|
Name |
Accession |
Description |
Interval |
E-value |
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-201 |
4.10e-83 |
|
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: 246.53 E-value: 4.10e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 1 MLIQLDQVGRMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTG-SVNLFGKMPGKVgySAETVRQH 79
Cdd:COG1119 2 PLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGE--DVWELRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 80 IGFVSHSLLEKFQEGERVIDVVISGAFKSIGVYQDIDDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMG 159
Cdd:COG1119 80 IGLVSPALQLRFPRDETVLDVVLSGFFDSIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 686428090 160 QPQVLILDEPAAGLDFIARESLLSILDSLSDSyPTLAMIYVT 201
Cdd:COG1119 160 DPELLILDEPTAGLDLGARELLLALLDKLAAE-GAPTLVLVT 200
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
14-179 |
2.86e-40 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 137.14 E-value: 2.86e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 14 GKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKVgysaetvRQHIGFVShsllekfQE 93
Cdd:COG1121 18 GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-------RRRIGYVP-------QR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 94 GE-------RVIDVVISGAFKSIGVYQDIDDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLIL 166
Cdd:COG1121 84 AEvdwdfpiTVRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLL 163
|
170
....*....|...
gi 686428090 167 DEPAAGLDFIARE 179
Cdd:COG1121 164 DEPFAGVDAATEE 176
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
15-178 |
1.34e-38 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 138.22 E-value: 1.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 15 KTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEP-ATTGSVNLFGKMPGkvgySAETV---RQHIGFVSHSLLEK 90
Cdd:PRK10938 273 RPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPqGYSNDLTLFGRRRG----SGETIwdiKKHIGYVSSSLHLD 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 91 FQEGERVIDVVISGAFKSIGVYQDIDDEVRNEAHQLLKLVGMSAK-AQQYIGYLSTGEKQRVMIARALMGQPQVLILDEP 169
Cdd:PRK10938 349 YRVSTSVRNVILSGFFDSIGIYQAVSDRQQKLAQQWLDILGIDKRtADAPFHSLSWGQQRLALIVRALVKHPTLLILDEP 428
|
....*....
gi 686428090 170 AAGLDFIAR 178
Cdd:PRK10938 429 LQGLDPLNR 437
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
3-179 |
1.82e-37 |
|
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: 129.37 E-value: 1.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 3 IQLDQVG-RMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKvgYSAETVRQHIG 81
Cdd:COG1122 1 IELENLSfSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITK--KNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 82 FVshsllekFQEGERVIdvvisgaFKSIgVYQDI----------DDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRV 151
Cdd:COG1122 79 LV-------FQNPDDQL-------FAPT-VEEDVafgpenlglpREEIRERVEEALELVGLEHLADRPPHELSGGQKQRV 143
|
170 180
....*....|....*....|....*...
gi 686428090 152 MIARALMGQPQVLILDEPAAGLDFIARE 179
Cdd:COG1122 144 AIAGVLAMEPEVLVLDEPTAGLDPRGRR 171
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
13-174 |
2.14e-37 |
|
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: 128.81 E-value: 2.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 13 QGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKVgysaetvRQHIGFVSHSLLEKFQ 92
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-------RKRIGYVPQRRSIDRD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 93 EGERVIDVVISGAFKSIGVYQDIDDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDEPAAG 172
Cdd:cd03235 83 FPISVRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAG 162
|
..
gi 686428090 173 LD 174
Cdd:cd03235 163 VD 164
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
12-179 |
3.85e-37 |
|
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: 127.97 E-value: 3.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 12 KQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKvgYSAETVRQHIGFVshsllekF 91
Cdd:cd03225 11 DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTK--LSLKELRRKVGLV-------F 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 92 QE------GERVIDVVISGaFKSIGVYQDiddEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLI 165
Cdd:cd03225 82 QNpddqffGPTVEEEVAFG-LENLGLPEE---EIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170
....*....|....
gi 686428090 166 LDEPAAGLDFIARE 179
Cdd:cd03225 158 LDEPTAGLDPAGRR 171
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
14-178 |
8.66e-37 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 127.87 E-value: 8.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 14 GKTILKNISWQINGGDkwiLYGL---NGAGKTTLLNILNAYEPATTGSVNLFGKmpgKVGYSAETVRQHIGFVSHSLLek 90
Cdd:COG1131 12 DKTALDGVSLTVEPGE---IFGLlgpNGAGKTTTIRMLLGLLRPTSGEVRVLGE---DVARDPAEVRRRIGYVPQEPA-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 91 FQEGERVIDVVISGAfksiGVYQDIDDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDEPA 170
Cdd:COG1131 84 LYPDLTVRENLRFFA----RLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPT 159
|
....*...
gi 686428090 171 AGLDFIAR 178
Cdd:COG1131 160 SGLDPEAR 167
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-174 |
5.86e-35 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 123.63 E-value: 5.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 1 MLIQLDQVG-RMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKVGYSAE-TVRQ 78
Cdd:COG3638 1 PMLELRNLSkRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALrRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 79 HIGFVshsllekFQEGE-----RVIDVVISGAFKSIGVYQDI----DDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQ 149
Cdd:COG3638 81 RIGMI-------FQQFNlvprlSVLTNVLAGRLGRTSTWRSLlglfPPEDRERALEALERVGLADKAYQRADQLSGGQQQ 153
|
170 180
....*....|....*....|....*
gi 686428090 150 RVMIARALMGQPQVLILDEPAAGLD 174
Cdd:COG3638 154 RVAIARALVQEPKLILADEPVASLD 178
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
14-175 |
1.35e-34 |
|
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: 122.84 E-value: 1.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 14 GKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKmpgKV-GYSAETVRQHIGFV--SHSLLEK 90
Cdd:COG1120 13 GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGR---DLaSLSRRELARRIAYVpqEPPAPFG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 91 FqegeRVIDVVISGAFKSIGVYQDIDDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDEPA 170
Cdd:COG1120 90 L----TVRELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPT 165
|
....*
gi 686428090 171 AGLDF 175
Cdd:COG1120 166 SHLDL 170
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
3-174 |
3.34e-34 |
|
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: 121.52 E-value: 3.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 3 IQLDQVG-RMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKVGYSAE-TVRQHI 80
Cdd:cd03256 1 IEVENLSkTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 81 GFV--SHSLLEKFqegeRVIDVVISGAFKSIGVYQDI----DDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIA 154
Cdd:cd03256 81 GMIfqQFNLIERL----SVLENVLSGRLGRRSTWRSLfglfPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180
....*....|....*....|
gi 686428090 155 RALMGQPQVLILDEPAAGLD 174
Cdd:cd03256 157 RALMQQPKLILADEPVASLD 176
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
3-174 |
1.32e-33 |
|
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: 119.13 E-value: 1.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 3 IQLDQV----GRMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKVGYSAETV-- 76
Cdd:cd03255 1 IELKNLsktyGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAfr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 77 RQHIGFV--SHSLLEKFQEGERV-IDVVISGAFKSigvyqdiddEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMI 153
Cdd:cd03255 81 RRHIGFVfqSFNLLPDLTALENVeLPLLLAGVPKK---------ERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAI 151
|
170 180
....*....|....*....|.
gi 686428090 154 ARALMGQPQVLILDEPAAGLD 174
Cdd:cd03255 152 ARALANDPKIILADEPTGNLD 172
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
3-174 |
6.43e-33 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 117.22 E-value: 6.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 3 IQLDQVGRMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGkvGYSAETVRQHIGF 82
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLS--AMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 83 VshsllekFQE----GERVIDvvisgAFKSIGVYQDIDDEvRNEAHQLLKLVGMSAKA-QQYIGYLSTGEKQRVMIARAL 157
Cdd:COG4619 79 V-------PQEpalwGGTVRD-----NLPFPFQLRERKFD-RERALELLERLGLPPDIlDKPVERLSGGERQRLALIRAL 145
|
170
....*....|....*..
gi 686428090 158 MGQPQVLILDEPAAGLD 174
Cdd:COG4619 146 LLQPDVLLLDEPTSALD 162
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
2-179 |
6.70e-32 |
|
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: 115.34 E-value: 6.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 2 LIQLDQVGRMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKVGYsaeTVRQHIG 81
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR---EARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 82 FVSHSL-LEKFQEGERVIDVVISgafksigVYQDIDDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQ 160
Cdd:COG4555 78 VLPDERgLYDRLTVRENIRYFAE-------LYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHD 150
|
170
....*....|....*....
gi 686428090 161 PQVLILDEPAAGLDFIARE 179
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARR 169
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-174 |
9.14e-31 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 112.07 E-value: 9.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 3 IQLDQVG-RMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFG----KMPGK-VGYsaetV 76
Cdd:COG2884 2 IRFENVSkRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdlsRLKRReIPY----L 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 77 RQHIGFVshsllekFQEgervidvvisgaFKSIG---VYQDI----------DDEVRNEAHQLLKLVGMSAKAQQYIGYL 143
Cdd:COG2884 78 RRRIGVV-------FQD------------FRLLPdrtVYENValplrvtgksRKEIRRRVREVLDLVGLSDKAKALPHEL 138
|
170 180 190
....*....|....*....|....*....|.
gi 686428090 144 STGEKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:COG2884 139 SGGEQQRVAIARALVNRPELLLADEPTGNLD 169
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-174 |
9.61e-31 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 112.06 E-value: 9.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 2 LIQLDQV----GRMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFG----KMPGKVgySA 73
Cdd:COG1136 4 LLELRNLtksyGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGqdisSLSERE--LA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 74 ETVRQHIGFV--SHSLLEKFqegeRVID-VVISGAFKSIGVyqdidDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQR 150
Cdd:COG1136 82 RLRRRHIGFVfqFFNLLPEL----TALEnVALPLLLAGVSR-----KERRERARELLERVGLGDRLDHRPSQLSGGQQQR 152
|
170 180
....*....|....*....|....
gi 686428090 151 VMIARALMGQPQVLILDEPAAGLD 174
Cdd:COG1136 153 VAIARALVNRPKLILADEPTGNLD 176
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-179 |
9.64e-31 |
|
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: 111.42 E-value: 9.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 1 MLIQLDQVGRMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKvgySAETVRQHI 80
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD---AREDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 81 GFVSH--------SLLE--KFQegervidvvisGAFKsiGVYQDiddevRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQR 150
Cdd:COG4133 78 AYLGHadglkpelTVREnlRFW-----------AALY--GLRAD-----REAIDEALEAVGLAGLADLPVRQLSAGQKRR 139
|
170 180
....*....|....*....|....*....
gi 686428090 151 VMIARALMGQPQVLILDEPAAGLDFIARE 179
Cdd:COG4133 140 VALARLLLSPAPLWLLDEPFTALDAAGVA 168
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
13-175 |
3.89e-30 |
|
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: 109.06 E-value: 3.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 13 QGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKvgYSAETVRQHIGFVShsllekfq 92
Cdd:cd03214 10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLAS--LSPKELARKIAYVP-------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 93 egervidvvisgafksigvyqdiddevrneahQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDEPAAG 172
Cdd:cd03214 80 --------------------------------QALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSH 127
|
...
gi 686428090 173 LDF 175
Cdd:cd03214 128 LDI 130
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
14-174 |
1.67e-29 |
|
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: 109.31 E-value: 1.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 14 GKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKV-GYSAETVRQHIGFVS--HSLLEK 90
Cdd:TIGR02315 14 GKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLrGKKLRKLRRRIGMIFqhYNLIER 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 91 FQegerVIDVVISGAFKSIGVYQDI----DDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLIL 166
Cdd:TIGR02315 94 LT----VLENVLHGRLGYKPTWRSLlgrfSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILA 169
|
....*...
gi 686428090 167 DEPAAGLD 174
Cdd:TIGR02315 170 DEPIASLD 177
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
18-171 |
1.79e-29 |
|
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: 106.58 E-value: 1.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 18 LKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKvgYSAETVRQHIGFVS-HSLLEKFQEGER 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTD--DERKSLRKEIGYVFqDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 686428090 97 VIDVVISGAFKSigvyqdiDDEVRNEAHQLLKLVGMSAKAQQYIGY----LSTGEKQRVMIARALMGQPQVLILDEPAA 171
Cdd:pfam00005 79 NLRLGLLLKGLS-------KREKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
14-178 |
5.73e-29 |
|
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: 105.94 E-value: 5.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 14 GKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKvgySAETVRQHIGFVshsllekFQE 93
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK---EPEEVKRRIGYL-------PEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 94 gervidvvisgafksIGVYQDiddevrneahqllklvgMSAKaqQYIgYLSTGEKQRVMIARALMGQPQVLILDEPAAGL 173
Cdd:cd03230 82 ---------------PSLYEN-----------------LTVR--ENL-KLSGGMKQRLALAQALLHDPELLILDEPTSGL 126
|
....*
gi 686428090 174 DFIAR 178
Cdd:cd03230 127 DPESR 131
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3-174 |
1.44e-28 |
|
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: 106.12 E-value: 1.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 3 IQLDQVGRMKQGKTILKNISWQINGGdKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGkmpGKVGYSAETVRQHIGF 82
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDG---QDVLKQPQKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 83 VSHSLLekFQEGERVIDVVisgafKSIGVYQDIDD-EVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQP 161
Cdd:cd03264 77 LPQEFG--VYPNFTVREFL-----DYIAWLKGIPSkEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDP 149
|
170
....*....|...
gi 686428090 162 QVLILDEPAAGLD 174
Cdd:cd03264 150 SILIVDEPTAGLD 162
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
14-174 |
1.78e-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: 105.69 E-value: 1.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 14 GKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKVGYSAETVRQHIGFVshsllekFQ- 92
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELRQKVGMV-------FQq 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 93 ----EGERVIDVVISGAFKSIGVYqdiDDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDE 168
Cdd:cd03262 85 fnlfPHLTVLENITLAPIKVKGMS---KAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDE 161
|
....*.
gi 686428090 169 PAAGLD 174
Cdd:cd03262 162 PTSALD 167
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
2-174 |
6.45e-28 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 104.25 E-value: 6.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 2 LIQLDQVGRMKQGKT-ILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGK----MPGKvgySAETV 76
Cdd:TIGR02673 1 MIEFHNVSKAYPGGVaALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEdvnrLRGR---QLPLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 77 RQHIGFVshsllekFQE----GERVIDVVISGAFKSIGVYQDiddEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVM 152
Cdd:TIGR02673 78 RRRIGVV-------FQDfrllPDRTVYENVALPLEVRGKKER---EIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVA 147
|
170 180
....*....|....*....|..
