173 NDTIVVVS-THD 183
Cdd:PRK13642 189 KYQLTVLSiTHD 200
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
5-185 |
2.68e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 63.65 E-value: 2.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 5 LDHVGHRYAdGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMRWifqNPHGVAQRTAI 84
Cdd:PRK10575 14 LRNVSFRVP-GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESW---SSKAFARKVAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 85 DHVSLP---------LLAKG-------LPR-----REAEEQARTLMDrfnLTRVTDRRFAELSGGEAQRLMLARAFAAQP 143
Cdd:PRK10575 90 LPQQLPaaegmtvreLVAIGrypwhgaLGRfgaadREKVEEAISLVG---LKPLAHRLVDSLSGGERQRAWIAMLVAQDS 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1447648657 144 SLMLVDEPTAQLDMHTAATVSESLSRIARNDTIVVVST-HDPN 185
Cdd:PRK10575 167 RCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVlHDIN 209
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
20-182 |
4.26e-12 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 62.16 E-value: 4.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 20 HDLTASLMPGHVYALTGPSGAGKSTLLGIIAGW--TTPAEGQVTRQGID---------SMRWI---FQNP---HGVaqrt 82
Cdd:cd03217 17 KGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDitdlppeerARLGIflaFQYPpeiPGV---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 83 aidhvslpllakglprreaeeqarTLMDrfnLTRVTDRRFaelSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAAT 162
Cdd:cd03217 93 ------------------------KNAD---FLRYVNEGF---SGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRL 142
|
170 180
....*....|....*....|
gi 1447648657 163 VSESLSRIARNDTIVVVSTH 182
Cdd:cd03217 143 VAEVINKLREEGKSVLIITH 162
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
14-180 |
4.98e-12 |
|
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: 61.40 E-value: 4.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 14 DGPLLFHDLTASLMPG-HVYaLTGPSGAGKSTLLGIIAG-WTTpAEGQVTR-QGIDSMrwiFqnphgVAQRtaidhvslP 90
Cdd:cd03223 12 DGRVLLKDLSFEIKPGdRLL-ITGPSGTGKSSLFRALAGlWPW-GSGRIGMpEGEDLL---F-----LPQR--------P 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 91 LLAKGLPRreaeEQ-ARTLMDrfnltrvtdrrfaELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATvsesLSR 169
Cdd:cd03223 74 YLPLGTLR----EQlIYPWDD-------------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDR----LYQ 132
|
170
....*....|.
gi 1447648657 170 IARNDTIVVVS 180
Cdd:cd03223 133 LLKELGITVIS 143
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
36-183 |
5.51e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 63.51 E-value: 5.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 36 GPSGAGKSTLLGIIAGWTTPAEGQVTrqgIDSMR------------WIFQN----PH-GVAqrtaiDHVSLPLLAKGLPR 98
Cdd:PRK11000 36 GPSGCGKSTLLRMIAGLEDITSGDLF---IGEKRmndvppaergvgMVFQSyalyPHlSVA-----ENMSFGLKLAGAKK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 99 REAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDmhtAATVSESLSRIAR-----N 173
Cdd:PRK11000 108 EEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD---AALRVQMRIEISRlhkrlG 184
|
170
....*....|
gi 1447648657 174 DTIVVVsTHD 183
Cdd:PRK11000 185 RTMIYV-THD 193
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-183 |
5.94e-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: 63.65 E-value: 5.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 25 SLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQ----------GIDSmrwifqnphgvaQRTAIDhvslpLLAK 94
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDlkisykpqyiSPDY------------DGTVEE-----FLRS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 95 GLPRREAEEQART-LMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVSESLSRIARN 173
Cdd:COG1245 425 ANTDDFGSSYYKTeIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAEN 504
|
170
....*....|..
gi 1447648657 174 D--TIVVVStHD 183
Cdd:COG1245 505 RgkTAMVVD-HD 515
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
20-157 |
6.50e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 62.97 E-value: 6.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 20 HDLTASL-MPGH-VYALTGPSGAGKSTLLGIIAGWTTPAEGQV---------TRQGID------SMRWIFQN----PH-- 76
Cdd:PRK11144 13 LCLTVNLtLPAQgITAIFGRSGAGKTSLINAISGLTRPQKGRIvlngrvlfdAEKGIClppekrRIGYVFQDarlfPHyk 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 77 -------GVAQRTAI---DHVSL----PLLakglprreaeeqartlmDRFNLTrvtdrrfaeLSGGEAQRLMLARAFAAQ 142
Cdd:PRK11144 93 vrgnlryGMAKSMVAqfdKIVALlgiePLL-----------------DRYPGS---------LSGGEKQRVAIGRALLTA 146
|
170
....*....|....*
gi 1447648657 143 PSLMLVDEPTAQLDM 157
Cdd:PRK11144 147 PELLLMDEPLASLDL 161
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-183 |
7.02e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 62.80 E-value: 7.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 20 HDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVT-------RQGIDSMRWIfqnphGV--AQRT-------A 83
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRvlgyvpfKRRKEFARRI-----GVvfGQRSqlwwdlpA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 84 IDhvSLPLLAK--GLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAA 161
Cdd:COG4586 114 ID--SFRLLKAiyRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKE 191
|
170 180
....*....|....*....|...
gi 1447648657 162 TVSESLSRI-ARNDTIVVVSTHD 183
Cdd:COG4586 192 AIREFLKEYnRERGTTILLTSHD 214
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
33-183 |
8.35e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 62.51 E-value: 8.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 33 ALTGPSGAGKSTLLGIIAGWTTPAEGQV-------TRQGIDSMR----WIFQNPHG------VAQRTAIDHVSLpllakG 95
Cdd:PRK13652 34 AVIGPNGAGKSTLFRHFNGILKPTSGSVlirgepiTKENIREVRkfvgLVFQNPDDqifsptVEQDIAFGPINL-----G 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 96 LPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVSESLSRIA-RND 174
Cdd:PRK13652 109 LDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPeTYG 188
|
....*....
gi 1447648657 175 TIVVVSTHD 183
Cdd:PRK13652 189 MTVIFSTHQ 197
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
12-157 |
8.61e-12 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 63.34 E-value: 8.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 12 YADGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGidSMRWIFQNPHGVaqrTAIDHVSLPL 91
Cdd:PLN03073 518 YPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSA--KVRMAVFSQHHV---DGLDLSSNPL 592
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1447648657 92 LA-----KGLPrreaEEQARTLMDRFNLT-RVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDM 157
Cdd:PLN03073 593 LYmmrcfPGVP----EQKLRAHLGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDL 660
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
21-183 |
8.68e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 62.82 E-value: 8.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 21 DLTASLMPGHVYALTGPSGAGKST-------LL---GIIAGWTT---------PaEGQVTRQGIDSMRWIFQ------NP 75
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSQtafalmgLLaanGRIGGSATfngreilnlP-EKELNKLRAEQISMIFQdpmtslNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 76 HgvaQRTAIDHVSLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFA---ELSGGEAQRLMLARAFAAQPSLMLVDEPT 152
Cdd:PRK09473 113 Y---MRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMyphEFSGGMRQRVMIAMALLCRPKLLIADEPT 189
|
170 180 190
....*....|....*....|....*....|..
gi 1447648657 153 AQLDMHTAATVSESLSRIARN-DTIVVVSTHD 183
Cdd:PRK09473 190 TALDVTVQAQIMTLLNELKREfNTAIIMITHD 221
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
31-183 |
1.16e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 62.04 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 31 VYALTGPSGAGKSTLLGI-------IAGWTTPAEGQVTRQGIDSMR----------WIFQNPHGVAQrTAIDHVSLPLLA 93
Cdd:PRK14271 49 VTSLMGPTGSGKTTFLRTlnrmndkVSGYRYSGDVLLGGRSIFNYRdvlefrrrvgMLFQRPNPFPM-SIMDNVLAGVRA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 94 -KGLPRREAEEQARTLMDRFNL-----TRVTDRRFaELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVSESL 167
Cdd:PRK14271 128 hKLVPRKEFRGVAQARLTEVGLwdavkDRLSDSPF-RLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFI 206
|
170
....*....|....*.
