|
Name |
Accession |
Description |
Interval |
E-value |
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
17-246 |
3.76e-72 |
|
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: 220.69 E-value: 3.76e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 17 GTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA-------------ALVPQDFARAFPYR 83
Cdd:COG1120 12 GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDlaslsrrelarriAYVPQEPPAPFGLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 84 VIDMVLMGRARHIGLLRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLG 163
Cdd:COG1120 92 VRELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 164 NQDRVLRLVRVLA-DRGLAVVMTTHQPNHALAVADTaLLMLPEGAV--FGPCHEALTETRIEMLYGLPVRILDVKAADRG 240
Cdd:COG1120 172 HQLEVLELLRRLArERGRTVVMVLHDLNLAARYADR-LVLLKDGRIvaQGPPEEVLTPELLEEVYGVEARVIEDPVTGRP 250
|
....*.
gi 500071482 241 FrsVVP 246
Cdd:COG1120 251 L--VLP 254
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-233 |
2.75e-64 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 200.32 E-value: 2.75e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 1 MAEPLIRAEGAAHSWDGtRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA--------ALV 72
Cdd:COG1121 2 MMMPAIELENLTVSYGG-RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPprrarrriGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 73 PQ--DFARAFPYRVIDMVLMGRARHIGLLRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAA 150
Cdd:COG1121 81 PQraEVDWDFPITVRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 151 LFLDEPASALDLGNQDRVLRLVRVLADRGLAVVMTTHQPNHALAVADTALLMLPEGAVFGPCHEALTETRIEMLYGLPVR 230
Cdd:COG1121 161 LLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAHGPPEEVLTPENLSRAYGGPVA 240
|
...
gi 500071482 231 ILD 233
Cdd:COG1121 241 LLA 243
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
23-202 |
8.63e-52 |
|
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: 167.33 E-value: 8.63e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGT--------AALVPQ--DFARAFPYRVIDMVLMGR 92
Cdd:cd03235 16 EDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKplekerkrIGYVPQrrSIDRDFPISVRDVVLMGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 93 ARHIGLLRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLV 172
Cdd:cd03235 96 YGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELL 175
|
170 180 190
....*....|....*....|....*....|
gi 500071482 173 RVLADRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:cd03235 176 RELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
17-202 |
1.24e-46 |
|
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: 153.36 E-value: 1.24e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 17 GTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGT--AALVPQDfarafpyrvidmvlmgRAR 94
Cdd:cd03214 10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKdlASLSPKE----------------LAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 95 HIGLLRmpgrrdreaamEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLVRV 174
Cdd:cd03214 74 KIAYVP-----------QALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRR 142
|
170 180
....*....|....*....|....*....
gi 500071482 175 LAD-RGLAVVMTTHQPNHALAVADTALLM 202
Cdd:cd03214 143 LAReRGKTVVMVLHDLNLAARYADRVILL 171
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
22-201 |
5.14e-44 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 147.00 E-value: 5.14e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 22 FRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA--ALVPQ--DFARAFPYRVIDMVLMGRARHIG 97
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGArvAYVPQrsEVPDSLPLTVRDLVAMGRWARRG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 98 LLRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLVRVLAD 177
Cdd:NF040873 88 LWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHA 167
|
170 180
....*....|....*....|....
gi 500071482 178 RGLAVVMTTHQPNHALAVADTALL 201
Cdd:NF040873 168 RGATVVVVTHDLELVRRADPCVLL 191
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-226 |
2.10e-43 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 147.13 E-value: 2.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 4 PLIRAEGAAHSWDGTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA-------------- 69
Cdd:COG3638 1 PMLELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDvtalrgralrrlrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 70 --ALVPQDFA---RAfpyRVIDMVLMGRARHIG----LLRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLI 140
Cdd:COG3638 81 riGMIFQQFNlvpRL---SVLTNVLAGRLGRTStwrsLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 141 ARAIAAEPAALFLDEPASALDLGNQDRVLRLVRVLA-DRGLAVVMTTHQPNHALAVADTaLLMLPEGAVF--GPChEALT 217
Cdd:COG3638 158 ARALVQEPKLILADEPVASLDPKTARQVMDLLRRIArEDGITVVVNLHQVDLARRYADR-IIGLRDGRVVfdGPP-AELT 235
|
....*....
gi 500071482 218 ETRIEMLYG 226
Cdd:COG3638 236 DAVLREIYG 244
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-231 |
3.70e-41 |
|
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: 141.38 E-value: 3.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 3 EPLIRAEGAAHSWDGtRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPT-----------RGRITVA----- 66
Cdd:COG1119 1 DPLLELRNVTVRRGG-KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTygndvrlfgerRGGEDVWelrkr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 67 -GtaaLVPQDFARAFPYR--VIDMVLMGRARHIGLLRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARA 143
Cdd:COG1119 80 iG---LVSPALQLRFPRDetVLDVVLSGFFDSIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 144 IAAEPAALFLDEPASALDLGNQDRVLRLVRVLADRG-LAVVMTTHQPnHALAVADTALLMLPEGAVF--GPCHEALTETR 220
Cdd:COG1119 157 LVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHV-EEIPPGITHVLLLKDGRVVaaGPKEEVLTSEN 235
|
250
....*....|.
gi 500071482 221 IEMLYGLPVRI 231
Cdd:COG1119 236 LSEAFGLPVEV 246
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
24-246 |
1.35e-39 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 137.60 E-value: 1.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 24 DLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA-------------ALVPQDFARAFPYRVIDMVLM 90
Cdd:PRK13548 20 DVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPladwspaelarrrAVLPQHSSLSFPFTVEEVVAM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 91 GRARHigllRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQ-----MVLI-ARAIAAEPAALFLDEPASALDLGN 164
Cdd:PRK13548 100 GRAPH----GLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQrvqlaRVLAqLWEPDGPPRWLLLDEPTSALDLAH 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 165 QDRVLRLVRVLA-DRGLAVVMTTHQPNHALAVADTaLLMLPEGAV--FGPCHEALTETRIEMLYGLPVRIldVKAADRGF 241
Cdd:PRK13548 176 QHHVLRLARQLAhERGLAVIVVLHDLNLAARYADR-IVLLHQGRLvaDGTPAEVLTPETLRRVYGADVLV--QPHPETGA 252
|
....*
gi 500071482 242 RSVVP 246
Cdd:PRK13548 253 PLVLP 257
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
23-202 |
2.21e-36 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 128.64 E-value: 2.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA------------ALVPQDFArAFPY-RVIDMVL 89
Cdd:COG1131 17 DGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDvardpaevrrriGYVPQEPA-LYPDlTVRENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 90 MgrarHIGLLRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVL 169
Cdd:COG1131 96 F----FARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELW 171
|
170 180 190
....*....|....*....|....*....|...
gi 500071482 170 RLVRVLADRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:COG1131 172 ELLRELAAEGKTVLLSTHYLEEAERLCDRVAII 204
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-202 |
2.79e-36 |
|
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: 128.22 E-value: 2.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 6 IRAEGAAHSWDGTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGtaalvpQDFARAFPYRVi 85
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDG------KDITKKNLREL- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 86 dmvlmgrARHIGL------------------------LRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIA 141
Cdd:COG1122 74 -------RRKVGLvfqnpddqlfaptveedvafgpenLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500071482 142 RAIAAEPAALFLDEPASALDLGNQDRVLRLVRVLADRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVL 207
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-225 |
3.98e-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: 128.07 E-value: 3.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 6 IRAEGAAHSWDGTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA---------------- 69
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDinklkgkalrqlrrqi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 70 ALVPQDFARAFPYRVIDMVLMGRARHI----GLLRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIA 145
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRLGRRstwrSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 146 AEPAALFLDEPASALDLGNQDRVLRLVRVLA-DRGLAVVMTTHQPNHALAVADTaLLMLPEGAVF--GPChEALTETRIE 222
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINrEEGITVIVSLHQVDLAREYADR-IVGLKDGRIVfdGPP-AELTDEVLD 238
|
...
gi 500071482 223 MLY 225
Cdd:cd03256 239 EIY 241
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
16-202 |
3.86e-35 |
|
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: 124.50 E-value: 3.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 16 DGTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTaalvpqdfarafpyRVIDMVLMGRARH 95
Cdd:cd03225 11 DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGK--------------DLTKLSLKELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 96 IGL------------------------LRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAAL 151
Cdd:cd03225 77 VGLvfqnpddqffgptveeevafglenLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 500071482 152 FLDEPASALDLGNQDRVLRLVRVLADRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVL 207
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-202 |
5.62e-34 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 122.89 E-value: 5.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 1 MAEPLIRAEGAAHSW---DGTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA-------- 69
Cdd:COG1116 3 AAAPALELRGVSKRFptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPvtgpgpdr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 70 ALVPQDFaRAFPYR-VIDMVLMG-RARHigllrMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAE 147
Cdd:COG1116 83 GVVFQEP-ALLPWLtVLDNVALGlELRG-----VPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAND 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500071482 148 PAALFLDEPASALD------LgnQDRVLRLVRvlaDRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:COG1116 157 PEVLLMDEPFGALDaltrerL--QDELLRLWQ---ETGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
27-202 |
8.77e-34 |
|
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: 121.50 E-value: 8.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 27 FAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAAL--------VPQ--DFARAFPYRVIDMVLMGRARHI 96
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGkgwrhigyVPQrhEFAWDFPISVAHTVMSGRTGHI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 97 GLLRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLVRVLA 176
Cdd:TIGR03771 81 GWLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFIELA 160
|
170 180
....*....|....*....|....*.
gi 500071482 177 DRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:TIGR03771 161 GAGTAILMTTHDLAQAMATCDRVVLL 186
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-202 |
1.08e-33 |
|
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: 121.04 E-value: 1.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 6 IRAEGAAHSWDGTRWQF---RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA--------ALVPQ 74
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVtalEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPvtgpgpdrGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 75 DFArAFPYR-VIDMVLMG-RARhigllRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALF 152
Cdd:cd03293 81 QDA-LLPWLtVLDNVALGlELQ-----GVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 500071482 153 LDEPASALD----LGNQDRVLRLVRvlaDRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:cd03293 155 LDEPFSALDaltrEQLQEELLDIWR---ETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-189 |
1.93e-33 |
|
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: 119.89 E-value: 1.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 4 PLIRAEGAAHSWDGtRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA-ALVPQDFAR---- 78
Cdd:COG4133 1 MMLEAENLSCRRGE-RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPiRDAREDYRRrlay 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 79 AFPYRVIDMVLMGRArHIGLLRM--PGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEP 156
Cdd:COG4133 80 LGHADGLKPELTVRE-NLRFWAAlyGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190
....*....|....*....|....*....|...
gi 500071482 157 ASALDLGNQDRVLRLVRVLADRGLAVVMTTHQP 189
Cdd:COG4133 159 FTALDAAGVALLAELIAAHLARGGAVLLTTHQP 191
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-202 |
4.37e-32 |
|
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: 116.85 E-value: 4.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 6 IRAEGAAHSWDGTRWqFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA-----------ALVPQ 74
Cdd:cd03259 1 LELKGLSKTYGSVRA-LDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDvtgvpperrniGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 75 DFArAFPY-RVIDMVLMGrarhIGLLRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFL 153
Cdd:cd03259 80 DYA-LFPHlTVAENIAFG----LKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 500071482 154 DEPASALDLGNQDRVLR-LVRVLADRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:cd03259 155 DEPLSALDAKLREELREeLKELQRELGITTIYVTHDQEEALALADRIAVM 204
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
5-226 |
1.32e-31 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 116.24 E-value: 1.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 5 LIRAEGAAHSWDGTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA--------------- 69
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDitklrgkklrklrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 70 -ALVPQDFARAFPYRVIDMVLMGR-ARHI---GLLRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAI 144
Cdd:TIGR02315 81 iGMIFQHYNLIERLTVLENVLHGRlGYKPtwrSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 145 AAEPAALFLDEPASALDLGNQDRVLRLVRVLA-DRGLAVVMTTHQPNHALAVADTaLLMLPEGAVF--GPCHEaLTETRI 221
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINkEDGITVIINLHQVDLAKKYADR-IVGLKAGEIVfdGAPSE-LDDEVL 238
|
....*
gi 500071482 222 EMLYG 226
Cdd:TIGR02315 239 RHIYG 243
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-190 |
8.68e-31 |
|
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: 113.35 E-value: 8.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 6 IRAEGAAHSWDGTRWQF---RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAALVPQDFARAfPY 82
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqalKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELA-AF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 83 RvidmvlmgrARHIG-----------------------LLRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVL 139
Cdd:cd03255 80 R---------RRHIGfvfqsfnllpdltalenvelpllLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 500071482 140 IARAIAAEPAALFLDEPASALDLGNQDRVLRLVRVLA-DRGLAVVMTTHQPN 190
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELNkEAGTTIVVVTHDPE 202
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
23-202 |
1.56e-30 |
|
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: 113.74 E-value: 1.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAalVPQDFARAFpYRVIDMV----------LMGR 92
Cdd:COG1124 22 KDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRP--VTRRRRKAF-RRRVQMVfqdpyaslhpRHTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 93 ARHIGL-LRMPGRRDREAAM-EALAVIGLAGKAAERF-DALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVL 169
Cdd:COG1124 99 DRILAEpLRIHGLPDREERIaELLEQVGLPPSFLDRYpHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEIL 178
|
170 180 190
....*....|....*....|....*....|....
gi 500071482 170 RLVRVL-ADRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:COG1124 179 NLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVM 212
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
24-226 |
3.22e-30 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 116.09 E-value: 3.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 24 DLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA-------------ALVPQDFARAFPYRVIDMVLM 90
Cdd:PRK09536 21 GVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDvealsaraasrrvASVPQDTSLSFEFDVRQVVEM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 91 GRARHIGLLRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLR 170
Cdd:PRK09536 101 GRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLE 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 500071482 171 LVRVLADRGLAVVMTTHQPNHALAVADTaLLMLPEGAVF--GPCHEALTETRIEMLYG 226
Cdd:PRK09536 181 LVRRLVDDGKTAVAAIHDLDLAARYCDE-LVLLADGRVRaaGPPADVLTADTLRAAFD 237
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-202 |
4.44e-30 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 111.67 E-value: 4.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 3 EPLIRAEGAAHSW---DGTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGT--AALVPQDFA 77
Cdd:COG1136 2 SPLLELRNLTKSYgtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQdiSSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 78 RAfpyrvidmvlmgRARHIG-----------------------LLRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQ 134
Cdd:COG1136 82 RL------------RRRHIGfvfqffnllpeltalenvalpllLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500071482 135 RQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLVRVLADR-GLAVVMTTHQPNHAlAVADTALLM 202
Cdd:COG1136 150 QQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELA-ARADRVIRL 217
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
7-202 |
1.22e-29 |
|
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: 110.04 E-value: 1.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 7 RAEGAAHSWDGTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAG----------TAALVPQDf 76
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGkpikakerrkSIGYVMQD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 77 arafPYRVIDMVLMGRARHIGLlrMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEP 156
Cdd:cd03226 80 ----VDYQLFTDSVREELLLGL--KELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 500071482 157 ASALDLGNQDRVLRLVRVLADRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:cd03226 154 TSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLL 199
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
22-202 |
2.79e-29 |
|
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: 107.72 E-value: 2.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 22 FRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGtaalvpQDFARAFPYRVidmvlmgrARHIGLLrm 101
Cdd:cd00267 15 LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDG------KDIAKLPLEEL--------RRRIGYV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 102 pgrrdreaamealaviglagkaaerfDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLVRVLADRGLA 181
Cdd:cd00267 79 --------------------------PQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRT 132
|
170 180
....*....|....*....|.
gi 500071482 182 VVMTTHQPNHALAVADTALLM 202
Cdd:cd00267 133 VIIVTHDPELAELAADRVIVL 153
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
24-197 |
3.32e-29 |
|
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: 109.12 E-value: 3.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 24 DLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGtaalvpQDFARAFPY-RVIDMVL--------MGRAR 94
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING------VDVTAAPPAdRPVSMLFqennlfahLTVEQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 95 HIGLLRMPGRR----DREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLR 170
Cdd:cd03298 90 NVGLGLSPGLKltaeDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLD 169
|
170 180
....*....|....*....|....*...
gi 500071482 171 LV-RVLADRGLAVVMTTHQPNHALAVAD 197
Cdd:cd03298 170 LVlDLHAETKMTVLMVTHQPEDAKRLAQ 197
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
23-231 |
3.83e-29 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 110.10 E-value: 3.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA-------------ALVPQDFARAFPYRVIDMVL 89
Cdd:PRK11231 19 NDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPismlssrqlarrlALLPQHHLTPEGITVRELVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 90 MGRARHIGLLRMPGRRDR---EAAMEALAVIGLAGKaaeRFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQD 166
Cdd:PRK11231 99 YGRSPWLSLWGRLSAEDNarvNQAMEQTRINHLADR---RLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQV 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500071482 167 RVLRLVRVLADRGLAVVMTTHQPNHALAVADtALLMLPEGAVF--GPCHEALTETRIEMLYGLPVRI 231
Cdd:PRK11231 176 ELMRLMRELNTQGKTVVTVLHDLNQASRYCD-HLVVLANGHVMaqGTPEEVMTPGLLRTVFDVEAEI 241
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
6-224 |
7.57e-29 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 108.69 E-value: 7.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 6 IRAEGAAHSWDGTRWQFrdlDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGtaalvpQDFARAFPY-RV 84
Cdd:COG3840 2 LRLDDLTYRYGDFPLRF---DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNG------QDLTALPPAeRP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 85 IDMVL--------MGRARHIGLLRMPGRR----DREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALF 152
Cdd:COG3840 73 VSMLFqennlfphLTVAQNIGLGLRPGLKltaeQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500071482 153 LDEPASALDLGNQDRVLRLVRVLAD-RGLAVVMTTHQPNHALAVADTALLmLPEGAVF--GPCHEALTETRIEML 224
Cdd:COG3840 153 LDEPFSALDPALRQEMLDLVDELCReRGLTVLMVTHDPEDAARIADRVLL-VADGRIAadGPTAALLDGEPPPAL 226
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
13-202 |
1.59e-28 |
|
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: 107.62 E-value: 1.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 13 HSWDGTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGT---------------AALVPQDFA 77
Cdd:cd03262 7 HKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLkltddkkninelrqkVGMVFQQFN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 78 rAFPYR-VIDMVLMGRarhIGLLRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEP 156
Cdd:cd03262 87 -LFPHLtVLENITLAP---IKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 500071482 157 ASALDLGNQDRVLRLVRVLADRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:cd03262 163 TSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFM 208
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-202 |
3.30e-28 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 106.44 E-value: 3.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 6 IRAEGAAHSWDGtRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA-------------ALV 72
Cdd:COG4619 1 LELEGLSFRVGG-KPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPlsampppewrrqvAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 73 PQDfARAFPYRVID-MVLMGRARHIgllrmpgRRDREAAMEALAVIGLAGKAAER-FDALSGGQRQMVLIARAIAAEPAA 150
Cdd:COG4619 80 PQE-PALWGGTVRDnLPFPFQLRER-------KFDRERALELLERLGLPPDILDKpVERLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 500071482 151 LFLDEPASALDLGNQDRVLRLVR-VLADRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLReYLAEEGRAVLWVSHDPEQIERVADRVLTL 204
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-202 |
4.26e-28 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 109.42 E-value: 4.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 1 MAEPLIRAEGAAHSWDGTRwQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA----------- 69
Cdd:COG3842 1 MAMPALELENVSKRYGDVT-ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDvtglppekrnv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 70 ALVPQDFArAFPYR-VIDMVLMG-RARhigllRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMV--------- 138
Cdd:COG3842 80 GMVFQDYA-LFPHLtVAENVAFGlRMR-----GVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRValaralape 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500071482 139 --LiaraiaaepaaLFLDEPASALDLGNQDRVLR-LVRVLADRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:COG3842 154 prV-----------LLLDEPLSALDAKLREEMREeLRRLQRELGITFIYVTHDQEEALALADRIAVM 209
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
17-202 |
4.60e-28 |
|
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: 106.87 E-value: 4.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 17 GTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAA------------LVPQdfARAFPYR- 83
Cdd:COG4555 12 GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVrkeprearrqigVLPD--ERGLYDRl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 84 -VIDMVLMgrarHIGLLRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDL 162
Cdd:COG4555 90 tVRENIRY----FAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDV 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 500071482 163 GNQDRVLRLVRVLADRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:COG4555 166 MARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVIL 205
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-202 |
7.64e-28 |
|
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: 104.05 E-value: 7.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 6 IRAEGAAHSWDGTRwQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTaalvPQDFARAFpyrvi 85
Cdd:cd03216 1 LELRGITKRFGGVK-ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK----EVSFASPR----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 86 dmvlmgRARHIGllrmpgrrdreaamealavIGLAGKaaerfdaLSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQ 165
Cdd:cd03216 71 ------DARRAG-------------------IAMVYQ-------LSVGERQMVEIARALARNARLLILDEPTAALTPAEV 118
|
170 180 190
....*....|....*....|....*....|....*..
gi 500071482 166 DRVLRLVRVLADRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:cd03216 119 ERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVL 155
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
16-202 |
8.24e-28 |
|
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: 110.76 E-value: 8.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 16 DGTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPT---RGRITVAGT-------------AALVPQDFARA 79
Cdd:COG1123 16 GGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRdllelsealrgrrIGMVFQDPMTQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 80 F-PYRVIDMVlmgrARHIGLLRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPAS 158
Cdd:COG1123 96 LnPVTVGDQI----AEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 500071482 159 ALDLGNQDRVLRLVRVL-ADRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:COG1123 172 ALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVM 216
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
23-234 |
1.50e-27 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 105.94 E-value: 1.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGT--AALVPQDFAR---------AFPYR--VIDMVL 89
Cdd:COG4604 18 DDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLdvATTPSRELAKrlailrqenHINSRltVRELVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 90 MGRARHIGllrmpGR---RDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQD 166
Cdd:COG4604 98 FGRFPYSK-----GRltaEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSV 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500071482 167 RVLRLVRVLAD-RGLAVVMTTHQPNHALAVADTALLMlPEGAV--FGPCHEALTETRIEMLYGLPVRILDV 234
Cdd:COG4604 173 QMMKLLRRLADeLGKTVVIVLHDINFASCYADHIVAM-KDGRVvaQGTPEEIITPEVLSDIYDTDIEVEEI 242
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-202 |
1.85e-27 |
|
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: 109.61 E-value: 1.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 1 MAEPLIRAEGAAHSWDGTRWQ----FRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGT-------- 68
Cdd:COG1123 256 AAEPLLEVRNLSKRYPVRGKGgvraVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKdltklsrr 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 69 --------AALVPQDfarafPY-------RVIDMVLMGRARHiglLRMPGRRDREAAMEALAVIGLAGKAAERF-DALSG 132
Cdd:COG1123 336 slrelrrrVQMVFQD-----PYsslnprmTVGDIIAEPLRLH---GLLSRAERRERVAELLERVGLPPDLADRYpHELSG 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500071482 133 GQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLVRVLADR-GLAVVMTTHQPNHALAVADTALLM 202
Cdd:COG1123 408 GQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVM 478
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
17-202 |
1.93e-27 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 105.92 E-value: 1.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 17 GTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRItVAGTAALVP---------QDfARAFPY-RVID 86
Cdd:PRK11247 23 GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLAEaredtrlmfQD-ARLLPWkKVID 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 87 MVLMGRARHIgllrmpgrrdREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALD----L 162
Cdd:PRK11247 101 NVGLGLKGQW----------RDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDaltrI 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 500071482 163 GNQDRVLRLVRvlaDRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:PRK11247 171 EMQDLIESLWQ---QHGFTVLLVTHDVSEAVAMADRVLLI 207
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
17-202 |
3.89e-27 |
|
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: 102.48 E-value: 3.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 17 GTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGtaalvpQDFARAfPYRVIdmvlmgraRHI 96
Cdd:cd03230 11 GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLG------KDIKKE-PEEVK--------RRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 97 GLlrMPgrrDREAAMEALaviglagKAAERFDaLSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLVRVLA 176
Cdd:cd03230 76 GY--LP---EEPSLYENL-------TVRENLK-LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELK 142
|
170 180
....*....|....*....|....*.