gi 686428090 153 IARALMGQPQVLILDEPAAGLD 174
Cdd:TIGR02673 148 IARAIVNSPPLLLADEPTGNLD 169
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-169 |
3.95e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 107.07 E-value: 3.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 2 LIQLDQVGRMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLfgkmpG---KVGYSAetvrQ 78
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-----GetvKIGYFD----Q 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 79 HigfvshslLEKFQEGERVIDVVISGAfksigvyqdiDDEVRNEAHQLLKLVGMS-AKAQQYIGYLSTGEKQRVMIARAL 157
Cdd:COG0488 386 H--------QEELDPDKTVLDELRDGA----------PGGTEQEVRGYLGRFLFSgDDAFKPVGVLSGGEKARLALAKLL 447
|
170
....*....|..
gi 686428090 158 MGQPQVLILDEP 169
Cdd:COG0488 448 LSPPNVLLLDEP 459
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
16-173 |
7.06e-27 |
|
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: 102.81 E-value: 7.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 16 TILKNISWQINGGDkwiLYGL---NGAGKTTLLNILNAYEPATTGSVNLFGK----MPgkvgySAETVRQHIG------- 81
Cdd:COG0411 18 VAVDDVSLEVERGE---IVGLigpNGAGKTTLFNLITGFYRPTSGRILFDGRditgLP-----PHRIARLGIArtfqnpr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 82 -FVSHSLLE------KFQEGERVIdvvisGAFKSIGVYQDIDDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIA 154
Cdd:COG0411 90 lFPELTVLEnvlvaaHARLGRGLL-----AALLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIA 164
|
170
....*....|....*....
gi 686428090 155 RALMGQPQVLILDEPAAGL 173
Cdd:COG0411 165 RALATEPKLLLLDEPAAGL 183
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-179 |
3.14e-26 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 100.93 E-value: 3.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 1 MLIQLDQVGR----MKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKVGysaetv 76
Cdd:COG1116 6 PALELRGVSKrfptGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 77 rQHIGFVshsllekFQEG-----ERVIDVVISGAfKSIGVYQDiddEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRV 151
Cdd:COG1116 80 -PDRGVV-------FQEPallpwLTVLDNVALGL-ELRGVPKA---ERRERARELLELVGLAGFEDAYPHQLSGGMRQRV 147
|
170 180
....*....|....*....|....*...
gi 686428090 152 MIARALMGQPQVLILDEPAAGLDFIARE 179
Cdd:COG1116 148 AIARALANDPEVLLMDEPFGALDALTRE 175
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
14-174 |
8.33e-26 |
|
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: 8.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 14 GKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKVGYSAETVRQHIGFVshsllekFQE 93
Cdd:COG1126 13 DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKLRRKVGMV-------FQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 94 GE-----RVIDVVISGAFKSIGVyqdIDDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDE 168
Cdd:COG1126 86 FNlfphlTVLENVTLAPIKVKKM---SKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDE 162
|
....*.
gi 686428090 169 PAAGLD 174
Cdd:COG1126 163 PTSALD 168
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
4-179 |
8.53e-26 |
|
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: 97.32 E-value: 8.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 4 QLDQVGRMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKvgYSAETVRQHIGFV 83
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAK--LPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 84 shsllekFQegervidvvisgafksigvyqdiddevrneahqllklvgmsakaqqyigyLSTGEKQRVMIARALMGQPQV 163
Cdd:cd00267 79 -------PQ--------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170
....*....|....*.
gi 686428090 164 LILDEPAAGLDFIARE 179
Cdd:cd00267 102 LLLDEPTSGLDPASRE 117
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
2-174 |
9.52e-26 |
|
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: 99.19 E-value: 9.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 2 LIQLDQVGRMKQGK----TILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKVGYSA-ETV 76
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 77 RQHIGFVshsllekFQEgervidvviSGAFKSIGVYQDI----------DDEVRNEAHQLLKLVGMSAKAQQYIGYLSTG 146
Cdd:cd03258 81 RRRIGMI-------FQH---------FNLLSSRTVFENValpleiagvpKAEIEERVLELLELVGLEDKADAYPAQLSGG 144
|
170 180
....*....|....*....|....*...
gi 686428090 147 EKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:cd03258 145 QKQRVGIARALANNPKVLLCDEATSALD 172
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
3-174 |
1.13e-25 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 98.44 E-value: 1.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 3 IQLDQVGRMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKvgysAETVRQHIGf 82
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK----NIEALRRIG- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 83 vshSLLEkfqegervidvviSGAF-------KSIGVYQDIDDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIAR 155
Cdd:cd03268 76 ---ALIE-------------APGFypnltarENLRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIAL 139
|
170
....*....|....*....
gi 686428090 156 ALMGQPQVLILDEPAAGLD 174
Cdd:cd03268 140 ALLGNPDLLILDEPTNGLD 158
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
18-173 |
1.59e-25 |
|
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: 98.66 E-value: 1.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 18 LKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGK----MPgkvgySAETVRQHIGfvshsllEKFQ- 92
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEditgLP-----PHEIARLGIG-------RTFQi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 93 ----EGERVIDVVISGAFKSIGV------YQDIDDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQ 162
Cdd:cd03219 84 prlfPELTVLENVMVAAQARTGSglllarARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPK 163
|
170
....*....|.
gi 686428090 163 VLILDEPAAGL 173
Cdd:cd03219 164 LLLLDEPAAGL 174
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-174 |
3.86e-25 |
|
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: 101.52 E-value: 3.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 2 LIQLDQV-----GRMKQGKTILKNISWQINGGDkwILyGL---NGAGKTTLLNILNAYEPATTGSVNLFGK-MPGKVGYS 72
Cdd:COG1123 260 LLEVRNLskrypVRGKGGVRAVDDVSLTLRRGE--TL-GLvgeSGSGKSTLARLLLGLLRPTSGSILFDGKdLTKLSRRS 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 73 AETVRQHIGFV----SHSLLEKFqegeRVIDVVISGafksIGVYQDID-DEVRNEAHQLLKLVGMSAK-AQQYIGYLSTG 146
Cdd:COG1123 337 LRELRRRVQMVfqdpYSSLNPRM----TVGDIIAEP----LRLHGLLSrAERRERVAELLERVGLPPDlADRYPHELSGG 408
|
170 180
....*....|....*....|....*...
gi 686428090 147 EKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:COG1123 409 QRQRVAIARALALEPKLLILDEPTSALD 436
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-174 |
4.04e-25 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 97.78 E-value: 4.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 1 MLIQLDQVGRMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKmpgKVGYSAET----- 75
Cdd:PRK11124 1 MSIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGN---HFDFSKTPsdkai 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 76 --VRQHIGFVshsllekFQEGE-----RVIDVVISGAFKSIGVyqdIDDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEK 148
Cdd:PRK11124 78 reLRRNVGMV-------FQQYNlwphlTVQQNLIEAPCRVLGL---SKDQALARAEKLLERLRLKPYADRFPLHLSGGQQ 147
|
170 180
....*....|....*....|....*.
gi 686428090 149 QRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:PRK11124 148 QRVAIARALMMEPQVLLFDEPTAALD 173
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
3-179 |
6.04e-25 |
|
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: 96.77 E-value: 6.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 3 IQLDQV----GRMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKmpgkvgySAETVRQ 78
Cdd:cd03293 1 LEVRNVsktyGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE-------PVTGPGP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 79 HIGFVshsllekFQEG-----ERVIDVVISGaFKSIGVyqdIDDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMI 153
Cdd:cd03293 74 DRGYV-------FQQDallpwLTVLDNVALG-LELQGV---PKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVAL 142
|
170 180
....*....|....*....|....*.
gi 686428090 154 ARALMGQPQVLILDEPAAGLDFIARE 179
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDALTRE 168
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
3-179 |
6.59e-25 |
|
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: 96.43 E-value: 6.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 3 IQLDQVGRMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVnLFGkmpGKVGYSAETVRQHIGF 82
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEI-LID---GRDVTGVPPERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 83 VshsllekFQEGervidvvisGAFKSIGVYQDI----------DDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVM 152
Cdd:cd03259 77 V-------FQDY---------ALFPHLTVAENIafglklrgvpKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVA 140
|
170 180
....*....|....*....|....*..
gi 686428090 153 IARALMGQPQVLILDEPAAGLDFIARE 179
Cdd:cd03259 141 LARALAREPSLLLLDEPLSALDAKLRE 167
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-174 |
1.19e-24 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 96.62 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 1 MLIQLDQVGRMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGK---MPGKVGYSA-ETV 76
Cdd:COG4161 1 MSIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdFSQKPSEKAiRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 77 RQHIGFVshsllekFQEGE-----RVIDVVISGAFKSIGVYQDiddEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRV 151
Cdd:COG4161 81 RQKVGMV-------FQQYNlwphlTVMENLIEAPCKVLGLSKE---QAREKAMKLLARLRLTDKADRFPLHLSGGQQQRV 150
|
170 180
....*....|....*....|...
gi 686428090 152 MIARALMGQPQVLILDEPAAGLD 174
Cdd:COG4161 151 AIARALMMEPQVLLFDEPTAALD 173
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
15-178 |
1.20e-24 |
|
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: 96.03 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 15 KTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKmpgKVGYSAETVRQHIGFVSHS--LLEKFQ 92
Cdd:cd03263 15 KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGY---SIRTDRKAARQSLGYCPQFdaLFDELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 93 egerVID-VVISGAFKSIGvyqdiDDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDEPAA 171
Cdd:cd03263 92 ----VREhLRFYARLKGLP-----KSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTS 162
|
....*..
gi 686428090 172 GLDFIAR 178
Cdd:cd03263 163 GLDPASR 169
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
2-179 |
1.27e-24 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 96.69 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 2 LIQLDQVGRMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKmpGKVGYSAEtvrQHIG 81
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK--PVEGPGAE---RGVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 82 FVSHSLLEkfqeGERVIDVVISGaFKSIGVYQDiddEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQP 161
Cdd:PRK11248 76 FQNEGLLP----WRNVQDNVAFG-LQLAGVEKM---QRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANP 147
|
170
....*....|....*...
gi 686428090 162 QVLILDEPAAGLDFIARE 179
Cdd:PRK11248 148 QLLLLDEPFGALDAFTRE 165
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-179 |
1.83e-24 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 96.47 E-value: 1.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 1 MLIQLDQV----GRMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKmpgKV-GYSAE- 74
Cdd:COG4525 2 SMLTVRHVsvryPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGV---PVtGPGADr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 75 -TVRQHigfvsHSLLEKFqegeRVIDVVISGaFKSIGVYQDiddEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMI 153
Cdd:COG4525 79 gVVFQK-----DALLPWL----NVLDNVAFG-LRLRGVPKA---ERRARAEELLALVGLADFARRRIWQLSGGMRQRVGI 145
|
170 180
....*....|....*....|....*.
gi 686428090 154 ARALMGQPQVLILDEPAAGLDFIARE 179
Cdd:COG4525 146 ARALAADPRFLLMDEPFGALDALTRE 171
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
16-174 |
1.00e-23 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 94.04 E-value: 1.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 16 TILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKVGysaE----TVR-QHIGFVshsllek 90
Cdd:COG4181 26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALD---EdaraRLRaRHVGFV------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 91 FQEgervidvvisgafksigvYQDI-----------------DDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMI 153
Cdd:COG4181 96 FQS------------------FQLLptltalenvmlplelagRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVAL 157
|
170 180
....*....|....*....|.
gi 686428090 154 ARALMGQPQVLILDEPAAGLD 174
Cdd:COG4181 158 ARAFATEPAILFADEPTGNLD 178
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
2-174 |
1.09e-23 |
|
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: 94.10 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 2 LIQLDQV----GRMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKmpgKVGYSAETV- 76
Cdd:COG1124 1 MLEVRNLsvsyGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGR---PVTRRRRKAf 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 77 RQHIGFVshsllekFQEGE------RVIDVVISGAFKSIGVyqdidDEVRNEAHQLLKLVGMSAK-AQQYIGYLSTGEKQ 149
Cdd:COG1124 78 RRRVQMV-------FQDPYaslhprHTVDRILAEPLRIHGL-----PDREERIAELLEQVGLPPSfLDRYPHQLSGGQRQ 145
|
170 180
....*....|....*....|....*
gi 686428090 150 RVMIARALMGQPQVLILDEPAAGLD 174
Cdd:COG1124 146 RVAIARALILEPELLLLDEPTSALD 170
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
3-179 |
1.77e-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: 93.07 E-value: 1.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 3 IQLDQVGRMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKVGysaeTVRQHIGF 82
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLP----PHKRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 83 VshsllekFQegervidvviSGA-FKSIGVYQDI----------DDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRV 151
Cdd:cd03300 77 V-------FQ----------NYAlFPHLTVFENIafglrlkklpKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRV 139
|
170 180
....*....|....*....|....*...
gi 686428090 152 MIARALMGQPQVLILDEPAAGLDFIARE 179
Cdd:cd03300 140 AIARALVNEPKVLLLDEPLGALDLKLRK 167
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
13-174 |
2.19e-23 |
|
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: 96.51 E-value: 2.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 13 QGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPAT---TGSVNLFGKMPgkVGYSAETVRQHIGFVshslle 89
Cdd:COG1123 17 GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDL--LELSEALRGRRIGMV------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 90 kFQEGERVIDVVISG---AFkSIGVYQDIDDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLIL 166
Cdd:COG1123 89 -FQDPMTQLNPVTVGdqiAE-ALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIA 166
|
....*...
gi 686428090 167 DEPAAGLD 174
Cdd:COG1123 167 DEPTTALD 174
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-174 |
2.79e-23 |
|
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: 2.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 1 MLIQLDQVGRMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKVgysaeTVRQ-H 79
Cdd:cd03296 1 MSIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDV-----PVQErN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 80 IGFVshsllekFQEgervidvviSGAFKSIGVYQDI--------------DDEVRNEAHQLLKLVGMSAKAQQYIGYLST 145
Cdd:cd03296 76 VGFV-------FQH---------YALFRHMTVFDNVafglrvkprserppEAEIRAKVHELLKLVQLDWLADRYPAQLSG 139
|
170 180
....*....|....*....|....*....