gi 1447648657 168 SRIARNDTIVVVsTHD 183
Cdd:PRK14271 207 RSLADRLTVIIV-THN 221
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
3-156 |
1.28e-11 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 62.17 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTrqgIDSMR------------W 70
Cdd:PRK11650 4 LKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIW---IGGRVvnelepadrdiaM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 71 IFQN----PH-GVAQRTAIDhvslpLLAKGLPRRE----AEEQARTLmdrfNLTRVTDRRFAELSGGEAQRLMLARAFAA 141
Cdd:PRK11650 81 VFQNyalyPHmSVRENMAYG-----LKIRGMPKAEieerVAEAARIL----ELEPLLDRKPRELSGGQRQRVAMGRAIVR 151
|
170
....*....|....*
gi 1447648657 142 QPSLMLVDEPTAQLD 156
Cdd:PRK11650 152 EPAVFLFDEPLSNLD 166
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
18-185 |
1.42e-11 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 62.56 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 18 LFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPA--EGQVTRQGIDSMRWIFQNPHGVAQRTAIDH----VSLPL 91
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFPKKQETFARISGYCEQNDIHSpqvtVRESL 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 92 LAKG---LPRREAEEQARTLMDR-FNLTRVTDRRFA--------ELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHT 159
Cdd:PLN03140 975 IYSAflrLPKEVSKEEKMMFVDEvMELVELDNLKDAivglpgvtGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARA 1054
|
170 180 190
....*....|....*....|....*....|
gi 1447648657 160 AATVseslSRIARN--DT--IVVVSTHDPN 185
Cdd:PLN03140 1055 AAIV----MRTVRNtvDTgrTVVCTIHQPS 1080
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1-185 |
2.53e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 60.95 E-value: 2.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 1 MRVDLDHVGHRYADG-PLLF---HDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMR------- 69
Cdd:PRK13646 1 MTIRFDNVSYTYQKGtPYEHqaiHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkyi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 70 --------WIFQNPHgvAQRTAiDHVSLPLLAK----GLPRREAEEQARTLMDRFNLTR-VTDRRFAELSGGEAQRLMLA 136
Cdd:PRK13646 81 rpvrkrigMVFQFPE--SQLFE-DTVEREIIFGpknfKMNLDEVKNYAHRLLMDLGFSRdVMSQSPFQMSGGQMRKIAIV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1447648657 137 RAFAAQPSLMLVDEPTAQLDMHTAATVSESLSRIA--RNDTIVVVsTHDPN 185
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILV-SHDMN 207
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
19-155 |
3.41e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 60.28 E-value: 3.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 19 FHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMRW---------IFQNPHG--VAQRTAIDHv 87
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWqtakimreaVAIVPEGrrVFSRMTVEE- 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1447648657 88 SLPLLAKGLPRREAEEQARTLMDRFnlTRVTDRRF---AELSGGEAQRLMLARAFAAQPSLMLVDEPTAQL 155
Cdd:PRK11614 100 NLAMGGFFAERDQFQERIKWVYELF--PRLHERRIqraGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1-156 |
4.28e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 60.61 E-value: 4.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 1 MRVDLDHVGHRYADGPLL----FHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVT-----------RQGI 65
Cdd:PRK13641 1 MSIKFENVDYIYSPGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITiagyhitpetgNKNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 66 DSMR----WIFQNPHG-VAQRTAIDHVSLPLLAKGLPRREAEEQARTLMDRFNL-TRVTDRRFAELSGGEAQRLMLARAF 139
Cdd:PRK13641 81 KKLRkkvsLVFQFPEAqLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVM 160
|
170
....*....|....*..
gi 1447648657 140 AAQPSLMLVDEPTAQLD 156
Cdd:PRK13641 161 AYEPEILCLDEPAAGLD 177
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
14-180 |
5.35e-11 |
|
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: 61.11 E-value: 5.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 14 DGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGidSMRWifqnphgVAQRTAIDHVSLP--- 90
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG--SVAY-------VPQQAWIQNDSLReni 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 91 LLAKGL--PRREAEEQARTLMDRFNLTRVTDR-----RFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMH----- 158
Cdd:TIGR00957 720 LFGKALneKYYQQVLEACALLPDLEILPSGDRteigeKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHvgkhi 799
|
170 180 190
....*....|....*....|....*....|....*.
gi 1447648657 159 --------------TAATVSESLSRIARNDTIVVVS 180
Cdd:TIGR00957 800 fehvigpegvlknkTRILVTHGISYLPQVDVIIVMS 835
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
3-180 |
5.39e-11 |
|
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: 60.91 E-value: 5.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGID-----------SMRWI 71
Cdd:TIGR01193 474 IVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSlkdidrhtlrqFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 72 FQNPHgVAQRTAIDHvslpLLAKGLPRREAEE--------QARTLMDRFNL---TRVTDRRFAeLSGGEAQRLMLARAFA 140
Cdd:TIGR01193 554 PQEPY-IFSGSILEN----LLLGAKENVSQDEiwaaceiaEIKDDIENMPLgyqTELSEEGSS-ISGGQKQRIALARALL 627
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1447648657 141 AQPSLMLVDEPTAQLDMHTAATVSESLSRIaRNDTIVVVS 180
Cdd:TIGR01193 628 TDSKVLILDESTSNLDTITEKKIVNNLLNL-QDKTIIFVA 666
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
96-182 |
5.41e-11 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 60.52 E-value: 5.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 96 LPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVSESLSRIARNDT 175
Cdd:NF000106 116 LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGA 195
|
....*..
gi 1447648657 176 IVVVSTH 182
Cdd:NF000106 196 TVLLTTQ 202
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-183 |
6.40e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.52 E-value: 6.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADgPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVT-------------RQGIDSMR 69
Cdd:PRK11819 325 IEAENLSKSFGD-RLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKigetvklayvdqsRDALDPNK 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 70 WIFQNPHGVAqrtaiDHVSLpllakGlprrEAEEQARTLMDRFNLtRVTD--RRFAELSGGEAQRLMLARAFAAQPSLML 147
Cdd:PRK11819 404 TVWEEISGGL-----DIIKV-----G----NREIPSRAYVGRFNF-KGGDqqKKVGVLSGGERNRLHLAKTLKQGGNVLL 468
|
170 180 190
....*....|....*....|....*....|....*.
gi 1447648657 148 VDEPTAQLDMHTAATVSESLSRIArnDTIVVVStHD 183
Cdd:PRK11819 469 LDEPTNDLDVETLRALEEALLEFP--GCAVVIS-HD 501
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
22-194 |
6.92e-11 |
|
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: 60.80 E-value: 6.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 22 LTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGID---SMRWIFQNPHGVAQR-------TAIDHVSLPL 91
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDietNLDAVRQSLGMCPQHnilfhhlTVAEHILFYA 1028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 92 LAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVSESLSRIa 171
Cdd:TIGR01257 1029 QLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKY- 1107
|
170 180
....*....|....*....|...
gi 1447648657 172 RNDTIVVVSTHDPNTRDACTDII 194
Cdd:TIGR01257 1108 RSGRTIIMSTHHMDEADLLGDRI 1130
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-155 |
1.01e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.80 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYadGPL-LFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMRW----------- 70
Cdd:PRK09700 6 ISMAGIGKSF--GPVhALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLdhklaaqlgig 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 71 -IFQnphgvaQRTAIDHVSL-------PLLAK---GLP---RREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLA 136
Cdd:PRK09700 84 iIYQ------ELSVIDELTVlenlyigRHLTKkvcGVNiidWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIA 157
|
170
....*....|....*....
gi 1447648657 137 RAFAAQPSLMLVDEPTAQL 155
Cdd:PRK09700 158 KTLMLDAKVIIMDEPTSSL 176
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
15-182 |
1.39e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 58.32 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 15 GPLLFHdltasLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQG-----IDSMRWIFQNPHGVAQRTAIDHVSL 89
Cdd:PRK13543 28 GPLDFH-----VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGktatrGDRSRFMAYLGHLPGLKADLSTLEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 90 PLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVSESLSR 169
Cdd:PRK13543 103 LHFLCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISA 182
|
170
....*....|...