gi 500071482 177 DRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:cd03230 143 KEGKTILLSSHILEEAERLCDRVAIL 168
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-225 |
5.48e-27 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 104.96 E-value: 5.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 1 MAEPLIRAEGAAHSWDGTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA----------A 70
Cdd:PRK15056 2 MQQAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPtrqalqknlvA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 71 LVPQ--DFARAFPYRVIDMVLMGRARHIGLLRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEP 148
Cdd:PRK15056 82 YVPQseEVDWSFPVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQG 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500071482 149 AALFLDEPASALDLGNQDRVLRLVRVLADRGLAVVMTTHQPNHALAVADTALLMlpEGAVF--GPCHEALTETRIEMLY 225
Cdd:PRK15056 162 QVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMV--KGTVLasGPTETTFTAENLELAF 238
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-202 |
7.50e-27 |
|
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: 103.35 E-value: 7.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 5 LIRAEGAAHSWDGTRWQFR---DLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA------------ 69
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKaldDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDllklsrrlrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 70 ----ALVPQDFARAFP--YRVIDMVLMGRARHIGLLRMpgRRDREAAMEALAVIGLAGKAAERF-DALSGGQRQMVLIAR 142
Cdd:cd03257 81 rkeiQMVFQDPMSSLNprMTIGEQIAEPLRIHGKLSKK--EARKEAVLLLLVGVGLPEEVLNRYpHELSGGQRQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500071482 143 AIAAEPAALFLDEPASALDLGNQDRVLRLVRVLAD-RGLAVVMTTHQPNHALAVADTALLM 202
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEeLGLTLLFITHDLGVVAKIADRVAVM 219
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
23-234 |
1.22e-26 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 104.14 E-value: 1.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATG-LRAP-------TRGRITVAGTA-------------ALVPQDFARAFP 81
Cdd:PRK13547 18 RDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGgaprgarVTGDVTLNGEPlaaidaprlarlrAVLPQAAQPAFA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 82 YRVIDMVLMGRARHIGLLRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARA---------IAAEPAALF 152
Cdd:PRK13547 98 FSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVlaqlwpphdAAQPPRYLL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 153 LDEPASALDLGNQDRVLRLVRVLA-DRGLAVVMTTHQPNHALAVADTaLLMLPEGAVF--GPCHEALTETRIEMLYGLPV 229
Cdd:PRK13547 178 LDEPTAALDLAHQHRLLDTVRRLArDWNLGVLAIVHDPNLAARHADR-IAMLADGAIVahGAPADVLTPAHIARCYGFAV 256
|
....*
gi 500071482 230 RILDV 234
Cdd:PRK13547 257 RLVDA 261
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
17-232 |
2.68e-26 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 102.94 E-value: 2.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 17 GTRWQFRDLDFAVA-------------AGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA-------------A 70
Cdd:PRK10575 9 DTTFALRNVSFRVPgrtllhplsltfpAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPleswsskafarkvA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 71 LVPQDFARAFPYRVIDMVLMGRARHIGLLRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAA 150
Cdd:PRK10575 89 YLPQQLPAAEGMTVRELVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRC 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 151 LFLDEPASALDLGNQDRVLRLVRVLA-DRGLAVVMTTHQPNHALAVADTaLLMLPEGAVF--GPCHEALTETRIEMLYGL 227
Cdd:PRK10575 169 LLLDEPTSALDIAHQVDVLALVHRLSqERGLTVIAVLHDINMAARYCDY-LVALRGGEMIaqGTPAELMRGETLEQIYGI 247
|
....*
gi 500071482 228 PVRIL 232
Cdd:PRK10575 248 PMGIL 252
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-198 |
1.33e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 104.33 E-value: 1.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 2 AEPLIRAEGAAHSWDGTRwQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA------------ 69
Cdd:COG1129 1 AEPLLEMRGISKSFGGVK-ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPvrfrsprdaqaa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 70 --ALVPQDFArAFPYR-VIDMVLMGR-ARHIGLLRMpgRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIA 145
Cdd:COG1129 80 giAIIHQELN-LVPNLsVAENIFLGRePRRGGLIDW--RAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALS 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 500071482 146 AEPAALFLDEPASALDLGNQDRVLRLVRVLADRGLAVVMTTHQPNHALAVADT 198
Cdd:COG1129 157 RDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADR 209
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
23-202 |
1.36e-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: 99.66 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTaalvPQDFA--RAFPY-----------RVIDMVL 89
Cdd:cd03269 17 DDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGK----PLDIAarNRIGYlpeerglypkmKVIDQLV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 90 mgrarHIGLLR-MPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRV 168
Cdd:cd03269 93 -----YLAQLKgLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELL 167
|
170 180 190
....*....|....*....|....*....|....
gi 500071482 169 LRLVRVLADRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:cd03269 168 KDVIRELARAGKTVILSTHQMELVEELCDRVLLL 201
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
23-249 |
2.07e-25 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 100.83 E-value: 2.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRI-------------TVAGTAALVPQDFARAFPYRVIDMVL 89
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwldgehiqhyaskEVARRIGLLAQNATTPGDITVQELVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 90 MGRARHIGLLRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVL 169
Cdd:PRK10253 104 RGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 170 RLVRVL-ADRGLAVVMTTHQPNHALAVAdTALLMLPEGAVF--GPCHEALTETRIEMLYGLPVRILDVKAAdrGFRSVVP 246
Cdd:PRK10253 184 ELLSELnREKGYTLAAVLHDLNQACRYA-SHLIALREGKIVaqGAPKEIVTAELIERIYGLRCMIIDDPVA--GTPLVVP 260
|
...
gi 500071482 247 LYR 249
Cdd:PRK10253 261 LGR 263
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
23-202 |
3.56e-25 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 99.30 E-value: 3.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA---------------ALVPQDFArAFPYR-VID 86
Cdd:COG1126 18 KGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDltdskkdinklrrkvGMVFQQFN-LFPHLtVLE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 87 MVLMGRARHiglLRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQD 166
Cdd:COG1126 97 NVTLAPIKV---KKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVG 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 500071482 167 RVLRLVRVLADRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:COG1126 174 EVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFM 209
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
16-202 |
7.70e-25 |
|
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: 96.52 E-value: 7.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 16 DGTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGtAALVPQDfarafpyrvidmvLMGRARH 95
Cdd:cd03246 12 GAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDG-ADISQWD-------------PNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 96 IGLLrmpgrrdreaameALAVIGLAGKAAErfDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLVRVL 175
Cdd:cd03246 78 VGYL-------------PQDDELFSGSIAE--NILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAAL 142
|
170 180
....*....|....*....|....*..
gi 500071482 176 ADRGLAVVMTTHQPNhALAVADTALLM 202
Cdd:cd03246 143 KAAGATRIVIAHRPE-TLASADRILVL 168
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
23-197 |
8.09e-25 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 99.77 E-value: 8.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAG-----TAALVPQDFARAFPYRVIDMVLMGRAR--- 94
Cdd:TIGR01188 10 DGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGydvvrEPRKVRRSIGIVPQYASVDEDLTGRENlem 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 95 HIGLLRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLVRV 174
Cdd:TIGR01188 90 MGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDYIRA 169
|
170 180
....*....|....*....|...
gi 500071482 175 LADRGLAVVMTTHQPNHALAVAD 197
Cdd:TIGR01188 170 LKEEGVTILLTTHYMEEADKLCD 192
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
25-234 |
1.35e-24 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 97.99 E-value: 1.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 25 LDFAVAAGQVTAVLGANGCGKSTLLRVATGLrAPTRGRITVAGTA-------------ALVPQDFARAFPYRVIdmvlmg 91
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPlsdwsaaelarhrAYLSQQQSPPFAMPVF------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 92 rarHIGLLRMPGRRDREAAMEALAVI----GLAGKAAERFDALSGGQRQMVLIAR-------AIAAEPAALFLDEPASAL 160
Cdd:COG4138 88 ---QYLALHQPAGASSEAVEQLLAQLaealGLEDKLSRPLTQLSGGEWQRVRLAAvllqvwpTINPEGQLLLLDEPMNSL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500071482 161 DLGNQDRVLRLVRVLADRGLAVVMTTHQPNHALAVADTALLMLPEGAVF-GPCHEALTETRIEMLYGLPVRILDV 234
Cdd:COG4138 165 DVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVAsGETAEVMTPENLSEVFGVKFRRLEV 239
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-214 |
7.57e-24 |
|
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: 95.33 E-value: 7.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 6 IRAEGAAHsWDGTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLR-----APTRGRITVAGTAALVPQD----- 75
Cdd:cd03260 1 IELRDLNV-YYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVdvlel 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 76 -------FARAFPYR--VIDMVLMGrARHIGLLRMPGRRDREAamEALAVIGLAGKAAERFDA--LSGGQRQMVLIARAI 144
Cdd:cd03260 80 rrrvgmvFQKPNPFPgsIYDNVAYG-LRLHGIKLKEELDERVE--EALRKAALWDEVKDRLHAlgLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500071482 145 AAEPAALFLDEPASALDLGNQDRVLRLVRVLADRgLAVVMTTHQPNHALAVAD-TALLMLPEGAVFGPCHE 214
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADrTAFLLNGRLVEFGPTEQ 226
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
23-202 |
9.48e-24 |
|
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: 93.79 E-value: 9.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAaLVPQDFARAFPYRVIDMVLmgraRHIGLlrMP 102
Cdd:cd03229 17 NDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGED-LTDLEDELPPLRRRIGMVF----QDFAL--FP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 103 GrrdreaaMEALAVIGLAgkaaerfdaLSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLVRVLADR-GLA 181
Cdd:cd03229 90 H-------LTVLENIALG---------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQlGIT 153
|
170 180
....*....|....*....|.
gi 500071482 182 VVMTTHQPNHALAVADTALLM 202
Cdd:cd03229 154 VVLVTHDLDEAARLADRVVVL 174
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
17-219 |
1.04e-23 |
|
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: 95.26 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 17 GTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGT--AALVPQDFARAFpyRVIDMVLMGRA- 93
Cdd:cd03261 11 GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdiSGLSEAELYRLR--RRMGMLFQSGAl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 94 -------RHIGL-----LRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALD 161
Cdd:cd03261 89 fdsltvfENVAFplrehTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500071482 162 LGNQDRVLRLVRVLADR-GLAVVMTTHQPNHALAVADTaLLMLPEGAV--FGPCHEALTET 219
Cdd:cd03261 169 PIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADR-IAVLYDGKIvaEGTPEELRASD 228
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
23-187 |
1.10e-23 |
|
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: 95.20 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGT--AALVPQDFARA-----F----PYR---VIDMV 88
Cdd:cd03219 17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEdiTGLPPHEIARLgigrtFqiprLFPeltVLENV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 89 LMG----RARHIGLLRMPGRRD--REAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDL 162
Cdd:cd03219 97 MVAaqarTGSGLLLARARREEReaRERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNP 176
|
170 180
....*....|....*....|....*
gi 500071482 163 GNQDRVLRLVRVLADRGLAVVMTTH 187
Cdd:cd03219 177 EETEELAELIRELRERGITVLLVEH 201
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
23-202 |
1.12e-23 |
|
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: 95.34 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAALVPQDFARAFPYRVIDMVLmgraRHIGLL--- 99
Cdd:cd03258 22 KDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKARRRIGMIF----QHFNLLssr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 100 -------------RMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQD 166
Cdd:cd03258 98 tvfenvalpleiaGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQ 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 500071482 167 RVLRLVRVL-ADRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:cd03258 178 SILALLRDInRELGLTIVLITHEMEVVKRICDRVAVM 214
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-202 |
1.63e-23 |
|
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: 94.61 E-value: 1.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 6 IRAEGAAHSWDGTRwQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGtaalvpQDFARAFPY-RV 84
Cdd:cd03300 1 IELENVSKFYGGFV-ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDG------KDITNLPPHkRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 85 IDMVL--------MGRARHIG----LLRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALF 152
Cdd:cd03300 74 VNTVFqnyalfphLTVFENIAfglrLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 500071482 153 LDEPASALDLG-NQDRVLRLVRVLADRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:cd03300 154 LDEPLGALDLKlRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVM 204
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-208 |
1.66e-23 |
|
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: 95.05 E-value: 1.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 1 MAEPLIRAEGAAHSWdGTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGtaalvpQDFARAf 80
Cdd:COG1127 1 MSEPMIEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDG------QDITGL- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 81 pyrvIDMVLMGRARHIGLL------------------------RMPGRRDREAAMEALAVIGLAGkAAERFDA-LSGGQ- 134
Cdd:COG1127 73 ----SEKELYELRRRIGMLfqggalfdsltvfenvafplrehtDLSEAEIRELVLEKLELVGLPG-AADKMPSeLSGGMr 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 135 ------RQMVL---IaraiaaepaaLFLDEPASALDLGNQDRVLRLVRVLADR-GLAVVMTTHQPNHALAVADTaLLMLP 204
Cdd:COG1127 148 krvalaRALALdpeI----------LLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADR-VAVLA 216
|
....
gi 500071482 205 EGAV 208
Cdd:COG1127 217 DGKI 220
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-202 |
1.68e-23 |
|
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: 94.36 E-value: 1.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 6 IRAEGAAHSWDGTRwQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAALVPQDFARA-----F 80
Cdd:cd03265 1 IEVENLVKKYGDFE-AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRrigivF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 81 PYRVIDMVLMGR---ARHIGLLRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPA 157
Cdd:cd03265 80 QDLSVDDELTGWenlYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 500071482 158 SALDLGNQDRVLRLVRVL-ADRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAII 205
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
23-204 |
2.33e-23 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 94.93 E-value: 2.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA--------ALVPQDFArAFPYR-VIDMVLMGra 93
Cdd:COG4525 24 QDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPvtgpgadrGVVFQKDA-LLPWLnVLDNVAFG-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 94 rhiglLRMPG--RRDREA-AMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLR 170
Cdd:COG4525 101 -----LRLRGvpKAERRArAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQE 175
|
170 180 190
....*....|....*....|....*....|....*
gi 500071482 171 LV-RVLADRGLAVVMTTHQPNHALAVADTALLMLP 204
Cdd:COG4525 176 LLlDVWQRTGKGVFLITHSVEEALFLATRLVVMSP 210
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
23-187 |
5.01e-23 |
|
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: 93.95 E-value: 5.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGT--AALVPQDFARA-----------FPYR-VIDMV 88
Cdd:COG0411 21 DDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRdiTGLPPHRIARLgiartfqnprlFPELtVLENV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 89 LMGRARHIG------LLRMPGRRDREA-----AMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPA 157
Cdd:COG0411 101 LVAAHARLGrgllaaLLRLPRARREERearerAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPA 180
|
170 180 190
....*....|....*....|....*....|.
gi 500071482 158 SALDLGNQDRVLRLVRVL-ADRGLAVVMTTH 187
Cdd:COG0411 181 AGLNPEETEELAELIRRLrDERGITILLIEH 211
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
23-202 |
1.13e-22 |
|
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: 92.79 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAA-----------LVPQDFArAFPY-RVIDMVLM 90
Cdd:cd03296 19 DDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAtdvpvqernvgFVFQHYA-LFRHmTVFDNVAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 91 G-RARHIGlLRMPGRRDREAAMEALAVIGLAGkAAERFDA-LSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRV 168
Cdd:cd03296 98 GlRVKPRS-ERPPEAEIRAKVHELLKLVQLDW-LADRYPAqLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKEL 175
|
170 180 190
....*....|....*....|....*....|....*
gi 500071482 169 LRLVRVLADR-GLAVVMTTHQPNHALAVADTALLM 202
Cdd:cd03296 176 RRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVM 210
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-202 |
1.19e-22 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 94.90 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 1 MAEPLIRAEGAAHSWDGtRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGtaalvpQDFARAF 80
Cdd:PRK11607 15 ALTPLLEIRNLTKSFDG-QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDG------VDLSHVP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 81 PY-RVIDMVLMGRA--RHI--------GLL--RMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAE 147
Cdd:PRK11607 88 PYqRPINMMFQSYAlfPHMtveqniafGLKqdKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 500071482 148 PAALFLDEPASALDLGNQDRV-LRLVRVLADRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:PRK11607 168 PKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIM 223
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
24-202 |
1.65e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 94.40 E-value: 1.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 24 DLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGtaalvpQDFA-RAFPYRVIDMVLMGRA--RHIGL-- 98
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDG------EDVThRSIQQRDICMVFQSYAlfPHMSLge 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 99 -----LRMPGRRDREAAM---EALAVIGLAGkAAERF-DALSGGQRQMVLIARAIAAEPAALFLDEPASALDlGNQDRVL 169
Cdd:PRK11432 98 nvgygLKMLGVPKEERKQrvkEALELVDLAG-FEDRYvDQISGGQQQRVALARALILKPKVLLFDEPLSNLD-ANLRRSM 175
|
170 180 190
....*....|....*....|....*....|....*
gi 500071482 170 R-LVRVLADR-GLAVVMTTHQPNHALAVADTALLM 202
Cdd:PRK11432 176 ReKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVM 210
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
23-202 |
3.63e-22 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 93.29 E-value: 3.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAA------------LVPQDFArAFPYrvidmvlM 90
Cdd:COG1118 19 DDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLftnlpprerrvgFVFQHYA-LFPH-------M 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 91 GRARHI--GL-LRMPGRRDREA-AMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDlgnqD 166
Cdd:COG1118 91 TVAENIafGLrVRPPSKAEIRArVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALD----A 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 500071482 167 RV---LR--LVRVLADRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:COG1118 167 KVrkeLRrwLRRLHDELGGTTVFVTHDQEEALELADRVVVM 207
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
22-158 |
3.90e-22 |
|
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: 88.86 E-value: 3.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 22 FRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA-------------ALVPQDFaRAFPYRVIDMV 88
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDltdderkslrkeiGYVFQDP-QLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500071482 89 LMGRARHIGLLRMPGRRDREAAMEALAVIGLAG-KAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPAS 158
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARAEEALEKLGLGDLADrPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
23-202 |
5.01e-22 |
|
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: 91.55 E-value: 5.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA-----------------ALVPQDFArAFPYR-V 84
Cdd:cd03294 41 NDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDiaamsrkelrelrrkkiSMVFQSFA-LLPHRtV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 85 IDMVLMGrarhIGLLRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALD--- 161
Cdd:cd03294 120 LENVAFG----LEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDpli 195
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 500071482 162 -LGNQDRVLRLVrvlADRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:cd03294 196 rREMQDELLRLQ---AELQKTIVFITHDLDEALRLGDRIAIM 234
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
23-202 |
5.06e-22 |
|
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: 90.57 E-value: 5.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA--------------ALVPQDfARAFPY-RVIDM 87
Cdd:cd03224 17 FGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDitglppheraragiGYVPEG-RRIFPElTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 88 VLMGRARhigllrmPGRRDREAAMEalAVIGLAGKAAERFDA----LSGGQRQMVLIARAIAAEPAALFLDEPASALDLG 163
Cdd:cd03224 96 LLLGAYA-------RRRAKRKARLE--RVYELFPRLKERRKQlagtLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPK 166
|
170 180 190
....*....|....*....|....*....|....*....
gi 500071482 164 NQDRVLRLVRVLADRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:cd03224 167 IVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVL 205
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
17-205 |
9.72e-22 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 89.46 E-value: 9.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 17 GTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAP---TRGRITVAGT--AALVPQdfarafpyrvidmvlmg 91
Cdd:COG4136 12 GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRrlTALPAE----------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 92 rARHIGLL----------------------RMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPA 149
Cdd:COG4136 75 -QRRIGILfqddllfphlsvgenlafalppTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 500071482 150 ALFLDEPASALDLGNQDRVLRLVR-VLADRGLAVVMTTHQPNHALAVAdtALLMLPE 205
Cdd:COG4136 154 ALLLDEPFSKLDAALRAQFREFVFeQIRQRGIPALLVTHDEEDAPAAG--RVLDLGN 208
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-202 |
1.47e-21 |
|
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: 89.17 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 6 IRAEGAAHSWDGtRWQFRDLDFAVAAGqVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAAL------------VP 73
Cdd:cd03264 1 LQLENLTKRYGK-KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLkqpqklrrrigyLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 74 QDFaRAFP-YRVIDMVlmgraRHIGLL-RMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAAL 151
Cdd:cd03264 79 QEF-GVYPnFTVREFL-----DYIAWLkGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 500071482 152 FLDEPASALDLGNQDRVLR-LVRVLADRglAVVMTTHQPNHALAVADTALLM 202
Cdd:cd03264 153 IVDEPTAGLDPEERIRFRNlLSELGEDR--IVILSTHIVEDVESLCNQVAVL 202
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
24-217 |
3.67e-21 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 88.61 E-value: 3.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 24 DLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAG---------------TAALVPQDFaRAFPY-RVIDM 87
Cdd:PRK09493 19 NIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkvndpkvderlirqEAGMVFQQF-YLFPHlTALEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 88 VLMGRARhiglLRMPGRRD-REAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQD 166
Cdd:PRK09493 98 VMFGPLR----VRGASKEEaEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRH 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 500071482 167 RVLRLVRVLADRGLAVVMTTHQPNHALAVAdTALLMLPEG--AVFGPCHEALT 217
Cdd:PRK09493 174 EVLKVMQDLAEEGMTMVIVTHEIGFAEKVA-SRLIFIDKGriAEDGDPQVLIK 225
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-202 |
5.87e-21 |
|
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: 91.36 E-value: 5.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 4 PLIRAEGAAHSWDGTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA-------------A 70
Cdd:COG4988 335 PSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDlsdldpaswrrqiA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 71 LVPQDfARAFPYRVIDMVLMGRArhigllrmpgRRDREAAMEALAVIGLAGKAAERFD-----------ALSGGQRQMVL 139
Cdd:COG4988 415 WVPQN-PYLFAGTIRENLRLGRP----------DASDEELEAALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQRLA 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500071482 140 IARAIAAEPAALFLDEPASALDLGNQDRVLRLVRVLAdRGLAVVMTTHQPnHALAVADTALLM 202
Cdd:COG4988 484 LARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRL-ALLAQADRILVL 544
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
23-202 |
1.12e-20 |
|
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: 87.34 E-value: 1.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGtaalvpQDFARAFPYRvidmvlmgRARH-IGL--- 98
Cdd:COG0410 20 HGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDG------EDITGLPPHR--------IARLgIGYvpe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 99 -------------LRMPG--RRDREAAMEALAVIG-----LAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPAs 158
Cdd:COG0410 86 grrifpsltveenLLLGAyaRRDRAEVRADLERVYelfprLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS- 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 500071482 159 aldLGNQ----DRVLRLVRVLADRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:COG0410 165 ---LGLAplivEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVL 209
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
23-202 |
1.30e-20 |
|
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: 86.87 E-value: 1.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGT--AALVPQDFARAFPYRVIDMVLM-GRARHIGLL 99
Cdd:cd03245 21 DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTdiRQLDPADLRRNIGYVPQDVTLFyGTLRDNITL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 100 RMPGRRDREAaMEALAVIGLAGKAA-----------ERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRV 168
Cdd:cd03245 101 GAPLADDERI-LRAAELAGVTDFVNkhpngldlqigERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERL 179
|
170 180 190
....*....|....*....|....*....|....*
gi 500071482 169 L-RLVRVLADRGLAVVmtTHQPNhALAVADTALLM 202
Cdd:cd03245 180 KeRLRQLLGDKTLIII--THRPS-LLDLVDRIIVM 211
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
23-192 |
1.72e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 87.86 E-value: 1.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAalVPQDFARAFPY-----------RVID-MVLM 90
Cdd:COG4152 18 DDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEP--LDPEDRRRIGYlpeerglypkmKVGEqLVYL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 91 GRarhiglLR-MPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMV------------LIaraiaaepaalfLDEPA 157
Cdd:COG4152 96 AR------LKgLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVqliaallhdpelLI------------LDEPF 157
|
170 180 190
....*....|....*....|....*....|....*
gi 500071482 158 SALDLGNQDRVLRLVRVLADRGLAVVMTTHQPNHA 192
Cdd:COG4152 158 SGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELV 192
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
24-202 |
2.27e-20 |
|
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: 85.81 E-value: 2.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 24 DLDFaVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA--------ALVPQD------FARA--FPYrvidm 87
Cdd:cd03297 16 KIDF-DLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkiNLPPQQrkiglvFQQYalFPH----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 88 vlMGRARHI--GLLRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQ 165
Cdd:cd03297 90 --LNVRENLafGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 500071482 166 DRVLRLVR-VLADRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:cd03297 168 LQLLPELKqIKKNLNIPVIFVTHDLSEAEYLADRIVVM 205
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
15-189 |
2.38e-20 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 86.17 E-value: 2.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 15 WDGTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGlRAP----TRGRITVAG---TAALVPQDFA------RAFP 81
Cdd:cd03234 16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISG-RVEgggtTSGQILFNGqprKPDQFQKCVAyvrqddILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 82 YRVIDMVLmgraRHIGLLRMP-----GRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEP 156
Cdd:cd03234 95 GLTVRETL----TYTAILRLPrkssdAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190
....*....|....*....|....*....|...