gi 686428090 146 GEKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:cd03296 140 GQRQRVALARALAVEPKVLLLDEPFGALD 168
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
14-174 |
4.19e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 92.91 E-value: 4.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 14 GKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKmpGKVGYSAETVRQHIGfV---SHSLLEK 90
Cdd:PRK13548 14 GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGR--PLADWSPAELARRRA-VlpqHSSLSFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 91 FqegeRVIDVVISGAfksiGVYQDIDDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALM------GQPQVL 164
Cdd:PRK13548 91 F----TVEEVVAMGR----APHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWL 162
|
170
....*....|
gi 686428090 165 ILDEPAAGLD 174
Cdd:PRK13548 163 LLDEPTSALD 172
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
14-169 |
6.26e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.13 E-value: 6.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 14 GKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMpgKVGY--------SAETVRQHI--GF- 82
Cdd:COG0488 10 GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL--RIGYlpqeppldDDLTVLDTVldGDa 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 83 -----------VSHSLLEKFQEGERVIDvvISGAFKSIGVYqdiddEVRNEAHQLLKLVGMS-AKAQQYIGYLSTGEKQR 150
Cdd:COG0488 88 elraleaeleeLEAKLAEPDEDLERLAE--LQEEFEALGGW-----EAEARAEEILSGLGFPeEDLDRPVSELSGGWRRR 160
|
170
....*....|....*....
gi 686428090 151 VMIARALMGQPQVLILDEP 169
Cdd:COG0488 161 VALARALLSEPDLLLLDEP 179
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
3-178 |
7.62e-23 |
|
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: 90.32 E-value: 7.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 3 IQLDQVGRMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKVGYSAETVRQHIGF 82
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 83 VshsllekFQEGervidvvisGAFKSIGVYQDIddevrneahqllklvgmsakaqqyiGY-LSTGEKQRVMIARALMGQP 161
Cdd:cd03229 81 V-------FQDF---------ALFPHLTVLENI-------------------------ALgLSGGQQQRVALARALAMDP 119
|
170
....*....|....*..
gi 686428090 162 QVLILDEPAAGLDFIAR 178
Cdd:cd03229 120 DVLLLDEPTSALDPITR 136
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
14-177 |
9.48e-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: 91.41 E-value: 9.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 14 GKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKVGYSAET-VRQHIGFVshsllekFQ 92
Cdd:cd03261 12 GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYrLRRRMGML-------FQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 93 egervidvviSGA-FKSIGVYQDI-----------DDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQ 160
Cdd:cd03261 85 ----------SGAlFDSLTVFENVafplrehtrlsEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALD 154
|
170
....*....|....*..
gi 686428090 161 PQVLILDEPAAGLDFIA 177
Cdd:cd03261 155 PELLLYDEPTAGLDPIA 171
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
12-174 |
1.75e-22 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 89.98 E-value: 1.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 12 KQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKVGySAETV---RQHIGFVshsll 88
Cdd:TIGR03608 8 FGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLN-SKKASkfrREKLGYL----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 89 ekFQ-----EGERV---IDVVISGAFKSIGvyqdiddEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQ 160
Cdd:TIGR03608 82 --FQnfaliENETVeenLDLGLKYKKLSKK-------EKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKP 152
|
170
....*....|....
gi 686428090 161 PQVLILDEPAAGLD 174
Cdd:TIGR03608 153 PPLILADEPTGSLD 166
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
14-174 |
5.04e-22 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 88.25 E-value: 5.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 14 GKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKmpgKVGYSAET---VRQHIGFVshsllek 90
Cdd:TIGR01166 4 GPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGE---PLDYSRKGlleRRQRVGLV------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 91 FQEGERVIdvvisgaFkSIGVYQDI----------DDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQ 160
Cdd:TIGR01166 74 FQDPDDQL-------F-AADVDQDVafgplnlglsEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMR 145
|
170
....*....|....
gi 686428090 161 PQVLILDEPAAGLD 174
Cdd:TIGR01166 146 PDVLLLDEPTAGLD 159
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
18-179 |
8.16e-22 |
|
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: 88.58 E-value: 8.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 18 LKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKmpgKVGYSAETVRQHIGFVSHSL-----LEKFQ 92
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGH---DVVREPREVRRRIGIVFQDLsvddeLTGWE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 93 egerviDVVISGAfksigVYQDIDDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDEPAAG 172
Cdd:cd03265 93 ------NLYIHAR-----LYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIG 161
|
....*..
gi 686428090 173 LDFIARE 179
Cdd:cd03265 162 LDPQTRA 168
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
18-179 |
2.07e-21 |
|
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: 87.91 E-value: 2.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 18 LKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKM---PGK------VGYSA---ETVRQHIGFVSH 85
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQitePGPdrmvvfQNYSLlpwLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 86 SLLEKFQEGERvidvvisgafksigvyQDIDDEvrneaHqlLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLI 165
Cdd:TIGR01184 81 RVLPDLSKSER----------------RAIVEE-----H--IALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLL 137
|
170
....*....|....
gi 686428090 166 LDEPAAGLDFIARE 179
Cdd:TIGR01184 138 LDEPFGALDALTRG 151
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
18-179 |
2.24e-21 |
|
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: 88.99 E-value: 2.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 18 LKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKmpgKVGYSAETVRQHIGFVshsllekFQEgeRV 97
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGY---DVVREPRKVRRSIGIV-------PQY--AS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 98 IDVVISGA--FKSIGVYQDI-DDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:TIGR01188 77 VDEDLTGRenLEMMGRLYGLpKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLD 156
|
....*
gi 686428090 175 FIARE 179
Cdd:TIGR01188 157 PRTRR 161
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
2-174 |
2.29e-21 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 87.56 E-value: 2.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 2 LIQLDQV-GRMKQGKT---ILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKVGYS--AET 75
Cdd:PRK11629 5 LLQCDNLcKRYQEGSVqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 76 VRQHIGFVS--HSLLEKFQEGERVIDVVISGAFKSigvyqdidDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMI 153
Cdd:PRK11629 85 RNQKLGFIYqfHHLLPDFTALENVAMPLLIGKKKP--------AEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAI 156
|
170 180
....*....|....*....|.
gi 686428090 154 ARALMGQPQVLILDEPAAGLD 174
Cdd:PRK11629 157 ARALVNNPRLVLADEPTGNLD 177
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
13-174 |
4.47e-21 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 87.50 E-value: 4.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 13 QGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNL----------FGKMPGKVgysaETVRQHIGF 82
Cdd:PRK11264 14 HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidtarsLSQQKGLI----RQLRQHVGF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 83 VSHSL--------LEKFQEGErvidVVISGAFKsigvyqdidDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIA 154
Cdd:PRK11264 90 VFQNFnlfphrtvLENIIEGP----VIVKGEPK---------EEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIA 156
|
170 180
....*....|....*....|
gi 686428090 155 RALMGQPQVLILDEPAAGLD 174
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALD 176
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
14-174 |
5.72e-21 |
|
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: 86.57 E-value: 5.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 14 GKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKVGYSA-ETVRQHIGFVshsllekFQ 92
Cdd:COG1127 17 DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElYELRRRIGML-------FQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 93 egervidvviSGA-FKSIGVYQDI-----------DDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQ 160
Cdd:COG1127 90 ----------GGAlFDSLTVFENVafplrehtdlsEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALD 159
|
170
....*....|....
gi 686428090 161 PQVLILDEPAAGLD 174
Cdd:COG1127 160 PEILLYDEPTAGLD 173
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-176 |
6.18e-21 |
|
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: 89.89 E-value: 6.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 3 IQLDQV--GRMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLN-ILNAYEPaTTGSVnLFGKMPGKvGYSAETVRQH 79
Cdd:COG2274 474 IELENVsfRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKlLLGLYEP-TSGRI-LIDGIDLR-QIDPASLRRQ 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 80 IGFVShsllekfQEGErvidvVISGafkSI-----GVYQDIDDEvrnEAHQLLKLVGmsakAQQYI-----GY------- 142
Cdd:COG2274 551 IGVVL-------QDVF-----LFSG---TIrenitLGDPDATDE---EIIEAARLAG----LHDFIealpmGYdtvvgeg 608
|
170 180 190
....*....|....*....|....*....|....*..
gi 686428090 143 ---LSTGEKQRVMIARALMGQPQVLILDEPAAGLDFI 176
Cdd:COG2274 609 gsnLSGGQRQRLAIARALLRNPRILILDEATSALDAE 645
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-178 |
1.02e-20 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 87.89 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 1 MLIQLDQVGrmKQ--GKTILKNISWQINGGDkwiLYGL---NGAGKTTLLNILNAYEPATTGSVnLFGkmpGKVGYSAET 75
Cdd:COG1118 1 MSIEVRNIS--KRfgSFTLLDDVSLEIASGE---LVALlgpSGSGKTTLLRIIAGLETPDSGRI-VLN---GRDLFTNLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 76 VRQ-HIGFVshsllekFQEgervidvviSGAFKSIGVYQDI----------DDEVRNEAHQLLKLVGMSAKAQQYIGYLS 144
Cdd:COG1118 72 PRErRVGFV-------FQH---------YALFPHMTVAENIafglrvrppsKAEIRARVEELLELVQLEGLADRYPSQLS 135
|
170 180 190
....*....|....*....|....*....|....
gi 686428090 145 TGEKQRVMIARALMGQPQVLILDEPAAGLDFIAR 178
Cdd:COG1118 136 GGQRQRVALARALAVEPEVLLLDEPFGALDAKVR 169
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
16-174 |
1.06e-20 |
|
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: 85.64 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 16 TILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGK-MPGKVGYSAETVRQHIGFVshsllekFQE- 93
Cdd:cd03257 19 KALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdLLKLSRRLRKIRRKEIQMV-------FQDp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 94 ----------GERVIDVVISgafksigVYQDIDDEVRNEA-HQLLKLVGMSAK-AQQYIGYLSTGEKQRVMIARALMGQP 161
Cdd:cd03257 92 msslnprmtiGEQIAEPLRI-------HGKLSKKEARKEAvLLLLVGVGLPEEvLNRYPHELSGGQRQRVAIARALALNP 164
|
170
....*....|...
gi 686428090 162 QVLILDEPAAGLD 174
Cdd:cd03257 165 KLLIADEPTSALD 177
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-174 |
1.33e-20 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 87.44 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 3 IQLDQVG---RMKQGK-TILKNISWQINGGDkwiLY---GLNGAGKTTLLNILNAYEPATTGSVNLFG----KMPGKvgy 71
Cdd:COG1135 2 IELENLSktfPTKGGPvTALDDVSLTIEKGE---IFgiiGYSGAGKSTLIRCINLLERPTSGSVLVDGvdltALSER--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 72 saE--TVRQHIGFVS-H-SLLEkfqegER-VIDVV-----ISGAFKSigvyqdiddEVRNEAHQLLKLVGMSAKAQQYIG 141
Cdd:COG1135 76 --ElrAARRKIGMIFqHfNLLS-----SRtVAENValpleIAGVPKA---------EIRKRVAELLELVGLSDKADAYPS 139
|
170 180 190
....*....|....*....|....*....|...
gi 686428090 142 YLSTGEKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:COG1135 140 QLSGGQKQRVGIARALANNPKVLLCDEATSALD 172
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-174 |
1.42e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 87.45 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 1 MLIQLDQVGRMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKVgySAETvrQHI 80
Cdd:PRK10851 1 MSIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL--HARD--RKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 81 GFVshsllekFQEgervidvviSGAFKSIGVYQDI--------------DDEVRNEAHQLLKLVGMSAKAQQYIGYLSTG 146
Cdd:PRK10851 77 GFV-------FQH---------YALFRHMTVFDNIafgltvlprrerpnAAAIKAKVTQLLEMVQLAHLADRYPAQLSGG 140
|
170 180
....*....|....*....|....*...
gi 686428090 147 EKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:PRK10851 141 QKQRVALARALAVEPQILLLDEPFGALD 168
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
2-174 |
1.72e-20 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 87.46 E-value: 1.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 2 LIQLDQVGRMKQGKTILKNISWQINGGDkwI--LYGLNGAGKTTLLNILNAYEPATTGSVNLFGKM-----PGKvgysae 74
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGE--FvaLLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDvtglpPEK------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 75 tvRqHIGFVshsllekFQE---------GERVidvvisgAF--KSIGVYQDiddEVRNEAHQLLKLVGMSAKAQQYIGYL 143
Cdd:COG3842 77 --R-NVGMV-------FQDyalfphltvAENV-------AFglRMRGVPKA---EIRARVAELLELVGLEGLADRYPHQL 136
|
170 180 190
....*....|....*....|....*....|.
gi 686428090 144 STGEKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:COG3842 137 SGGQQQRVALARALAPEPRVLLLDEPLSALD 167
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
14-179 |
8.99e-20 |
|
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: 83.38 E-value: 8.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 14 GKTILKNISWQINGGDKWILYGLNGAGKTTLLNILN------AYEPaTTGSVNLFGKMPGKVGYSAETVRQHIGFVshsl 87
Cdd:cd03260 12 DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNrlndliPGAP-DEGEVLLDGKDIYDLDVDVLELRRRVGMV---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 88 lekFQEgerviDVVISGAfksigVYQDI-----------DDEVRNEAHQLLKLVGM--SAKAQQYIGYLSTGEKQRVMIA 154
Cdd:cd03260 87 ---FQK-----PNPFPGS-----IYDNVayglrlhgiklKEELDERVEEALRKAALwdEVKDRLHALGLSGGQQQRLCLA 153
|
170 180
....*....|....*....|....*
gi 686428090 155 RALMGQPQVLILDEPAAGLDFIARE 179
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTA 178
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
16-174 |
9.86e-20 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 83.60 E-value: 9.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 16 TILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVnLFGKMPGKVGYSAE-TVRQHIGFV--SHSLLEKFQ 92
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDL-IVDGLKVNDPKVDErLIRQEAGMVfqQFYLFPHLT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 93 EGERVidvvisgAFKSIGVYQDIDDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDEPAAG 172
Cdd:PRK09493 94 ALENV-------MFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSA 166
|
..