gi 1447648657 170 IARNDTIVVVSTH 182
Cdd:PRK13543 183 HLRGGGAALVTTH 195
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
29-178 |
1.62e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 58.91 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 29 GHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGID------SMRWI-------FQNP-HGVAQRTAIDHVSLPLLAK 94
Cdd:PRK13637 33 GEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDitdkkvKLSDIrkkvglvFQYPeYQLFEETIEKDIAFGPINL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 95 GLPRREAEEQARTLMDRFNLTRVT--DRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLD-------------MH- 158
Cdd:PRK13637 113 GLSEEEIENRVKRAMNIVGLDYEDykDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDpkgrdeilnkikeLHk 192
|
170 180
....*....|....*....|....*
gi 1447648657 159 ----TAATVSESLSRIAR-NDTIVV 178
Cdd:PRK13637 193 eynmTIILVSHSMEDVAKlADRIIV 217
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
14-198 |
1.95e-10 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 57.48 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 14 DGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGidSMR------WI----------FQNPHG 77
Cdd:cd03250 16 ETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--SIAyvsqepWIqngtirenilFGKPFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 78 vAQR--TAID----HVSLPLLAKGLprreaeeqartlmdrfnLTRVTDRRFAeLSGGEAQRLMLARAFAAQPSLMLVDEP 151
Cdd:cd03250 94 -EERyeKVIKacalEPDLEILPDGD-----------------LTEIGEKGIN-LSGGQKQRISLARAVYSDADIYLLDDP 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1447648657 152 TAQLDMHTAATVSES--LSRIARNDTIVVVsTHDPNTRDACTDIIDLKN 198
Cdd:cd03250 155 LSAVDAHVGRHIFENciLGLLLNNKTRILV-THQLQLLPHADQIVVLDN 202
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
12-196 |
2.01e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.19 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 12 YADGPLLFH-DLTasLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMRWIFQNPHGVAQRTAIDHVS-- 88
Cdd:PRK11147 13 FSDAPLLDNaELH--IEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPRNVEGTVYDFVAeg 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 89 LPLLAKGLPRR-------EAEEQARTL---------MDRFNL----TRVT----------DRRFAELSGGEAQRLMLARA 138
Cdd:PRK11147 91 IEEQAEYLKRYhdishlvETDPSEKNLnelaklqeqLDHHNLwqleNRINevlaqlgldpDAALSSLSGGWLRKAALGRA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1447648657 139 FAAQPSLMLVDEPTAQLDMHTAATVSESLsrIARNDTIVVVStHDPN-TRDACTDIIDL 196
Cdd:PRK11147 171 LVSNPDVLLLDEPTNHLDIETIEWLEGFL--KTFQGSIIFIS-HDRSfIRNMATRIVDL 226
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
3-182 |
2.11e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 58.56 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADG-----PLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMR----W--- 70
Cdd:PRK13633 5 IKCKNVSYKYESNeesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDeenlWdir 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 71 -----IFQNPHGVAQRTAIDH-VSLPLLAKGLPRREAEEQARTLMDRFNLTRVtdRRFAE--LSGGEAQRLMLARAFAAQ 142
Cdd:PRK13633 85 nkagmVFQNPDNQIVATIVEEdVAFGPENLGIPPEEIRERVDESLKKVGMYEY--RRHAPhlLSGGQKQRVAIAGILAMR 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1447648657 143 PSLMLVDEPTAQLDMHTAATVSESLSRIARNDTI-VVVSTH 182
Cdd:PRK13633 163 PECIIFDEPTAMLDPSGRREVVNTIKELNKKYGItIILITH 203
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-182 |
3.56e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 58.30 E-value: 3.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADGPL-LFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMRW----IFQNPHG 77
Cdd:PRK11160 339 LTLNNVSFTYPDQPQpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYseaaLRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 78 VAQRTAIDHVSLP---LLAKGlprREAEEQARTLMDRFNLTRVTD-------------RrfaELSGGEAQRLMLARAFAA 141
Cdd:PRK11160 419 VSQRVHLFSATLRdnlLLAAP---NASDEALIEVLQQVGLEKLLEddkglnawlgeggR---QLSGGEQRRLGIARALLH 492
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1447648657 142 QPSLMLVDEPTAQLDMHTAATVSESLSRIARNDTIVVVsTH 182
Cdd:PRK11160 493 DAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMI-TH 532
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-195 |
3.65e-10 |
|
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: 57.12 E-value: 3.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 2 RVDLDHVGHRYADG-PLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGID-----------SMR 69
Cdd:cd03244 2 DIEFKNVSLRYRPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDiskiglhdlrsRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 70 WIFQN-------------PHGVAQRTAIDHVslpLLAKGLprREAEEQARTLMDrfnlTRVTDRRfAELSGGEAQRLMLA 136
Cdd:cd03244 82 IIPQDpvlfsgtirsnldPFGEYSDEELWQA---LERVGL--KEFVESLPGGLD----TVVEEGG-ENLSVGQRQLLCLA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1447648657 137 RAFAAQPSLMLVDEPTAQLDMHTAATVSESLsRIARNDTIVVVSTHDPNTrdactdIID 195
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPETDALIQKTI-REAFKDCTVLTIAHRLDT------IID 203
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
31-182 |
4.61e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 57.55 E-value: 4.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 31 VYALTGPSGAGKSTLLGIIAGWTTPAEGQVtrqgidSMRWIFQNPHGVAQRTAIDHVSLPL------------------- 91
Cdd:PRK13631 54 IYFIIGNSGSGKSTLVTHFNGLIKSKYGTI------QVGDIYIGDKKNNHELITNPYSKKIknfkelrrrvsmvfqfpey 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 92 ---------------LAKGLPRREAEEQARTLMDRFNL-TRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQL 155
Cdd:PRK13631 128 qlfkdtiekdimfgpVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGL 207
|
170 180
....*....|....*....|....*..
gi 1447648657 156 DMHTAATVSESLSRIARNDTIVVVSTH 182
Cdd:PRK13631 208 DPKGEHEMMQLILDAKANNKTVFVITH 234
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
20-182 |
5.16e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 56.96 E-value: 5.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 20 HDLTASLMPGHVYALTGPSGAGKSTLLGIIAGwtTPA----EGQVTRQGID---------SMRWI---FQNPHGVAQRTA 83
Cdd:CHL00131 24 KGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESildlepeerAHLGIflaFQYPIEIPGVSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 84 IDHVSLPLLAK----GLPRREAEEQARTLMDRFNLTRVtDRRFAE------LSGGEAQRLMLARAFAAQPSLMLVDEPTA 153
Cdd:CHL00131 102 ADFLRLAYNSKrkfqGLPELDPLEFLEIINEKLKLVGM-DPSFLSrnvnegFSGGEKKRNEILQMALLDSELAILDETDS 180
|
170 180
....*....|....*....|....*....
gi 1447648657 154 QLDMHTAATVSESLSRIARNDTIVVVSTH 182
Cdd:CHL00131 181 GLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
21-183 |
6.02e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.82 E-value: 6.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 21 DLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQ-GIdSMRWIFQNPH-------------GVAQRTAI-- 84
Cdd:PRK11819 25 DISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPApGI-KVGYLPQEPQldpektvrenveeGVAEVKAAld 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 85 --DHVSLpllAKGLPRRE----AEEQAR--TLMDRFNLTRVtDRRF----------------AELSGGEAQRLMLARAFA 140
Cdd:PRK11819 104 rfNEIYA---AYAEPDADfdalAAEQGElqEIIDAADAWDL-DSQLeiamdalrcppwdakvTKLSGGERRRVALCRLLL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1447648657 141 AQPSLMLVDEPTAQLDMHTAATVSESLSRIArnDTIVVVsTHD 183
Cdd:PRK11819 180 EKPDMLLLDEPTNHLDAESVAWLEQFLHDYP--GTVVAV-THD 219
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-183 |
6.86e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 57.65 E-value: 6.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 4 DLDHVGHRYADGPLLfHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQV---TRQGI---DSMRWIFqNPhg 77
Cdd:PRK11147 321 EMENVNYQIDGKQLV-KDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhcgTKLEVayfDQHRAEL-DP-- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 78 vaQRTAIDHvslplLAKGlpRREAEEQARtlmDRFNLTRVTDRRFA---------ELSGGEAQRLMLARAFAAQPSLMLV 148
Cdd:PRK11147 397 --EKTVMDN-----LAEG--KQEVMVNGR---PRHVLGYLQDFLFHpkramtpvkALSGGERNRLLLARLFLKPSNLLIL 464
|
170 180 190
....*....|....*....|....*....|....*
gi 1447648657 149 DEPTAQLDMHTAATVSESLSriARNDTIVVVStHD 183
Cdd:PRK11147 465 DEPTNDLDVETLELLEELLD--SYQGTVLLVS-HD 496
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-152 |
7.68e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 57.44 E-value: 7.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADGPLLfHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDsmrwifqnphgVAQRT 82
Cdd:NF033858 2 ARLEGVSHRYGKTVAL-DDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGD-----------MADAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 83 AIDHVS-----LPL-LAK-------------------GLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLAR 137
Cdd:NF033858 70 HRRAVCpriayMPQgLGKnlyptlsvfenldffgrlfGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCC 149
|
170
....*....|....*
gi 1447648657 138 AFAAQPSLMLVDEPT 152
Cdd:NF033858 150 ALIHDPDLLILDEPT 164
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
28-188 |
7.95e-10 |
|
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: 55.07 E-value: 7.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 28 PGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVtrqgidsmrwIFQNPhgvaqrtaidhvslpllakglprreaeEQART 107
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV----------IYIDG---------------------------EDILE 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 108 LMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVSES------LSRIARNDTIVVVST 181
Cdd:smart00382 44 EVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrllLLLKSEKNLTVILTT 123
|
....*..