gi 500071482 157 ASALDLGNQDRVLRLVRVLADRGLAVVMTTHQP 189
Cdd:cd03234 171 TSGLDSFTALNLVSTLSQLARRNRIVILTIHQP 203
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
23-202 |
2.40e-20 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 89.54 E-value: 2.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAA--LVPQDFARAFPYRVIDMVLM-GRARHIGLL 99
Cdd:TIGR03375 482 DNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIrqIDPADLRRNIGYVPQDPRLFyGTLRDNIAL 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 100 RMPGRRDrEAAMEALAVIGLAGKAA-----------ERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRV 168
Cdd:TIGR03375 562 GAPYADD-EEILRAAELAGVTEFVRrhpdgldmqigERGRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERF 640
|
170 180 190
....*....|....*....|....*....|....*
gi 500071482 169 L-RLVRVLADRGLAVVmtTHQPnHALAVADTALLM 202
Cdd:TIGR03375 641 KdRLKRWLAGKTLVLV--THRT-SLLDLVDRIIVM 672
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-202 |
2.93e-20 |
|
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: 86.20 E-value: 2.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 6 IRAEGAAHSWDGTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAG--TAALVPQDFARA---- 79
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedIREQDPVELRRKigyv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 80 ------FPYRVIdmvlmgrARHIG----LLRMPGRRDREAAMEALAVIGL-AGKAAERF-DALSGGQRQMVLIARAIAAE 147
Cdd:cd03295 81 iqqiglFPHMTV-------EENIAlvpkLLKWPKEKIRERADELLALVGLdPAEFADRYpHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 500071482 148 PAALFLDEPASALD----LGNQDRVLRLVRVLadrGLAVVMTTHQPNHALAVADTALLM 202
Cdd:cd03295 154 PPLLLMDEPFGALDpitrDQLQEEFKRLQQEL---GKTIVFVTHDIDEAFRLADRIAIM 209
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
23-202 |
9.20e-20 |
|
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: 84.48 E-value: 9.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGT-------AAL-----VPQDfarafpyRVIDMVLM 90
Cdd:cd03263 19 DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYsirtdrkAARqslgyCPQF-------DALFDELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 91 GRaRHIGLL-RMPGRRDREAAMEALAVI---GLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQD 166
Cdd:cd03263 92 VR-EHLRFYaRLKGLPKSEIKEEVELLLrvlGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRR 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 500071482 167 RVLRLVRVLAdRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:cd03263 171 AIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIM 205
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
16-202 |
1.02e-19 |
|
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: 87.97 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 16 DGTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA-------------ALVPQDfARAFPY 82
Cdd:COG2274 485 GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDlrqidpaslrrqiGVVLQD-VFLFSG 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 83 RVIDMVLMGRArhigllrmpgRRDREAAMEALAVIGLAGKAA-----------ERFDALSGGQRQMVLIARAIAAEPAAL 151
Cdd:COG2274 564 TIRENITLGDP----------DATDEEIIEAARLAGLHDFIEalpmgydtvvgEGGSNLSGGQRQRLAIARALLRNPRIL 633
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 500071482 152 FLDEPASALDLGNQDRVLRLVRVLAdRGLAVVMTTHQPNHaLAVADTALLM 202
Cdd:COG2274 634 ILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLST-IRLADRIIVL 682
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
23-204 |
1.65e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 84.37 E-value: 1.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA--------ALVPQDFArAFPYR-VIDMVLMGra 93
Cdd:PRK11248 18 EDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPvegpgaerGVVFQNEG-LLPWRnVQDNVAFG-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 94 rhIGLLRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLR-LV 172
Cdd:PRK11248 95 --LQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTlLL 172
|
170 180 190
....*....|....*....|....*....|..
gi 500071482 173 RVLADRGLAVVMTTHQPNHALAVADTALLMLP 204
Cdd:PRK11248 173 KLWQETGKQVLLITHDIEEAVFMATELVLLSP 204
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
16-202 |
1.76e-19 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 83.76 E-value: 1.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 16 DGTRWQFRDL----DFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGtaalvpQDFARAFPY-RVIDMVL- 89
Cdd:TIGR01277 4 DKVRYEYEHLpmefDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVND------QSHTGLAPYqRPVSMLFq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 90 -------MGRARHIGLLRMPGRR----DREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPAS 158
Cdd:TIGR01277 78 ennlfahLTVRQNIGLGLHPGLKlnaeQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFS 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 500071482 159 ALDLGNQDRVLRLVRVLAD-RGLAVVMTTHQPNHALAVADTALLM 202
Cdd:TIGR01277 158 ALDPLLREEMLALVKQLCSeRQRTLLMVTHHLSDARAIASQIAVV 202
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
23-187 |
4.86e-19 |
|
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: 84.33 E-value: 4.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGL---RAPTRGRITVAGT-----------------AALVPQDFARAF-P 81
Cdd:COG0444 22 DGVSFDVRRGETLGLVGESGSGKSTLARAILGLlppPGITSGEILFDGEdllklsekelrkirgreIQMIFQDPMTSLnP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 82 -YRVIDMVLMGRARHiglLRMPGRRDREAAMEALAVIGLAGkAAERFDA----LSGGQRQMVLIARAIAAEPAALFLDEP 156
Cdd:COG0444 102 vMTVGDQIAEPLRIH---GGLSKAEARERAIELLERVGLPD-PERRLDRypheLSGGMRQRVMIARALALEPKLLIADEP 177
|
170 180 190
....*....|....*....|....*....|..
gi 500071482 157 ASALDLGNQDRVLRLVRVL-ADRGLAVVMTTH 187
Cdd:COG0444 178 TTALDVTIQAQILNLLKDLqRELGLAILFITH 209
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
37-202 |
4.94e-19 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 84.47 E-value: 4.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 37 VLGANGCGKSTLLRVATGLRAPTRGRITVAGTA-ALVPqdfarafPY-RVIDMVL--------MGRARHIGL-LRMPGRR 105
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDvTNVP-------PHlRHINMVFqsyalfphMTVEENVAFgLKMRKVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 106 DREAA---MEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRV-LRLVRVLADRGLA 181
Cdd:TIGR01187 74 RAEIKprvLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMqLELKTIQEQLGIT 153
|
170 180
....*....|....*....|.
gi 500071482 182 VVMTTHQPNHALAVADTALLM 202
Cdd:TIGR01187 154 FVFVTHDQEEAMTMSDRIAIM 174
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
17-189 |
4.97e-19 |
|
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: 82.16 E-value: 4.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 17 GTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA-ALVPQDFARAFPYRVIDMVLMGRARH 95
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPlDFQRDSIARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 96 IGLLRMPGR-RDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLVRV 174
Cdd:cd03231 91 LENLRFWHAdHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAG 170
|
170
....*....|....*
gi 500071482 175 LADRGLAVVMTTHQP 189
Cdd:cd03231 171 HCARGGMVVLTTHQD 185
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
6-193 |
6.97e-19 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 82.02 E-value: 6.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 6 IRAEGAAHSWDGTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGT----------AAL---- 71
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQdlsrlkrreiPYLrrri 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 72 --VPQDFaR-----------AFPYRVIdmvlmgrarhigllRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMV 138
Cdd:COG2884 82 gvVFQDF-RllpdrtvyenvALPLRVT--------------GKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRV 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 500071482 139 LIARAIAAEPAALFLDEPASALDLGNQDRVLRLVRVLADRGLAVVMTTHqpNHAL 193
Cdd:COG2884 147 AIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATH--DLEL 199
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-194 |
7.10e-19 |
|
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: 82.48 E-value: 7.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 1 MAEPLIRAEGAAHSWDGTRWQ---FRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTaALVPQDF- 76
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGEltiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQ-DLFALDEd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 77 ARAfpyRVidmvlmgRARHIG-------LL---------RMP----GRRD-REAAMEALAVIGLAGKAAERFDALSGGQR 135
Cdd:COG4181 83 ARA---RL-------RARHVGfvfqsfqLLptltalenvMLPlelaGRRDaRARARALLERVGLGHRLDHYPAQLSGGEQ 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 136 QMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLVRVL-ADRGLAVVMTTHQPnhALA 194
Cdd:COG4181 153 QRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELnRERGTTLVLVTHDP--ALA 210
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
24-217 |
8.02e-19 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 84.00 E-value: 8.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 24 DLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA-----------------ALVPQDfARAFP-YRVI 85
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlqdsargiflpphrrriGYVFQE-ARLFPhLSVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 86 DMVLMGRARhigllrMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQ 165
Cdd:COG4148 96 GNLLYGRKR------APRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARK 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 500071482 166 DRVLRLVRVLADR-GLAVVMTTHQPNHALAVADTaLLMLPEGAV--FGPCHEALT 217
Cdd:COG4148 170 AEILPYLERLRDElDIPILYVSHSLDEVARLADH-VVLLEQGRVvaSGPLAEVLS 223
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
22-189 |
1.24e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 81.07 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 22 FRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAALVPqDFARAFPY-----------RVIDMVLM 90
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDP-DVAEACHYlghrnamkpalTVAENLEF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 91 GRARHigllrmpGRRDREAAmEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLR 170
Cdd:PRK13539 97 WAAFL-------GGEELDIA-AALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAE 168
|
170
....*....|....*....
gi 500071482 171 LVRVLADRGLAVVMTTHQP 189
Cdd:PRK13539 169 LIRAHLAQGGIVIAATHIP 187
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
24-230 |
1.26e-18 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 82.55 E-value: 1.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 24 DLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAG----------------TAALVPQDFARAF-PYRVID 86
Cdd:TIGR02769 29 NVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGqdlyqldrkqrrafrrDVQLVFQDSPSAVnPRMTVR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 87 MVLMGRARHigLLRMPGRRDREAAMEALAVIGLAGKAAERFDA-LSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQ 165
Cdd:TIGR02769 109 QIIGEPLRH--LTSLDESEQKARIAELLDMVGLRSEDADKLPRqLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQ 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500071482 166 DRVLRLVRVLADR-GLAVVMTTHQPNHALAVADTALLM--------LPEGAVFGPCHEALTETRIEMLYGLPVR 230
Cdd:TIGR02769 187 AVILELLRKLQQAfGTAYLFITHDLRLVQSFCQRVAVMdkgqiveeCDVAQLLSFKHPAGRNLQSAVLPEHPVR 260
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
25-202 |
1.48e-18 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 81.72 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 25 LDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGT---------------------AALVPQDFaRAFPYR 83
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDItidtarslsqqkglirqlrqhVGFVFQNF-NLFPHR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 84 -VIDMVLMGRarhIGLLRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDL 162
Cdd:PRK11264 101 tVLENIIEGP---VIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDP 177
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 500071482 163 GNQDRVLRLVRVLADRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:PRK11264 178 ELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFM 217
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-202 |
1.62e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.07 E-value: 1.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 1 MAEPLIRAEGAAHSWDGTRwQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA--ALVPQDFAR 78
Cdd:PRK09700 1 MATPYISMAGIGKSFGPVH-ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINynKLDHKLAAQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 79 ---AFPYR---VIDMVLMGRARHIGllRMPGRR-------D----REAAMEALAVIGLAGKAAERFDALSGGQRQMVLIA 141
Cdd:PRK09700 80 lgiGIIYQelsVIDELTVLENLYIG--RHLTKKvcgvniiDwremRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500071482 142 RAIAAEPAALFLDEPASALDLGNQDRVLRLVRVLADRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:PRK09700 158 KTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVM 218
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
23-206 |
1.80e-18 |
|
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: 81.36 E-value: 1.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRG---------------RITVAGTAALVPQDFARAFPYRVIDM 87
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGgvilegkqitepgpdRMVVFQNYSLLPWLTVRENIALAVDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 88 VLmgraRHigllrMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALD-LGNQD 166
Cdd:TIGR01184 82 VL----PD-----LSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDaLTRGN 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 500071482 167 RVLRLVRVLADRGLAVVMTTHQPNHALAVADTaLLMLPEG 206
Cdd:TIGR01184 153 LQEELMQIWEEHRVTVLMVTHDVDEALLLSDR-VVMLTNG 191
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
23-188 |
2.62e-18 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 82.43 E-value: 2.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGT--AAL--------------VPQDF----AR---- 78
Cdd:COG1135 22 DDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVdlTALserelraarrkigmIFQHFnllsSRtvae 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 79 --AFPyrvidMVLMGrarhigllrMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEP 156
Cdd:COG1135 102 nvALP-----LEIAG---------VPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEA 167
|
170 180 190
....*....|....*....|....*....|...
gi 500071482 157 ASALDLGNQDRVLRLVRVLADR-GLAVVMTTHQ 188
Cdd:COG1135 168 TSALDPETTRSILDLLKDINRElGLTIVLITHE 200
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
16-202 |
3.35e-18 |
|
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: 78.96 E-value: 3.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 16 DGTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA-------------ALVPQDfarafPY 82
Cdd:cd03228 12 GRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDlrdldleslrkniAYVPQD-----PF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 83 RvidmvlmgrarhigllrmpgrrdreaamealaviglagkaaerFDA------LSGGQRQMVLIARAIAAEPAALFLDEP 156
Cdd:cd03228 87 L-------------------------------------------FSGtireniLSGGQRQRIAIARALLRDPPILILDEA 123
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 500071482 157 ASALDLGNQDRVLRLVRVLAdRGLAVVMTTHQPnHALAVADTALLM 202
Cdd:cd03228 124 TSALDPETEALILEALRALA-KGKTVIVIAHRL-STIRDADRIIVL 167
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-202 |
5.28e-18 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 81.92 E-value: 5.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 1 MAEPLIRAEGAAHSWDGTRwQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAG-TAALVP------ 73
Cdd:PRK09452 10 SLSPLVELRGISKSFDGKE-VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGqDITHVPaenrhv 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 74 ----QDFArAFPY-RVIDMVLMGrarhiglLRM---PGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIA 145
Cdd:PRK09452 89 ntvfQSYA-LFPHmTVFENVAFG-------LRMqktPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500071482 146 AEPAALFLDEPASALD----LGNQDRVLRLVRVLadrGLAVVMTTHQPNHALAVADTALLM 202
Cdd:PRK09452 161 NKPKVLLLDESLSALDyklrKQMQNELKALQRKL---GITFVFVTHDQEEALTMSDRIVVM 218
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
22-189 |
7.32e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 79.08 E-value: 7.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 22 FRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA-ALVPQDFARafpyrviDMVLMGRARHIG--- 97
Cdd:PRK13538 17 FSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPiRRQRDEYHQ-------DLLYLGHQPGIKtel 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 98 --------LLRMPGRRDREAAMEALAVIGLAGkaaeRFDA----LSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQ 165
Cdd:PRK13538 90 talenlrfYQRLHGPGDDEALWEALAQVGLAG----FEDVpvrqLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGV 165
|
170 180
....*....|....*....|....
gi 500071482 166 DRVLRLVRVLADRGLAVVMTTHQP 189
Cdd:PRK13538 166 ARLEALLAQHAEQGGMVILTTHQD 189
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
24-187 |
8.08e-18 |
|
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: 78.99 E-value: 8.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 24 DLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA----------------ALVPQDFaRAFPYR-VID 86
Cdd:cd03292 19 GINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDvsdlrgraipylrrkiGVVFQDF-RLLPDRnVYE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 87 MVlmgrARHIGLLRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQD 166
Cdd:cd03292 98 NV----AFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTW 173
|
170 180
....*....|....*....|.
gi 500071482 167 RVLRLVRVLADRGLAVVMTTH 187
Cdd:cd03292 174 EIMNLLKKINKAGTTVVVATH 194
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
3-202 |
1.36e-17 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 78.63 E-value: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 3 EPLIRAEGAA-----HSWDGTRWQ-FRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAALVpqDF 76
Cdd:COG4778 2 TTLLEVENLSktftlHLQGGKRLPvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWV--DL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 77 ARAFPYRVIDMvlmgRARHIG----LLR-MPGRRDREAAMEALAVIGLA-----GKAAERFDAL--------------SG 132
Cdd:COG4778 80 AQASPREILAL----RRRTIGyvsqFLRvIPRVSALDVVAEPLLERGVDreearARARELLARLnlperlwdlppatfSG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 133 GQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLVRVLADRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:COG4778 156 GEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDV 225
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
17-202 |
1.79e-17 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 79.42 E-value: 1.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 17 GTRWQFR---DLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAaLVPQDFARAFPYRvidmvlmgra 93
Cdd:TIGR04521 13 GTPFEKKaldDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRD-ITAKKKKKLKDLR---------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 94 RHIGL------------------------LRMPGRRDREAAMEALAVIGLAGKAAER--FDaLSGGQRQMVLIARAIAAE 147
Cdd:TIGR04521 82 KKVGLvfqfpehqlfeetvykdiafgpknLGLSEEEAEERVKEALELVGLDEEYLERspFE-LSGGQMRRVAIAGVLAME 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 500071482 148 PAALFLDEPASALDLGNQDRVLRLVRVLAD-RGLAVVMTTHQPNHALAVADTALLM 202
Cdd:TIGR04521 161 PEVLILDEPTAGLDPKGRKEILDLFKRLHKeKGLTVILVTHSMEDVAEYADRVIVM 216
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
22-239 |
1.87e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 78.97 E-value: 1.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 22 FRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGtaalvpQDFARAFPYRVIDMV-------LMG--- 91
Cdd:COG1101 22 LDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDG------KDVTKLPEYKRAKYIgrvfqdpMMGtap 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 92 -------------RARHIGLLRMPGRRDREAAMEALAVI--GLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEP 156
Cdd:COG1101 96 smtieenlalayrRGKRRGLRRGLTKKRRELFRELLATLglGLENRLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEH 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 157 ASALDLGNQDRVLRL-VRVLADRGLAVVMTTHQPNHALAVADTaLLMLPEGavfgpchealtetRIemlyglpvrILDVK 235
Cdd:COG1101 176 TAALDPKTAALVLELtEKIVEENNLTTLMVTHNMEQALDYGNR-LIMMHEG-------------RI---------ILDVS 232
|
....
gi 500071482 236 AADR 239
Cdd:COG1101 233 GEEK 236
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-196 |
2.80e-17 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 78.43 E-value: 2.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 1 MAEPLIRAEGAAHSWdGTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAG-------TAAL-- 71
Cdd:PRK11701 2 MDQPLLSVRGLTKLY-GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlrdLYALse 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 72 -------------VPQDFARAFPYRV-----IDMVLMGR-ARHIGllrmpgrRDREAAMEALAVIGLAgkaAERFD---- 128
Cdd:PRK11701 81 aerrrllrtewgfVHQHPRDGLRMQVsaggnIGERLMAVgARHYG-------DIRATAGDWLERVEID---AARIDdlpt 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500071482 129 ALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLVRVL-ADRGLAVVMTTHQpnhaLAVA 196
Cdd:PRK11701 151 TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHD----LAVA 215
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
17-187 |
3.02e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 80.49 E-value: 3.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 17 GTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAG--TAALVPQDfARAFP-YRVIDMVLMGRA 93
Cdd:COG0488 9 GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglRIGYLPQE-PPLDDdLTVLDTVLDGDA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 94 RhigLLRMPGRRDR-EAAM-EALAVIGLAGKAAERFDA------------------------------LSGGQRQMVLIA 141
Cdd:COG0488 88 E---LRALEAELEElEAKLaEPDEDLERLAELQEEFEAlggweaearaeeilsglgfpeedldrpvseLSGGWRRRVALA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 500071482 142 RAIAAEPAALFLDEPASALDLgnqDRVLRLVRVLADRGLAVVMTTH 187
Cdd:COG0488 165 RALLSEPDLLLLDEPTNHLDL---ESIEWLEEFLKNYPGTVLVVSH 207
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-202 |
3.06e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.48 E-value: 3.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 4 PLIRAEGAAHSWDGTRwQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAA------------- 70
Cdd:PRK15439 10 PLLCARSISKQYSGVE-VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCarltpakahqlgi 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 71 -LVPQDfARAFPYRVIdmvlmgraRHIGLLRMPGRRDREAAMEAL-----AVIGLAGKAAerfdALSGGQRQMVLIARAI 144
Cdd:PRK15439 89 yLVPQE-PLLFPNLSV--------KENILFGLPKRQASMQKMKQLlaalgCQLDLDSSAG----SLEVADRQIVEILRGL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 500071482 145 AAEPAALFLDEPASALDLGNQDRVLRLVRVLADRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:PRK15439 156 MRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVM 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-202 |
3.28e-17 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 79.35 E-value: 3.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 1 MAEplIRAEGAAHSWDGTRWqFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA----------- 69
Cdd:COG3839 1 MAS--LELENVSKSYGGVEA-LKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDvtdlppkdrni 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 70 ALVPQDFA-------R---AFPYRvidmvlmgrarhigLLRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVL 139
Cdd:COG3839 78 AMVFQSYAlyphmtvYeniAFPLK--------------LRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500071482 140 IARAIAAEPAALFLDEPASALD--LGNQDRVlRLVRVLADRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLDakLRVEMRA-EIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVM 207
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
6-202 |
4.59e-17 |
|
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: 80.02 E-value: 4.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 6 IRAEGAAHSWDGTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAG-------------TAALV 72
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGvpladadadswrdQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 73 PQDfARAFPYRVIDMVLMGRARHIGLLrMPGRRDREAAMEALAVI--GLAGKAAERFDALSGGQRQMVLIARAIAAEPAA 150
Cdd:TIGR02857 402 PQH-PFLFAGTIAENIRLARPDASDAE-IREALERAGLDEFVAALpqGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPL 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 500071482 151 LFLDEPASALDLGNQDRVLRLVRVLAdRGLAVVMTTHQPNHAlAVADTALLM 202
Cdd:TIGR02857 480 LLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRLALA-ALADRIVVL 529
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-187 |
5.04e-17 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 78.62 E-value: 5.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 1 MAEPLIRAEGAAHSWDGTRWQFR----------DLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGT-- 68
Cdd:COG4608 3 MAEPLLEVRDLKKHFPVRGGLFGrtvgvvkavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQdi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 69 -----AALVP---------QDfarafPY-------RVIDMVLMGRARHiGLLRMPGRRDReaAMEALAVIGLAGKAAERF 127
Cdd:COG4608 83 tglsgRELRPlrrrmqmvfQD-----PYaslnprmTVGDIIAEPLRIH-GLASKAERRER--VAELLELVGLRPEHADRY 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500071482 128 -DALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLVRVLADR-GLAVVMTTH 187
Cdd:COG4608 155 pHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISH 216
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
23-189 |
5.40e-17 |
|
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: 76.44 E-value: 5.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAP--TRGRITVAGT----------AALVPQDFArAFPYRVIdmvlm 90
Cdd:cd03213 26 KNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRpldkrsfrkiIGYVPQDDI-LHPTLTV----- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 91 grarhigllrmpgrrdREAAMEALAVIGLagkaaerfdalSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLR 170
Cdd:cd03213 100 ----------------RETLMFAAKLRGL-----------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMS 152
|
170
....*....|....*....