gi 686428090 173 LD 174
Cdd:PRK09493 167 LD 168
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
13-174 |
1.10e-19 |
|
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: 81.66 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 13 QGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKmPGKvGYSAETVRQHIGFVShsllekfq 92
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGV-DLR-DLDLESLRKNIAYVP-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 93 egervidvvisgafksigvyQDI---DDEVRNEahqllklvgmsakaqqyIgyLSTGEKQRVMIARALMGQPQVLILDEP 169
Cdd:cd03228 83 --------------------QDPflfSGTIREN-----------------I--LSGGQRQRIAIARALLRDPPILILDEA 123
|
....*
gi 686428090 170 AAGLD 174
Cdd:cd03228 124 TSALD 128
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
14-174 |
1.62e-19 |
|
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: 82.46 E-value: 1.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 14 GKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKV-GYSAETVRQHIGFVshsllekFQ 92
Cdd:cd03292 13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrGRAIPYLRRKIGVV-------FQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 93 EGERVID--VVISGAFkSIGVYQDIDDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDEPA 170
Cdd:cd03292 86 DFRLLPDrnVYENVAF-ALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPT 164
|
....
gi 686428090 171 AGLD 174
Cdd:cd03292 165 GNLD 168
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-174 |
3.53e-19 |
|
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: 84.42 E-value: 3.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 3 IQLDQVG-RMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKvgYSAETVRQHIG 81
Cdd:COG4988 337 IELEDVSfSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSD--LDPASWRRQIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 82 FVSH-------SLLEKFQEGERvidvvisgafksigvyqDIDDEvrnEAHQLLKLVGMSAKAQQY-------IGY----L 143
Cdd:COG4988 415 WVPQnpylfagTIRENLRLGRP-----------------DASDE---ELEAALEAAGLDEFVAALpdgldtpLGEggrgL 474
|
170 180 190
....*....|....*....|....*....|.
gi 686428090 144 STGEKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:COG4988 475 SGGQAQRLALARALLRDAPLLLLDEPTAHLD 505
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-179 |
3.72e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 82.85 E-value: 3.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 3 IQLDQVGRMKQGKTILKNISWQINGGDkwiLYGL---NGAGKTTLLNILNAYEPATTGSVNLFGKmpgKVGYSaetVRQH 79
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGE---IFGLlgpNGAGKTTTIRIILGILAPDSGEVLWDGE---PLDPE---DRRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 80 IGFvshsLLEkfqegER-------VIDVVIS-GAFKSIGvyqdiDDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRV 151
Cdd:COG4152 73 IGY----LPE-----ERglypkmkVGEQLVYlARLKGLS-----KAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKV 138
|
170 180
....*....|....*....|....*...
gi 686428090 152 MIARALMGQPQVLILDEPAAGLDFIARE 179
Cdd:COG4152 139 QLIAALLHDPELLILDEPFSGLDPVNVE 166
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-178 |
5.57e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 81.65 E-value: 5.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 5 LDQVGRMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVnLFGKMPgkvgysAETVRQHIGFVs 84
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAP------LAEAREDTRLM- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 85 hsllekFQEG-----ERVIDVV---ISGAFksigvyqdiddevRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARA 156
Cdd:PRK11247 87 ------FQDArllpwKKVIDNVglgLKGQW-------------RDAALQALAAVGLADRANEWPAALSGGQKQRVALARA 147
|
170 180
....*....|....*....|..
gi 686428090 157 LMGQPQVLILDEPAAGLDFIAR 178
Cdd:PRK11247 148 LIHRPGLLLLDEPLGALDALTR 169
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-174 |
5.70e-19 |
|
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: 84.05 E-value: 5.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 3 IQLDQV--GRMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKvgYSAETVRQHI 80
Cdd:COG4987 334 LELEDVsfRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRD--LDEDDLRRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 81 GFVS---H----SLLEKFqegeRVIDvvisgafksigvyQDIDDEvrnEAHQLLKLVGMSA-KAQQYIGY---------- 142
Cdd:COG4987 412 AVVPqrpHlfdtTLRENL----RLAR-------------PDATDE---ELWAALERVGLGDwLAALPDGLdtwlgeggrr 471
|
170 180 190
....*....|....*....|....*....|..
gi 686428090 143 LSTGEKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:COG4987 472 LSGGERRRLALARALLRDAPILLLDEPTEGLD 503
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
10-174 |
7.02e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 81.71 E-value: 7.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 10 RMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMpgkvgYSAET---VRQHIGFVshs 86
Cdd:PRK13647 13 RYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGRE-----VNAENekwVRSKVGLV--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 87 llekFQEGErviDVVISGAfksigVYQDI----------DDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARA 156
Cdd:PRK13647 85 ----FQDPD---DQVFSST-----VWDDVafgpvnmgldKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGV 152
|
170
....*....|....*...
gi 686428090 157 LMGQPQVLILDEPAAGLD 174
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLD 170
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
12-174 |
7.48e-19 |
|
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: 80.38 E-value: 7.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 12 KQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGK------VGYSAETVRQHIGFVSh 85
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAkerrksIGYVMQDVDYQLFTDS- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 86 sllekfqegerVIDVVISGAfksigvyqDIDDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLI 165
Cdd:cd03226 89 -----------VREELLLGL--------KELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
....*....
gi 686428090 166 LDEPAAGLD 174
Cdd:cd03226 150 FDEPTSGLD 158
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-175 |
9.39e-19 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 82.69 E-value: 9.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 2 LIQLDQVGRMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKVgySAEtvRQHIG 81
Cdd:PRK09452 14 LVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHV--PAE--NRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 82 FVshsllekFQegervidvviSGA-FKSIGVYQDI----------DDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQR 150
Cdd:PRK09452 90 TV-------FQ----------SYAlFPHMTVFENVafglrmqktpAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQR 152
|
170 180
....*....|....*....|....*
gi 686428090 151 VMIARALMGQPQVLILDEPAAGLDF 175
Cdd:PRK09452 153 VAIARAVVNKPKVLLLDESLSALDY 177
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
20-179 |
1.30e-18 |
|
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: 80.03 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 20 NISWQINGGDKWILyGLNGAGKTTLLNILNAYEPATTGSVNLFGKM--PGKVGYSAETVRQHIGFVshsllekFQEgerv 97
Cdd:cd03297 16 KIDFDLNEEVTGIF-GASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfDSRKKINLPPQQRKIGLV-------FQQ---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 98 idvviSGAFKSIGVYQDI--------DDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDEP 169
Cdd:cd03297 84 -----YALFPHLNVRENLafglkrkrNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEP 158
|
170
....*....|
gi 686428090 170 AAGLDFIARE 179
Cdd:cd03297 159 FSALDRALRL 168
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
10-174 |
2.61e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 80.66 E-value: 2.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 10 RMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVnLFGKMPgkVGYSAE---TVRQHIGFVshs 86
Cdd:PRK13636 14 NYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRI-LFDGKP--IDYSRKglmKLRESVGMV--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 87 llekFQEGERvidvvisgAFKSIGVYQDI----------DDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARA 156
Cdd:PRK13636 88 ----FQDPDN--------QLFSASVYQDVsfgavnlklpEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGV 155
|
170
....*....|....*...
gi 686428090 157 LMGQPQVLILDEPAAGLD 174
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLD 173
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
3-179 |
4.71e-18 |
|
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: 78.88 E-value: 4.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 3 IQLDQVG-RMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILN-AYEPaTTGSVNLFGKmpGKVGYSAETVRQHI 80
Cdd:cd03295 1 IEFENVTkRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINrLIEP-TSGEIFIDGE--DIREQDPVELRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 81 GFVSHSLlekfqegervidvvisGAFKSIGVYQDI----------DDEVRNEAHQLLKLVGMSAK--AQQYIGYLSTGEK 148
Cdd:cd03295 78 GYVIQQI----------------GLFPHMTVEENIalvpkllkwpKEKIRERADELLALVGLDPAefADRYPHELSGGQQ 141
|
170 180 190
....*....|....*....|....*....|.
gi 686428090 149 QRVMIARALMGQPQVLILDEPAAGLDFIARE 179
Cdd:cd03295 142 QRVGVARALAADPPLLLMDEPFGALDPITRD 172
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
18-179 |
4.90e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 79.67 E-value: 4.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 18 LKNISWQINGGDkWI-LYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMpgkvgYSAETV---RQHIGFVshsllekFQE 93
Cdd:PRK13635 23 LKDVSFSVYEGE-WVaIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV-----LSEETVwdvRRQVGMV-------FQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 94 ------GERVIDVVISGaFKSIGVYQDiddEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILD 167
Cdd:PRK13635 90 pdnqfvGATVQDDVAFG-LENIGVPRE---EMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILD 165
|
170
....*....|..
gi 686428090 168 EPAAGLDFIARE 179
Cdd:PRK13635 166 EATSMLDPRGRR 177
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
14-174 |
7.36e-18 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 78.42 E-value: 7.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 14 GKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVnLFGKMPGKvGYSAETVRQHIGFV-------SHS 86
Cdd:cd03254 15 KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQI-LIDGIDIR-DISRKSLRSMIGVVlqdtflfSGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 87 LLEKFQEG-ERVIDVVISGAFKSIGvyqdIDDEVRNEAHQLLKLVGMSAkaqqyiGYLSTGEKQRVMIARALMGQPQVLI 165
Cdd:cd03254 93 IMENIRLGrPNATDEEVIEAAKEAG----AHDFIMKLPNGYDTVLGENG------GNLSQGERQLLAIARAMLRDPKILI 162
|
....*....
gi 686428090 166 LDEPAAGLD 174
Cdd:cd03254 163 LDEATSNID 171
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
13-179 |
1.05e-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 upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 78.63 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 13 QGKTILKNISWQINGGDkWI-LYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGkvgySAETV---RQHIGFVshsll 88
Cdd:TIGR04520 13 SEKPALKNVSLSIEKGE-FVaIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTL----DEENLweiRKKVGMV----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 89 ekFQE------GERVIDVVisgAF--KSIGVYQDiddEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQ 160
Cdd:TIGR04520 83 --FQNpdnqfvGATVEDDV---AFglENLGVPRE---EMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMR 154
|
170
....*....|....*....
gi 686428090 161 PQVLILDEPAAGLDFIARE 179
Cdd:TIGR04520 155 PDIIILDEATSMLDPKGRK 173
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
14-174 |
1.06e-17 |
|
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: 77.40 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 14 GKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKVgysAETVRQHIGFVSH-------- 85
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQ---RDEPHENILYLGHlpglkpel 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 86 SLLEKFQegervidvvisgafksigVYQDIDDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLI 165
Cdd:TIGR01189 89 SALENLH------------------FWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWI 150
|
....*....
gi 686428090 166 LDEPAAGLD 174
Cdd:TIGR01189 151 LDEPTTALD 159
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-178 |
1.10e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 79.08 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 3 IQLDQVGRMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGK-MPGKvgysAETVRQHIG 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEpVPSR----ARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 82 FVSH--SLLEKFQEGErviDVVISGAFKSIGVYQdiddeVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMG 159
Cdd:PRK13537 84 VVPQfdNLDPDFTVRE---NLLVFGRYFGLSAAA-----ARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVN 155
|
170
....*....|....*....
gi 686428090 160 QPQVLILDEPAAGLDFIAR 178
Cdd:PRK13537 156 DPDVLVLDEPTTGLDPQAR 174
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
3-174 |
1.20e-17 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 77.87 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 3 IQLDQVgRMKQGKTILkNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKVGYSAETVrqhigf 82
Cdd:COG3840 2 LRLDDL-TYRYGDFPL-RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPV------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 83 vshSLLekFQEGErvidvvisgAFKSIGVYQDI----------DDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVM 152
Cdd:COG3840 74 ---SML--FQENN---------LFPHLTVAQNIglglrpglklTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVA 139
|
170 180
....*....|....*....|...
gi 686428090 153 IARAL-MGQPqVLILDEPAAGLD 174
Cdd:COG3840 140 LARCLvRKRP-ILLLDEPFSALD 161
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
2-174 |
1.79e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 77.75 E-value: 1.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 2 LIQLDQVGRMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAY---EPATTGSVNLFGKMPGKVGYSAETVRQ 78
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRLARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 79 ---HIGFVshslLEKFQEGER--VIDVVISGAFKSIGVYQD----IDDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQ 149
Cdd:PRK09984 84 sraNTGYI----FQQFNLVNRlsVLENVLIGALGSTPFWRTcfswFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQ 159
|
170 180
....*....|....*....|....*
gi 686428090 150 RVMIARALMGQPQVLILDEPAAGLD 174
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLD 184
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
18-178 |
2.96e-17 |
|
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: 76.64 E-value: 2.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 18 LKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKmpgKVGYSAETVRQHIGFVShsllekfqEGERV 97
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGF---DVVKEPAEARRRLGFVS--------DSTGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 98 IDVVisGAFKSIGVYQDIDDEVRNEAHQ----LLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDEPAAGL 173
Cdd:cd03266 90 YDRL--TARENLEYFAGLYGLKGDELTArleeLADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGL 167
|
....*
gi 686428090 174 DFIAR 178
Cdd:cd03266 168 DVMAT 172
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1-174 |
3.02e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 77.75 E-value: 3.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 1 MLIQLDQVGRMKQGKT-----ILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKM--PGKVGYSA 73
Cdd:PRK13634 1 MDITFQKVEHRYQYKTpferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVitAGKKNKKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 74 ETVRQHIGFV----SHSLLEKFQEGErvidvvISGAFKSIGVYQDiddEVRNEAHQLLKLVGMSAKAQQYIGY-LSTGEK 148
Cdd:PRK13634 81 KPLRKKVGIVfqfpEHQLFEETVEKD------ICFGPMNFGVSEE---DAKQKAREMIELVGLPEELLARSPFeLSGGQM 151
|
170 180
....*....|....*....|....*.
gi 686428090 149 QRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:PRK13634 152 RRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
7-174 |
3.16e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 76.74 E-value: 3.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 7 QVGRMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKVGYS--AETVRQHIGFVS 84
Cdd:PRK10584 15 SVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEarAKLRAKHVGFVF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 85 HS--LLEKFQEGERV-IDVVISGafksigvyqDIDDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQP 161
Cdd:PRK10584 95 QSfmLIPTLNALENVeLPALLRG---------ESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165
|
170
....*....|...