gi 1447648657 182 HDPNTRD 188
Cdd:smart00382 124 NDEKDLG 130
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
20-163 |
9.06e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 57.02 E-value: 9.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 20 HDLTASLMPGHVYALTGPSGAGKS-TLLGIIAGWTTPA----------EGQV-------TRQGI--DSMRWIFQNPHgva 79
Cdd:PRK15134 26 NDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypsgdirfHGESllhaseqTLRGVrgNKIAMIFQEPM--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 80 qrtaidhVSL-PL------------LAKGLPRREAEEQARTLMDRFNLtRVTDRRFA----ELSGGEAQRLMLARAFAAQ 142
Cdd:PRK15134 103 -------VSLnPLhtlekqlyevlsLHRGMRREAARGEILNCLDRVGI-RQAAKRLTdyphQLSGGERQRVMIAMALLTR 174
|
170 180
....*....|....*....|.
gi 1447648657 143 PSLMLVDEPTAQLDMHTAATV 163
Cdd:PRK15134 175 PELLIADEPTTALDVSVQAQI 195
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
14-185 |
9.71e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 56.37 E-value: 9.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 14 DGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPA--------EGQVTRQG-----IDSMRWIFQN---PHG 77
Cdd:PRK13547 12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGeplaaIDAPRLARLRavlPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 78 VAQRTAIDHVSLPLLAK-------GLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFA---------A 141
Cdd:PRK13547 92 AQPAFAFSAREIVLLGRypharraGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAqlwpphdaaQ 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1447648657 142 QPSLMLVDEPTAQLDMHTAATVSESLSRIARNDTIVVVS-THDPN 185
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAiVHDPN 216
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
12-182 |
9.74e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 55.73 E-value: 9.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 12 YADGPLLfHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVT--RQGIDSMRWIFQNPHG-VAQRTAIDhvs 88
Cdd:PRK13540 11 YHDQPLL-QQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILfeRQSIKKDLCTYQKQLCfVGHRSGIN--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 89 lPLLA------KGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAAT 162
Cdd:PRK13540 87 -PYLTlrenclYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLT 165
|
170 180
....*....|....*....|
gi 1447648657 163 VSESLSRIARNDTIVVVSTH 182
Cdd:PRK13540 166 IITKIQEHRAKGGAVLLTSH 185
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
26-157 |
1.42e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.79 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 26 LMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQG--IDS------------MRWIFQNPHGV--AQRTAIDHVSL 89
Cdd:PRK10261 347 LWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqrIDTlspgklqalrrdIQFIFQDPYASldPRQTVGDSIME 426
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 90 PLLAKGL-PRREAEEQARTLMDRFNLTRVTDRRFA-ELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDM 157
Cdd:PRK10261 427 PLRVHGLlPGKAAAARVAWLLERVGLLPEHAWRYPhEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
16-197 |
1.60e-09 |
|
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: 54.29 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 16 PLLFHDLTASLMPGHVYALTGPSGAGKSTLL---GIIAGwttpaegqvtrqgidsMRWIFQNPHGVAQRTAIdhvslpll 92
Cdd:cd03227 8 PSYFVPNDVTFGEGSLTIITGPNGSGKSTILdaiGLALG----------------GAQSATRRRSGVKAGCI-------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 93 akgLPRREAEeqartlmdrFNLTRVTdrrfaeLSGGEAQRLMLARAFA----AQPSLMLVDEPTAQLDMHTAATVSESLS 168
Cdd:cd03227 64 ---VAAVSAE---------LIFTRLQ------LSGGEKELSALALILAlaslKPRPLYILDEIDRGLDPRDGQALAEAIL 125
|
170 180
....*....|....*....|....*....
gi 1447648657 169 RIARNDTIVVVSTHDPNTRDACTDIIDLK 197
Cdd:cd03227 126 EHLVKGAQVIVITHLPELAELADKLIHIK 154
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
29-183 |
1.75e-09 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 56.07 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 29 GHVYALTGPSGAGKSTLLGIIAGwTTPAEGQVTrqgIDSMRW-----------------------IFQNPhgvaqRTAID 85
Cdd:COG4170 33 GEIRGLVGESGSGKSLIAKAICG-ITKDNWHVT---ADRFRWngidllklsprerrkiigreiamIFQEP-----SSCLD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 86 HvSLPL---LAKGLPRREAEeqaRTLMDRFN---------LTRV--TDRRFA------ELSGGEAQRLMLARAFAAQPSL 145
Cdd:COG4170 104 P-SAKIgdqLIEAIPSWTFK---GKWWQRFKwrkkraielLHRVgiKDHKDImnsyphELTEGECQKVMIAMAIANQPRL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1447648657 146 MLVDEPTAQLDMHTAATVSESLSRIARND--TIVVVStHD 183
Cdd:COG4170 180 LIADEPTNAMESTTQAQIFRLLARLNQLQgtSILLIS-HD 218
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
25-161 |
2.28e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.17 E-value: 2.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 25 SLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSmrwIFQNP-HGVAQRTAIDHVSLPLLAK--------- 94
Cdd:PRK10762 26 NVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEV---TFNGPkSSQEAGIGIIHQELNLIPQltiaenifl 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1447648657 95 ---------GLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQL-DMHTAA 161
Cdd:PRK10762 103 grefvnrfgRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETES 179
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
21-193 |
2.46e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 55.21 E-value: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 21 DLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMrwIFQNPHGVAQRTAIDHVSLPLLAKGLPRRE 100
Cdd:PRK13546 42 DISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSV--IAISAGLSGQLTGIENIEFKMLCMGFKRKE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 101 AEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAatvSESLSRI----ARNDTI 176
Cdd:PRK13546 120 IKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFA---QKCLDKIyefkEQNKTI 196
|
170
....*....|....*..
gi 1447648657 177 VVVSTHDPNTRDACTDI 193
Cdd:PRK13546 197 FFVSHNLGQVRQFCTKI 213
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
18-180 |
3.09e-09 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 54.19 E-value: 3.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 18 LFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPA---EGQVTRQGIDSMrwIFQNPHgvaQRTAI----DHVSLP 90
Cdd:cd03233 22 ILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYK--EFAEKY---PGEIIyvseEDVHFP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 91 LLAKGlprreaeeqaRTLmdRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTA---ATVSESL 167
Cdd:cd03233 97 TLTVR----------ETL--DFALRCKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTAleiLKCIRTM 164
|
170
....*....|...
gi 1447648657 168 SRIARNDTIVVVS 180
Cdd:cd03233 165 ADVLKTTTFVSLY 177
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-157 |
3.38e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 55.67 E-value: 3.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRYADGPLlFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVtrqgidsmRWIFQNPHGV-AQR 81
Cdd:PRK15064 320 LEVENLTKGFDNGPL-FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV--------KWSENANIGYyAQD 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 82 TAIDhvslplLAKGLPRREAEEQARTLMDRFNLTRVTDRR--FAE---------LSGGEAQRLMLARAFAAQPSLMLVDE 150
Cdd:PRK15064 391 HAYD------FENDLTLFDWMSQWRQEGDDEQAVRGTLGRllFSQddikksvkvLSGGEKGRMLFGKLMMQKPNVLVMDE 464
|
....*..