gi 500071482 171 LVRVLADRGLAVVMTTHQP 189
Cdd:cd03213 153 LLRRLADTGRTIICSIHQP 171
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
3-189 |
5.74e-17 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 79.71 E-value: 5.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 3 EPLIRAEGAAHSWDGTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAG-------------TA 69
Cdd:TIGR02868 332 KPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGvpvssldqdevrrRV 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 70 ALVPQDfARAFPYRVIDMVLMGRarhigllrmpGRRDREAAMEALAVIGLAGKAAERFD-----------ALSGGQRQMV 138
Cdd:TIGR02868 412 SVCAQD-AHLFDTTVRENLRLAR----------PDATDEELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRL 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 500071482 139 LIARAIAAEPAALFLDEPASALDLGNQDRVLRLVRVlADRGLAVVMTTHQP 189
Cdd:TIGR02868 481 ALARALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
27-202 |
6.25e-17 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 78.47 E-value: 6.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 27 FAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAALVPQDFARAFPYRVIDMV-------LMGRaRHIGL- 98
Cdd:PRK11308 36 FTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKIQIVfqnpygsLNPR-KKVGQi 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 99 ----------LRMPGRRDREAAMeaLAVIGLAGKAAERFDAL-SGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDR 167
Cdd:PRK11308 115 leepllintsLSAAERREKALAM--MAKVGLRPEHYDRYPHMfSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQ 192
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 500071482 168 VLRLVRVL-ADRGLAVVMTTHQpnhaLAV----ADTALLM 202
Cdd:PRK11308 193 VLNLMMDLqQELGLSYVFISHD----LSVvehiADEVMVM 228
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
24-187 |
8.43e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 79.18 E-value: 8.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 24 DLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGtaalVPQDFAR---------AFPYRVIDMVL-MGRA 93
Cdd:PRK11288 22 DISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDG----QEMRFASttaalaagvAIIYQELHLVPeMTVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 94 RHIGLLRMPGRR---DREA----AMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQD 166
Cdd:PRK11288 98 ENLYLGQLPHKGgivNRRLlnyeAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIE 177
|
170 180
....*....|....*....|.
gi 500071482 167 RVLRLVRVLADRGLAVVMTTH 187
Cdd:PRK11288 178 QLFRVIRELRAEGRVILYVSH 198
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-202 |
1.09e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 77.36 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 1 MAEPLIRAEGAAHSWDGT-RWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA---------- 69
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVlseetvwdvr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 70 ---ALVPQD----FARAfpyRVIDMVLMGrARHIGLLR--MPGRRDreaamEALAVIGLAGKAAERFDALSGGQRQMVLI 140
Cdd:PRK13635 81 rqvGMVFQNpdnqFVGA---TVQDDVAFG-LENIGVPReeMVERVD-----QALRQVGMEDFLNREPHRLSGGQKQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500071482 141 ARAIAAEPAALFLDEPASALDLGNQDRVLRLVRVLAD-RGLAVVMTTHQPNHAlAVADTALLM 202
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEqKGITVLSITHDLDEA-AQADRVIVM 213
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
24-207 |
1.24e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 76.29 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 24 DLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGT--AALVPQDFARAFPYRVIDMVLMGRARHIGLL-- 99
Cdd:PRK10247 25 NISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdiSTLKPEIYRQQVSYCAQTPTLFGDTVYDNLIfp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 100 -RMPGRRDREAAMEA-LAVIGLAGKAAE-RFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLV-RVL 175
Cdd:PRK10247 105 wQIRNQQPDPAIFLDdLERFALPDTILTkNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIhRYV 184
|
170 180 190
....*....|....*....|....*....|..
gi 500071482 176 ADRGLAVVMTTHQPNHaLAVADTALLMLPEGA 207
Cdd:PRK10247 185 REQNIAVLWVTHDKDE-INHADKVITLQPHAG 215
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-202 |
2.34e-16 |
|
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: 77.88 E-value: 2.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 2 AEPLIRAEGAAHSWDG-TRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA----------- 69
Cdd:COG4987 330 GGPSLELEDVSFRYPGaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDlrdldeddlrr 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 70 --ALVPQDfARAFPYRVIDMVLMGRarhigllrmpGRRDREAAMEALAVIGLAGKAAERFD-----------ALSGGQRQ 136
Cdd:COG4987 410 riAVVPQR-PHLFDTTLRENLRLAR----------PDATDEELWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERR 478
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500071482 137 MVLIARAIAAEPAALFLDEPASALDLGNQDRVLR-LVRVLADRglAVVMTTHQPnHALAVADTALLM 202
Cdd:COG4987 479 RLALARALLRDAPILLLDEPTEGLDAATEQALLAdLLEALAGR--TVLLITHRL-AGLERMDRILVL 542
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
5-202 |
2.65e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 76.18 E-value: 2.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 5 LIRAEGAAHSW-DGTRwQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAAlvpQDFARAFPYR 83
Cdd:PRK13644 1 MIRLENVSYSYpDGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDT---GDFSKLQGIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 84 VI--------DMVLMGRARHIGL------LRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPA 149
Cdd:PRK13644 77 KLvgivfqnpETQFVGRTVEEDLafgpenLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 500071482 150 ALFLDEPASALDLGNQDRVLRLVRVLADRGLAVVMTTHQPNHaLAVADTALLM 202
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEE-LHDADRIIVM 208
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
25-234 |
2.91e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 75.35 E-value: 2.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 25 LDFAVAAGQVTAVLGANGCGKSTLLRVATGLrAPTRGRITVAGTA--ALVPQDFARAFPY---RVIDMVLMGRARHIGLL 99
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPleAWSAAELARHRAYlsqQQTPPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 100 RMPGRR--DREAAMEALA-VIGLAGKAAERFDALSGGQRQMV-------LIARAIAAEPAALFLDEPASALDLGNQDRVL 169
Cdd:PRK03695 94 QPDKTRteAVASALNEVAeALGLDDKLGRSVNQLSGGEWQRVrlaavvlQVWPDINPAGQLLLLDEPMNSLDVAQQAALD 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500071482 170 RLVRVLADRGLAVVMTTHQPNHALAVADTALLmLPEGAVF--GPCHEALTETRIEMLYGLPVRILDV 234
Cdd:PRK03695 174 RLLSELCQQGIAVVMSSHDLNHTLRHADRVWL-LKQGKLLasGRRDEVLTPENLAQVFGVNFRRLDV 239
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
24-202 |
3.46e-16 |
|
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: 76.69 E-value: 3.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 24 DLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA-----------------ALVPQDfARAFP-YRVI 85
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTlfdsrkgiflppekrriGYVFQE-ARLFPhLSVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 86 DMVLMGRARhiglLRMPGRRDREAAMEALAVIG-LAGKAAERfdaLSGGQRQMVLIARAIAAEPAALFLDEPASALDLGN 164
Cdd:TIGR02142 94 GNLRYGMKR----ARPSERRISFERVIELLGIGhLLGRLPGR---LSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPR 166
|
170 180 190
....*....|....*....|....*....|....*....
gi 500071482 165 QDRVL-RLVRVLADRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:TIGR02142 167 KYEILpYLERLHAEFGIPILYVSHSLQEVLRLADRVVVL 205
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
17-189 |
4.35e-16 |
|
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: 73.93 E-value: 4.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 17 GTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTaalvPQDFARAFPYRVIDMV-------- 88
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGT----PLAEQRDEPHENILYLghlpglkp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 89 LMGRARHIGLLRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRV 168
Cdd:TIGR01189 87 ELSALENLHFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALL 166
|
170 180
....*....|....*....|.
gi 500071482 169 LRLVRVLADRGLAVVMTTHQP 189
Cdd:TIGR01189 167 AGLLRAHLARGGIVLLTTHQD 187
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
21-202 |
5.31e-16 |
|
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: 73.62 E-value: 5.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 21 QFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGtaalvpQDFARAFPYRVIdmvlmgrARHIGLLr 100
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDG------KPVTRRSPRDAI-------RAGIAYV- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 101 mPGRRDREAAMEALAV---IGLAgkaaerfDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLVRVLAD 177
Cdd:cd03215 81 -PEDRKREGLVLDLSVaenIALS-------SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELAD 152
|
170 180
....*....|....*....|....*
gi 500071482 178 RGLAVVMTTHQPNHALAVADTALLM 202
Cdd:cd03215 153 AGKAVLLISSELDELLGLCDRILVM 177
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
26-217 |
6.51e-16 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 74.23 E-value: 6.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 26 DFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGtaalvpQDFARAFP-YRVIDMVL--------MGRARHI 96
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG------QDHTTTPPsRRPVSMLFqennlfshLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 97 GLLRMPGRRDREAAMEALAVIglAGKAA-----ERFDA-LSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLR 170
Cdd:PRK10771 93 GLGLNPGLKLNAAQREKLHAI--ARQMGiedllARLPGqLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 500071482 171 LVR-VLADRGLAVVMTTHQPNHALAVADTALLMLpEGAVF--GPCHEALT 217
Cdd:PRK10771 171 LVSqVCQERQLTLLMVSHSLEDAARIAPRSLVVA-DGRIAwdGPTDELLS 219
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
31-208 |
9.12e-16 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 74.24 E-value: 9.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 31 AGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA--------------------------ALVPQDFARAFPYRV 84
Cdd:PRK10619 30 AGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlvrdkdgqlkvadknqlrllrtrlTMVFQHFNLWSHMTV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 85 IDMVLMGRARHIGLLRMPGRrdrEAAMEALAVIGLAGKAAERFDA-LSGGQRQMVLIARAIAAEPAALFLDEPASALDLG 163
Cdd:PRK10619 110 LENVMEAPIQVLGLSKQEAR---ERAVKYLAKVGIDERAQGKYPVhLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPE 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 500071482 164 NQDRVLRLVRVLADRGLAVVMTTHQPNHALAVAdTALLMLPEGAV 208
Cdd:PRK10619 187 LVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVS-SHVIFLHQGKI 230
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
23-187 |
9.66e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 74.34 E-value: 9.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA----------------ALVPQDFARAF-PYRVI 85
Cdd:PRK10419 29 NNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPlaklnraqrkafrrdiQMVFQDSISAVnPRKTV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 86 DMVLMGRARHigLLRMPGRRDREAAMEALAVIGLAGKAAERFDA-LSGGQRQMVLIARAIAAEPAALFLDEPASALDLGN 164
Cdd:PRK10419 109 REIIREPLRH--LLSLDKAERLARASEMLRAVDLDDSVLDKRPPqLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVL 186
|
170 180
....*....|....*....|....
gi 500071482 165 QDRVLRLVRVLADR-GLAVVMTTH 187
Cdd:PRK10419 187 QAGVIRLLKKLQQQfGTACLFITH 210
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
22-216 |
1.33e-15 |
|
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: 75.55 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 22 FRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA--ALVPQDFARafpyrvidmvlmgrarHIGLL 99
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADlsQWDREELGR----------------HIGYL 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 100 ----------------RMPGRRDR---EAAMEALA-------------VIGLAGKAaerfdaLSGGQRQMVLIARAIAAE 147
Cdd:COG4618 412 pqdvelfdgtiaeniaRFGDADPEkvvAAAKLAGVhemilrlpdgydtRIGEGGAR------LSGGQRQRIGLARALYGD 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500071482 148 PAALFLDEPASALDLGNQDRVLRLVRVLADRGLAVVMTTHQPNhALAVADTaLLMLPEGAV--FGPCHEAL 216
Cdd:COG4618 486 PRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS-LLAAVDK-LLVLRDGRVqaFGPRDEVL 554
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
24-202 |
1.63e-15 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 74.74 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 24 DLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGT-----------AALVPQDFARAFPYRVIDMVLMGr 92
Cdd:PRK10851 20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlhardrkVGFVFQHYALFRHMTVFDNIAFG- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 93 arhiglLRMPGRRDREAA-------MEALAVIGLAgKAAERFDA-LSGGQRQMVLIARAIAAEPAALFLDEPASALDLGN 164
Cdd:PRK10851 99 ------LTVLPRRERPNAaaikakvTQLLEMVQLA-HLADRYPAqLSGGQKQRVALARALAVEPQILLLDEPFGALDAQV 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 500071482 165 QDRVLRLVRVLADR-GLAVVMTTHQPNHALAVADTALLM 202
Cdd:PRK10851 172 RKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVM 210
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-225 |
1.64e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 73.89 E-value: 1.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 3 EPLIRAEGAAHSWDGTRwQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGL----RAP------------TRGRI--- 63
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQ-ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdKSAgshiellgrtvqREGRLard 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 64 ---TVAGTAALVpQDFARAFPYRVIDMVLMGRARHIGL----LRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQ 136
Cdd:PRK09984 81 irkSRANTGYIF-QQFNLVNRLSVLENVLIGALGSTPFwrtcFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 137 MVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLVR-VLADRGLAVVMTTHQPNHALAVADTaLLMLPEGAVF-GPCHE 214
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRdINQNDGITVVVTLHQVDYALRYCER-IVALRQGHVFyDGSSQ 238
|
250
....*....|.
gi 500071482 215 ALTETRIEMLY 225
Cdd:PRK09984 239 QFDNERFDHLY 249
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
23-187 |
1.72e-15 |
|
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: 73.14 E-value: 1.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGtaaLVPQDFARAFPYRVidMVLMGRA--------- 93
Cdd:cd03267 38 KGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG---LVPWKRRKKFLRRI--GVVFGQKtqlwwdlpv 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 94 -------RHIglLRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQD 166
Cdd:cd03267 113 idsfyllAAI--YDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQE 190
|
170 180
....*....|....*....|..
gi 500071482 167 RVLRLVRVL-ADRGLAVVMTTH 187
Cdd:cd03267 191 NIRNFLKEYnRERGTTVLLTSH 212
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
17-202 |
2.30e-15 |
|
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: 72.29 E-value: 2.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 17 GTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAG-----------TAALVPQDFArAFP-YRV 84
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdvtdlppkdrDIAMVFQNYA-LYPhMTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 85 IDMVLMGrarhiglLRMPGRRDREAA---MEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALD 161
Cdd:cd03301 90 YDNIAFG-------LKLRKVPKDEIDervREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 500071482 162 --LGNQDRvLRLVRVLADRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:cd03301 163 akLRVQMR-AELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVM 204
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
16-208 |
2.72e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 73.23 E-value: 2.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 16 DGTRwQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA-------------ALVPQD-FARAFP 81
Cdd:PRK13647 16 DGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREvnaenekwvrskvGLVFQDpDDQVFS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 82 YRVIDMVLMGrARHIGLLRMPGRRDREAAMEALAVIGLAGKAAERfdaLSGGQRQMVLIARAIAAEPAALFLDEPASALD 161
Cdd:PRK13647 95 STVWDDVAFG-PVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYH---LSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 500071482 162 LGNQDRVLRLVRVLADRGLAVVMTTHQPNHALAVADTaLLMLPEGAV 208
Cdd:PRK13647 171 PRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQ-VIVLKEGRV 216
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
23-188 |
2.90e-15 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 74.07 E-value: 2.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGT--AALVPQDFARAfpYRVIDMV------LMGR-- 92
Cdd:PRK11153 22 NNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQdlTALSEKELRKA--RRQIGMIfqhfnlLSSRtv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 93 ARHIGL-LRMPGRRDRE---AAMEALAVIGLAGKaAERFDA-LSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDR 167
Cdd:PRK11153 100 FDNVALpLELAGTPKAEikaRVTELLELVGLSDK-ADRYPAqLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRS 178
|
170 180
....*....|....*....|..
gi 500071482 168 VLRLVRVLADR-GLAVVMTTHQ 188
Cdd:PRK11153 179 ILELLKDINRElGLTIVLITHE 200
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
23-187 |
3.09e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 72.54 E-value: 3.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAALVPQDFARAfpyrvidmvlMGRARHIGLL--- 99
Cdd:PRK11629 26 HNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKA----------ELRNQKLGFIyqf 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 100 -------------RMP----GRRDREA---AMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASA 159
Cdd:PRK11629 96 hhllpdftalenvAMPlligKKKPAEInsrALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGN 175
|
170 180
....*....|....*....|....*....
gi 500071482 160 LDLGNQDRVLRLVRVLADR-GLAVVMTTH 187
Cdd:PRK11629 176 LDARNADSIFQLLGELNRLqGTAFLVVTH 204
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
24-202 |
3.98e-15 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 72.35 E-value: 3.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 24 DLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAG------------TAALVPQDFARAF------PYR-V 84
Cdd:COG4161 20 DINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsqkpsekAIRLLRQKVGMVFqqynlwPHLtV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 85 IDMVLMGRARhigLLRMPGRRDREAAMEALAVIGLAGKAaERFD-ALSGGQRQMVLIARAIAAEPAALFLDEPASALDLG 163
Cdd:COG4161 100 MENLIEAPCK---VLGLSKEQAREKAMKLLARLRLTDKA-DRFPlHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 500071482 164 NQDRVLRLVRVLADRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:COG4161 176 ITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYM 214
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
28-193 |
6.16e-15 |
|
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: 70.74 E-value: 6.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 28 AVAAGQVTAVLGANGCGKSTLLRVATGLR--APTRGRITVAGTAalVPQDFARAFPY-RVIDMvlmgrarHIGLLRMpgr 104
Cdd:cd03232 29 YVKPGTLTALMGESGAGKTTLLDVLAGRKtaGVITGEILINGRP--LDKNFQRSTGYvEQQDV-------HSPNLTV--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 105 rdREAamealavigLAGKAAERfdALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLVRVLADRGLAVVM 184
Cdd:cd03232 97 --REA---------LRFSALLR--GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILC 163
|
....*....
gi 500071482 185 TTHQPNHAL 193
Cdd:cd03232 164 TIHQPSASI 172
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
25-209 |
6.17e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 72.35 E-value: 6.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 25 LDFAVAAgqVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA---------------ALVPQDFARAFPYRVIDMVL 89
Cdd:PRK13638 22 LDFSLSP--VTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPldyskrgllalrqqvATVFQDPEQQIFYTDIDSDI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 90 MGRARHIGLLRMPGRRDREaamEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVL 169
Cdd:PRK13638 100 AFSLRNLGVPEAEITRRVD---EALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 500071482 170 RLVRVLADRGLAVVMTTHQPNHALAVADtALLMLPEGAVF 209
Cdd:PRK13638 177 AIIRRIVAQGNHVIISSHDIDLIYEISD-AVYVLRQGQIL 215
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
16-203 |
6.70e-15 |
|
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: 71.60 E-value: 6.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 16 DGTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGT-----------AALVPQDFArAFPY-R 83
Cdd:cd03299 9 DWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppekrdISYVPQNYA-LFPHmT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 84 VIDMVLMGrarhIGLLRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLG 163
Cdd:cd03299 88 VYKNIAYG----LKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVR 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 500071482 164 NQDRVLRLVRVLADR-GLAVVMTTHQPNHALAVADTALLML 203
Cdd:cd03299 164 TKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIML 204
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
31-240 |
9.67e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 71.67 E-value: 9.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 31 AGQVTAVLGANGCGKSTLLRV-------ATGLRapTRGRITVAGTAALVPQD-----------FARA--FPYRVIDMVLM 90
Cdd:PRK14271 46 ARAVTSLMGPTGSGKTTFLRTlnrmndkVSGYR--YSGDVLLGGRSIFNYRDvlefrrrvgmlFQRPnpFPMSIMDNVLA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 91 G-RARHIgllrMPGRRDREAAMEALAVIGLAGKAAERFD----ALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQ 165
Cdd:PRK14271 124 GvRAHKL----VPRKEFRGVAQARLTEVGLWDAVKDRLSdspfRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTT 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 166 DRVLRLVRVLADRgLAVVMTTHQPNHALAVADTALLML--------PEGAVFGPCHEALTETRIEMLYGlpvrilDVKAA 237
Cdd:PRK14271 200 EKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFdgrlveegPTEQLFSSPKHAETARYVAGLSG------DVKDA 272
|
...
gi 500071482 238 DRG 240
Cdd:PRK14271 273 KRG 275
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
16-231 |
1.93e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 71.03 E-value: 1.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 16 DGTRwQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTaalvPQDFARA---------------- 79
Cdd:PRK13636 17 DGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGK----PIDYSRKglmklresvgmvfqdp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 80 ----FPYRVIDMVLMGRARhiglLRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDE 155
Cdd:PRK13636 92 dnqlFSASVYQDVSFGAVN----LKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDE 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500071482 156 PASALDLGNQDRVLRLVRVLADR-GLAVVMTTHQPNHALAVADTALLMLPEGAVF-GPCHEALTETriEMLYGLPVRI 231
Cdd:PRK13636 168 PTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILqGNPKEVFAEK--EMLRKVNLRL 243
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
31-187 |
2.22e-14 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 70.60 E-value: 2.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 31 AGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA---------ALVPQDFARAFPYRV-IDMV------------ 88
Cdd:COG4598 33 KGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEirlkpdrdgELVPADRRQLQRIRTrLGMVfqsfnlwshmtv 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 89 ---LMGRARHIglLRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQ 165
Cdd:COG4598 113 lenVIEAPVHV--LGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELV 190
|
170 180
....*....|....*....|..
gi 500071482 166 DRVLRLVRVLADRGLAVVMTTH 187
Cdd:COG4598 191 GEVLKVMRDLAEEGRTMLVVTH 212
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
23-202 |
2.31e-14 |
|
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: 69.70 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAALV-PQDFARAFPYRVIDMVLMGR------ARH 95
Cdd:cd03266 22 DGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKePAEARRRLGFVSDSTGLYDRltarenLEY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 96 IGLLRMPGRRDREAAMEALA-VIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLVRV 174
Cdd:cd03266 102 FAGLYGLKGDELTARLEELAdRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQ 181
|
170 180
....*....|....*....|....*...
gi 500071482 175 LADRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:cd03266 182 LRALGKCILFSTHIMQEVERLCDRVVVL 209
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
16-202 |
2.68e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 70.49 E-value: 2.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 16 DGTRwQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAG---------------TAALV---PQDfa 77
Cdd:PRK13639 13 DGTE-ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepikydkksllevrkTVGIVfqnPDD-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 78 RAFPYRVIDMVLMGRARhiglLRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPA 157
Cdd:PRK13639 90 QLFAPTVEEDVAFGPLN----LGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPT 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 500071482 158 SALDLGNQDRVLRLVRVLADRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:PRK13639 166 SGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVM 210
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
24-202 |
3.12e-14 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 69.66 E-value: 3.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 24 DLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA------------ALVPQDFARAF------PY-RV 84
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdfsktpsdkaiRELRRNVGMVFqqynlwPHlTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 85 IDMVLMGRARHIGLLRmpgRRDREAAMEALAVIGLAGKAaERFD-ALSGGQRQMVLIARAIAAEPAALFLDEPASALDLG 163
Cdd:PRK11124 100 QQNLIEAPCRVLGLSK---DQALARAEKLLERLRLKPYA-DRFPlHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 500071482 164 NQDRVLRLVRVLADRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:PRK11124 176 ITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYM 214
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
23-202 |
3.34e-14 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 69.48 E-value: 3.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGtaalvpQDFARAFPYRvidmvlmgRARHiGLLRMP 102
Cdd:TIGR03410 17 RGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDG------EDITKLPPHE--------RARA-GIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 103 GRRD-------REAAMEALAVIGLAGKAA-----ERFDA-----------LSGGQRQMVLIARAIAAEPAALFLDEPASA 159
Cdd:TIGR03410 82 QGREifprltvEENLLTGLAALPRRSRKIpdeiyELFPVlkemlgrrggdLSGGQQQQLAIARALVTRPKLLLLDEPTEG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 500071482 160 L------DLGnqdRVLRLVRvlADRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:TIGR03410 162 IqpsiikDIG---RVIRRLR--AEGGMAILLVEQYLDFARELADRYYVM 205
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
23-199 |
4.87e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 70.83 E-value: 4.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAG--------TAAL------VPQDFARAFPYRVIDMV 88
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpvrirspRDAIalgigmVHQHFMLVPNLTVAENI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 89 LMGRARhigllRMPGRRDREAAMEALAVIglagkaAERF------DA----LSGGQRQMVLIARAIAAEPAALFLDEPAS 158
Cdd:COG3845 102 VLGLEP-----TKGGRLDRKAARARIREL------SERYgldvdpDAkvedLSVGEQQRVEILKALYRGARILILDEPTA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 500071482 159 ALDLGNQDRVLRLVRVLADRGLAVVMTTHQPNHALAVADTA 199
Cdd:COG3845 171 VLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRV 211
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
23-202 |
7.48e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 70.06 E-value: 7.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGT-----------------AALVPQDFARAFPYRVI 85
Cdd:PRK10070 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVdiakisdaelrevrrkkIAMVFQSFALMPHMTVL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 86 DMVLMGrarhIGLLRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALD-LGN 164
Cdd:PRK10070 125 DNTAFG----MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDpLIR 200
|
170 180 190
....*....|....*....|....*....|....*...