gi 686428090 162 QVLILDEPAAGLD 174
Cdd:PRK10584 166 DVLFADEPTGNLD 178
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
17-177 |
3.98e-17 |
|
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: 76.16 E-value: 3.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 17 ILKNISWQINGGDKWILYGLNGAGKTTLLNILNA---YEPATTGSVNLFGK------MPGKVGY--------SAETVRQH 79
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQprkpdqFQKCVAYvrqddillPGLTVRET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 80 IGFVSHSLL-EKFQEGERVIDVVISGafksigvyqdiddevrneahqlLKLVGMSAKAQQYIGYLSTGEKQRVMIARALM 158
Cdd:cd03234 102 LTYTAILRLpRKSSDAIRKKRVEDVL----------------------LRDLALTRIGGNLVKGISGGERRRVSIAVQLL 159
|
170 180
....*....|....*....|
gi 686428090 159 GQPQVLILDEPAAGLD-FIA 177
Cdd:cd03234 160 WDPKVLILDEPTSGLDsFTA 179
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-173 |
4.08e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 76.69 E-value: 4.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 18 LKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVnLFG-----KMPgkvgySAETVRQHIG--------FVS 84
Cdd:COG4674 26 LNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSV-LFGgtdltGLD-----EHEIARLGIGrkfqkptvFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 85 HSLLEKFQ---EGERvidvvisGAFKSIGvyQDIDDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQP 161
Cdd:COG4674 100 LTVFENLElalKGDR-------GVFASLF--ARLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDP 170
|
170
....*....|..
gi 686428090 162 QVLILDEPAAGL 173
Cdd:COG4674 171 KLLLLDEPVAGM 182
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
12-174 |
4.90e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 76.85 E-value: 4.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 12 KQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGkMPgkvgySAETVRQH-IGFVSHSLLEK 90
Cdd:PRK15056 17 RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILG-QP-----TRQALQKNlVAYVPQSEEVD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 91 FQEGERVIDVVISGAFKSIGVYQDIDDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDEPA 170
Cdd:PRK15056 91 WSFPVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPF 170
|
....
gi 686428090 171 AGLD 174
Cdd:PRK15056 171 TGVD 174
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
37-173 |
5.27e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.14 E-value: 5.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 37 NGAGKTTLLNILNAYEPATTGSVNLFGKmPGKVGYSAETVRQHIGFVS-H-SLLEKFqegeRVIDVVISGAFKSIGVYQD 114
Cdd:COG3845 40 NGAGKSTLMKILYGLYQPDSGEILIDGK-PVRIRSPRDAIALGIGMVHqHfMLVPNL----TVAENIVLGLEPTKGGRLD 114
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 686428090 115 IDdEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDEPAAGL 173
Cdd:COG3845 115 RK-AARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVL 172
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
14-177 |
5.38e-17 |
|
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: 76.04 E-value: 5.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 14 GKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFG----KMPGKvgysaETVRQHIGFVShslle 89
Cdd:cd03218 12 KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGqditKLPMH-----KRARLGIGYLP----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 90 kfQEgervidvviSGAFKSIGVYQDI----------DDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMG 159
Cdd:cd03218 82 --QE---------ASIFRKLTVEENIlavleirglsKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALAT 150
|
170
....*....|....*...
gi 686428090 160 QPQVLILDEPAAGLDFIA 177
Cdd:cd03218 151 NPKFLLLDEPFAGVDPIA 168
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
15-179 |
5.69e-17 |
|
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: 75.39 E-value: 5.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 15 KTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKmpgKVGYSAetvRQHIGFV--SHSLLEKfq 92
Cdd:cd03269 13 VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGK---PLDIAA---RNRIGYLpeERGLYPK-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 93 egERVIDVVIS-GAFKSIGVyqdidDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDEPAA 171
Cdd:cd03269 85 --MKVIDQLVYlAQLKGLKK-----EEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
....*...
gi 686428090 172 GLDFIARE 179
Cdd:cd03269 158 GLDPVNVE 165
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
17-174 |
7.19e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 77.84 E-value: 7.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 17 ILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKVGYS--AETVRQHIGFV--SHSLLEKFQ 92
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADalAQLRREHFGFIfqRYHLLSHLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 93 EGERV-IDVVISGAFKSigvyqdiddEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDEPAA 171
Cdd:PRK10535 103 AAQNVeVPAVYAGLERK---------QRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTG 173
|
...
gi 686428090 172 GLD 174
Cdd:PRK10535 174 ALD 176
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
14-174 |
9.58e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 77.19 E-value: 9.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 14 GKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKVgySAETVRQHIGFVSH--SLLEKF 91
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEAL--SARAASRRVASVPQdtSLSFEF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 92 qegeRVIDVVISGAFKSIGVYQDIDDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDEPAA 171
Cdd:PRK09536 93 ----DVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTA 168
|
...
gi 686428090 172 GLD 174
Cdd:PRK09536 169 SLD 171
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
14-179 |
1.23e-16 |
|
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: 72.87 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 14 GKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMpgKVGYsaetVRQhigfvshsllekfqe 93
Cdd:cd03221 12 GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV--KIGY----FEQ--------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 94 gervidvvisgafksigvyqdiddevrneahqllklvgmsakaqqyigyLSTGEKQRVMIARALMGQPQVLILDEPAAGL 173
Cdd:cd03221 71 -------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHL 101
|
....*.
gi 686428090 174 DFIARE 179
Cdd:cd03221 102 DLESIE 107
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
9-174 |
1.56e-16 |
|
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: 74.12 E-value: 1.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 9 GRMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAY--EPATTGSVNLFGKMPGKvgysaETVRQHIGFVShs 86
Cdd:cd03213 16 SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDK-----RSFRKIIGYVP-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 87 llekfQEgerviDVVISgafksigvyqdiDDEVRnEAhqllklVGMSAKAQQyigyLSTGEKQRVMIARALMGQPQVLIL 166
Cdd:cd03213 89 -----QD-----DILHP------------TLTVR-ET------LMFAAKLRG----LSGGERKRVSIALELVSNPSLLFL 135
|
....*...
gi 686428090 167 DEPAAGLD 174
Cdd:cd03213 136 DEPTSGLD 143
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
14-174 |
1.64e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 75.50 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 14 GKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKmpgKVGYSAET---VRQHIGFVshsllek 90
Cdd:PRK13639 14 GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGE---PIKYDKKSlleVRKTVGIV------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 91 FQEGERVI-------DVvisgAFKSIGVYQDiDDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQV 163
Cdd:PRK13639 84 FQNPDDQLfaptveeDV----AFGPLNLGLS-KEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEI 158
|
170
....*....|.
gi 686428090 164 LILDEPAAGLD 174
Cdd:PRK13639 159 IVLDEPTSGLD 169
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
18-179 |
2.14e-16 |
|
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: 74.99 E-value: 2.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 18 LKNISWQINGGDKWILYGLNGAGKTTLLNILNA-YEPaTTGSVNLFGKMPGKVgySAETVR-----------QHIGFVSH 85
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRlIEP-TSGKVLIDGQDIAAM--SRKELRelrrkkismvfQSFALLPH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 86 -SLLEKFQEGERVidvvisgafksigvyQDIDDEVRNE-AHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQV 163
Cdd:cd03294 117 rTVLENVAFGLEV---------------QGVPRAEREErAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDI 181
|
170
....*....|....*..
gi 686428090 164 LILDEPAAGLD-FIARE 179
Cdd:cd03294 182 LLMDEAFSALDpLIRRE 198
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
38-174 |
3.57e-16 |
|
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: 75.09 E-value: 3.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 38 GAGKTTL-LNILNAYEPA--TTGSVnLFGkmpGK--VGYSAETVRQ----HIGFVshsllekFQE-----------GERV 97
Cdd:COG0444 41 GSGKSTLaRAILGLLPPPgiTSGEI-LFD---GEdlLKLSEKELRKirgrEIQMI-------FQDpmtslnpvmtvGDQI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 98 IDVVIsgafksigVYQDID-DEVRNEAHQLLKLVGMSAKAQQYIGY---LSTGEKQRVMIARALMGQPQVLILDEPAAGL 173
Cdd:COG0444 110 AEPLR--------IHGGLSkAEARERAIELLERVGLPDPERRLDRYpheLSGGMRQRVMIARALALEPKLLIADEPTTAL 181
|
.
gi 686428090 174 D 174
Cdd:COG0444 182 D 182
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
33-174 |
4.00e-16 |
|
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: 75.14 E-value: 4.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 33 LYGLNGAGKTTLLNILNAYEPATTGSVNLFGKmpgkVGYSAETV------RQHIGFVshsllekFQE------------- 93
Cdd:COG4148 30 LFGPSGSGKTTLLRAIAGLERPDSGRIRLGGE----VLQDSARGiflpphRRRIGYV-------FQEarlfphlsvrgnl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 94 --GERVIDVvisgafksigvyqdidDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDEPAA 171
Cdd:COG4148 99 lyGRKRAPR----------------AERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLA 162
|
...
gi 686428090 172 GLD 174
Cdd:COG4148 163 ALD 165
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
15-179 |
5.76e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 73.93 E-value: 5.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 15 KTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKVGYSAETVRQHIGFVSHslLEKFQEG 94
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIRKKVGLVFQ--YPEYQLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 95 ERVIDVVISGAFKSIGVYqdiDDEVRNEAHQLLKLVGMSakaqqYIGY-------LSTGEKQRVMIARALMGQPQVLILD 167
Cdd:PRK13637 98 EETIEKDIAFGPINLGLS---EEEIENRVKRAMNIVGLD-----YEDYkdkspfeLSGGQKRRVAIAGVVAMEPKILILD 169
|
170
....*....|..
gi 686428090 168 EPAAGLDFIARE 179
Cdd:PRK13637 170 EPTAGLDPKGRD 181
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-178 |
6.15e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 74.48 E-value: 6.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 1 MLIQLDQVGRMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFG-KMPGKvgysAETVRQH 79
Cdd:PRK13536 40 VAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGvPVPAR----ARLARAR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 80 IGFVSH--SLLEKFQEGErviDVVISGAFKSIGVyqdidDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARAL 157
Cdd:PRK13536 116 IGVVPQfdNLDLEFTVRE---NLLVFGRYFGMST-----REIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARAL 187
|
170 180
....*....|....*....|.
gi 686428090 158 MGQPQVLILDEPAAGLDFIAR 178
Cdd:PRK13536 188 INDPQLLILDEPTTGLDPHAR 208
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
17-173 |
6.84e-16 |
|
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: 72.85 E-value: 6.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 17 ILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGK----MPgkvgySAETVRQHIGFVshsllekfQ 92
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditgLP-----PHERARAGIGYV--------P 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 93 EGERVidvvisgaFKS--------IGVYQDIDDEVR---NEAHQL---LKlvgmsAKAQQYIGYLSTGEKQRVMIARALM 158
Cdd:cd03224 82 EGRRI--------FPEltveenllLGAYARRRAKRKarlERVYELfprLK-----ERRKQLAGTLSGGEQQMLAIARALM 148
|
170
....*....|....*
gi 686428090 159 GQPQVLILDEPAAGL 173
Cdd:cd03224 149 SRPKLLLLDEPSEGL 163
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
18-174 |
6.87e-16 |
|
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: 72.62 E-value: 6.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 18 LKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVnLFGKMPGKVgYSAETVRQHIGFVSH-------SLLEK 90
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSV-LLDGTDIRQ-LDPADLRRNIGYVPQdvtlfygTLRDN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 91 FQEGERVI-DVVISGAFKSIGVyqdiDDEVRNEAHQLLKLVGMSAKAqqyigyLSTGEKQRVMIARALMGQPQVLILDEP 169
Cdd:cd03245 98 ITLGAPLAdDERILRAAELAGV----TDFVNKHPNGLDLQIGERGRG------LSGGQRQAVALARALLNDPPILLLDEP 167
|
....*
gi 686428090 170 AAGLD 174
Cdd:cd03245 168 TSAMD 172
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
2-174 |
6.92e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 72.99 E-value: 6.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 2 LIQLDQVGRMK-QGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKVGYS-AETVRQH 79
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNReVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 80 IGFV---SHSLLEKFQEGERVIDVVISGAFksigvyqdiDDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARA 156
Cdd:PRK10908 81 IGMIfqdHHLLMDRTVYDNVAIPLIIAGAS---------GDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARA 151
|
170
....*....|....*...
gi 686428090 157 LMGQPQVLILDEPAAGLD 174
Cdd:PRK10908 152 VVNKPAVLLADEPTGNLD 169
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
10-178 |
8.18e-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: 74.38 E-value: 8.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 10 RMKQGKTILKnISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKM--PGKVGYSAETVRQHIGFVshsl 87
Cdd:TIGR02142 6 SKRLGDFSLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTlfDSRKGIFLPPEKRRIGYV---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 88 lekFQEGE-----RVIDVVISGAFKSIGVYQDIDDEvrneahQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQ 162
Cdd:TIGR02142 81 ---FQEARlfphlSVRGNLRYGMKRARPSERRISFE------RVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPR 151
|
170
....*....|....*.
gi 686428090 163 VLILDEPAAGLDFIAR 178
Cdd:TIGR02142 152 LLLMDEPLAALDDPRK 167
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-174 |
1.03e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 72.44 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 1 MLIQLDQVGRMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKmpGKVGYSAETVRQHi 80
Cdd:PRK10247 6 PLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGE--DISTLKPEIYRQQ- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 81 gfVSHSLLEKFQEGERVIDVVIsgaFKsigvYQdiddeVRNEAHQLLKLVGMSAK-------AQQYIGYLSTGEKQRVMI 153
Cdd:PRK10247 83 --VSYCAQTPTLFGDTVYDNLI---FP----WQ-----IRNQQPDPAIFLDDLERfalpdtiLTKNIAELSGGEKQRISL 148
|
170 180
....*....|....*....|.
gi 686428090 154 ARALMGQPQVLILDEPAAGLD 174
Cdd:PRK10247 149 IRNLQFMPKVLLLDEITSALD 169
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
20-174 |
1.16e-15 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 72.72 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 20 NISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGK----MPGKVGYSAETVR--QHIG-FVSHSLLEKF- 91
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQhiegLPGHQIARMGVVRtfQHVRlFREMTVIENLl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 92 -QEGERVIDVVISGAFKSIGvYQDIDDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDEPA 170
Cdd:PRK11300 103 vAQHQQLKTGLFSGLLKTPA-FRRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPA 181
|
....