gi 1447648657 151 PTAQLDM 157
Cdd:PRK15064 465 PTNHMDM 471
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-183 |
3.96e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 54.66 E-value: 3.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 12 YADGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWT-----TPAEGQVT---------RQGIDSMR----WIFQ 73
Cdd:PRK14258 16 YYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNeleseVRVEGRVEffnqniyerRVNLNRLRrqvsMVHP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 74 NPHgVAQRTAIDHVSLPLLAKGL-PRREAE---EQARTLMDRFNLTRVTDRRFA-ELSGGEAQRLMLARAFAAQPSLMLV 148
Cdd:PRK14258 96 KPN-LFPMSVYDNVAYGVKIVGWrPKLEIDdivESALKDADLWDEIKHKIHKSAlDLSGGQQQRLCIARALAVKPKVLLM 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 1447648657 149 DEPTAQLDMHTAATVsESL--SRIARNDTIVVVSTHD 183
Cdd:PRK14258 175 DEPCFGLDPIASMKV-ESLiqSLRLRSELTMVIVSHN 210
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
18-183 |
1.13e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.13 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 18 LFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMRWIFQNPHGVAQRTAIDHV---------- 87
Cdd:PRK15064 16 LFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFEEFTVLDTVimghtelwev 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 88 --------SLP--------------------------------LLAKGLPrreaEEQARTLMdrfnltrvtdrrfAELSG 127
Cdd:PRK15064 96 kqerdriyALPemseedgmkvadlevkfaemdgytaearagelLLGVGIP----EEQHYGLM-------------SEVAP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1447648657 128 GEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVSESLSriARNDTIVVVStHD 183
Cdd:PRK15064 159 GWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLN--ERNSTMIIIS-HD 211
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
28-184 |
1.16e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.96 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 28 PGHVYALTGPSGAGKSTLLGIIA-----GWTTPAEGQVTRQGIDSMrwiFQNPHGVAQRTAIdHV-------SLPLLA-- 93
Cdd:TIGR00956 788 PGTLTALMGASGAGKTTLLNVLAervttGVITGGDRLVNGRPLDSS---FQRSIGYVQQQDL-HLptstvreSLRFSAyl 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 94 ---KGLPRREAEEQARTLMDRFNLTRVTDRRFAE----LSGGEAQRLMLARAFAAQPSLML-VDEPTAQLDMHTAATVSE 165
Cdd:TIGR00956 864 rqpKSVSKSEKMEYVEEVIKLLEMESYADAVVGVpgegLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICK 943
|
170
....*....|....*....
gi 1447648657 166 SLSRIARNDTIVVVSTHDP 184
Cdd:TIGR00956 944 LMRKLADHGQAILCTIHQP 962
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-183 |
3.12e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 52.75 E-value: 3.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 5 LDHVGHRY---ADGPLL---------FHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSmrwif 72
Cdd:PRK15439 253 LELPGNRRqqaAGAPVLtvedltgegFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEI----- 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 73 qNPHGVAQRTAIDHVSLP--LLAKGL-----------------------PRREA---EEQARTLMDRFNLTRVTDRRfae 124
Cdd:PRK15439 328 -NALSTAQRLARGLVYLPedRQSSGLyldaplawnvcalthnrrgfwikPARENavlERYRRALNIKFNHAEQAART--- 403
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1447648657 125 LSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVSESLSRIARNDTIVVVSTHD 183
Cdd:PRK15439 404 LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSD 462
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
26-179 |
3.31e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.71 E-value: 3.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 26 LMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQgidsmrwiFQNPHGVA------------QRTAIDHVSLPLLA 93
Cdd:PRK10938 26 LNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQ--------FSHITRLSfeqlqklvsdewQRNNTDMLSPGEDD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 94 KGLPRRE-------AEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVSES 166
Cdd:PRK10938 98 TGRTTAEiiqdevkDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAEL 177
|
170
....*....|....
gi 1447648657 167 LSRIARND-TIVVV 179
Cdd:PRK10938 178 LASLHQSGiTLVLV 191
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-156 |
3.44e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.32 E-value: 3.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 2 RVDLDHVGHRYADGPLLfHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGwTTPA--EGQVT----RQGIDSMRW-IFQN 74
Cdd:PRK10938 260 RIVLNNGVVSYNDRPIL-HNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQgySNDLTlfgrRRGSGETIWdIKKH 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 75 PHGVAQRTAIDH-VSLPLL---------AKGLPRREAEEQ---ARTLMDRFNL-TRVTDRRFAELSGGEaQRLML-ARAF 139
Cdd:PRK10938 338 IGYVSSSLHLDYrVSTSVRnvilsgffdSIGIYQAVSDRQqklAQQWLDILGIdKRTADAPFHSLSWGQ-QRLALiVRAL 416
|
170
....*....|....*..
gi 1447648657 140 AAQPSLMLVDEPTAQLD 156
Cdd:PRK10938 417 VKHPTLLILDEPLQGLD 433
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1-182 |
3.56e-08 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 52.41 E-value: 3.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 1 MRVDLDHVGHRYADGPLLfHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGI-------DSMRWIF- 72
Cdd:PRK10789 314 LDVNIRQFTYPQTDHPAL-ENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIpltklqlDSWRSRLa 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 73 ---QNPHGVAQRTAIDhvslplLAKGLP---RREAEEQARTLM---DRFNL-----TRVTDRRFAeLSGGEAQRLMLARA 138
Cdd:PRK10789 393 vvsQTPFLFSDTVANN------IALGRPdatQQEIEHVARLASvhdDILRLpqgydTEVGERGVM-LSGGQKQRISIARA 465
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1447648657 139 FAAQPSLMLVDEPTAQLDMHTAATVSESLSRIARNDTiVVVSTH 182
Cdd:PRK10789 466 LLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRT-VIISAH 508
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
95-183 |
3.60e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 52.01 E-value: 3.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 95 GLPRREAEEQARTLMDRFNL-TRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVSESLSRIARN 173
Cdd:PRK13651 135 GVSKEEAKKRAAKYIELVGLdESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ 214
|
90
....*....|
gi 1447648657 174 DTIVVVSTHD 183
Cdd:PRK13651 215 GKTIILVTHD 224
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
3-179 |
3.60e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 52.33 E-value: 3.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 3 VDLDHVGHRY--ADGPLLfHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGID-------SMR---- 69
Cdd:PRK11176 342 IEFRNVTFTYpgKEVPAL-RNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDlrdytlaSLRnqva 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 70 WIFQNPH----GVAQRTAI---DHVSlpllakglpRREAEEQART--LMDRFN-----LTRVTDRRFAELSGGEAQRLML 135
Cdd:PRK11176 421 LVSQNVHlfndTIANNIAYartEQYS---------REQIEEAARMayAMDFINkmdngLDTVIGENGVLLSGGQRQRIAI 491
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1447648657 136 ARAFAAQPSLMLVDEPTAQLDMHTAATVSESLSRIARNDTIVVV 179
Cdd:PRK11176 492 ARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVI 535
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
33-196 |
3.89e-08 |
|
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: 50.78 E-value: 3.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 33 ALTGPSGAGKSTLLgiiagwttpaegqvtrqgidsmrwifqnphgvaqRTAIDHVSLPLLAKGLPRREAE-----EQART 107
Cdd:cd03238 25 VVTGVSGSGKSTLV----------------------------------NEGLYASGKARLISFLPKFSRNklifiDQLQF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 108 LMDrFNLTRVT-DRRFAELSGGEAQRLMLARAFAAQP--SLMLVDEPTAQLDMHTAATVSESLSRIARNDTIVVVSTHDP 184
Cdd:cd03238 71 LID-VGLGYLTlGQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNL 149
|
170
....*....|..
gi 1447648657 185 NTRDACTDIIDL 196
Cdd:cd03238 150 DVLSSADWIIDF 161
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
11-157 |
4.21e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 51.71 E-value: 4.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 11 RYADGplLFH--------DLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTrqgIDS--------------M 68
Cdd:PRK15112 15 RYRTG--WFRrqtveavkPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELL---IDDhplhfgdysyrsqrI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 69 RWIFQNP-HGVAQRTAIDHV-SLPL-LAKGLPRREAEEQARTLMDRFNLTRVTDRRFAE-LSGGEAQRLMLARAFAAQPS 144
Cdd:PRK15112 90 RMIFQDPsTSLNPRQRISQIlDFPLrLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHmLAPGQKQRLGLARALILRPK 169
|
170
....*....|...
gi 1447648657 145 LMLVDEPTAQLDM 157
Cdd:PRK15112 170 VIIADEALASLDM 182
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
124-183 |
4.65e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 51.73 E-value: 4.65e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1447648657 124 ELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVSESLSRIARND--TIVVVStHD 183
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNntTILLIS-HD 218
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
28-172 |
5.17e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 51.84 E-value: 5.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 28 PGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQV-----------TRQGIDS-MRWIFQNPHGVAQRTAIDHVSLPLL-AK 94
Cdd:PRK11288 29 AGQVHALMGENGAGKSTLLKILSGNYQPDAGSIlidgqemrfasTTAALAAgVAIIYQELHLVPEMTVAENLYLGQLpHK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 95 G--LPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLdmhtAATVSESLSRIAR 172
Cdd:PRK11288 109 GgiVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSL----SAREIEQLFRVIR 184
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-181 |
6.04e-08 |
|
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: 51.40 E-value: 6.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 16 PLLfHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDS----MRWIFQNP------HGVAQ----- 80
Cdd:cd03291 51 PVL-KNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISfssqFSWIMPGTikeniiFGVSYdeyry 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 81 RTAIDHVSLPLLAKGLPrreaeEQARTLMDRFNLTrvtdrrfaeLSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTA 160
Cdd:cd03291 130 KSVVKACQLEEDITKFP-----EKDNTVLGEGGIT---------LSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195
|
170 180
....*....|....*....|..