gi 500071482 165 QDRVLRLVRVLADRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:PRK10070 201 TEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIM 238
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
24-187 |
9.88e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 69.47 E-value: 9.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 24 DLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA------------ALVPQ--DFARAFPYRViDMVL 89
Cdd:PRK13536 59 GLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPvpararlarariGVVPQfdNLDLEFTVRE-NLLV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 90 MGRarhigLLRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVL 169
Cdd:PRK13536 138 FGR-----YFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIW 212
|
170
....*....|....*...
gi 500071482 170 RLVRVLADRGLAVVMTTH 187
Cdd:PRK13536 213 ERLRSLLARGKTILLTTH 230
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
22-173 |
1.10e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 69.84 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 22 FRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITV--AGTAALVPQDfarafPYrvidMVLmgrarhiGLL 99
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpaGARVLFLPQR-----PY----LPL-------GTL 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 100 R-------MPGRRDREAAMEALAVIGLaGKAAERFDA-------LSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQ 165
Cdd:COG4178 443 ReallypaTAEAFSDAELREALEAVGL-GHLAERLDEeadwdqvLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENE 521
|
....*...
gi 500071482 166 DRVLRLVR 173
Cdd:COG4178 522 AALYQLLR 529
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
23-188 |
1.25e-13 |
|
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: 68.28 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAG--TAALVPQDFARAFPYRVIDMVLMGR--ARHIGL 98
Cdd:cd03252 19 DNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdLALADPAWLRRQVGVVLQENVLFNRsiRDNIAL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 99 LR--MPGRRDREAAMEALA-------VIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALD-------L 162
Cdd:cd03252 99 ADpgMSMERVIEAAKLAGAhdfiselPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDyesehaiM 178
|
170 180
....*....|....*....|....*...
gi 500071482 163 GNQDRVL--RLVRVLADRgLAVVMTTHQ 188
Cdd:cd03252 179 RNMHDICagRTVIIIAHR-LSTVKNADR 205
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
23-218 |
1.53e-13 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 69.68 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGtAALV---PQDFARAFPYRVIDMVLMGRARHIGLL 99
Cdd:TIGR01842 335 RGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDG-ADLKqwdRETFGKHIGYLPQDVELFPGTVAENIA 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 100 RMPGRRDREAAMEA--LA---------------VIGLAGKAaerfdaLSGGQRQMVLIARAIAAEPAALFLDEPASALDL 162
Cdd:TIGR01842 414 RFGENADPEKIIEAakLAgvhelilrlpdgydtVIGPGGAT------LSGGQRQRIALARALYGDPKLVVLDEPNSNLDE 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 500071482 163 GNQDRVLRLVRVLADRGLAVVMTTHQPNhALAVADTaLLMLPEG--AVFGPCHEALTE 218
Cdd:TIGR01842 488 EGEQALANAIKALKARGITVVVITHRPS-LLGCVDK-ILVLQDGriARFGERDEVLAK 543
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
32-216 |
2.19e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 69.31 E-value: 2.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 32 GQVTAVLGANGCGKSTLLRVATGLRAP---TRGRITVAGTA----------ALVPQD--FaraFPYRVIDMVLMGRARhi 96
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPidakemraisAYVQQDdlF---IPTLTVREHLMFQAH-- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 97 glLRMP------GRRDR-EAAMEALA-------VIGLAGkaaeRFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDL 162
Cdd:TIGR00955 126 --LRMPrrvtkkEKRERvDEVLQALGlrkcantRIGVPG----RVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDS 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 500071482 163 GNQDRVLRLVRVLADRGLAVVMTTHQPNHALAVADTALLMLPEGAV--FGPCHEAL 216
Cdd:TIGR00955 200 FMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVayLGSPDQAV 255
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
22-190 |
3.36e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 66.52 E-value: 3.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 22 FRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTrgriTVAGTAALVPQDFARAFPyrVIDMVLMgrarhigllrm 101
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGT----PVAGCVDVPDNQFGREAS--LIDAIGR----------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 102 pgRRDREAAMEALAVIGLAGKAA--ERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLVRVLADR- 178
Cdd:COG2401 109 --KGDFKDAVELLNAVGLSDAVLwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRa 186
|
170
....*....|..
gi 500071482 179 GLAVVMTTHQPN 190
Cdd:COG2401 187 GITLVVATHHYD 198
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
6-187 |
6.02e-13 |
|
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: 66.10 E-value: 6.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 6 IRAEGAAHSWDGTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAG-------------TAALV 72
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirevtldslrrAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 73 PQD---FARAFPYRV---------IDMVLMGRARHIG--LLRMPGrrdreaamealaviGLAGKAAERFDALSGGQRQMV 138
Cdd:cd03253 81 PQDtvlFNDTIGYNIrygrpdatdEEVIEAAKAAQIHdkIMRFPD--------------GYDTIVGERGLKLSGGEKQRV 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 500071482 139 LIARAIAAEPAALFLDEPASALDLGNQDRVLR-LVRVLADRglAVVMTTH 187
Cdd:cd03253 147 AIARAILKNPPILLLDEATSALDTHTEREIQAaLRDVSKGR--TTIVIAH 194
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
2-203 |
7.55e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 65.64 E-value: 7.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 2 AEPLIRAEGAAHSWDGTRwQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAALVPQdfarafp 81
Cdd:PRK13543 8 APPLLAAHALAFSRNEEP-VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 82 yrvidmvlmgRARHIGLLR--------------------MPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIA 141
Cdd:PRK13543 80 ----------RSRFMAYLGhlpglkadlstlenlhflcgLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500071482 142 RAIAAEPAALFLDEPASALDLGNQDRVLRLVRVLADRGLAVVMTTHQPNHALAVAdTALLML 203
Cdd:PRK13543 150 RLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHLRGGGAALVTTHGAYAAPPVR-TRMLTL 210
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
6-187 |
1.02e-12 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 67.11 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 6 IRAEGAAHSWDGTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA-------------ALV 72
Cdd:COG1132 340 IEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDirdltleslrrqiGVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 73 PQD---FARAfpyrVIDMVLMGRarhigllrmPGRRD---REAAMEALA--VI-----GLAGKAAERFDALSGGQRQM-- 137
Cdd:COG1132 420 PQDtflFSGT----IRENIRYGR---------PDATDeevEEAAKAAQAheFIealpdGYDTVVGERGVNLSGGQRQRia 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500071482 138 ----------VLIaraiaaepaalfLDEPASALDLGNQDRVLR-LVRVLADRglAVVMTTH 187
Cdd:COG1132 487 iarallkdppILI------------LDEATSALDTETEALIQEaLERLMKGR--TTIVIAH 533
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
23-192 |
1.04e-12 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 67.06 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGT----------AALVPQDFARAFP-YRVIDMVLMG 91
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQdvatldadalAQLRREHFGFIFQrYHLLSHLTAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 92 R-----ARHIGLLRmpgRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQD 166
Cdd:PRK10535 105 QnvevpAVYAGLER---KQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGE 181
|
170 180
....*....|....*....|....*.
gi 500071482 167 RVLRLVRVLADRGLAVVMTTHQPNHA 192
Cdd:PRK10535 182 EVMAILHQLRDRGHTVIIVTHDPQVA 207
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
24-202 |
1.06e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 66.30 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 24 DLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVA--------------------GTAALVPQdfARAFPYR 83
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGdivvsstskqkeikpvrkkvGVVFQFPE--SQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 84 VIDMVLMGrARHIGLLRMPGRRdreAAMEALAVIGLAGKAAER--FDaLSGGQRQMVLIARAIAAEPAALFLDEPASALD 161
Cdd:PRK13643 102 VLKDVAFG-PQNFGIPKEKAEK---IAAEKLEMVGLADEFWEKspFE-LSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 500071482 162 LGNQDRVLRLVRVLADRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:PRK13643 177 PKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLL 217
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
29-211 |
1.14e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 67.44 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 29 VAAGQVTAVLGANGCGKSTLL-----RVATGLraPTRGRITVAGTaalvPQD--FARAFPYRVIDMVLMGRA------RH 95
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLnvlaeRVTTGV--ITGGDRLVNGR----PLDssFQRSIGYVQQQDLHLPTStvreslRF 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 96 IGLLRMPGRRDREAAME--------------ALAVIGLAGkaaerfDALSGGQRQMVLIARAIAAEPAAL-FLDEPASAL 160
Cdd:TIGR00956 860 SAYLRQPKSVSKSEKMEyveevikllemesyADAVVGVPG------EGLNVEQRKRLTIGVELVAKPKLLlFLDEPTSGL 933
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 500071482 161 DLGNQDRVLRLVRVLADRGLAVVMTTHQPNHALAVADTALLMLPEG---AVFGP 211
Cdd:TIGR00956 934 DSQTAWSICKLMRKLADHGQAILCTIHQPSAILFEEFDRLLLLQKGgqtVYFGD 987
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-209 |
1.17e-12 |
|
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: 65.26 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 6 IRAEGAAHSWdGTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGT----------AAL---- 71
Cdd:cd03218 1 LRAENLSKRY-GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQditklpmhkrARLgigy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 72 VPQDfARAFPYRVIDMVLMGRARHIGLLRMPGRRDREAAMEALAVIGLAGKAAerfDALSGGQRQMVLIARAIAAEPAAL 151
Cdd:cd03218 80 LPQE-ASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKA---SSLSGGERRRVEIARALATNPKFL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 500071482 152 FLDEPASALD-LGNQDrVLRLVRVLADRGLAVVMTTHQPNHALAVADTALLMLpEGAVF 209
Cdd:cd03218 156 LLDEPFAGVDpIAVQD-IQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIY-EGKVL 212
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
24-187 |
1.27e-12 |
|
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: 66.63 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 24 DLDFAVAAGQVTAVLGANGCGKSTLLRVATGLrAPTRGRITVAGT-------AALVP---------QDfarafPY----- 82
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQdldglsrRALRPlrrrmqvvfQD-----PFgslsp 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 83 --RVIDMVLMG-RARHIGLlrmpGRRDREA-AMEALAVIGLAGKAAERF-DALSGGQRQMVLIARAIAAEPAALFLDEPA 157
Cdd:COG4172 378 rmTVGQIIAEGlRVHGPGL----SAAERRArVAEALEEVGLDPAARHRYpHEFSGGQRQRIAIARALILEPKLLVLDEPT 453
|
170 180 190
....*....|....*....|....*....|.
gi 500071482 158 SALDLGNQDRVLRLVRVL-ADRGLAVVMTTH 187
Cdd:COG4172 454 SALDVSVQAQILDLLRDLqREHGLAYLFISH 484
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
17-72 |
1.30e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 65.49 E-value: 1.30e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 500071482 17 GTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGT-AALV 72
Cdd:COG1134 37 EEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRvSALL 93
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-162 |
2.04e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 66.24 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 4 PLIRAEGAAHSWDGtRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAAL--VPQDFARAFP 81
Cdd:COG0488 314 KVLELEGLSKSYGD-KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIgyFDQHQEELDP 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 82 -YRVIDMVLMGrarhigllrMPGRRDREaAMEALAVIGLAGKAAERF-DALSGGQRQMVLIARAIAAEPAALFLDEPASA 159
Cdd:COG0488 393 dKTVLDELRDG---------APGGTEQE-VRGYLGRFLFSGDDAFKPvGVLSGGEKARLALAKLLLSPPNVLLLDEPTNH 462
|
...
gi 500071482 160 LDL 162
Cdd:COG0488 463 LDI 465
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
5-187 |
2.12e-12 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 64.51 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 5 LIRAEGAAHSWDGTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAALVPQDFARAFPYRV 84
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 85 IDMV------LMGRARHIGLlRMP-------GRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAAL 151
Cdd:PRK10908 81 IGMIfqdhhlLMDRTVYDNV-AIPliiagasGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 500071482 152 FLDEPASALDLGNQDRVLRLVRVLADRGLAVVMTTH 187
Cdd:PRK10908 160 LADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATH 195
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
24-202 |
2.41e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 65.21 E-value: 2.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 24 DLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAP---TRGRITVAGT-------------AALVPQDFARAF-PYRVID 86
Cdd:PRK13640 25 DISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGItltaktvwdirekVGIVFQNPDNQFvGATVGD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 87 MVLMG---RArhigllrMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLG 163
Cdd:PRK13640 105 DVAFGlenRA-------VPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 500071482 164 NQDRVLRLVRVLA-DRGLAVVMTTHQPNHAlAVADTALLM 202
Cdd:PRK13640 178 GKEQILKLIRKLKkKNNLTVISITHDIDEA-NMADQVLVL 216
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
6-161 |
3.62e-12 |
|
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: 63.78 E-value: 3.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 6 IRAEGAAHSWDGTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA-------------ALV 72
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDirdisrkslrsmiGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 73 PQDfARAFPYRVIDMVLMGRarhigllrmPGRRDREAAMEALAV-----I-----GLAGKAAERFDALSGGQRQMVLIAR 142
Cdd:cd03254 83 LQD-TFLFSGTIMENIRLGR---------PNATDEEVIEAAKEAgahdfImklpnGYDTVLGENGGNLSQGERQLLAIAR 152
|
170
....*....|....*....
gi 500071482 143 AIAAEPAALFLDEPASALD 161
Cdd:cd03254 153 AMLRDPKILILDEATSNID 171
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
25-197 |
3.70e-12 |
|
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: 65.81 E-value: 3.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 25 LDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAALVPQDFARAF----PYRVIDMVLMGRARHIGLL- 99
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSlgmcPQHNILFHHLTVAEHILFYa 1028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 100 RMPGRRDREAAMEALAVI---GLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLvrVLA 176
Cdd:TIGR01257 1029 QLKGRSWEEAQLEMEAMLedtGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDL--LLK 1106
|
170 180
....*....|....*....|..
gi 500071482 177 DR-GLAVVMTTHQPNHALAVAD 197
Cdd:TIGR01257 1107 YRsGRTIIMSTHHMDEADLLGD 1128
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
17-202 |
3.92e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 64.47 E-value: 3.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 17 GTRWQFRDLD---FAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAG-----------------TAALVPQdF 76
Cdd:PRK13641 15 GTPMEKKGLDnisFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnknlkklrkKVSLVFQ-F 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 77 ARA--FPYRVIDMVLMGrARHIGLLRmpgRRDREAAMEALAVIGLAGKAAER--FDaLSGGQRQMVLIARAIAAEPAALF 152
Cdd:PRK13641 94 PEAqlFENTVLKDVEFG-PKNFGFSE---DEAKEKALKWLKKVGLSEDLISKspFE-LSGGQMRRVAIAGVMAYEPEILC 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 500071482 153 LDEPASALDLGNQDRVLRLVRVLADRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:PRK13641 169 LDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVL 218
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
24-202 |
4.72e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 64.38 E-value: 4.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 24 DLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA-----------------ALVPQdFARA--FPYRV 84
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLitstsknkdikqirkkvGLVFQ-FPESqlFEETV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 85 IDMVLMGrARHIGLlrmpGRRDREA-AMEALAVIGLAGKAAER--FDaLSGGQRQMVLIARAIAAEPAALFLDEPASALD 161
Cdd:PRK13649 104 LKDVAFG-PQNFGV----SQEEAEAlAREKLALVGISESLFEKnpFE-LSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 500071482 162 LGNQDRVLRLVRVLADRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:PRK13649 178 PKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVL 218
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
3-209 |
5.42e-12 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 63.51 E-value: 5.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 3 EPLIRAEGAAHSWdGTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGtaalvpQDFARAFPY 82
Cdd:COG1137 1 MMTLEAENLVKSY-GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDG------EDITHLPMH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 83 RvidmvlmgRARH-IGLL----------------------RMPGRRDREAAMEAL-AVIGLAGKAAERFDALSGGQRQMV 138
Cdd:COG1137 74 K--------RARLgIGYLpqeasifrkltvednilavlelRKLSKKEREERLEELlEEFGITHLRKSKAYSLSGGERRRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500071482 139 LIARAIAAEPAALFLDEPASALD-LGNQDrVLRLVRVLADRGLAVVMTTHQPNHALAVADTALLMLpEGAVF 209
Cdd:COG1137 146 EIARALATNPKFILLDEPFAGVDpIAVAD-IQKIIRHLKERGIGVLITDHNVRETLGICDRAYIIS-EGKVL 215
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-198 |
5.45e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.95 E-value: 5.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 1 MAEPLIRAEGAAHSWDGTRwQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATG-----------------LRAPTRGRI 63
Cdd:PRK13549 1 MMEYLLEMKNITKTFGGVK-ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvyphgtyegeiifegeeLQASNIRDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 64 TVAGTA------ALVPQdfarafpYRVIDMVLMGRARHIGllrmpGRRDREA----AMEALAVIGLAGKAAERFDALSGG 133
Cdd:PRK13549 80 ERAGIAiihqelALVKE-------LSVLENIFLGNEITPG-----GIMDYDAmylrAQKLLAQLKLDINPATPVGNLGLG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500071482 134 QRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLVRVLADRGLAVVMTTHQPNHALAVADT 198
Cdd:PRK13549 148 QQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDT 212
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
16-68 |
9.34e-12 |
|
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: 62.55 E-value: 9.34e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 500071482 16 DGTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGT 68
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR 84
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-223 |
1.53e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 62.37 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 22 FRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAALVPQDFARAFPYRVIDMVLMGRAR-----HI 96
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQpnpfpHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 97 GL-------LRMPGRRD----REAAMEALAVIGLAGKAAERFDA----LSGGQRQMVLIARAIAAEPAALFLDEPASALD 161
Cdd:PRK14246 106 SIydniaypLKSHGIKEkreiKKIVEECLRKVGLWKEVYDRLNSpasqLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500071482 162 LGNQDRVLRLVRVLADRgLAVVMTTHQPNHALAVAD-TALLMLPEGAVFGPCHEALTETRIEM 223
Cdd:PRK14246 186 IVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADyVAFLYNGELVEWGSSNEIFTSPKNEL 247
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
23-189 |
2.89e-11 |
|
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: 60.25 E-value: 2.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAAL--VPQDfarafPYrvidmvlMGRarhiGLLR 100
Cdd:cd03223 18 KDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLlfLPQR-----PY-------LPL----GTLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 101 mpgrrdreaamEALAviglagkaaerF---DALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLVRvlaD 177
Cdd:cd03223 82 -----------EQLI-----------YpwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLK---E 136
|
170
....*....|..
gi 500071482 178 RGLAVVMTTHQP 189
Cdd:cd03223 137 LGITVISVGHRP 148
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
24-210 |
3.69e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 61.57 E-value: 3.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 24 DLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVaGTAALVPQDFARAF-PYRvidmvlmgraRHIGLL-RM 101
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKKNKKLkPLR----------KKVGIVfQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 102 P--------------------GRRDREA---AMEALAVIGLAGKAAER--FDaLSGGQRQMVLIARAIAAEPAALFLDEP 156
Cdd:PRK13634 94 PehqlfeetvekdicfgpmnfGVSEEDAkqkAREMIELVGLPEELLARspFE-LSGGQMRRVAIAGVLAMEPEVLVLDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 500071482 157 ASALD-LGNQDRVLRLVRVLADRGLAVVMTTHQPNHALAVADTALLMlPEGAVFG 210
Cdd:PRK13634 173 TAGLDpKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVM-HKGTVFL 226
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
6-202 |
4.50e-11 |
|
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: 60.18 E-value: 4.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 6 IRAEGAAHSWDGTRWQ----FRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAALVPQdFARAFP 81
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsftLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQ-EPWIQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 82 YRVIDMVLMGRarhigllrmPGRRDR-EAAMEA--------------LAVIGlagkaaERFDALSGGQRQMVLIARAIAA 146
Cdd:cd03250 80 GTIRENILFGK---------PFDEERyEKVIKAcalepdleilpdgdLTEIG------EKGINLSGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 147 EPAALFLDEPASALD--LGNQ--DRVLRlvRVLADrGLAVVMTTHQPnHALAVADTALLM 202
Cdd:cd03250 145 DADIYLLDDPLSAVDahVGRHifENCIL--GLLLN-NKTRILVTHQL-QLLPHADQIVVL 200
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
23-187 |
4.91e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 60.87 E-value: 4.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAP----TRGRITVAG-----------TAALVPQDFARAF-PYRVId 86
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGkpvapcalrgrKIATIMQNPRSAFnPLHTM- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 87 mvlmgRARHIGLLRMPGRRDREAAM-EALAVIGL--AGKAAERFD-ALSGGQRQMVLIARAIAAEPAALFLDEPASALDL 162
Cdd:PRK10418 99 -----HTHARETCLALGKPADDATLtAALEAVGLenAARVLKLYPfEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDV 173
|
170 180
....*....|....*....|....*.