gi 686428090 171 AGLD 174
Cdd:PRK11300 182 AGLN 185
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
2-173 |
1.27e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 72.60 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 2 LIQLDQVGRMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKvGYSAETVRQHIG 81
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITD-WQTAKIMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 82 FVShsllekfqEGERVI-------DVVISGAFKSIGVYQDIDDEVRNEAHQLLKlvgmsaKAQQYIGYLSTGEKQRVMIA 154
Cdd:PRK11614 84 IVP--------EGRRVFsrmtveeNLAMGGFFAERDQFQERIKWVYELFPRLHE------RRIQRAGTMSGGEQQMLAIG 149
|
170
....*....|....*....
gi 686428090 155 RALMGQPQVLILDEPAAGL 173
Cdd:PRK11614 150 RALMSQPRLLLLDEPSLGL 168
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
12-175 |
1.56e-15 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 72.56 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 12 KQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKmpgKVGYSAETVR-QHIGFV----SHS 86
Cdd:COG4167 23 RQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGH---KLEYGDYKYRcKHIRMIfqdpNTS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 87 LLEKFQEGeRVIDVVISGAfksigvyQDIDDEVRNEA-HQLLKLVGMSAK-AQQYIGYLSTGEKQRVMIARALMGQPQVL 164
Cdd:COG4167 100 LNPRLNIG-QILEEPLRLN-------TDLTAEEREERiFATLRLVGLLPEhANFYPHMLSSGQKQRVALARALILQPKII 171
|
170
....*....|.
gi 686428090 165 ILDEPAAGLDF 175
Cdd:COG4167 172 IADEALAALDM 182
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
14-177 |
1.62e-15 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 72.31 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 14 GKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFG----KMPgkvgySAETVRQHIGFVShslle 89
Cdd:TIGR04406 13 KRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGqditHLP-----MHERARLGIGYLP----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 90 kfQEgervidvviSGAFKSIGVYQDI-----------DDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALM 158
Cdd:TIGR04406 83 --QE---------ASIFRKLTVEENImavleirkdldRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALA 151
|
170
....*....|....*....
gi 686428090 159 GQPQVLILDEPAAGLDFIA 177
Cdd:TIGR04406 152 TNPKFILLDEPFAGVDPIA 170
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
17-174 |
1.78e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 72.31 E-value: 1.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 17 ILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKM-------PGKVGYSAET-----------VRQ 78
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlvrdkDGQLKVADKNqlrllrtrltmVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 79 HIGFVSH-SLLEKFQEGErvidVVISGAFKSigvyqdiddEVRNEAHQLLKLVGMSAKAQQ-YIGYLSTGEKQRVMIARA 156
Cdd:PRK10619 100 HFNLWSHmTVLENVMEAP----IQVLGLSKQ---------EARERAVKYLAKVGIDERAQGkYPVHLSGGQQQRVSIARA 166
|
170
....*....|....*...
gi 686428090 157 LMGQPQVLILDEPAAGLD 174
Cdd:PRK10619 167 LAMEPEVLLFDEPTSALD 184
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3-174 |
2.19e-15 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 73.66 E-value: 2.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 3 IQLDQVG-RMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVnLFGKMPGKvGYSAETVRQHIG 81
Cdd:COG1132 340 IEFENVSfSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRI-LIDGVDIR-DLTLESLRRQIG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 82 FVshsllekFQEGervidVVISGafkSIgvYQDI--------DDEVRN-----EAHQLLKlvGMSAKAQQYIG----YLS 144
Cdd:COG1132 418 VV-------PQDT-----FLFSG---TI--RENIrygrpdatDEEVEEaakaaQAHEFIE--ALPDGYDTVVGergvNLS 478
|
170 180 190
....*....|....*....|....*....|
gi 686428090 145 TGEKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:COG1132 479 GGQRQRIAIARALLKDPPILILDEATSALD 508
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-173 |
2.50e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 73.28 E-value: 2.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 2 LIQLDQVGRMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILN-AYEPaTTGSVNLFGKMPGKVGY--SAE---- 74
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSgIHEP-TKGTITINNINYNKLDHklAAQlgig 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 75 TVRQHIGFVSH-SLLEKFQEGERVIDvvisgafKSIGVyqDIDD--EVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRV 151
Cdd:PRK09700 84 IIYQELSVIDElTVLENLYIGRHLTK-------KVCGV--NIIDwrEMRVRAAMMLLRVGLKVDLDEKVANLSISHKQML 154
|
170 180
....*....|....*....|..
gi 686428090 152 MIARALMGQPQVLILDEPAAGL 173
Cdd:PRK09700 155 EIAKTLMLDAKVIIMDEPTSSL 176
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
25-178 |
2.76e-15 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 73.13 E-value: 2.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 25 INGGDKWILYGLNGAGKTTLLNILNAYEPATTGS-VNLFgkmpgkvgysaetvrQHIGFVSHSLLEKF--QEGERVIDVV 101
Cdd:PRK10938 26 LNAGDSWAFVGANGSGKSALARALAGELPLLSGErQSQF---------------SHITRLSFEQLQKLvsDEWQRNNTDM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 102 ISGAFKSIG--VYQDIDDEVRNEA--HQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDEPAAGLDFIA 177
Cdd:PRK10938 91 LSPGEDDTGrtTAEIIQDEVKDPArcEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVAS 170
|
.
gi 686428090 178 R 178
Cdd:PRK10938 171 R 171
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
18-174 |
3.70e-15 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 72.53 E-value: 3.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 18 LKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKVGYSAET-VRQHIGFVshsllekFQE--- 93
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRkARRQIGMI-------FQHfnl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 94 --GERVIDVV-----ISGAFKSigvyqDIDDEVrneaHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLIL 166
Cdd:PRK11153 94 lsSRTVFDNValpleLAGTPKA-----EIKARV----TELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLC 164
|
....*...
gi 686428090 167 DEPAAGLD 174
Cdd:PRK11153 165 DEATSALD 172
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
14-174 |
4.08e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 72.56 E-value: 4.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 14 GKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKVGYSAETVrqHIGFVSHSLLEKFQE 93
Cdd:PRK11607 31 GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPI--NMMFQSYALFPHMTV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 94 GERVidvvisgAFksiGVYQD--IDDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDEPAA 171
Cdd:PRK11607 109 EQNI-------AF---GLKQDklPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
...
gi 686428090 172 GLD 174
Cdd:PRK11607 179 ALD 181
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
12-174 |
5.35e-15 |
|
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: 70.72 E-value: 5.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 12 KQGKTILKNISWQINGGDKWILYGLNGAGKTTLLN-ILNAYEPaTTGSVNLFGKmpGKVGYSAETVRQHIGFVSHsllek 90
Cdd:cd03251 12 GDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNlIPRFYDV-DSGRILIDGH--DVRDYTLASLRRQIGLVSQ----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 91 fqegerviDVVI-SGAFK---SIGVYQDIDDEVRNEAHQllklvgmsAKAQQYI-----GY----------LSTGEKQRV 151
Cdd:cd03251 84 --------DVFLfNDTVAeniAYGRPGATREEVEEAARA--------ANAHEFImelpeGYdtvigergvkLSGGQRQRI 147
|
170 180
....*....|....*....|...
gi 686428090 152 MIARALMGQPQVLILDEPAAGLD 174
Cdd:cd03251 148 AIARALLKDPPILILDEATSALD 170
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
18-174 |
6.49e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 71.97 E-value: 6.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 18 LKNISWQINGGDkwI--LYGLNGAGKTTLLNILNAYEPATTGSVNLFGKmpgKVGYS--AETVRQHIGFVshsllekFQE 93
Cdd:COG1129 20 LDGVSLELRPGE--VhaLLGENGAGKSTLMKILSGVYQPDSGEILLDGE---PVRFRspRDAQAAGIAII-------HQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 94 gervIDVV----------ISGAFKSIGVyqdIDD-EVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQ 162
Cdd:COG1129 88 ----LNLVpnlsvaenifLGREPRRGGL---IDWrAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDAR 160
|
170
....*....|..
gi 686428090 163 VLILDEPAAGLD 174
Cdd:COG1129 161 VLILDEPTASLT 172
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
3-174 |
1.06e-14 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 71.26 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 3 IQLDQVGRMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGK-----MPGK--VG----- 70
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRdvtdlPPKDrnIAmvfqs 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 71 ---YSAETVRQHIGFvshsllekfqegervidvvisgAFKSIGVY-QDIDDEVRneahQLLKLVGMSAKAQQYIGYLSTG 146
Cdd:COG3839 84 yalYPHMTVYENIAF----------------------PLKLRKVPkAEIDRRVR----EAAELLGLEDLLDRKPKQLSGG 137
|
170 180
....*....|....*....|....*...
gi 686428090 147 EKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:COG3839 138 QRQRVALGRALVREPKVFLLDEPLSNLD 165
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
6-174 |
1.41e-14 |
|
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: 69.06 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 6 DQVGRMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLfgkMPGKVGYSAETVRQHIGFVSH 85
Cdd:cd03231 4 DELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLL---NGGPLDFQRDSIARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 86 sllekfQEGervIDVVISgAFKSIGVYQDIDDevRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLI 165
Cdd:cd03231 81 ------APG---IKTTLS-VLENLRFWHADHS--DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWI 148
|
....*....
gi 686428090 166 LDEPAAGLD 174
Cdd:cd03231 149 LDEPTTALD 157
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
12-179 |
2.05e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 69.86 E-value: 2.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 12 KQGktiLKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGK--MPGKVGYSAETVRQHIGFVShslle 89
Cdd:PRK13641 20 KKG---LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYhiTPETGNKNLKKLRKKVSLVF----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 90 KFQEG----ERVIDVVISGAfKSIGVYqdiDDEVRNEAHQLLKLVGMSAKAQQYIGY-LSTGEKQRVMIARALMGQPQVL 164
Cdd:PRK13641 92 QFPEAqlfeNTVLKDVEFGP-KNFGFS---EDEAKEKALKWLKKVGLSEDLISKSPFeLSGGQMRRVAIAGVMAYEPEIL 167
|
170
....*....|....*
gi 686428090 165 ILDEPAAGLDFIARE 179
Cdd:PRK13641 168 CLDEPAAGLDPEGRK 182
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
13-174 |
2.46e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 70.64 E-value: 2.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 13 QGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPaTTGSVnlfgkmpgKVG------YSAETVRQHIGFVSHS 86
Cdd:PRK11174 361 DGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP-YQGSL--------KINgielreLDPESWRKHLSWVGQN 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 87 ------------LLEKFQEGERVIDVVISGAfksigvyqDIDDEVRNEAHQLLKLVGmsakaQQYIGyLSTGEKQRVMIA 154
Cdd:PRK11174 432 pqlphgtlrdnvLLGNPDASDEQLQQALENA--------WVSEFLPLLPQGLDTPIG-----DQAAG-LSVGQAQRLALA 497
|
170 180
....*....|....*....|
gi 686428090 155 RALMGQPQVLILDEPAAGLD 174
Cdd:PRK11174 498 RALLQPCQLLLLDEPTASLD 517
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
18-174 |
2.55e-14 |
|
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: 68.90 E-value: 2.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 18 LKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGK----MPGKvgysaetvRQHIGFV--SHSLlekf 91
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnLPPE--------KRDISYVpqNYAL---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 92 qegervidvvisgaFKSIGVYQDID----------DEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQP 161
Cdd:cd03299 83 --------------FPHMTVYKNIAyglkkrkvdkKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNP 148
|
170
....*....|...
gi 686428090 162 QVLILDEPAAGLD 174
Cdd:cd03299 149 KILLLDEPFSALD 161
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
24-178 |
2.66e-14 |
|
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: 68.29 E-value: 2.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 24 QINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKVGYSAETVrqhigfvshSLLekFQEgervidvviS 103
Cdd:cd03298 20 TFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPV---------SML--FQE---------N 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 104 GAFKSIGVYQDID----------DEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDEPAAGL 173
Cdd:cd03298 80 NLFAHLTVEQNVGlglspglkltAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAAL 159
|
....*
gi 686428090 174 DFIAR 178
Cdd:cd03298 160 DPALR 164
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
10-179 |
3.27e-14 |
|
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: 68.51 E-value: 3.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 10 RMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKvgYSAETVRQhIGFVshslle 89
Cdd:cd03267 29 RKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWK--RRKKFLRR-IGVV------ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 90 kFQEGERVI-DV-VISGAFKSIGVYQDIDDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILD 167
Cdd:cd03267 100 -FGQKTQLWwDLpVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLD 178
|
170
....*....|..
gi 686428090 168 EPAAGLDFIARE 179
Cdd:cd03267 179 EPTIGLDVVAQE 190
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
18-174 |
4.60e-14 |
|
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: 69.62 E-value: 4.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 18 LKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKmpGKVGYSAETVRQHIGFVSH-------SLLEK 90
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGV--PLADADADSWRDQIAWVPQhpflfagTIAEN 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 91 FQEGERVIDvvisgafksigvyqdiDDEVRNEAHQ--LLKLV-GMSAKAQQYIGY----LSTGEKQRVMIARALMGQPQV 163
Cdd:TIGR02857 416 IRLARPDAS----------------DAEIREALERagLDEFVaALPQGLDTPIGEggagLSGGQAQRLALARAFLRDAPL 479
|
170
....*....|.
gi 686428090 164 LILDEPAAGLD 174
Cdd:TIGR02857 480 LLLDEPTAHLD 490
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
3-174 |
6.48e-14 |
|
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: 67.28 E-value: 6.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 3 IQLDQVGRMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKVG------------ 70
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPpkdrdiamvfqn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 71 ---YSAETVRQHIGFvshsllekfqegervidvvisgAFKSIGVYQD-IDDEVRNEAhqllKLVGMSAKAQQYIGYLSTG 146
Cdd:cd03301 81 yalYPHMTVYDNIAF----------------------GLKLRKVPKDeIDERVREVA----ELLQIEHLLDRKPKQLSGG 134
|
170 180
....*....|....*....|....*...