gi 1447648657 161 ATVSES-LSRIARNDTIVVVST 181
Cdd:cd03291 196 KEIFEScVCKLMANKTRILVTS 217
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-181 |
8.39e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 51.45 E-value: 8.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 16 PLLfHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDS----MRWIFQnphGVAQRTAI-----DH 86
Cdd:TIGR01271 440 PVL-KNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISfspqTSWIMP---GTIKDNIIfglsyDE 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 87 VSLPLLAKGLPRRE-----AEEQARTLMDrfnlTRVTdrrfaeLSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAA 161
Cdd:TIGR01271 516 YRYTSVIKACQLEEdialfPEKDKTVLGE----GGIT------LSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEK 585
|
170 180
....*....|....*....|.
gi 1447648657 162 TVSES-LSRIARNDTIVVVST 181
Cdd:TIGR01271 586 EIFEScLCKLMSNKTRILVTS 606
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
124-183 |
1.25e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 50.51 E-value: 1.25e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1447648657 124 ELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVSESLSRIARNDTI-VVVSTHD 183
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMaLVLITHD 213
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
21-183 |
1.90e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 50.24 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 21 DLTASLMPGHVYALTGPSGAGKS-TLLGII-----AGWTTPAEGQV----TRQGID---------------SMRWIFQNP 75
Cdd:PRK10261 34 NLSFSLQRGETLAIVGESGSGKSvTALALMrlleqAGGLVQCDKMLlrrrSRQVIElseqsaaqmrhvrgaDMAMIFQEP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 76 hgvaqRTAIDHVsLPL---------LAKGLPRREAEEQARTLMDRFNLTR---VTDRRFAELSGGEAQRLMLARAFAAQP 143
Cdd:PRK10261 114 -----MTSLNPV-FTVgeqiaesirLHQGASREEAMVEAKRMLDQVRIPEaqtILSRYPHQLSGGMRQRVMIAMALSCRP 187
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1447648657 144 SLMLVDEPTAQLDMHTAATVSESLSRIARNDTI-VVVSTHD 183
Cdd:PRK10261 188 AVLIADEPTTALDVTIQAQILQLIKVLQKEMSMgVIFITHD 228
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
21-185 |
2.32e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 49.10 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 21 DLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMRwiFQNPHGvaqrTAIDH-----VSLPLLAKG 95
Cdd:PRK13541 18 DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINN--IAKPYC----TYIGHnlglkLEMTVFENL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 96 LPRREAEEQARTL---MDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVSESLSRIAR 172
Cdd:PRK13541 92 KFWSEIYNSAETLyaaIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKAN 171
|
170
....*....|...
gi 1447648657 173 NDTIVVVSTHDPN 185
Cdd:PRK13541 172 SGGIVLLSSHLES 184
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
10-194 |
2.74e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 48.72 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 10 HRYADGPLLFHdlTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIdsmrwifqnphgvaqrtaidhvsl 89
Cdd:cd03222 8 KRYGVFFLLVE--LGVVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGI------------------------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 90 pllakglprreaeeqartlmdrfnlTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVSESLSR 169
Cdd:cd03222 62 -------------------------TPVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRR 116
|
170 180
....*....|....*....|....*.
gi 1447648657 170 -IARNDTIVVVSTHDPNTRDACTDII 194
Cdd:cd03222 117 lSEEGKKTALVVEHDLAVLDYLSDRI 142
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
2-184 |
3.16e-07 |
|
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: 49.75 E-value: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 2 RVDLDHVGHRYADGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAG-WTTPAeGQVTRQGIDSMRWIFQNPHgVAQ 80
Cdd:TIGR00954 451 GIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGElWPVYG-GRLTKPAKGKLFYVPQRPY-MTL 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 81 RTAIDHVSLPLLAKGLPRREAEEQA-RTLMDRFNLTRVTDRRFA---------ELSGGEAQRLMLARAFAAQPSLMLVDE 150
Cdd:TIGR00954 529 GTLRDQIIYPDSSEDMKRRGLSDKDlEQILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDE 608
|
170 180 190
....*....|....*....|....*....|....*
gi 1447648657 151 PTAQLdmhtAATVSESLSRIARNDTIVVVS-THDP 184
Cdd:TIGR00954 609 CTSAV----SVDVEGYMYRLCREFGITLFSvSHRK 639
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
29-150 |
4.50e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 49.12 E-value: 4.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 29 GHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMRWIFQNPHGvaQRTAIDHVSLPLLAKGLPRREAEEQARTL 108
Cdd:PRK13545 50 GEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNG--QLTGIENIELKGLMMGLTKEKIKEIIPEI 127
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1447648657 109 MDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDE 150
Cdd:PRK13545 128 IEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE 169
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
33-196 |
5.24e-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: 48.41 E-value: 5.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 33 ALTGPSGAGKSTLlgiiAGWTTPAEGQvtRQGIDSMRWIFQNPHGVAQRTAIDHVslpllaKGLPRREAEEQART----- 107
Cdd:cd03270 25 VITGVSGSGKSSL----AFDTIYAEGQ--RRYVESLSAYARQFLGQMDKPDVDSI------EGLSPAIAIDQKTTsrnpr 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 108 --------LMDRFNL--------TRVT------------DRRFAELSGGEAQRLMLARAFAAQPS--LMLVDEPTAQLDM 157
Cdd:cd03270 93 stvgtvteIYDYLRLlfarvgirERLGflvdvglgyltlSRSAPTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1447648657 158 HTAATVSESLSRI-ARNDTIVVVStHDPNTRDACTDIIDL 196
Cdd:cd03270 173 RDNDRLIETLKRLrDLGNTVLVVE-HDEDTIRAADHVIDI 211
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
21-198 |
5.26e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 49.01 E-value: 5.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 21 DLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGID------------SMRWIFQNPH--------GVAQ 80
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDisprspldavkkGMAYITESRRdngffpnfSIAQ 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 81 RTAIDHV--------SLPLLAKGLPRREAEEQARTLMDRfnlTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPT 152
Cdd:PRK09700 361 NMAISRSlkdggykgAMGLFHEVDEQRTAENQRELLALK---CHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPT 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1447648657 153 AQLDMHTAATVSESLSRIARN-DTIVVVSTHDPNTRDACTDIIDLKN 198
Cdd:PRK09700 438 RGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVCDRIAVFCE 484
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
101-198 |
6.23e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.09 E-value: 6.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 101 AEEQARTLMDRFNLT-RVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVSESLSRIARndTIVVV 179
Cdd:PLN03073 320 AEARAASILAGLSFTpEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK--TFIVV 397
|
90
....*....|....*....
gi 1447648657 180 STHDPNTRDACTDIIDLKN 198
Cdd:PLN03073 398 SHAREFLNTVVTDILHLHG 416
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
28-155 |
6.27e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.96 E-value: 6.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 28 PGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGID--------------SMrwIFQNPHGVAQRTAIDHVSL---P 90
Cdd:PRK10982 23 PHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEidfksskealengiSM--VHQELNLVLQRSVMDNMWLgryP 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1447648657 91 LLAKGLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQL 155
Cdd:PRK10982 101 TKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
22-182 |
6.94e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 48.25 E-value: 6.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 22 LTASLMPGHVYALTGPSGAGKSTLLGIIAGWT--TPAEGQVTRQGIDSMRW------------IFQNP---HGVAQR--- 81
Cdd:PRK09580 20 LNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELspedragegifmAFQYPveiPGVSNQffl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 82 -TAIDHVslpllakglprREAEEQARtlMDRFNLTRVTDRRFAEL---------------SGGEAQRLMLARAFAAQPSL 145
Cdd:PRK09580 100 qTALNAV-----------RSYRGQEP--LDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGEKKRNDILQMAVLEPEL 166
|
170 180 190
....*....|....*....|....*....|....*..