gi 500071482 163 GNQDRVLRLV-RVLADRGLAVVMTTH 187
Cdd:PRK10418 174 VAQARILDLLeSIVQKRALGMLLVTH 199
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
18-208 |
9.45e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 60.41 E-value: 9.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 18 TRWQFRDLD---FAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRiTVAGtaalvpqDFARAFPYRVIDMVLMGRaR 94
Cdd:PRK13645 20 TPFEFKALNntsLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQ-TIVG-------DYAIPANLKKIKEVKRLR-K 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 95 HIGLL-RMP--------------------GRRDREAAM---EALAVIGLAGKAAER--FDaLSGGQRQMVLIARAIAAEP 148
Cdd:PRK13645 91 EIGLVfQFPeyqlfqetiekdiafgpvnlGENKQEAYKkvpELLKLVQLPEDYVKRspFE-LSGGQKRRVALAGIIAMDG 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500071482 149 AALFLDEPASALD-LGNQDRVLRLVRVLADRGLAVVMTTHQPNHALAVADTALLMlPEGAV 208
Cdd:PRK13645 170 NTLVLDEPTGGLDpKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVM-HEGKV 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-187 |
9.57e-11 |
|
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: 61.24 E-value: 9.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 1 MAEPLIRAEG---AAHSWDGTRWQFRDLDFAVAAGQVTAVLGANGCGKS----TLLRVATGLRAPTRGRITVAGTAAL-V 72
Cdd:COG4172 2 MSMPLLSVEDlsvAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLgL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 73 PQDFARAFPYRVIDMV----------LMGRARHIG--LL---RMPGRRDREAAMEALAVIGLAgKAAERFDA----LSGG 133
Cdd:COG4172 82 SERELRRIRGNRIAMIfqepmtslnpLHTIGKQIAevLRlhrGLSGAAARARALELLERVGIP-DPERRLDAyphqLSGG 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 500071482 134 QRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLVRVL-ADRGLAVVMTTH 187
Cdd:COG4172 161 QRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLITH 215
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-187 |
9.64e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 60.59 E-value: 9.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 1 MAEPLIRAEGAAHSWdGTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGT------------ 68
Cdd:PRK13537 3 MSVAPIDFRNVEKRY-GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEpvpsrarharqr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 69 AALVPQdFARAFPYRVIDMVLMGRARHIGllrMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEP 148
Cdd:PRK13537 82 VGVVPQ-FDNLDPDFTVRENLLVFGRYFG---LSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDP 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 500071482 149 AALFLDEPASALDLGNQDRVLRLVRVLADRGLAVVMTTH 187
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTH 196
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-184 |
1.01e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 61.19 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 2 AEPLIRAEGAahSWDGtrwQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA------------ 69
Cdd:COG1129 253 GEVVLEVEGL--SVGG---VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPvrirsprdaira 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 70 --ALVPQDfarafpyR-----VIDM--------VLMGRARHIGLLRmpGRRDREAA---MEALAViglagKAAERFDA-- 129
Cdd:COG1129 328 giAYVPED-------RkgeglVLDLsirenitlASLDRLSRGGLLD--RRRERALAeeyIKRLRI-----KTPSPEQPvg 393
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 500071482 130 -LSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLVRVLADRGLAVVM 184
Cdd:COG1129 394 nLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIV 449
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
20-202 |
1.03e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 60.63 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 20 WQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAALVPQDFARAFPY-------------RVID 86
Cdd:PRK13631 40 VALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELITNpyskkiknfkelrRRVS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 87 MVLM---------GRARHIGL----LRMPGRRDREAAMEALAVIGLAGKAAER--FDaLSGGQRQMVLIARAIAAEPAAL 151
Cdd:PRK13631 120 MVFQfpeyqlfkdTIEKDIMFgpvaLGVKKSEAKKLAKFYLNKMGLDDSYLERspFG-LSGGQKRRVAIAGILAIQPEIL 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 500071482 152 FLDEPASALDLGNQDRVLRLVRVLADRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:PRK13631 199 IFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVM 249
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
23-173 |
1.17e-10 |
|
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: 59.41 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAAlvpQDFARAFPYRVIDMV-----LMGR--ARH 95
Cdd:cd03248 31 QDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPI---SQYEHKYLHSKVSLVgqepvLFARslQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 96 I--GLLRMPGRRDREAAMEALA-------VIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQD 166
Cdd:cd03248 108 IayGLQSCSFECVKEAAQKAHAhsfiselASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQ 187
|
....*..
gi 500071482 167 RVLRLVR 173
Cdd:cd03248 188 QVQQALY 194
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
24-175 |
1.23e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.80 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 24 DLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRaptrgritvagtaalvPQDFARafpyrviDMVLMGRAR--------- 94
Cdd:PRK10938 278 NLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDH----------------PQGYSN-------DLTLFGRRRgsgetiwdi 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 95 --HIGL----LRMPGR-------------------------RDREAAMEALAVIGLAGKAAER-FDALSGGQRQMVLIAR 142
Cdd:PRK10938 335 kkHIGYvsssLHLDYRvstsvrnvilsgffdsigiyqavsdRQQKLAQQWLDILGIDKRTADApFHSLSWGQQRLALIVR 414
|
170 180 190
....*....|....*....|....*....|...
gi 500071482 143 AIAAEPAALFLDEPASALDLGNQDRVLRLVRVL 175
Cdd:PRK10938 415 ALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVL 447
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
24-209 |
1.92e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 59.38 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 24 DLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRItVAGTAALVPQDFARAfpyrvidmvlmgrARHIGLL---- 99
Cdd:PRK13648 27 DVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEI-FYNNQAITDDNFEKL-------------RKHIGIVfqnp 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 100 --------------------RMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASA 159
Cdd:PRK13648 93 dnqfvgsivkydvafglenhAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSM 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 500071482 160 LDLGNQDRVLRLVR-VLADRGLAVVMTTHQPNHALAvADTaLLMLPEGAVF 209
Cdd:PRK13648 173 LDPDARQNLLDLVRkVKSEHNITIISITHDLSEAME-ADH-VIVMNKGTVY 221
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
16-202 |
2.71e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 58.97 E-value: 2.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 16 DGTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAG--------------------------TA 69
Cdd:PRK13650 17 DQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGdllteenvwdirhkigmvfqnpdnqfVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 70 ALVPQDFARAFPYRVIDMVLMgrarhigllrmpgrrdREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPA 149
Cdd:PRK13650 97 ATVEDDVAFGLENKGIPHEEM----------------KERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 500071482 150 ALFLDEPASALDLGNQDRVLRLVRVLADR-GLAVVMTTHQPNHaLAVADTALLM 202
Cdd:PRK13650 161 IIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDE-VALSDRVLVM 213
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-218 |
3.07e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 58.70 E-value: 3.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 13 HSWDGTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGL-----RAPTRGRITVAGTAALVPQ------------- 74
Cdd:PRK14267 11 RVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDvdpievrrevgmv 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 75 -DFARAFPYRVI-DMVLMGrARHIGLLRMPGRRDrEAAMEALAVIGLAGKAAERFD----ALSGGQRQMVLIARAIAAEP 148
Cdd:PRK14267 91 fQYPNPFPHLTIyDNVAIG-VKLNGLVKSKKELD-ERVEWALKKAALWDEVKDRLNdypsNLSGGQRQRLVIARALAMKP 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500071482 149 AALFLDEPASALDLGNQDRVLRLVRVLADRgLAVVMTTHQPNHALAVAD-TALLML-------PEGAVF-GPCHEaLTE 218
Cdd:PRK14267 169 KILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDyVAFLYLgklievgPTRKVFeNPEHE-LTE 245
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
28-207 |
3.15e-10 |
|
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: 60.03 E-value: 3.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 28 AVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAAL-----VPQDFARAFPYRVIDMVLMGRaRHIGL---L 99
Cdd:TIGR01257 1961 GVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILtnisdVHQNMGYCPQFDAIDDLLTGR-EHLYLyarL 2039
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 100 R-MPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLVRVLADR 178
Cdd:TIGR01257 2040 RgVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE 2119
|
170 180
....*....|....*....|....*....
gi 500071482 179 GLAVVMTTHQPNHALAVAdTALLMLPEGA 207
Cdd:TIGR01257 2120 GRAVVLTSHSMEECEALC-TRLAIMVKGA 2147
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
32-216 |
4.76e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 59.12 E-value: 4.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 32 GQVTAVLGANGCGKSTLLRVATGL--------------RAPTRGRITVAGtaaLVPQDfARAFPYRVIDMVLMgrarHIG 97
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRiqgnnftgtilannRKPTKQILKRTG---FVTQD-DILYPHLTVRETLV----FCS 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 98 LLRMPGRRDRE----AAMEALAVIGLA-------GKAAERfdALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQD 166
Cdd:PLN03211 166 LLRLPKSLTKQekilVAESVISELGLTkcentiiGNSFIR--GISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAY 243
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 500071482 167 RVLRLVRVLADRGLAVVMTTHQPNHALAVADTALLMLPEGAV--FGPCHEAL 216
Cdd:PLN03211 244 RLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRClfFGKGSDAM 295
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
17-200 |
5.04e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 58.20 E-value: 5.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 17 GTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRI--TVAGTAALVPQDFArafpyrvIDMVLMGRAR 94
Cdd:PRK09544 15 GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIkrNGKLRIGYVPQKLY-------LDTTLPLTVN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 95 HIGLLRmPGRRdREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLVRV 174
Cdd:PRK09544 88 RFLRLR-PGTK-KEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQ 165
|
170 180
....*....|....*....|....*..
gi 500071482 175 L-ADRGLAVVMTTHQPNHALAVADTAL 200
Cdd:PRK09544 166 LrRELDCAVLMVSHDLHLVMAKTDEVL 192
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
25-198 |
5.77e-10 |
|
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: 59.07 E-value: 5.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 25 LDFAVAAGQVTAVLGANGCGKSTLLRVATGLR-------------APTRG---RITVAGTAALVPQDFARAFPYRVIDMV 88
Cdd:TIGR02633 20 IDLEVRPGECVGLCGENGAGKSTLMKILSGVYphgtwdgeiywsgSPLKAsniRDTERAGIVIIHQELTLVPELSVAENI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 89 LMGRArhiglLRMPGRRDREAAM-----EALAVIGL-AGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDL 162
Cdd:TIGR02633 100 FLGNE-----ITLPGGRMAYNAMylrakNLLRELQLdADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTE 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 500071482 163 GNQDRVLRLVRVLADRGLAVVMTTHQPNHALAVADT 198
Cdd:TIGR02633 175 KETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDT 210
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
18-211 |
5.86e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 59.09 E-value: 5.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 18 TRWQF-RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAP--TRGRITVAGTAAlVPQDFARAF----------PYRV 84
Cdd:PLN03140 891 DRLQLlREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISGFPK-KQETFARISgyceqndihsPQVT 969
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 85 IDMVLMGRArhigLLRMPGRRDREAAM------------EAL--AVIGLAGkaaerFDALSGGQRQMVLIARAIAAEPAA 150
Cdd:PLN03140 970 VRESLIYSA----FLRLPKEVSKEEKMmfvdevmelvelDNLkdAIVGLPG-----VTGLSTEQRKRLTIAVELVANPSI 1040
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500071482 151 LFLDEPASALDLGNQDRVLRLVRVLADRGLAVVMTTHQPNHALAVA-DTALLMLPEGAVF--GP 211
Cdd:PLN03140 1041 IFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAfDELLLMKRGGQVIysGP 1104
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
23-203 |
7.08e-10 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 57.74 E-value: 7.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRV-------ATGLRapTRGRITVAGTAALVPQdfarafpyrvIDMVLMgRaRH 95
Cdd:COG1117 28 KDINLDIPENKVTALIGPSGCGKSTLLRClnrmndlIPGAR--VEGEILLDGEDIYDPD----------VDVVEL-R-RR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 96 IGL-------------------LRMPGRRDR----EAAMEALaviglagKAAERFD-----------ALSGGQRQMVLIA 141
Cdd:COG1117 94 VGMvfqkpnpfpksiydnvaygLRLHGIKSKseldEIVEESL-------RKAALWDevkdrlkksalGLSGGQQQRLCIA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500071482 142 RAIAAEPAALFLDEPASALDLGNQDRVLRLVRVLADRgLAVVMTTHQPNHALAVAD-TALLML 203
Cdd:COG1117 167 RALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDyTAFFYL 228
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
19-183 |
1.04e-09 |
|
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: 56.86 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 19 RWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA-------------ALVPQDfARAFPYRVI 85
Cdd:cd03251 15 PPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDvrdytlaslrrqiGLVSQD-VFLFNDTVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 86 DMVLMGRarhiglLRMPGRRDREAAMEALA--VI-----GLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPAS 158
Cdd:cd03251 94 ENIAYGR------PGATREEVEEAARAANAheFImelpeGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATS 167
|
170 180
....*....|....*....|....*.
gi 500071482 159 ALDLGNQDRVLR-LVRVLADRGLAVV 183
Cdd:cd03251 168 ALDTESERLVQAaLERLMKNRTTFVI 193
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
23-98 |
1.14e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 57.40 E-value: 1.14e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGtaaLVPQDFARAFpyrvidmvlmgrARHIGL 98
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG---YVPFKRRKEF------------ARRIGV 99
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
5-202 |
1.23e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 57.12 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 5 LIRAEGAAHSWDGTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAG-------------TAAL 71
Cdd:PRK13652 3 LIETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGepitkenirevrkFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 72 V---PQDfaRAFPYRVIDMVLMGRArHIGLlrmpgrrDREAAM----EALAVIGLAGKAAERFDALSGGQRQMVLIARAI 144
Cdd:PRK13652 83 VfqnPDD--QIFSPTVEQDIAFGPI-NLGL-------DEETVAhrvsSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 500071482 145 AAEPAALFLDEPASALDLGNQDRVLRLVRVLADR-GLAVVMTTHQPNHALAVADTALLM 202
Cdd:PRK13652 153 AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVM 211
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-197 |
1.42e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 56.97 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 4 PLIRAEGAAHSWDgTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLrAPTRGRITVAGTAALVPQDF------- 76
Cdd:PRK14258 6 PAIKVNNLSFYYD-TQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM-NELESEVRVEGRVEFFNQNIyerrvnl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 77 -------------ARAFPYRVIDMVLMGrarhiglLRMPGRRDReaaMEALAVIGLAGKAAERFDA-----------LSG 132
Cdd:PRK14258 84 nrlrrqvsmvhpkPNLFPMSVYDNVAYG-------VKIVGWRPK---LEIDDIVESALKDADLWDEikhkihksaldLSG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500071482 133 GQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLVRVLADRG-LAVVMTTHQPNHALAVAD 197
Cdd:PRK14258 154 GQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSeLTMVIVSHNLHQVSRLSD 219
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-202 |
1.71e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 56.44 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 5 LIRAEGAAHSWDGTRwQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITV---------------AGTA 69
Cdd:PRK10895 3 TLTAKNLAKAYKGRR-VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIddedisllplhararRGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 70 ALvPQD---FARAFPYRVIDMVLMGRARhiglLRMPGRRDR-EAAMEALAVIGLAGKAAErfdALSGGQRQMVLIARAIA 145
Cdd:PRK10895 82 YL-PQEasiFRRLSVYDNLMAVLQIRDD----LSAEQREDRaNELMEEFHIEHLRDSMGQ---SLSGGERRRVEIARALA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 500071482 146 AEPAALFLDEPASALDLGNQDRVLRLVRVLADRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:PRK10895 154 ANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIV 210
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
22-188 |
2.34e-09 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 57.04 E-value: 2.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 22 FRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGtaalVP-QDFARAFPYRVIDMV-----LMGRA-R 94
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDG----VPlVQYDHHYLHRQVALVgqepvLFSGSvR 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 95 H---IGLLRMPGRRDREAAMEALA-------VIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGN 164
Cdd:TIGR00958 573 EniaYGLTDTPDEEIMAAAKAANAhdfimefPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAEC 652
|
170 180
....*....|....*....|....
gi 500071482 165 QdRVLRLVRVLADRglAVVMTTHQ 188
Cdd:TIGR00958 653 E-QLLQESRSRASR--TVLLIAHR 673
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-197 |
2.43e-09 |
|
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: 56.22 E-value: 2.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 32 GQVTAVLGANGCGKSTLLRVATGLRAPTRGRIT-----------VAGTA------ALVPQDFARAFPYRVIDMVLMGRAR 94
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDdppdwdeildeFRGSElqnyftKLLEGDVKVIVKPQYVDLIPKAVKG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 95 HIGLLrMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLVRV 174
Cdd:cd03236 106 KVGEL-LKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRE 184
|
170 180
....*....|....*....|...
gi 500071482 175 LADRGLAVVMTTHQpnhaLAVAD 197
Cdd:cd03236 185 LAEDDNYVLVVEHD----LAVLD 203
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
8-90 |
2.48e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.82 E-value: 2.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 8 AEGAAHSWDGtRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAAL--VPQDFARAFPyrvI 85
Cdd:PRK15064 322 VENLTKGFDN-GPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIgyYAQDHAYDFE---N 397
|
....*
gi 500071482 86 DMVLM 90
Cdd:PRK15064 398 DLTLF 402
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-187 |
3.03e-09 |
|
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: 53.99 E-value: 3.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 6 IRAEGAAHSWDGtRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAalvpqdfarAFPYrvi 85
Cdd:cd03221 1 IELENLSKTYGG-KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV---------KIGY--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 86 dmvlmgrarhigllrmpgrrdreaamealaviglagkaaerFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQ 165
Cdd:cd03221 68 -----------------------------------------FEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESI 106
|
170 180
....*....|....*....|...
gi 500071482 166 DrvlRLVRVLAD-RGlAVVMTTH 187
Cdd:cd03221 107 E---ALEEALKEyPG-TVILVSH 125
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
23-222 |
3.11e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.10 E-value: 3.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAALVPQDfARAFPYRVIDMVLMGRARHIGLLRMP 102
Cdd:PTZ00243 677 RDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSIAYVPQQ-AWIMNATVRGNILFFDEEDAARLADA 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 103 GRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLVRVLADRGLAV 182
Cdd:PTZ00243 756 VRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTR 835
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 500071482 183 VMTTHQPnHALAVADTALLMLPEGAVFGPCHEALTETRIE 222
Cdd:PTZ00243 836 VLATHQV-HVVPRADYVVALGDGRVEFSGSSADFMRTSLY 874
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
14-168 |
3.69e-09 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 56.51 E-value: 3.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 14 SWDGTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAAlvpQDFARAFPYRVIDMVL---M 90
Cdd:PRK13657 343 SYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDI---RTVTRASLRRNIAVVFqdaG 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 91 GRARHIGL-LRMpGRRD------REAA--MEALAVI-----GLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEP 156
Cdd:PRK13657 420 LFNRSIEDnIRV-GRPDatdeemRAAAerAQAHDFIerkpdGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEA 498
|
170
....*....|..
gi 500071482 157 ASALDLGNQDRV 168
Cdd:PRK13657 499 TSALDVETEAKV 510
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
6-202 |
4.53e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 55.44 E-value: 4.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 6 IRAEGAAHSW-DGTRWQFRDLD---FAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAG---TAALVPQDFAR 78
Cdd:PRK13637 3 IKIENLTHIYmEGTPFEKKALDnvnIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvdiTDKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 79 -----AFPY-------RVIDMVLMGRARHIGLlrmpgrRDREAAM---EALAVIGLAG---KAAERFDaLSGGQRQMVLI 140
Cdd:PRK13637 83 kkvglVFQYpeyqlfeETIEKDIAFGPINLGL------SEEEIENrvkRAMNIVGLDYedyKDKSPFE-LSGGQKRRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500071482 141 ARAIAAEPAALFLDEPASALDLGNQDRVLRLVRVLADR-GLAVVMTTHQPNHALAVADTALLM 202
Cdd:PRK13637 156 AGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVM 218
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
25-161 |
4.88e-09 |
|
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: 56.49 E-value: 4.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 25 LDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAALVPQDfARAFPYRVIDMVLMGRArhiglLRMPGR 104
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQ-AWIQNDSLRENILFGKA-----LNEKYY 730
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500071482 105 RdreAAMEALAVI--------GLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALD 161
Cdd:TIGR00957 731 Q---QVLEACALLpdleilpsGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
20-187 |
5.04e-09 |
|
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: 54.24 E-value: 5.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 20 WQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAALVPQDFARAFpyrvidMVLMGRARHI--- 96
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSL------ISVLNQRPYLfdt 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 97 GLLRMPGRRdreaamealaviglagkaaerfdaLSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLV-RVL 175
Cdd:cd03247 90 TLRNNLGRR------------------------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIfEVL 145
|
170
....*....|..
gi 500071482 176 ADRglAVVMTTH 187
Cdd:cd03247 146 KDK--TLIWITH 155
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
21-162 |
6.65e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 55.27 E-value: 6.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 21 QFRDLDFAV-----AAGqVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA--------ALVP---------QDfAR 78
Cdd:PRK11144 9 QLGDLCLTVnltlpAQG-ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVlfdaekgiCLPPekrrigyvfQD-AR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 79 AFP-YRVIDMVLMGRARhigllRMPGRRDReaamealaVIGLAGKAA--ERFDA-LSGGQRQMVLIARAIAAEPAALFLD 154
Cdd:PRK11144 87 LFPhYKVRGNLRYGMAK-----SMVAQFDK--------IVALLGIEPllDRYPGsLSGGEKQRVAIGRALLTAPELLLMD 153
|
....*...
gi 500071482 155 EPASALDL 162
Cdd:PRK11144 154 EPLASLDL 161
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-161 |
6.88e-09 |
|
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: 55.71 E-value: 6.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 6 IRAEGAAHSWdGTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAALVPQDFARAF----- 80
Cdd:TIGR03719 323 IEAENLTKAF-GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRDAldpnk 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 81 -PYRVI----DMVLMGRArhigllRMPGRrdreaamealAVIGLAG-KAAE---RFDALSGGQRQMVLIARAIAAEPAAL 151
Cdd:TIGR03719 402 tVWEEIsgglDIIKLGKR------EIPSR----------AYVGRFNfKGSDqqkKVGQLSGGERNRVHLAKTLKSGGNVL 465
|
170
....*....|
gi 500071482 152 FLDEPASALD 161
Cdd:TIGR03719 466 LLDEPTNDLD 475
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-223 |
6.92e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 54.92 E-value: 6.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLrAPTRGRITVAGTAALVPQDFARafpyrvIDMVLMgRARHIGLLRMP 102
Cdd:PRK14247 20 DGVNLEIPDNTITALMGPSGSGKSTLLRVFNRL-IELYPEARVSGEVYLDGQDIFK------MDVIEL-RRRVQMVFQIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 103 G------------------------RRDREAAMEALAVIGLAGKAAERFDA----LSGGQRQMVLIARAIAAEPAALFLD 154
Cdd:PRK14247 92 NpipnlsifenvalglklnrlvkskKELQERVRWALEKAQLWDEVKDRLDApagkLSGGQQQRLCIARALAFQPEVLLAD 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 155 EPASALDLGNQDRVLRLVRVLaDRGLAVVMTTHQPNHALAVAD-TALLMLPEGAVFGPCHEALTETRIEM 223
Cdd:PRK14247 172 EPTANLDPENTAKIESLFLEL-KKDMTIVLVTHFPQQAARISDyVAFLYKGQIVEWGPTREVFTNPRHEL 240
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-161 |
7.06e-09 |
|
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: 55.88 E-value: 7.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 2 AEPLIRAEGAAHSWDGT-RWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA----------- 69
Cdd:TIGR02203 327 ARGDVEFRNVTFRYPGRdRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDladytlaslrr 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 70 --ALVPQDFArAFPYRVIDMVLMGRARHIGLLRMpgrRDREAAMEALAVI-----GLAGKAAERFDALSGGQRQMVLIAR 142
Cdd:TIGR02203 407 qvALVSQDVV-LFNDTIANNIAYGRTEQADRAEI---ERALAAAYAQDFVdklplGLDTPIGENGVLLSGGQRQRLAIAR 482
|
170
....*....|....*....
gi 500071482 143 AIAAEPAALFLDEPASALD 161
Cdd:TIGR02203 483 ALLKDAPILILDEATSALD 501
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-210 |
7.14e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 55.56 E-value: 7.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 32 GQVTAVLGANGCGKSTLLRVATGLRAPTRGRITV-----------AGT---------------AALVPQdfarafpYrvI 85
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGELKPNLGDYDEepswdevlkrfRGTelqdyfkklangeikVAHKPQ-------Y--V 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 86 DM---VLMGRARHigLLRmpgRRD-REAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALD 161
Cdd:COG1245 170 DLipkVFKGTVRE--LLE---KVDeRGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 500071482 162 LGNQDRVLRLVRVLADRGLAVVMTTHQpnhaLAV----ADTALLMLPEGAVFG 210
Cdd:COG1245 245 IYQRLNVARLIRELAEEGKYVLVVEHD----LAIldylADYVHILYGEPGVYG 293
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
23-197 |
7.75e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 54.79 E-value: 7.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLR-------VATGLRAptRGRITVAGTAALVPQ-D-----------FARA--FP 81
Cdd:PRK14243 27 KNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRV--EGKVTFHGKNLYAPDvDpvevrrrigmvFQKPnpFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 82 YRVIDMVLMGrARHIG----LLRMPGRRDREAAM-----EALAVIGLAgkaaerfdaLSGGQRQMVLIARAIAAEPAALF 152
Cdd:PRK14243 105 KSIYDNIAYG-ARINGykgdMDELVERSLRQAALwdevkDKLKQSGLS---------LSGGQQQRLCIARAIAVQPEVIL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 500071482 153 LDEPASALDLGNQDRVLRLVRVLADRgLAVVMTTHQPNHALAVAD 197
Cdd:PRK14243 175 MDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSD 218
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
6-188 |
8.41e-09 |
|
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: 54.26 E-value: 8.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 6 IRAEGAAHSWDGTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAALVPQDFARAFPYRVI 85
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 86 -------DMVLMGRARHIGLLRMPGRRDR-EAAMEALAV--------IGLAGKAAERFDALSGGQRQMVLIARAIAAEPA 149
Cdd:cd03290 81 vayaaqkPWLLNATVEENITFGSPFNKQRyKAVTDACSLqpdidllpFGDQTEIGERGINLSGGQRQRICVARALYQNTN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 500071482 150 ALFLDEPASALDLGNQDRVLR--LVRVLADRGLAVVMTTHQ 188
Cdd:cd03290 161 IVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHK 201
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
25-192 |
9.79e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 54.01 E-value: 9.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 25 LDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAALVPQDFARAfpyrvidmvlMGRARHIG------- 97
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARA----------KLRAKHVGfvfqsfm 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 98 ---------------LLR-MPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALD 161
Cdd:PRK10584 99 liptlnalenvelpaLLRgESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
170 180 190
....*....|....*....|....*....|..