gi 686428090 147 EKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:cd03301 135 QRQRVALGRAIVREPKVFLMDEPLSNLD 162
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
13-174 |
7.61e-14 |
|
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: 67.46 E-value: 7.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 13 QGKTI--LKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGS---------VNLFGKMPGKVGYsaetVRQH-I 80
Cdd:COG4778 20 GGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSilvrhdggwVDLAQASPREILA----LRRRtI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 81 GFVSHSLlekfqegeRVI------DVVISGAFKSiGVYqdiDDEVRNEAHQLLKLVGMSAK-AQQYIGYLSTGEKQRVMI 153
Cdd:COG4778 96 GYVSQFL--------RVIprvsalDVVAEPLLER-GVD---REEARARARELLARLNLPERlWDLPPATFSGGEQQRVNI 163
|
170 180
....*....|....*....|.
gi 686428090 154 ARALMGQPQVLILDEPAAGLD 174
Cdd:COG4778 164 ARGFIADPPLLLLDEPTASLD 184
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
16-174 |
1.53e-13 |
|
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: 65.14 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 16 TILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKmPGKVGYSAETVRQHIGFVshsllekfqege 95
Cdd:cd03216 14 KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK-EVSFASPRDARRAGIAMV------------ 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 686428090 96 rvidvvisgafksigvyqdiddevrneaHQLlklvgmsakaqqyigylSTGEKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:cd03216 81 ----------------------------YQL-----------------SVGERQMVEIARALARNARLLILDEPTAALT 114
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
17-174 |
1.88e-13 |
|
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: 66.34 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 17 ILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKvgYSAETVRQHIGFVShsllekfQEger 96
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQ--YEHKYLHSKVSLVG-------QE--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 97 viDVVISGAFK---SIGVYQDIDDEVRN-----EAHQLLKLV--GMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLIL 166
Cdd:cd03248 97 --PVLFARSLQdniAYGLQSCSFECVKEaaqkaHAHSFISELasGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLIL 174
|
....*...
gi 686428090 167 DEPAAGLD 174
Cdd:cd03248 175 DEATSALD 182
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
4-174 |
2.02e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 66.73 E-value: 2.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 4 QLDQVGRMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGkvGYSAETVRQHIGFV 83
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLE--SWSSKAFARKVAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 84 SHSLLEKfqEGERVIDVVISGAFKSIGVYQDIDDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQV 163
Cdd:PRK10575 91 PQQLPAA--EGMTVRELVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRC 168
|
170
....*....|.
gi 686428090 164 LILDEPAAGLD 174
Cdd:PRK10575 169 LLLDEPTSALD 179
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
17-173 |
2.87e-13 |
|
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: 65.77 E-value: 2.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 17 ILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGK----MPgkvgySAETVRQHIGFVShsllekfq 92
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEditgLP-----PHRIARLGIGYVP-------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 93 EGERVidvvisgaFKS--------IGVY----QDIDDEVRNEAHQL---LKlvgmsAKAQQYIGYLSTGEKQRVMIARAL 157
Cdd:COG0410 85 EGRRI--------FPSltveenllLGAYarrdRAEVRADLERVYELfprLK-----ERRRQRAGTLSGGEQQMLAIGRAL 151
|
170
....*....|....*.
gi 686428090 158 MGQPQVLILDEPAAGL 173
Cdd:COG0410 152 MSRPKLLLLDEPSLGL 167
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-174 |
2.98e-13 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 67.52 E-value: 2.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 3 IQLDQVGRMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNIL---NAYEPaTTGSV---------NLFGKMPGKVG 70
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgmDQYEP-TSGRIiyhvalcekCGYVERPSKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 71 YS------------------AETVRQHIGFVSHSLLEK---FQEGERVIDVVISgAFKSIGvYQDidDEVRNEAHQLLKL 129
Cdd:TIGR03269 80 EPcpvcggtlepeevdfwnlSDKLRRRIRKRIAIMLQRtfaLYGDDTVLDNVLE-ALEEIG-YEG--KEAVGRAVDLIEM 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 686428090 130 VGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:TIGR03269 156 VQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLD 200
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
12-174 |
2.98e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 66.36 E-value: 2.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 12 KQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKVgySAETVRQHIGFVshsllekF 91
Cdd:PRK13652 14 SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKE--NIREVRKFVGLV-------F 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 92 QEGErviDVVISGAfksigVYQDI---------DDE-VRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQP 161
Cdd:PRK13652 85 QNPD---DQIFSPT-----VEQDIafgpinlglDEEtVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170
....*....|...
gi 686428090 162 QVLILDEPAAGLD 174
Cdd:PRK13652 157 QVLVLDEPTAGLD 169
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
10-174 |
3.32e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 67.38 E-value: 3.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 10 RMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATT---GSVNLFG------KMPGKVGYSAE------ 74
Cdd:TIGR00955 33 RERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVkgsGSVLLNGmpidakEMRAISAYVQQddlfip 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 75 --TVRQHIGFVSHsllekFQEGERVIDvvisgafksigvyqdidDEVRNEAHQLLKLVGMSAKAQQYIGY------LSTG 146
Cdd:TIGR00955 113 tlTVREHLMFQAH-----LRMPRRVTK-----------------KEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGG 170
|
170 180
....*....|....*....|....*...
gi 686428090 147 EKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:TIGR00955 171 ERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
15-179 |
4.00e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 66.26 E-value: 4.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 15 KTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGkMPGKVGYSAETVRQHIGFVshsllekFQEG 94
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG-LDTSDEENLWDIRNKAGMV-------FQNP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 95 ERVIDVVI---SGAF--KSIGVYQDiddEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDEP 169
Cdd:PRK13633 95 DNQIVATIveeDVAFgpENLGIPPE---EIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEP 171
|
170
....*....|
gi 686428090 170 AAGLDFIARE 179
Cdd:PRK13633 172 TAMLDPSGRR 181
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
13-174 |
5.09e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 65.91 E-value: 5.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 13 QGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMpgkvgYSAETV---RQHIGFVSHSLLE 89
Cdd:PRK13650 18 QEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDL-----LTEENVwdiRHKIGMVFQNPDN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 90 KFQeGERVIDVVISGaFKSIGVYQDiddEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDEP 169
Cdd:PRK13650 93 QFV-GATVEDDVAFG-LENKGIPHE---EMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEA 167
|
....*
gi 686428090 170 AAGLD 174
Cdd:PRK13650 168 TSMLD 172
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
33-178 |
5.60e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 65.80 E-value: 5.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 33 LYGLNGAGKTTLLNILNAYEPATTGSVNLFGKmpgKVGYSAE---TVRQHIGFVshsllekFQEGERVI-----DVVISG 104
Cdd:PRK13638 32 LVGANGCGKSTLFMNLSGLLRPQKGAVLWQGK---PLDYSKRgllALRQQVATV-------FQDPEQQIfytdiDSDIAF 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 686428090 105 AFKSIGVyqdIDDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDEPAAGLDFIAR 178
Cdd:PRK13638 102 SLRNLGV---PEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGR 172
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
13-174 |
5.98e-13 |
|
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: 66.62 E-value: 5.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 13 QGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKVGYSAetVRQHIGFVS---H---- 85
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDE--VRRRVSVCAqdaHlfdt 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 86 SLLEKFQEG-ERVIDVVISGAFKSIGvyqdIDDEVRNEAHQLLKLVGMSAKAqqyigyLSTGEKQRVMIARALMGQPQVL 164
Cdd:TIGR02868 424 TVRENLRLArPDATDEELWAALERVG----LADWLRALPDGLDTVLGEGGAR------LSGGERQRLALARALLADAPIL 493
|
170
....*....|
gi 686428090 165 ILDEPAAGLD 174
Cdd:TIGR02868 494 LLDEPTEHLD 503
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
14-174 |
8.16e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 64.12 E-value: 8.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 14 GKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKmpgkvGYSAETVRQHIGFVSH-------- 85
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGG-----DIDDPDVAEACHYLGHrnamkpal 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 86 SLLEKFQegervidvvisgaFksigvYQDIDDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLI 165
Cdd:PRK13539 89 TVAENLE-------------F-----WAAFLGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWI 150
|
....*....
gi 686428090 166 LDEPAAGLD 174
Cdd:PRK13539 151 LDEPTAALD 159
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
17-174 |
9.83e-13 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 65.90 E-value: 9.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 17 ILKNISWQINGGDKWILYGLNGAGKTTLLNIL-NAYEPaTTGSVNLFGKmPgKVGYSAETVRQHIGFVShsllekfQEge 95
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLqNLYQP-TGGQVLLDGV-P-LVQYDHHYLHRQVALVG-------QE-- 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 96 rviDVVISGAFK---SIGVYQDIDDEVRNEAHQLLKLVGMSAKAQQY---IG----YLSTGEKQRVMIARALMGQPQVLI 165
Cdd:TIGR00958 564 ---PVLFSGSVReniAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYdteVGekgsQLSGGQKQRIAIARALVRKPRVLI 640
|
....*....
gi 686428090 166 LDEPAAGLD 174
Cdd:TIGR00958 641 LDEATSALD 649
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
13-174 |
1.13e-12 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 64.71 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 13 QGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKV-GYSAETVRQHIGFVshsllekF 91
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnRAQRKAFRRDIQMV-------F 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 92 QEGervidvviSGAF---KSIGvyQDIDDEVR-----NEAHQ------LLKLVGMSAK-AQQYIGYLSTGEKQRVMIARA 156
Cdd:PRK10419 96 QDS--------ISAVnprKTVR--EIIREPLRhllslDKAERlaraseMLRAVDLDDSvLDKRPPQLSGGQLQRVCLARA 165
|
170
....*....|....*...
gi 686428090 157 LMGQPQVLILDEPAAGLD 174
Cdd:PRK10419 166 LAVEPKLLILDEAVSNLD 183
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
17-174 |
1.28e-12 |
|
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: 64.10 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 17 ILKNISWQINGGDKWILYGLNGAGKTTLLN-ILNAYEPaTTGSVNLFGKMPGKvgYSAETVRQHIGFVSH-------SLL 88
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSlLERFYDP-TSGEILLDGVDIRD--LNLRWLRSQIGLVSQepvlfdgTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 89 E--KFQEGERVIDVVISGAFKSigvyqDIDDEVRNEAHQLLKLVGmsAKAQQyigyLSTGEKQRVMIARALMGQPQVLIL 166
Cdd:cd03249 95 EniRYGKPDATDEEVEEAAKKA-----NIHDFIMSLPDGYDTLVG--ERGSQ----LSGGQKQRIAIARALLRNPKILLL 163
|
....*...
gi 686428090 167 DEPAAGLD 174
Cdd:cd03249 164 DEATSALD 171
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
17-174 |
1.49e-12 |
|
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: 63.00 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 17 ILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKVGYSAetVRQHIGFVShsllekfqeger 96
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNE--LGDHVGYLP------------ 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 686428090 97 vidvvisgafksigvyQDIddevrneahQLLklvgmSAKAQQYIgyLSTGEKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:cd03246 83 ----------------QDD---------ELF-----SGSIAENI--LSGGQRQRLGLARALYGNPRILVLDEPNSHLD 128
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
14-174 |
1.62e-12 |
|
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: 63.79 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 14 GKTILKNISWQINGGDKWILYGLNGAGKTTLLNIL-NAYEPaTTGSVNLFGKMPGKVgySAETVRQHIGFVSHsllekfq 92
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLfRFYDV-SSGSILIDGQDIREV--TLDSLRRAIGVVPQ------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 93 egerviDVVIsgaFKSIgVYQDI--------DDEVRNEA-----HQllKLVGMSAKAQQYIG----YLSTGEKQRVMIAR 155
Cdd:cd03253 83 ------DTVL---FNDT-IGYNIrygrpdatDEEVIEAAkaaqiHD--KIMRFPDGYDTIVGerglKLSGGEKQRVAIAR 150
|
170
....*....|....*....
gi 686428090 156 ALMGQPQVLILDEPAAGLD 174
Cdd:cd03253 151 AILKNPPILLLDEATSALD 169
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
14-174 |
1.93e-12 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 63.57 E-value: 1.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 14 GKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFG-----KMPGKVGYSAEtvrqhigfvSHSLL 88
Cdd:TIGR03740 12 KQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGhpwtrKDLHKIGSLIE---------SPPLY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 89 EKF--QEGERVIDVVISGAFKSIgvyqdidDEVrneahqlLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLIL 166
Cdd:TIGR03740 83 ENLtaRENLKVHTTLLGLPDSRI-------DEV-------LNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLIL 148
|
....*...
gi 686428090 167 DEPAAGLD 174
Cdd:TIGR03740 149 DEPTNGLD 156
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
13-174 |
2.08e-12 |
|
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: 62.72 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 13 QGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKVGysaETVRQHIGFVShsllekfq 92
Cdd:cd03247 13 QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE---KALSSLISVLN-------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 93 egervidvvisgafKSIGVYqdiDDEVRNEahqllklVGMSakaqqyigyLSTGEKQRVMIARALMGQPQVLILDEPAAG 172
Cdd:cd03247 82 --------------QRPYLF---DTTLRNN-------LGRR---------FSGGERQRLALARILLQDAPIVLLDEPTVG 128
|
..
gi 686428090 173 LD 174
Cdd:cd03247 129 LD 130
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
2-179 |
2.08e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 64.00 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 2 LIQLDQVGRMKQGKT--ILKNISWQINGGdKWI-LYGLNGAGKTTLLNILNAYEPATTGSVnLFGKMPGKvGYSAETVRQ 78
Cdd:PRK13648 7 IIVFKNVSFQYQSDAsfTLKDVSFNIPKG-QWTsIVGHNGSGKSTIAKLMIGIEKVKSGEI-FYNNQAIT-DDNFEKLRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 79 HIGFVSHSLLEKFQEGERVIDVVISGAFKSIGVyqdidDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALM 158
Cdd:PRK13648 84 HIGIVFQNPDNQFVGSIVKYDVAFGLENHAVPY-----DEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLA 158
|
170 180
....*....|....*....|.