gi 1447648657 146 MLVDEPTAQLDMHTAATVSESLSRIARNDTIVVVSTH 182
Cdd:PRK09580 167 CILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
125-185 |
7.83e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.87 E-value: 7.83e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1447648657 125 LSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMH------------------TAATVSESLSRIARNDTIVVVSTHDPN 185
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNsekliektivdikdkadkTIITIAHRIASIKRSDKIVVFNNPDRT 1437
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
95-182 |
9.12e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 48.58 E-value: 9.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 95 GLPRREAEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDmhtaaTVS-----ESLSR 169
Cdd:NF033858 368 HLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD-----PVArdmfwRLLIE 442
|
90
....*....|....*
gi 1447648657 170 IARND--TIvVVSTH 182
Cdd:NF033858 443 LSREDgvTI-FISTH 456
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
17-195 |
1.07e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.24 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 17 LLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMRWIFQNPHGVAQrTAIDHV--------- 87
Cdd:PRK10636 15 VLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPQ-PALEYVidgdreyrq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 88 ---------------SLPLLAKGLPRREA---EEQARTLMDRFNLTRVT-DRRFAELSGGEAQRLMLARAFAAQPSLMLV 148
Cdd:PRK10636 94 leaqlhdanerndghAIATIHGKLDAIDAwtiRSRAASLLHGLGFSNEQlERPVSDFSGGWRMRLNLAQALICRSDLLLL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1447648657 149 DEPTAQLDMHTAATVSESLSriARNDTIVVVStHDpntRDACTDIID 195
Cdd:PRK10636 174 DEPTNHLDLDAVIWLEKWLK--SYQGTLILIS-HD---RDFLDPIVD 214
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
25-155 |
1.12e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.12 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 25 SLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMR------------WIFQNPHGVAQRTAIDHVSLpll 92
Cdd:PRK15439 33 TLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARltpakahqlgiyLVPQEPLLFPNLSVKENILF--- 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1447648657 93 akGLPRRE-AEEQARTLMDRFNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQL 155
Cdd:PRK15439 110 --GLPKRQaSMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASL 171
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
5-156 |
1.22e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 47.70 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 5 LDHVGHRYADG-PLLFHDL---TASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVT------RQGIDSMR----- 69
Cdd:PRK13645 9 LDNVSYTYAKKtPFEFKALnntSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIvgdyaiPANLKKIKevkrl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 70 -----WIFQNP-HGVAQRTAIDHVSLPLLAKGLPRREAEEQARTLMDRFNLTRVTDRRFA-ELSGGEAQRLMLARAFAAQ 142
Cdd:PRK13645 89 rkeigLVFQFPeYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPfELSGGQKRRVALAGIIAMD 168
|
170
....*....|....
gi 1447648657 143 PSLMLVDEPTAQLD 156
Cdd:PRK13645 169 GNTLVLDEPTGGLD 182
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
11-200 |
1.94e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 47.66 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 11 RYADG-PLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMRWIFQNphgVAQRTAIDHVSl 89
Cdd:PLN03232 1243 RYRPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTD---LRRVLSIIPQS- 1318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 90 PLLAKGLPR--------------REAEEQA--RTLMDR--FNLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEP 151
Cdd:PLN03232 1319 PVLFSGTVRfnidpfsehndadlWEALERAhiKDVIDRnpFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEA 1398
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1447648657 152 TAQLDMHTAATVSESLSRIARNDTIVVVStHDPNTRDACTDIIDLKNYQ 200
Cdd:PLN03232 1399 TASVDVRTDSLIQRTIREEFKSCTMLVIA-HRLNTIIDCDKILVLSSGQ 1446
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
124-196 |
2.36e-06 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 46.45 E-value: 2.36e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1447648657 124 ELSGGEAQRLMLARAFAAQ---PSLMLVDEPTAQLDMHTAATVSESLSRIARNDTIVVVSTHDPNTRDACTDIIDL 196
Cdd:cd03271 169 TLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWIIDL 244
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-166 |
4.39e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.51 E-value: 4.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 21 DLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAE-GQVTRQG----IDSMRWIFQnphgvaqRTAIDHVslpLLAKG 95
Cdd:PLN03232 635 DINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAEtSSVVIRGsvayVPQVSWIFN-------ATVRENI---LFGSD 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 96 LprrEAEEQARTL--------MDRF---NLTRVTDRRfAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVS 164
Cdd:PLN03232 705 F---ESERYWRAIdvtalqhdLDLLpgrDLTEIGERG-VNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVF 780
|
..
gi 1447648657 165 ES 166
Cdd:PLN03232 781 DS 782
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
125-194 |
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: 44.52 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 125 LSGGE------AQRLMLARAFAAQPSLMLVDEPTAQLDmhtAATVSESLSRIAR------NDTIVVVsTHDPNTRDACTD 192
Cdd:cd03240 116 CSGGEkvlaslIIRLALAETFGSNCGILALDEPTTNLD---EENIEESLAEIIEerksqkNFQLIVI-THDEELVDAADH 191
|
..
gi 1447648657 193 II 194
Cdd:cd03240 192 IY 193
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
123-198 |
1.08e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.41 E-value: 1.08e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1447648657 123 AELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVSESLSRIARNDT-IVVVSTHDPNTRDACTDIIDLKN 198
Cdd:PTZ00265 578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENrITIIIAHRLSTIRYANTIFVLSN 654
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
21-184 |
1.10e-05 |
|
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: 45.20 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 21 DLTASLMPGHVYALTGPSGAGKSTLLGIIAG-WTTPAEGQV--------TRQGIDSMRW-IFQNP-----HGVAQRTAID 85
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGaYPGKFEGNVfingkpvdIRNPAQAIRAgIAMVPedrkrHGIVPILGVG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 86 H-VSLPLL----AKGLPRREAEEQA-RTLMDRFNL-TRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMH 158
Cdd:TIGR02633 358 KnITLSVLksfcFKMRIDAAAELQIiGSAIQRLKVkTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVG 437
|
170 180
....*....|....*....|....*..
gi 1447648657 159 TAATVSESLSRIARND-TIVVVSTHDP 184
Cdd:TIGR02633 438 AKYEIYKLINQLAQEGvAIIVVSSELA 464
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
14-182 |
1.35e-05 |
|
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: 44.90 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 14 DGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTpAEGQVTrqgIDSMRW------IFQNPHGVAQRTAIdhV 87
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQ---IDGVSWnsvtlqTWRKAFGVIPQKVF--I 1303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 88 SLPLLAKGLPRRE----------AEEQA-RTLMDRF--NLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQ 154
Cdd:TIGR01271 1304 FSGTFRKNLDPYEqwsdeeiwkvAEEVGlKSVIEQFpdKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAH 1383
|
170 180
....*....|....*....|....*...
gi 1447648657 155 LDMHTAATVSESLSRIARNDTiVVVSTH 182
Cdd:TIGR01271 1384 LDPVTLQIIRKTLKQSFSNCT-VILSEH 1410
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
125-196 |
1.43e-05 |
|
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: 45.00 E-value: 1.43e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1447648657 125 LSGGEAQRLMLARAFAAQ---PSLMLVDEPTAQLDMHTAATVSESLSRIARNDTIVVVSTHDPNTRDACTDIIDL 196
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIKTADYIIDL 904
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
16-182 |
2.09e-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: 43.74 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 16 PLLFHdLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDsmrwIFQNP-HGVAQRTAIDhVSLPLLAK 94
Cdd:cd03288 35 PVLKH-VKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGID----ISKLPlHTLRSRLSII-LQDPILFS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 95 GLPRREAEEQARTLMDRF------------------NLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLD 156
Cdd:cd03288 109 GSIRFNLDPECKCTDDRLwealeiaqlknmvkslpgGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASID 188
|
170 180
....*....|....*....|....*.
gi 1447648657 157 MHTaATVSESLSRIARNDTIVVVSTH 182
Cdd:cd03288 189 MAT-ENILQKVVMTAFADRTVVTIAH 213
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
31-184 |
6.25e-05 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 42.26 E-value: 6.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 31 VYALTGPSGAGKSTLLGII--AGWttpaeGQVTRQGIDSMRWIFQNPhgvAQRTAidHVSLPLLAKGLPRR-------EA 101
Cdd:cd03279 30 LFLICGPTGAGKSTILDAItyALY-----GKTPRYGRQENLRSVFAP---GEDTA--EVSFTFQLGGKKYRversrglDY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 102 EEQARTLM------DRFnLTRVTdrrfAELSGGEAQRLMLARAFA----AQPS------LMLVDEPTAQLDMHTAATVSE 165
Cdd:cd03279 100 DQFTRIVLlpqgefDRF-LARPV----STLSGGETFLASLSLALAlsevLQNRggarleALFIDEGFGTLDPEALEAVAT 174
|
170
....*....|....*....