gi 500071482 162 LGNQDRVLRLVRVL-ADRGLAVVMTTHQPNHA 192
Cdd:PRK10584 179 RQTGDKIADLLFSLnREHGTTLILVTHDLQLA 210
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
23-197 |
1.63e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 54.27 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAA--LVPQDfarafpyRVIDMVLMGRA--RHIGL 98
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMndVPPAE-------RGVGMVFQSYAlyPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 99 -------LRMPGRRDREAAM---EALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALD--LGNQD 166
Cdd:PRK11000 93 aenmsfgLKLAGAKKEEINQrvnQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaaLRVQM 172
|
170 180 190
....*....|....*....|....*....|...
gi 500071482 167 RV--LRLVRVLadrGLAVVMTTHQPNHALAVAD 197
Cdd:PRK11000 173 RIeiSRLHKRL---GRTMIYVTHDQVEAMTLAD 202
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
26-202 |
2.67e-08 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 53.07 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 26 DFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGT--AALVPQDFARAFPYR------------VIDMVLMG 91
Cdd:PRK11300 25 NLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQhiEGLPGHQIARMGVVRtfqhvrlfremtVIENLLVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 92 RARHI------GLLRMPG--RRDREA---AMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASAL 160
Cdd:PRK11300 105 QHQQLktglfsGLLKTPAfrRAESEAldrAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 500071482 161 DLGNQDRVLRLVRVLADR-GLAVVMTTHQPNHALAVADTALLM 202
Cdd:PRK11300 185 NPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVV 227
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
21-202 |
2.85e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 53.17 E-value: 2.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 21 QFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAG---TA----------ALVPQDFARAFPYRVIDM 87
Cdd:PRK13642 22 QLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGellTAenvwnlrrkiGMVFQNPDNQFVGATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 88 VLMGRARHIGLLRMPGRRDREAAMEALAVIGLAGKAAERfdaLSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDR 167
Cdd:PRK13642 102 DVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPAR---LSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQE 178
|
170 180 190
....*....|....*....|....*....|....*.
gi 500071482 168 VLRLVRVLADR-GLAVVMTTHQPNHAlAVADTALLM 202
Cdd:PRK13642 179 IMRVIHEIKEKyQLTVLSITHDLDEA-ASSDRILVM 213
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
23-203 |
3.67e-08 |
|
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: 52.14 E-value: 3.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRA--PTRGRITVAG--TAALVPQDFAR-----AFPYRV-IDMVlmgr 92
Cdd:cd03217 17 KGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGedITDLPPEERARlgiflAFQYPPeIPGV---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 93 aRHIGLLRmpgrrdreaamealaviglagkaaERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLV 172
Cdd:cd03217 93 -KNADFLR------------------------YVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVI 147
|
170 180 190
....*....|....*....|....*....|..
gi 500071482 173 RVLADRGLAVVMTTHQPNHALAV-ADTALLML 203
Cdd:cd03217 148 NKLREEGKSVLIITHYQRLLDYIkPDRVHVLY 179
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
4-169 |
3.80e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.59 E-value: 3.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 4 PLIRAEGAAHSWDGT--RWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATG-LRAPTRGRITVAGTAALVPQdFARAF 80
Cdd:PLN03130 613 PAISIKNGYFSWDSKaeRPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRGTVAYVPQ-VSWIF 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 81 PYRVIDMVLMG---------RARHIGLLR-----MPGRRDREaamealavIGlagkaaERFDALSGGQRQMVLIARAIAA 146
Cdd:PLN03130 692 NATVRDNILFGspfdperyeRAIDVTALQhdldlLPGGDLTE--------IG------ERGVNISGGQKQRVSMARAVYS 757
|
170 180 190
....*....|....*....|....*....|....*...
gi 500071482 147 EPAALFLDEPASALD---------------LGNQDRVL 169
Cdd:PLN03130 758 NSDVYIFDDPLSALDahvgrqvfdkcikdeLRGKTRVL 795
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-210 |
3.85e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.27 E-value: 3.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 32 GQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAALVPQDFARA--FPY---------RV---------IDMVLMG 91
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPSWDEVLKRFRGTelQNYfkklyngeiKVvhkpqyvdlIPKVFKG 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 92 RARHigLLRmpgRRDREAAMEALA-VIGLaGKAAER-FDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVL 169
Cdd:PRK13409 179 KVRE--LLK---KVDERGKLDEVVeRLGL-ENILDRdISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVA 252
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 500071482 170 RLVRVLA-DRGLAVVmtthqpNHALAV----ADTALLMLPEGAVFG 210
Cdd:PRK13409 253 RLIRELAeGKYVLVV------EHDLAVldylADNVHIAYGEPGAYG 292
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
33-161 |
6.64e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 52.09 E-value: 6.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 33 QVTAVLGANGCGKSTLLR------------VATG--------LRAPTRGRITVAGTAALVPQDfARAFPYRVIDMVLMGr 92
Cdd:PRK14239 32 EITALIGPSGSGKSTLLRsinrmndlnpevTITGsivynghnIYSPRTDTVDLRKEIGMVFQQ-PNPFPMSIYENVVYG- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 93 arhiglLRMPGRRDREAAMEAlavIGLAGKAAERFD-----------ALSGGQRQMVLIARAIAAEPAALFLDEPASALD 161
Cdd:PRK14239 110 ------LRLKGIKDKQVLDEA---VEKSLKGASIWDevkdrlhdsalGLSGGQQQRVCIARVLATSPKIILLDEPTSALD 180
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
29-197 |
7.02e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.42 E-value: 7.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 29 VAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGT--------------AALVPQDFARAFPYRVIDMVLMGRAR 94
Cdd:PRK10982 21 VRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeidfksskealengISMVHQELNLVLQRSVMDNMWLGRYP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 95 HIGLLRMPGR--RDREAAMEALAV-IGLAGKAAErfdaLSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRL 171
Cdd:PRK10982 101 TKGMFVDQDKmyRDTKAIFDELDIdIDPRAKVAT----LSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTI 176
|
170 180
....*....|....*....|....*.
gi 500071482 172 VRVLADRGLAVVMTTHQPNHALAVAD 197
Cdd:PRK10982 177 IRKLKERGCGIVYISHKMEEIFQLCD 202
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-226 |
7.94e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 52.31 E-value: 7.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 3 EPLIRAEGAAHSWDGTRwqfrDLDFA---VAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAA--------- 70
Cdd:PRK10762 2 QALLQLKGIDKAFPGVK----ALSGAalnVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfngpkssq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 71 ------------LVPQdfarafpYRVIDMVLMGR--ARHIGllRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQ 136
Cdd:PRK10762 78 eagigiihqelnLIPQ-------LTIAENIFLGRefVNRFG--RIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 137 MVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLVRVLADRGLAVVMTTHQPNHALAVADtALLMLPEGAVFGPCH-EA 215
Cdd:PRK10762 149 MVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICD-DVTVFRDGQFIAEREvAD 227
|
250
....*....|..
gi 500071482 216 LTETR-IEMLYG 226
Cdd:PRK10762 228 LTEDSlIEMMVG 239
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
22-161 |
9.66e-08 |
|
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: 51.39 E-value: 9.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 22 FRDLDFAVAAGQVTAVLGANGCGKST----LLRvatgLRAPTRGRITVAG--TAALVPQDFARAFPYRVIDMVLMGR--A 93
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTvvslLER----FYDPTSGEILLDGvdIRDLNLRWLRSQIGLVSQEPVLFDGtiA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 94 RHIGLlrmpGRRDR------EAAMEALA---VIGLAGK----AAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASAL 160
Cdd:cd03249 95 ENIRY----GKPDAtdeeveEAAKKANIhdfIMSLPDGydtlVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSAL 170
|
.
gi 500071482 161 D 161
Cdd:cd03249 171 D 171
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
25-202 |
1.16e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 52.15 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 25 LDFAVAAGQVTAVLGANGCGKSTLLRVATGLrAPTRGRITVAGT--AALVPQDFARA----------FPYRVIDMVLMGR 92
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIelRELDPESWRKHlswvgqnpqlPHGTLRDNVLLGN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 93 ARhigllrmpgrRDREAAMEALA-----------VIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALD 161
Cdd:PRK11174 448 PD----------ASDEQLQQALEnawvseflpllPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 500071482 162 LGNQDRVLRLVRVlADRGLAVVMTTHQPNhALAVADTALLM 202
Cdd:PRK11174 518 AHSEQLVMQALNA-ASRRQTTLMVTHQLE-DLAQWDQIWVM 556
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
4-208 |
1.22e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.17 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 4 PLIRAEGAAHSWDGTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGriTVAGTA----ALVPQDFARA 79
Cdd:PLN03073 507 PIISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSG--TVFRSAkvrmAVFSQHHVDG 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 80 FPYRVIDMVLMGRArhigllrMPGRrdREAAMEA-LAVIGLAGK-AAERFDALSGGQRQMVLIARAIAAEPAALFLDEPA 157
Cdd:PLN03073 585 LDLSSNPLLYMMRC-------FPGV--PEQKLRAhLGSFGVTGNlALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPS 655
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 500071482 158 SALDLgnqDRVLRLVRVLADRGLAVVMTTHQpNHALAVADTALLMLPEGAV 208
Cdd:PLN03073 656 NHLDL---DAVEALIQGLVLFQGGVLMVSHD-EHLISGSVDELWVVSEGKV 702
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
25-135 |
1.26e-07 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 51.72 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 25 LDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGtAALVPQDFARafpYR----VI--DMVLMGRarhigL 98
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDG-QPVTADNREA---YRqlfsAVfsDFHLFDR-----L 421
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 500071482 99 LRMPGRRDREAAMEALAVIGLAGKAAE---RFD--ALSGGQR 135
Cdd:COG4615 422 LGLDGEADPARARELLERLELDHKVSVedgRFSttDLSQGQR 463
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-184 |
1.44e-07 |
|
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: 50.87 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 32 GQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAG-TAALVPQDFARAFPYRVIDMvLMGRARHIGllrmpgrRDREAA 110
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdTVSYKPQYIKADYEGTVRDL-LSSITKDFY-------THPYFK 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500071482 111 MEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLVRVLADRGLAVVM 184
Cdd:cd03237 97 TEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAF 170
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-202 |
2.00e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 50.76 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 3 EPLIRAEGAAHSWDG-TRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA------------ 69
Cdd:PRK13632 5 SVMIKVENVSFSYPNsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITiskenlkeirkk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 70 --------------ALVPQDFA-----RAFPYRVIDMVLMGRARHIGllrMPGRRDREAamealaviglagkaaerfDAL 130
Cdd:PRK13632 85 igiifqnpdnqfigATVEDDIAfglenKKVPPKKMKDIIDDLAKKVG---MEDYLDKEP------------------QNL 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500071482 131 SGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLVRVLADRGLAVVMT-THQPNHALaVADTALLM 202
Cdd:PRK13632 144 SGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISiTHDMDEAI-LADKVIVF 215
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
23-173 |
2.57e-07 |
|
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: 49.72 E-value: 2.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAG-------------TAALVPQDfarafPyrvidMVL 89
Cdd:cd03369 25 KNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlrsSLTIIPQD-----P-----TLF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 90 MGRARHIglLRMPGRRDREAAMEALAViglagkaAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVL 169
Cdd:cd03369 95 SGTIRSN--LDPFDEYSDEEIYGALRV-------SEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQ 165
|
....
gi 500071482 170 RLVR 173
Cdd:cd03369 166 KTIR 169
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
24-202 |
3.13e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 50.09 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 24 DLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAG--------------TAALVPQDfarafPYRVIDMVL 89
Cdd:PRK13633 28 DVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsdeenlwdirnKAGMVFQN-----PDNQIVATI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 90 MGRARHIGL--LRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDR 167
Cdd:PRK13633 103 VEEDVAFGPenLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRRE 182
|
170 180 190
....*....|....*....|....*....|....*.
gi 500071482 168 VLRLVRVLADR-GLAVVMTTHQPNHAlAVADTALLM 202
Cdd:PRK13633 183 VVNTIKELNKKyGITIILITHYMEEA-VEADRIIVM 217
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
24-198 |
3.35e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.56 E-value: 3.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 24 DLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRaPT---RGRITVAGTA---------------------ALVPqdfara 79
Cdd:NF040905 19 DVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEVcrfkdirdsealgiviihqelALIP------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 80 fpyrvidmvLMGRARHIGLLRMPGRR---DREA----AMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALF 152
Cdd:NF040905 92 ---------YLSIAENIFLGNERAKRgviDWNEtnrrARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLI 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 500071482 153 LDEPASALDLGNQDRVLRLVRVLADRGLAVVMTTHQPNHALAVADT 198
Cdd:NF040905 163 LDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADS 208
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
24-202 |
3.63e-07 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 50.09 E-value: 3.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 24 DLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAALVPQDFARAFPYRVIDMVL----------MGRA 93
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFqdplaslnprMTIG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 94 RHIGL-LR-----MPGRRDREAAMEALAVIGLAGKAAERF-DALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQD 166
Cdd:PRK15079 119 EIIAEpLRtyhpkLSRQEVKDRVKAMMLKVGLLPNLINRYpHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQA 198
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 500071482 167 RVLRLVRVL-ADRGLAVVMTTHQpnhaLAV----ADTALLM 202
Cdd:PRK15079 199 QVVNLLQQLqREMGLSLIFIAHD----LAVvkhiSDRVLVM 235
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
130-228 |
4.84e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 50.17 E-value: 4.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 130 LSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLVRVLADRGLAVVMTTHQPNHALAVADTALLMLpEG--- 206
Cdd:PRK09700 410 LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFC-EGrlt 488
|
90 100
....*....|....*....|..
gi 500071482 207 AVFGPChEALTETRIeMLYGLP 228
Cdd:PRK09700 489 QILTNR-DDMSEEEI-MAWALP 508
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
23-184 |
4.91e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 50.03 E-value: 4.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA--------------ALVPQD-FARAFpyrVIDM 87
Cdd:COG3845 275 KDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDitglsprerrrlgvAYIPEDrLGRGL---VPDM 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 88 -----VLMGRARHIGLLRMpGRRDREAAMEalavigLAGKAAERFD-----------ALSGGQRQMVLIARAIAAEPAAL 151
Cdd:COG3845 352 svaenLILGRYRRPPFSRG-GFLDRKAIRA------FAEELIEEFDvrtpgpdtparSLSGGNQQKVILARELSRDPKLL 424
|
170 180 190
....*....|....*....|....*....|...
gi 500071482 152 FLDEPASALDLGNQDRVLRLVRVLADRGLAVVM 184
Cdd:COG3845 425 IAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLL 457
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
24-202 |
7.72e-07 |
|
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: 49.44 E-value: 7.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 24 DLDFAVAAGQVTAVLGANGCGKSTLLRVATG------------------LRAPTRgriTVAGTAALVPQDFARafpYRVI 85
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGaypgkfegnvfingkpvdIRNPAQ---AIRAGIAMVPEDRKR---HGIV 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 86 DMVLMGRARHIGLLRMPGRRDREAAMEALAVIG-----LAGKAAERFDA---LSGGQRQMVLIARAIAAEPAALFLDEPA 157
Cdd:TIGR02633 352 PILGVGKNITLSVLKSFCFKMRIDAAAELQIIGsaiqrLKVKTASPFLPigrLSGGNQQKAVLAKMLLTNPRVLILDEPT 431
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 500071482 158 SALDLGNQDRVLRLVRVLADRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:TIGR02633 432 RGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVI 476
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
23-161 |
1.16e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.18 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVaGT---AALVPQDFARAFPYR-VIDMV--------LM 90
Cdd:PRK11147 336 KDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTkleVAYFDQHRAELDPEKtVMDNLaegkqevmVN 414
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500071482 91 GRARHI-GLLR----MPGRrdreaAMEALAviglagkaaerfdALSGGQRQMVLIARAIAAEPAALFLDEPASALD 161
Cdd:PRK11147 415 GRPRHVlGYLQdflfHPKR-----AMTPVK-------------ALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-187 |
1.30e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 48.67 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 22 FRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA-------------ALVPQdfarafpyRVidMV 88
Cdd:PRK11160 356 LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPiadyseaalrqaiSVVSQ--------RV--HL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 89 LMGRARHIGLLRMPGRRDrEAAMEALAVIGLAG--KAAERFDA--------LSGGQRQMVLIARAIAAEPAALFLDEPAS 158
Cdd:PRK11160 426 FSATLRDNLLLAAPNASD-EALIEVLQQVGLEKllEDDKGLNAwlgeggrqLSGGEQRRLGIARALLHDAPLLLLDEPTE 504
|
170 180
....*....|....*....|....*....
gi 500071482 159 ALDLGNQDRVLRLVRVLAdRGLAVVMTTH 187
Cdd:PRK11160 505 GLDAETERQILELLAEHA-QNKTVLMITH 532
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
39-107 |
1.48e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 48.73 E-value: 1.48e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500071482 39 GANGCGKSTLLRVATGLRAPTrgritvAGTAALVP--------QD-FarAFP-YRVIDMVLMGrarHIGLLRMPGRRDR 107
Cdd:PRK15064 34 GANGCGKSTFMKILGGDLEPS------AGNVSLDPnerlgklrQDqF--AFEeFTVLDTVIMG---HTELWEVKQERDR 101
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
4-208 |
1.66e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.82 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 4 PLIRAEGAAHSWDG--TRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTR-GRITVAGTAALVPQdFARAF 80
Cdd:PLN03232 613 PAISIKNGYFSWDSktSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAEtSSVVIRGSVAYVPQ-VSWIF 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 81 PYRVIDMVLMG---------RARHIGLLR-----MPGRRDREaamealavIGlagkaaERFDALSGGQRQMVLIARAIAA 146
Cdd:PLN03232 692 NATVRENILFGsdfeserywRAIDVTALQhdldlLPGRDLTE--------IG------ERGVNISGGQKQRVSMARAVYS 757
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500071482 147 EPAALFLDEPASALDLGNQDRVLRLVRVLADRGLAVVMTTHQPnHALAVADTaLLMLPEGAV 208
Cdd:PLN03232 758 NSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQL-HFLPLMDR-IILVSEGMI 817
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
17-202 |
1.77e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 47.85 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 17 GTRWQF---RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAG-----------------TAALVPQdF 76
Cdd:PRK13646 15 GTPYEHqaiHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdkyirpvrkRIGMVFQ-F 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 77 --ARAFPYRVIDMVLMGRARhiglLRMPGRRDREAAMEALAVIGLAGKAAER--FDaLSGGQRQMVLIARAIAAEPAALF 152
Cdd:PRK13646 94 peSQLFEDTVEREIIFGPKN----FKMNLDEVKNYAHRLLMDLGFSRDVMSQspFQ-MSGGQMRKIAIVSILAMNPDIIV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 500071482 153 LDEPASALDLGNQDRVLRLVRVLA-DRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:PRK13646 169 LDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVM 219
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-208 |
1.97e-06 |
|
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: 48.26 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 6 IRAEGAAHSWDGTRwQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRA--PTRGRI-------------------- 63
Cdd:TIGR03269 1 IEVKNLTKKFDGKE-VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyhvalcekcgyverpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 64 ----TVAGTAALVPQDF---ARAFPYRVIDMVLMGRARHIGLLRmpGRRDREAAMEALAVIGLAGK-----AAERFDA-- 129
Cdd:TIGR03269 80 epcpVCGGTLEPEEVDFwnlSDKLRRRIRKRIAIMLQRTFALYG--DDTVLDNVLEALEEIGYEGKeavgrAVDLIEMvq 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 130 -----------LSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLVRVLA-DRGLAVVMTTHQPNHALAVAD 197
Cdd:TIGR03269 158 lshrithiardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkASGISMVLTSHWPEVIEDLSD 237
|
250
....*....|.
gi 500071482 198 TALLmLPEGAV 208
Cdd:TIGR03269 238 KAIW-LENGEI 247
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
32-197 |
2.62e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 47.18 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 32 GQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAG-------TAALVPQDFA------RAFPYRVIDMVL-MGrarhiG 97
Cdd:PRK11614 31 GEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGkditdwqTAKIMREAVAivpegrRVFSRMTVEENLaMG-----G 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 98 LLrmpgrRDREAAMEALAVI-----GLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLV 172
Cdd:PRK11614 106 FF-----AERDQFQERIKWVyelfpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTI 180
|
170 180
....*....|....*....|....*
gi 500071482 173 RVLADRGLAVVMTTHQPNHALAVAD 197
Cdd:PRK11614 181 EQLREQGMTIFLVEQNANQALKLAD 205
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
130-208 |
3.08e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 47.93 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 130 LSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLVRVL-ADRGLAVVMTTHQPNHALAVADTALLMLPEGAV 208
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLqKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-187 |
4.04e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.39 E-value: 4.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 2 AEPLIRAEGAAHSWDGTRWQFR----------DLDFAVAAGQVTAVLGANGCGKST----LLRVAtglraPTRGRITVAG 67
Cdd:PRK15134 272 ASPLLDVEQLQVAFPIRKGILKrtvdhnvvvkNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDG 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 68 TA-------ALVP---------QDFARAFPYR--VIDMVLMGRARHIGLLRMPGRRDReaAMEALAVIGLAGKAAERFDA 129
Cdd:PRK15134 347 QPlhnlnrrQLLPvrhriqvvfQDPNSSLNPRlnVLQIIEEGLRVHQPTLSAAQREQQ--VIAVMEEVGLDPETRHRYPA 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 130 -LSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLVRVLADR-GLAVVMTTH 187
Cdd:PRK15134 425 eFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKhQLAYLFISH 484
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
17-202 |
4.27e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 46.68 E-value: 4.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 17 GTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAG----------------TAALVPQDFARAF 80
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGenipamsrsrlytvrkRMSMLFQSGALFT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 81 PYRVIDMVLMGRARHIgllRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASAL 160
Cdd:PRK11831 98 DMNVFDNVAYPLREHT---QLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 500071482 161 DLGNQDRVLRLVRVLADR-GLAVVMTTHQPNHALAVADTALLM 202
Cdd:PRK11831 175 DPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIV 217
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
23-202 |
5.05e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 46.32 E-value: 5.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTaalvPQDFARaFPYRV--IDMV-------LMGRA 93
Cdd:PRK15112 30 KPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDH----PLHFGD-YSYRSqrIRMIfqdpstsLNPRQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 94 RHIGLLRMPGR-------RDREAAM-EALAVIGLAGKAAERF-DALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGN 164
Cdd:PRK15112 105 RISQILDFPLRlntdlepEQREKQIiETLRQVGLLPDHASYYpHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSM 184
|
170 180 190
....*....|....*....|....*....|....*....
gi 500071482 165 QDRVLRLVRVLADR-GLAVVMTTHQPNHALAVADTALLM 202
Cdd:PRK15112 185 RSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVM 223
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
22-209 |
5.11e-06 |
|
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: 47.21 E-value: 5.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 22 FRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAALVPQdFARAFPYRVIDMVLMG------RARH 95
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQ-TSWIMPGTIKDNIIFGlsydeyRYTS 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 96 I--------GLLRMPgRRDREAAMEAlaviGLagkaaerfdALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDR 167
Cdd:TIGR01271 521 VikacqleeDIALFP-EKDKTVLGEG----GI---------TLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKE 586
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 500071482 168 VLR--LVRVLADRGLAVVmtTHQPNHaLAVADTaLLMLPEGAVF 209
Cdd:TIGR01271 587 IFEscLCKLMSNKTRILV--TSKLEH-LKKADK-ILLLHEGVCY 626
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
14-161 |
7.40e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 46.38 E-value: 7.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 14 SWDGTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA--ALVPQDfarafpyRVIDMVL-- 89
Cdd:PRK11650 12 SYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVvnELEPAD-------RDIAMVFqn 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 90 ------MGRARHIGL-LRMPG-------RRDREAA----MEALavigLAGKAAErfdaLSGGQRQMVLIARAIAAEPAAL 151
Cdd:PRK11650 85 yalyphMSVRENMAYgLKIRGmpkaeieERVAEAArileLEPL----LDRKPRE----LSGGQRQRVAMGRAIVREPAVF 156
|
170
....*....|
gi 500071482 152 FLDEPASALD 161
Cdd:PRK11650 157 LFDEPLSNLD 166
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
22-188 |
8.52e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 45.33 E-value: 8.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 22 FRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAalVPQDFArafPYRViDMVLMGRARHIG---L 98
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQS--IKKDLC---TYQK-QLCFVGHRSGINpylT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 99 LRMPGRRDREAAMEALAVIGLAG--KAAERFD----ALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLV 172
Cdd:PRK13540 91 LRENCLYDIHFSPGAVGITELCRlfSLEHLIDypcgLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKI 170
|
170
....*....|....*.
gi 500071482 173 RVLADRGLAVVMTTHQ 188
Cdd:PRK13540 171 QEHRAKGGAVLLTSHQ 186
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-161 |
1.01e-05 |
|
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: 45.97 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 2 AEPLIRAEGAAH------SWDGTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGT------- 68
Cdd:COG5265 348 APPLVVGGGEVRfenvsfGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQdirdvtq 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 69 ----AAL--VPQDfarafpyrvidMVLM----------GRarhigllrmPG--RRDREAAMEAlAVI---------GLAG 121
Cdd:COG5265 428 aslrAAIgiVPQD-----------TVLFndtiayniayGR---------PDasEEEVEAAARA-AQIhdfieslpdGYDT 486
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 500071482 122 KAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALD 161
Cdd:COG5265 487 RVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALD 526
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
24-202 |
1.09e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 45.85 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 24 DLDFAVAAGQVTAVLGANGCGKS-TLLRVATGLRAP----TRGRITVAGTAAL-VPQDFARAFPYRVIDM---------- 87
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLhASEQTLRGVRGNKIAMifqepmvsln 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 88 -----------VLmgrARHIGLLRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEP 156
Cdd:PRK15134 107 plhtlekqlyeVL---SLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGGERQRVMIAMALLTRPELLIADEP 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 500071482 157 ASALDLGNQDRVLRLVRVL-ADRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:PRK15134 184 TTALDVSVQAQILQLLRELqQELNMGLLFITHNLSIVRKLADRVAVM 230
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
24-72 |
1.23e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 46.04 E-value: 1.23e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 500071482 24 DLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAALV 72
Cdd:PRK13545 42 NISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALI 90
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
23-209 |
1.25e-05 |
|
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: 45.23 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAALVPQdFARAFPYRVIDMVLMGRA----RHIGL 98
Cdd:cd03291 54 KNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQ-FSWIMPGTIKENIIFGVSydeyRYKSV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 99 LRMPGRRDREAAM--EALAVIGLAGKaaerfdALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLR--LVRV 174
Cdd:cd03291 133 VKACQLEEDITKFpeKDNTVLGEGGI------TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFEscVCKL 206
|
170 180 190
....*....|....*....|....*....|....*
gi 500071482 175 LADRglAVVMTTHQPNHaLAVADTaLLMLPEGAVF 209
Cdd:cd03291 207 MANK--TRILVTSKMEH-LKKADK-ILILHEGSSY 237
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
24-208 |
1.27e-05 |
|
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: 45.89 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 24 DLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTA-------------ALVPQDfarafPY----RVID 86
Cdd:TIGR01193 492 DISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSlkdidrhtlrqfiNYLPQE-----PYifsgSILE 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 87 MVLMGRARHIG---LLRMPGRRDREAAMEALAvIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLG 163
Cdd:TIGR01193 567 NLLLGAKENVSqdeIWAACEIAEIKDDIENMP-LGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTI 645
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 500071482 164 NQDRVLRLVRVLADRGLAVVMtthqpnHALAVADTA--LLMLPEGAV 208
Cdd:TIGR01193 646 TEKKIVNNLLNLQDKTIIFVA------HRLSVAKQSdkIIVLDHGKI 686
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
25-202 |
1.37e-05 |
|
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: 45.56 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 25 LDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVagtaaLVPQDFarafpyrvIDMV-----LMGRA-RHIGL 98
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNV-----RVGDEW--------VDMTkpgpdGRGRAkRYIGI 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 99 L----------------------RMPGRRDREAAMEALAVIGLAGKAAERF-----DALSGGQRQMVLIARAIAAEPAAL 151
Cdd:TIGR03269 370 LhqeydlyphrtvldnlteaiglELPDELARMKAVITLKMVGFDEEKAEEIldkypDELSEGERHRVALAQVLIKEPRIV 449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 500071482 152 FLDEPASALDLGNQDRVLR-LVRVLADRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:TIGR03269 450 ILDEPTGTMDPITKVDVTHsILKAREEMEQTFIIVSHDMDFVLDVCDRAALM 501
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
24-190 |
1.39e-05 |
|
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: 44.27 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 24 DLDFAvaAGQVTAVLGANGCGKSTLLRvATGLraptrgritvagtaalvpqdfarafpyrvidmVLMGRARHIGLLRMPG 103
Cdd:cd03227 15 DVTFG--EGSLTIITGPNGSGKSTILD-AIGL--------------------------------ALGGAQSATRRRSGVK 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 104 RRDREAAMEALAVIglagkaaeRFDALSGGQRQMV----LIARAIAAEPAALFLDEPASALDLGNQDRVLRLVRVLADRG 179
Cdd:cd03227 60 AGCIVAAVSAELIF--------TRLQLSGGEKELSalalILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKG 131
|
170
....*....|.
gi 500071482 180 LAVVMTTHQPN 190
Cdd:cd03227 132 AQVIVITHLPE 142
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
127-189 |
1.51e-05 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 45.07 E-value: 1.51e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500071482 127 FDALSGGQRQM---VLIARAIAAEPAALFLDEPASALDLGNQDRVLRLVRVLADRGLAVVMTTHQP 189
Cdd:pfam13304 234 AFELSDGTKRLlalLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSP 299
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
93-197 |
1.56e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.50 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 93 ARHIGLLRMPGRRDREAAMEALAVIGLAGKAAERFdalSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLV 172
Cdd:NF000106 111 GR*LDLSRKDARARADELLERFSLTEAAGRAAAKY---SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEV 187
|
90 100 110
....*....|....*....|....*....|.
gi 500071482 173 RVLADRGLAVVMTTH------QPNHALAVAD 197
Cdd:NF000106 188 RSMVRDGATVLLTTQymeeaeQLAHELTVID 218
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-71 |
1.78e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.49 E-value: 1.78e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500071482 6 IRAEGAAHSWdGTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAAL 71
Cdd:PRK11819 325 IEAENLSKSF-GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKL 389
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
27-221 |
2.30e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 44.90 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 27 FAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAALV--PQDFARA--------------FPYR-VIDMVL 89
Cdd:PRK11288 274 FSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIrsPRDAIRAgimlcpedrkaegiIPVHsVADNIN 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 90 MGRARH---IGLLRMPGRRDREAA--MEALAVIGLAGKAAERFdaLSGGQRQMVLIARAIAAEPAALFLDEPASALDLGN 164
Cdd:PRK11288 354 ISARRHhlrAGCLINNRWEAENADrfIRSLNIKTPSREQLIMN--LSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGA 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 500071482 165 QDRVLRLVRVLADRGLAVVMTTHQPNHALAVADTALLMlPEGAVFGPC-HEALTETRI 221
Cdd:PRK11288 432 KHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVM-REGRIAGELaREQATERQA 488
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
22-65 |
2.43e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.41 E-value: 2.43e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 500071482 22 FRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITV 65
Cdd:PTZ00265 401 YKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIII 444
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
24-202 |
2.79e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 44.33 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 24 DLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTrGRITvaGTAALVPQDFARaFPYRVIDMVlmgRARHIGLL---R 100
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAN-GRIG--GSATFNGREILN-LPEKELNKL---RAEQISMIfqdP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 101 M----PGRRDREAAMEALAVIGLAGKAaERF-------DAL----------------SGGQRQMVLIARAIAAEPAALFL 153
Cdd:PRK09473 107 MtslnPYMRVGEQLMEVLMLHKGMSKA-EAFeesvrmlDAVkmpearkrmkmyphefSGGMRQRVMIAMALLCRPKLLIA 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 500071482 154 DEPASALDLGNQDRVLRLVRVLADR-GLAVVMTTHQPNHALAVADTALLM 202
Cdd:PRK09473 186 DEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVM 235
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
6-194 |
2.96e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 44.31 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 6 IRAEGAAHSWD-GTRWQFRDLD---FAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRI----------TVAGTAAL 71
Cdd:PRK13651 3 IKVKNIVKIFNkKLPTELKALDnvsVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 72 VPQDFARAFPY-RVIDMVLMGRaRHIGL------------------------LRMPGRRDREAAMEALAVIGLAGKAAER 126
Cdd:PRK13651 83 VLEKLVIQKTRfKKIKKIKEIR-RRVGVvfqfaeyqlfeqtiekdiifgpvsMGVSKEEAKKRAAKYIELVGLDESYLQR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 127 --FDaLSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLVRVLADRGLAVVMTTHQPNHALA 194
Cdd:PRK13651 162 spFE-LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLE 230
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
24-189 |
3.47e-05 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 44.74 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 24 DLDFAVAAGQVTAVLGANGCGKSTLLRVATGLrAPTR-GRITVAGTAAL--VPQDfarafPYrvidmvlMGRarhiGLLR 100
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFRILGEL-WPVYgGRLTKPAKGKLfyVPQR-----PY-------MTL----GTLR 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 101 -----------MPGRRDREAAMEALAVIGLAGKAAER----------FDALSGGQRQMVLIARAIAAEPAALFLDEPASA 159
Cdd:TIGR00954 533 dqiiypdssedMKRRGLSDKDLEQILDNVQLTHILEReggwsavqdwMDVLSGGEKQRIAMARLFYHKPQFAILDECTSA 612
|
170 180 190
....*....|....*....|....*....|
gi 500071482 160 LDLGNQDRVLRLVRvlaDRGLAVVMTTHQP 189
Cdd:TIGR00954 613 VSVDVEGYMYRLCR---EFGITLFSVSHRK 639
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
23-190 |
4.10e-05 |
|
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: 43.41 E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPT---RGRITVAGtaaLVPQDFARAFPYRVI-----DmvlmgraR 94
Cdd:cd03233 24 KDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNG---IPYKEFAEKYPGEIIyvseeD-------V 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 95 HIGLLRMpgRRDREAAMEAlaviglagKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLVRV 174
Cdd:cd03233 94 HFPTLTV--RETLDFALRC--------KGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRT 163
|
170
....*....|....*..
gi 500071482 175 LADR-GLAVVMTTHQPN 190
Cdd:cd03233 164 MADVlKTTTFVSLYQAS 180
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-161 |
5.85e-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: 44.13 E-value: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 16 DGTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLrAPTRGRITVAGTA--ALVPQDFARAF---PYRVidMVLM 90
Cdd:TIGR01271 1229 EAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSwnSVTLQTWRKAFgviPQKV--FIFS 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 91 GRARHIglLRMPGRRDREAAMEALAVIGLAgKAAERFD------------ALSGGQRQMVLIARAIAAEPAALFLDEPAS 158
Cdd:TIGR01271 1306 GTFRKN--LDPYEQWSDEEIWKVAEEVGLK-SVIEQFPdkldfvlvdggyVLSNGHKQLMCLARSILSKAKILLLDEPSA 1382
|
...
gi 500071482 159 ALD 161
Cdd:TIGR01271 1383 HLD 1385
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-202 |
1.13e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 42.73 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 22 FRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAG---TAALVPQDFARAFPYRVIDMVLMG------- 91
Cdd:PRK15439 279 FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGkeiNALSTAQRLARGLVYLPEDRQSSGlyldapl 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 92 RARHIGLL--RMP--GRRDREAAM--EALAVIGLAGKAAER-FDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGN 164
Cdd:PRK15439 359 AWNVCALThnRRGfwIKPARENAVleRYRRALNIKFNHAEQaARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
|
170 180 190
....*....|....*....|....*....|....*...
gi 500071482 165 QDRVLRLVRVLADRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:PRK15439 439 RNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVM 476
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
26-184 |
1.14e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.69 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 26 DFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRG----------RITVAGTAALVPQDFARafpyRVIDMVL-----M 90
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGerqsqfshitRLSFEQLQKLVSDEWQR----NNTDMLSpgeddT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 91 GR-ARHIGLLrmpGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVL 169
Cdd:PRK10938 99 GRtTAEIIQD---EVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLA 175
|
170
....*....|....*
gi 500071482 170 RLVRVLADRGLAVVM 184
Cdd:PRK10938 176 ELLASLHQSGITLVL 190
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
24-187 |
1.78e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 42.54 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 24 DLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAG-------TAALVP---------QD-FARAFPYRVID 86
Cdd:PRK10261 342 KVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqridtlsPGKLQAlrrdiqfifQDpYASLDPRQTVG 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 87 MVLMGRARHIGLLrmPGRRDREAAMEALAVIGLAGKAAERF-DALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQ 165
Cdd:PRK10261 422 DSIMEPLRVHGLL--PGKAAAARVAWLLERVGLLPEHAWRYpHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIR 499
|
170 180
....*....|....*....|...
gi 500071482 166 DRVLRLVRVLA-DRGLAVVMTTH 187
Cdd:PRK10261 500 GQIINLLLDLQrDFGIAYLFISH 522
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
130-202 |
2.45e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 41.84 E-value: 2.45e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500071482 130 LSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLVRVLADRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVM 478
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
24-63 |
2.58e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 41.01 E-value: 2.58e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 500071482 24 DLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRI 63
Cdd:PRK13541 18 DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNI 57
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
32-177 |
2.71e-04 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 40.91 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 32 GQVTAVLGANGCGKSTL---------LRVATGLRAPTRGRITVAGTAALVPQDFARafpyrvIDMVLMGRARHIGLLrMP 102
Cdd:cd03278 22 PGLTAIVGPNGSGKSNIidairwvlgEQSAKSLRGEKMSDVIFAGSETRKPANFAE------VTLTFDNSDGRYSII-SQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 103 GRRDReaamealaVIGLAGKAAERFDALSGGQRQMVLIaraiaaepAALF------------LDEPASALDLGNQDRVLR 170
Cdd:cd03278 95 GDVSE--------IIEAPGKKVQRLSLLSGGEKALTAL--------ALLFaifrvrpspfcvLDEVDAALDDANVERFAR 158
|
....*..
gi 500071482 171 LVRVLAD 177
Cdd:cd03278 159 LLKEFSK 165
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-191 |
2.72e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 40.05 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 32 GQVTAVLGANGCGKSTLLR-VATGLRAPTRGRITVAGtaalvpqdfarafpyrvidmvlmgrarhigllrmpgrrdrEAA 110
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARaLARELGPPGGGVIYIDG----------------------------------------EDI 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 111 MEALAVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLVRVLAD------RGLAVVM 184
Cdd:smart00382 42 LEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLlllkseKNLTVIL 121
|
....*..
gi 500071482 185 TTHQPNH 191
Cdd:smart00382 122 TTNDEKD 128
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
24-192 |
3.11e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 41.65 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 24 DLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGtAALVPQDFA-RafpYRVIDM--------------- 87
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFG-QPVDAGDIAtR---RRVGYMsqafslygeltvrqn 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 88 -VLmgrarHIGLLRMPGRRDREAAMEALAVIGLAGKAAERFDALSGGQRQ-------MV-----LIaraiaaepaalfLD 154
Cdd:NF033858 360 lEL-----HARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQrlslavaVIhkpelLI------------LD 422
|
170 180 190
....*....|....*....|....*....|....*....
gi 500071482 155 EPASALDLGNQDRVLRLVRVLA-DRGLAVVMTTHQPNHA 192
Cdd:NF033858 423 EPTSGVDPVARDMFWRLLIELSrEDGVTIFISTHFMNEA 461
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
129-202 |
6.17e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.48 E-value: 6.17e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500071482 129 ALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLVRVLADRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:PRK10982 391 SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVM 464
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
23-161 |
6.75e-04 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 40.39 E-value: 6.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGT-------------AALVPQDFarafpYRVIDMVl 89
Cdd:PRK11176 360 RNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHdlrdytlaslrnqVALVSQNV-----HLFNDTI- 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 90 mgrARHIGLLRMP--GRRDREAAMEALAVIGLAGKAAERFDA--------LSGGQRQMVLIARAIAAEPAALFLDEPASA 159
Cdd:PRK11176 434 ---ANNIAYARTEqySREQIEEAARMAYAMDFINKMDNGLDTvigengvlLSGGQRQRIAIARALLRDSPILILDEATSA 510
|
..
gi 500071482 160 LD 161
Cdd:PRK11176 511 LD 512
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-67 |
9.39e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 40.11 E-value: 9.39e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500071482 6 IRAEGAAHSWDGTRwQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAG 67
Cdd:NF033858 2 ARLEGVSHRYGKTV-ALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLG 62
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
25-173 |
1.41e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 39.96 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 25 LDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAAlvpQDFARAFPYRVIDMVLMGRARHIGLLRM--- 101
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDV---AKFGLTDLRRVLSIIPQSPVLFSGTVRFnid 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 102 PGRRDREAAM-EAL-----------AVIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVL 169
Cdd:PLN03232 1332 PFSEHNDADLwEALerahikdvidrNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQ 1411
|
....
gi 500071482 170 RLVR 173
Cdd:PLN03232 1412 RTIR 1415
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
6-220 |
1.63e-03 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 39.32 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 6 IRAEGAAHSWDGTRWQFRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAG-------------TAALV 72
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGrplsslshsvlrqGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 73 PQD---FARAFpyrvIDMVLMGRarHIgllrmpgrrDREAAMEALAVIGLAGKA-----------AERFDALSGGQRQMV 138
Cdd:PRK10790 421 QQDpvvLADTF----LANVTLGR--DI---------SEEQVWQALETVQLAELArslpdglytplGEQGNNLSVGQKQLL 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 139 LIARAIAAEPAALFLDEPASALDLGNQDRVLRLVRVLADRGLAVVMTthqpnHALAV---ADTALLMLPEGAVFGPCHEA 215
Cdd:PRK10790 486 ALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIA-----HRLSTiveADTILVLHRGQAVEQGTHQQ 560
|
....*
gi 500071482 216 LTETR 220
Cdd:PRK10790 561 LLAAQ 565
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
23-210 |
2.65e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 37.69 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLlrVATGLRAPTRGRITvagtaalvpqDFARAFPYR---VID----MVLMGrarh 95
Cdd:cd03238 12 QNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLYASGKARLI----------SFLPKFSRNkliFIDqlqfLIDVG---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 96 IGLLRMpgrrDREAAmealaviglagkaaerfdALSGGQRQMV-LIARAIAAEPAALF-LDEPASALDLGNQDRVLRLVR 173
Cdd:cd03238 76 LGYLTL----GQKLS------------------TLSGGELQRVkLASELFSEPPGTLFiLDEPSTGLHQQDINQLLEVIK 133
|
170 180 190
....*....|....*....|....*....|....*..
gi 500071482 174 VLADRGLAVVMTTHQPNhALAVADTALLMLPEGAVFG 210
Cdd:cd03238 134 GLIDLGNTVILIEHNLD-VLSSADWIIDFGPGSGKSG 169
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
104-187 |
3.20e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 38.18 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 104 RRDReaAMEALAVIGLAGKAAeRFDA----LSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLVRVLADR- 178
Cdd:PRK11022 127 RRQR--AIDLLNQVGIPDPAS-RLDVyphqLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKe 203
|
....*....
gi 500071482 179 GLAVVMTTH 187
Cdd:PRK11022 204 NMALVLITH 212
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
23-173 |
3.21e-03 |
|
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: 37.86 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKST----LLRVATglraPTRGRITVAGTA-------------ALVPQDfarafPyrvi 85
Cdd:cd03244 21 KNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLVE----LSSGSILIDGVDiskiglhdlrsriSIIPQD-----P---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 86 dmVLMGrarhiGLLRM---P-GRRDREAAMEALA-----------VIGLAGKAAERFDALSGGQRQMVLIARAIAAEPAA 150
Cdd:cd03244 88 --VLFS-----GTIRSnldPfGEYSDEELWQALErvglkefveslPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180
....*....|....*....|...
gi 500071482 151 LFLDEPASALDLGNQDRVLRLVR 173
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIR 183
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
22-51 |
3.30e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 38.37 E-value: 3.30e-03
10 20 30
....*....|....*....|....*....|
gi 500071482 22 FRDLDFAVaaGQVTAVLGANGCGKSTLLRV 51
Cdd:COG4637 13 LRDLELPL--GPLTVLIGANGSGKSNLLDA 40
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-208 |
4.55e-03 |
|
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: 38.00 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 22 FRDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAG--TAALVPQDFAraFPYRVI--DMVLMGrarhiG 97
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGlnIAKIGLHDLR--FKITIIpqDPVLFS-----G 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 98 LLRMP----GRRDREAAMEALAVIGLAG-----------KAAERFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDL 162
Cdd:TIGR00957 1375 SLRMNldpfSQYSDEEVWWALELAHLKTfvsalpdkldhECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDL 1454
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 500071482 163 GNQDRVLRLVRVLADrGLAVVMTTHQPNhalAVAD-TALLMLPEGAV 208
Cdd:TIGR00957 1455 ETDNLIQSTIRTQFE-DCTVLTIAHRLN---TIMDyTRVIVLDKGEV 1497
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
29-197 |
5.03e-03 |
|
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: 36.78 E-value: 5.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 29 VAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAG-TAALVPQdfarafpyrvidmvlmgrarhigllrmpgrrdr 107
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGiTPVYKPQ--------------------------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 108 eaamealaviglagkaaerFDALSGGQRQMVLIARAIAAEPAALFLDEPASALDLGNQDRVLRLVRVLADRGLAVVMTTH 187
Cdd:cd03222 69 -------------------YIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVE 129
|
170
....*....|
gi 500071482 188 qpnHALAVAD 197
Cdd:cd03222 130 ---HDLAVLD 136
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
23-202 |
6.80e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 37.29 E-value: 6.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 23 RDLDFAVAAGQVTAVLGANGCGKSTLLRVATGLRAPTRGRITVAGTAALV--PQD-FARAFPY----RVIDMVLMGRA-- 93
Cdd:PRK10762 269 NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTrsPQDgLANGIVYisedRKRDGLVLGMSvk 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500071482 94 --------RHigLLRMPGRRDREAAMEAL---------------AVIGLagkaaerfdaLSGGQRQMVLIARAIAAEPAA 150
Cdd:PRK10762 349 enmsltalRY--FSRAGGSLKHADEQQAVsdfirlfniktpsmeQAIGL----------LSGGNQQKVAIARGLMTRPKV 416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 500071482 151 LFLDEPASALDLGNQDRVLRLVRVLADRGLAVVMTTHQPNHALAVADTALLM 202
Cdd:PRK10762 417 LILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVM 468
|
|
| |