gi 1447648657 166 SLSRIARNDTIVVVSTHDP 184
Cdd:cd03279 175 ALELIRTENRMVGVISHVE 193
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
21-182 |
8.82e-05 |
|
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: 41.93 E-value: 8.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 21 DLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQGIDSMRWIFQNPHGVAQRTAIDHVSLPLLAK------ 94
Cdd:cd03290 19 NINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLLNatveen 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 95 ---GLP----RREAEEQARTLMDRFNLTRVTDR-----RFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTA-A 161
Cdd:cd03290 99 itfGSPfnkqRYKAVTDACSLQPDIDLLPFGDQteigeRGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSdH 178
|
170 180
....*....|....*....|...
gi 1447648657 162 TVSESLSRIARND--TIVVVsTH 182
Cdd:cd03290 179 LMQEGILKFLQDDkrTLVLV-TH 200
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-180 |
9.11e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 42.21 E-value: 9.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 1 MRVDLDHVghryaDGPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTrqgIDSMRWIFQNP----- 75
Cdd:PRK11288 256 VRLRLDGL-----KGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVY---LDGKPIDIRSPrdair 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 76 ------------------HGVAQRTAID----HVSLPLLAKglPRREAEeQARTLMDRFNL-TRVTDRRFAELSGGEAQR 132
Cdd:PRK11288 328 agimlcpedrkaegiipvHSVADNINISarrhHLRAGCLIN--NRWEAE-NADRFIRSLNIkTPSREQLIMNLSGGNQQK 404
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1447648657 133 LMLARAFAAQPSLMLVDEPTAQLDMHTAATVSESLSRIA-RNDTIVVVS 180
Cdd:PRK11288 405 AILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAaQGVAVLFVS 453
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
125-196 |
1.05e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 42.32 E-value: 1.05e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1447648657 125 LSGGEAQRLMLARAFA---AQPSLMLVDEPTAQLDMHTAATVSESLSR-IARNDTIVVVStHDPntrD--ACTD-IIDL 196
Cdd:COG0178 827 LSGGEAQRVKLASELSkrsTGKTLYILDEPTTGLHFHDIRKLLEVLHRlVDKGNTVVVIE-HNL---DviKTADwIIDL 901
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
120-196 |
1.32e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.12 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 120 RRFAELSGGEAQRLMLARAFAA---QPSLMLVDEPTAQLDMHTAATVSESLSRIARNDTIVVVSTHDPNTRDACTDIIDL 196
Cdd:PRK00635 805 RPLSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLEL 884
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-156 |
1.79e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 41.53 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 20 HDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVT-----------RQGIDS-MRWIFQNPHG---VAQRTAI 84
Cdd:PRK10762 269 NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTldghevvtrspQDGLANgIVYISEDRKRdglVLGMSVK 348
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1447648657 85 DHVSLPLLAK-----GLPRREAEEQART-LMDRFNL-TRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLD 156
Cdd:PRK10762 349 ENMSLTALRYfsragGSLKHADEQQAVSdFIRLFNIkTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
19-46 |
1.93e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 37.96 E-value: 1.93e-04
10 20
....*....|....*....|....*...
gi 1447648657 19 FHDLTASLMPGHVYALTGPSGAGKSTLL 46
Cdd:pfam13555 12 FDGHTIPIDPRGNTLLTGPSGSGKSTLL 39
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
115-169 |
2.30e-04 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 38.76 E-value: 2.30e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1447648657 115 TRVTDRRFAELSGGEAQRLM---LARAFAAQ----------PSLMLVDEPTAQLDMHTAATVSESLSR 169
Cdd:pfam13558 23 EVETYRRSGGLSGGEKQLLAylpLAAALAAQygsaegrppaPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
28-180 |
2.86e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 41.26 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 28 PGHVYALTGPSGAGKSTLLGIIAGWTTP-AEGQVTRQG----IDSMRWIFQ----------NPHGVAQR------TAIDH 86
Cdd:PLN03130 642 VGSLVAIVGSTGEGKTSLISAMLGELPPrSDASVVIRGtvayVPQVSWIFNatvrdnilfgSPFDPERYeraidvTALQH 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 87 vSLPLLAKGlprreaeeqartlmdrfNLTRVTDRRfAELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVSES 166
Cdd:PLN03130 722 -DLDLLPGG-----------------DLTEIGERG-VNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDK 782
|
170
....*....|....*
gi 1447648657 167 -LSRIARNDTIVVVS 180
Cdd:PLN03130 783 cIKDELRGKTRVLVT 797
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
24-46 |
6.04e-04 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 39.30 E-value: 6.04e-04
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
11-182 |
6.71e-04 |
|
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: 39.45 E-value: 6.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 11 RYAD-GPLLFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTpAEGQVTrqgIDSMRW------IFQNPHGV-AQRT 82
Cdd:cd03289 11 KYTEgGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQ---IDGVSWnsvplqKWRKAFGViPQKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 83 AIdhVSLPLLAKGLPR---------REAEEQA-RTLMDRF--NLTRVTDRRFAELSGGEAQRLMLARAFAAQPSLMLVDE 150
Cdd:cd03289 87 FI--FSGTFRKNLDPYgkwsdeeiwKVAEEVGlKSVIEQFpgQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDE 164
|
170 180 190
....*....|....*....|....*....|..
gi 1447648657 151 PTAQLDMHTAATVSESLsRIARNDTIVVVSTH 182
Cdd:cd03289 165 PSAHLDPITYQVIRKTL-KQAFADCTVILSEH 195
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-182 |
1.34e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 38.99 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 18 LFHDLTASLMPGHVYALTGPSGAGKSTLLGIIAGWTTPAEGQVTRQG----IDSMRWI----------FQNPHGVAQRTA 83
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERsiayVPQQAWImnatvrgnilFFDEEDAARLAD 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 84 IDHVS-----LPLLAKGLPRREAEEQArtlmdrfnltrvtdrrfaELSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMH 158
Cdd:PTZ00243 755 AVRVSqleadLAQLGGGLETEIGEKGV------------------NLSGGQKARVSLARAVYANRDVYLLDDPLSALDAH 816
|
170 180
....*....|....*....|....
gi 1447648657 159 TAATVSESLSRIARNDTIVVVSTH 182
Cdd:PTZ00243 817 VGERVVEECFLGALAGKTRVLATH 840
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
125-184 |
1.99e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 38.17 E-value: 1.99e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1447648657 125 LSGGEAQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVSESLSRIARNDT-IVVVSTHDP 184
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKgIIIISSEMP 452
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
119-196 |
2.90e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.07 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 119 DRRFAELSGGEAQRLMLARAFAAQPS--LMLVDEPTAQLDMHTAATVSESLSRIaRN--DTIVVVStHDPNTRDACTDII 194
Cdd:TIGR00630 483 SRAAGTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHQRDNRRLINTLKRL-RDlgNTLIVVE-HDEDTIRAADYVI 560
|
..
gi 1447648657 195 DL 196
Cdd:TIGR00630 561 DI 562
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
111-185 |
3.60e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 37.29 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447648657 111 RFNLTRVTDRRFAELSGGEAQRLMLA--RAFA-----AQPSLMLVDEPTAQLDMHTAATVSESLSRIARNDTIVVVSTHD 183
Cdd:COG3593 149 SLRIEDGKELPLDRLGSGFQRLILLAllSALAelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHS 228
|
..
gi 1447648657 184 PN 185
Cdd:COG3593 229 PH 230
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
125-194 |
4.78e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 37.35 E-value: 4.78e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1447648657 125 LSGGE------AQRLMLARAFAAQPSLMLVDEPTAQLDMHTAATVSESLSRIARNDTIVVVSTHDPNTRDACTDII 194
Cdd:PRK03918 789 LSGGErialglAFRLALSLYLAGNIPLLILDEPTPFLDEERRRKLVDIMERYLRKIPQVIIVSHDEELKDAADYVI 864
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
122-184 |
5.93e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 36.60 E-value: 5.93e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1447648657 122 FAELSGGEaQRL--MLARAFAAQP--SLMLVDEPTAQLDMHTAATVSESLSRIARNDTIVVVSTHDP 184
Cdd:pfam13304 234 AFELSDGT-KRLlaLLAALLSALPkgGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSP 299
|
|
|