gi 686428090 159 GQPQVLILDEPAAGLDFIARE 179
Cdd:PRK13648 159 LNPSVIILDEATSMLDPDARQ 179
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
14-174 |
2.18e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 64.96 E-value: 2.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 14 GKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLfgkMPG-KVGYSAE--------TVRQHIGFVS 84
Cdd:TIGR03719 17 KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP---QPGiKVGYLPQepqldptkTVRENVEEGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 85 HSLLEKFQEGERVI------DVVISGAFKSIGVYQDIDDEVrnEAHQLLKLVGMSAKA------QQYIGYLSTGEKQRVM 152
Cdd:TIGR03719 94 AEIKDALDRFNEISakyaepDADFDKLAAEQAELQEIIDAA--DAWDLDSQLEIAMDAlrcppwDADVTKLSGGERRRVA 171
|
170 180
....*....|....*....|..
gi 686428090 153 IARALMGQPQVLILDEPAAGLD 174
Cdd:TIGR03719 172 LCRLLLSKPDMLLLDEPTNHLD 193
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
14-177 |
2.73e-12 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 63.12 E-value: 2.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 14 GKTILKNISWQINGGDkwI--LYGLNGAGKTTLLNILNAYEPATTGSVNLFGK----MP-------GkVGYSAE------ 74
Cdd:COG1137 15 KRTVVKDVSLEVNQGE--IvgLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdithLPmhkrarlG-IGYLPQeasifr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 75 --TVRQHIGFVshslLEkfqegervidvvisgafksigvYQDIDDEVRNE-AHQLLKLVGMSAKAQQYIGYLSTGEKQRV 151
Cdd:COG1137 92 klTVEDNILAV----LE----------------------LRKLSKKEREErLEELLEEFGITHLRKSKAYSLSGGERRRV 145
|
170 180
....*....|....*....|....*.
gi 686428090 152 MIARALMGQPQVLILDEPAAGLDFIA 177
Cdd:COG1137 146 EIARALATNPKFILLDEPFAGVDPIA 171
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3-174 |
2.86e-12 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 64.74 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 3 IQLDQVG-RMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGkvGYSAETVRQHIG 81
Cdd:PRK10790 341 IDIDNVSfAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLS--SLSHSVLRQGVA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 82 FVSHSllekfqegerviDVVISGAF-KSIGVYQDIDDEV---RNEAHQLLKLV-GMSAKAQQYIG----YLSTGEKQRVM 152
Cdd:PRK10790 419 MVQQD------------PVVLADTFlANVTLGRDISEEQvwqALETVQLAELArSLPDGLYTPLGeqgnNLSVGQKQLLA 486
|
170 180
....*....|....*....|..
gi 686428090 153 IARALMGQPQVLILDEPAAGLD 174
Cdd:PRK10790 487 LARVLVQTPQILILDEATANID 508
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
18-174 |
2.91e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 64.64 E-value: 2.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 18 LKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKmPGKVGYSAETVRQHIGFVSHsllekfqegERV 97
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGH-EVVTRSPQDGLANGIVYISE---------DRK 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 98 IDVVISG-------------AFKSIGVYQDIDDEvRNEAHQLLKLVGM-SAKAQQYIGYLSTGEKQRVMIARALMGQPQV 163
Cdd:PRK10762 338 RDGLVLGmsvkenmsltalrYFSRAGGSLKHADE-QQAVSDFIRLFNIkTPSMEQAIGLLSGGNQQKVAIARGLMTRPKV 416
|
170
....*....|.
gi 686428090 164 LILDEPAAGLD 174
Cdd:PRK10762 417 LILDEPTRGVD 427
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1-174 |
3.49e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 63.61 E-value: 3.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 1 MLIQLDQVGRMKQGKT-----ILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKM--PGKVGYSA 73
Cdd:PRK13649 1 MGINLQNVSYTYQAGTpfegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLitSTSKNKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 74 ETVRQHIGFVShslleKFQEG----ERVIDVVISGAfKSIGVYQDiddEVRNEAHQLLKLVGMSAKAQQYIGY-LSTGEK 148
Cdd:PRK13649 81 KQIRKKVGLVF-----QFPESqlfeETVLKDVAFGP-QNFGVSQE---EAEALAREKLALVGISESLFEKNPFeLSGGQM 151
|
170 180
....*....|....*....|....*.
gi 686428090 149 QRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:PRK13649 152 RRVAIAGILAMEPKILVLDEPTAGLD 177
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1-174 |
3.74e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 63.65 E-value: 3.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 1 MLIQLDQVGRMKQGKT-----ILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFG-----KMPGKVg 70
Cdd:PRK13646 1 MTIRFDNVSYTYQKGTpyehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithKTKDKY- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 71 ysAETVRQHIGFVShslleKFQEGERVIDVV---ISGAFKSIGVyqDIDdEVRNEAHQLLKLVGMSAKAQQYIGY-LSTG 146
Cdd:PRK13646 80 --IRPVRKRIGMVF-----QFPESQLFEDTVereIIFGPKNFKM--NLD-EVKNYAHRLLMDLGFSRDVMSQSPFqMSGG 149
|
170 180
....*....|....*....|....*...
gi 686428090 147 EKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:PRK13646 150 QMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
18-174 |
3.94e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 63.88 E-value: 3.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 18 LKNISWQINGGDkwIL--YGLNGAGKTTLLNILNAYEPATTGSVNLFGKmPGKVGYSAETVRQHIGFVS----------- 84
Cdd:COG1129 268 VRDVSFSVRAGE--ILgiAGLVGAGRTELARALFGADPADSGEIRLDGK-PVRIRSPRDAIRAGIAYVPedrkgeglvld 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 85 HSLLEKfqegervIDVVISGAFKSIGVyqdIDD-EVRNEAHQLLKLVGMSAK-AQQYIGYLSTGEKQRVMIARALMGQPQ 162
Cdd:COG1129 345 LSIREN-------ITLASLDRLSRGGL---LDRrRERALAEEYIKRLRIKTPsPEQPVGNLSGGNQQKVVLAKWLATDPK 414
|
170
....*....|..
gi 686428090 163 VLILDEPAAGLD 174
Cdd:COG1129 415 VLILDEPTRGID 426
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
16-174 |
3.95e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 63.97 E-value: 3.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 16 TILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKmpgKVGYSAETVRQ-HIGFVSHSLLEKFQEG 94
Cdd:PRK11432 20 TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGE---DVTHRSIQQRDiCMVFQSYALFPHMSLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 95 ERVidvviSGAFKSIGVYQDiddEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:PRK11432 97 ENV-----GYGLKMLGVPKE---ERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
14-174 |
4.45e-12 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 62.78 E-value: 4.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 14 GKTILKNISWQINGGDKWILYGLNGAGKTTLLNIL---NAYEPaTTGSVNLFGK----MPgkvgysaETVRQHIG-FVSh 85
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghPKYEV-TSGSILLDGEdileLS-------PDERARAGiFLA- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 86 sllekFQ-----EGERVIDVVISgAFKSIGVYQDIDDEVRNEAHQLLKLVGMSAK-AQQYIGY-LSTGEKQRVMIARALM 158
Cdd:COG0396 83 -----FQypveiPGVSVSNFLRT-ALNARRGEELSAREFLKLLKEKMKELGLDEDfLDRYVNEgFSGGEKKRNEILQMLL 156
|
170
....*....|....*.
gi 686428090 159 GQPQVLILDEPAAGLD 174
Cdd:COG0396 157 LEPKLAILDETDSGLD 172
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
2-174 |
5.12e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 62.82 E-value: 5.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 2 LIQLDQVGRMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMpgKVGYSAETVrqHIG 81
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKL--RIGYVPQKL--YLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 82 FVSHSLLEKF---QEGERVIDvvISGAFKsigvyqdiddevRNEAHQLLklvgmsakaQQYIGYLSTGEKQRVMIARALM 158
Cdd:PRK09544 80 TTLPLTVNRFlrlRPGTKKED--ILPALK------------RVQAGHLI---------DAPMQKLSGGETQRVLLARALL 136
|
170
....*....|....*.
gi 686428090 159 GQPQVLILDEPAAGLD 174
Cdd:PRK09544 137 NRPQLLVLDEPTQGVD 152
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
13-174 |
5.65e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 63.67 E-value: 5.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 13 QGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLfgkmPgkvgysaetvrqhigfvshsllekfq 92
Cdd:COG4178 374 DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR----P-------------------------- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 93 EGERVIDV-----VISGAFKSIGVY----QDIDDEvrnEAHQLLKLVGMSAKAQQY--------IgyLSTGEKQRVMIAR 155
Cdd:COG4178 424 AGARVLFLpqrpyLPLGTLREALLYpataEAFSDA---ELREALEAVGLGHLAERLdeeadwdqV--LSLGEQQRLAFAR 498
|
170
....*....|....*....
gi 686428090 156 ALMGQPQVLILDEPAAGLD 174
Cdd:COG4178 499 LLLHKPDWLFLDEATSALD 517
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
14-176 |
5.95e-12 |
|
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: 63.61 E-value: 5.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 14 GKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKVgySAETVRQHIGFVSHsllEKFQE 93
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI--DRHTLRQFINYLPQ---EPYIF 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 94 GERVIDVVISGAFKsiGVYQD----------IDDEVRNEAhqllklVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQV 163
Cdd:TIGR01193 561 SGSILENLLLGAKE--NVSQDeiwaaceiaeIKDDIENMP------LGYQTELSEEGSSISGGQKQRIALARALLTDSKV 632
|
170
....*....|...
gi 686428090 164 LILDEPAAGLDFI 176
Cdd:TIGR01193 633 LILDESTSNLDTI 645
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-174 |
6.56e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 63.65 E-value: 6.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 19 KNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGK-MPGKVGYSAetVRQHIGFVSHSLLEK--FQEGE 95
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdISPRSPLDA--VKKGMAYITESRRDNgfFPNFS 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 96 RVIDVVISGAFK------SIGVYQDiDDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDEP 169
Cdd:PRK09700 358 IAQNMAISRSLKdggykgAMGLFHE-VDEQRTAENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEP 436
|
....*
gi 686428090 170 AAGLD 174
Cdd:PRK09700 437 TRGID 441
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
13-177 |
6.85e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 62.22 E-value: 6.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 13 QGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNL----FGKMPgkvgySAETVRQHIGFVSH--S 86
Cdd:PRK10895 14 KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIddedISLLP-----LHARARRGIGYLPQeaS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 87 LLEKFQEGERVIDVvisgafksIGVYQDIDDEVRNE-AHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLI 165
Cdd:PRK10895 89 IFRRLSVYDNLMAV--------LQIRDDLSAEQREDrANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170
....*....|..
gi 686428090 166 LDEPAAGLDFIA 177
Cdd:PRK10895 161 LDEPFAGVDPIS 172
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
9-174 |
7.42e-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: 63.16 E-value: 7.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 9 GRMKQGKTILKNISWQINGGDKWILYGLNGAGKT-TLLNI--LNAYEPA-TTGSVNLFGK-MpgkVGYSAETVRQ----H 79
Cdd:COG4172 17 GQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSIlrLLPDPAAhPSGSILFDGQdL---LGLSERELRRirgnR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 80 IGFVshsllekFQE-----------GERVIDVV-----ISGAfksigvyqdiddEVRNEAHQLLKLVGMSAKAQQYIGY- 142
Cdd:COG4172 94 IAMI-------FQEpmtslnplhtiGKQIAEVLrlhrgLSGA------------AARARALELLERVGIPDPERRLDAYp 154
|
170 180 190
....*....|....*....|....*....|....
gi 686428090 143 --LSTGEKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:COG4172 155 hqLSGGQRQRVMIAMALANEPDLLIADEPTTALD 188
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
14-174 |
7.96e-12 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 61.74 E-value: 7.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 14 GKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKVGysAETVRQHIGFVShsllekfQE 93
Cdd:cd03244 16 LPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG--LHDLRSRISIIP-------QD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 94 gerviDVVISGAFKS----IGVYqdiDDEvrnEAHQLLKLVGMSAKAQQYIGYL-----------STGEKQRVMIARALM 158
Cdd:cd03244 87 -----PVLFSGTIRSnldpFGEY---SDE---ELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALL 155
|
170
....*....|....*.
gi 686428090 159 GQPQVLILDEPAAGLD 174
Cdd:cd03244 156 RKSKILVLDEATASVD 171
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
17-176 |
1.09e-11 |
|
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: 61.27 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 17 ILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKVGYsaETVRQHIGFVShsllekfQEger 96
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPL--EDLRSSLTIIP-------QD--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 97 viDVVISGAFKS-IGVYQDIDDEvrneahQLLKLVGMSAKAQQyigyLSTGEKQRVMIARALMGQPQVLILDEPAAGLDF 175
Cdd:cd03369 91 --PTLFSGTIRSnLDPFDEYSDE------EIYGALRVSEGGLN----LSQGQRQLLCLARALLKRPRVLVLDEATASIDY 158
|
.
gi 686428090 176 I 176
Cdd:cd03369 159 A 159
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
14-174 |
1.11e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 62.83 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 14 GKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLfgkMPG-KVGY--------SAETVRQHI--Gf 82
Cdd:PRK11819 19 KKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP---APGiKVGYlpqepqldPEKTVRENVeeG- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 83 VSH--SLLEKFQEgervidvvISGAF-----------KSIGVYQDIDDEVrnEAHQLLKLVGMSAKA------QQYIGYL 143
Cdd:PRK11819 95 VAEvkAALDRFNE--------IYAAYaepdadfdalaAEQGELQEIIDAA--DAWDLDSQLEIAMDAlrcppwDAKVTKL 164
|
170 180 190
....*....|....*....|....*....|.
gi 686428090 144 STGEKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:PRK11819 165 SGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
18-179 |
1.23e-11 |
|
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: 60.52 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 18 LKNISWQINGGDkwIL--YGLNGAGKTTLLNILNAYEPATTGSVNLFGKmPGKVGYSAETVRQHIGFVShsllekfqeGE 95
Cdd:cd03215 16 VRDVSFEVRAGE--IVgiAGLVGNGQTELAEALFGLRPPASGEITLDGK-PVTRRSPRDAIRAGIAYVP---------ED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 96 RVIDvvisGAFKSIGVYQDIddevrneahqllklvGMSAkaqqyigYLSTGEKQRVMIARALMGQPQVLILDEPAAGLDF 175
Cdd:cd03215 84 RKRE----GLVLDLSVAENI---------------ALSS-------LLSGGNQQKVVLARWLARDPRVLILDEPTRGVDV 137
|
....
gi 686428090 176 IARE 179
Cdd:cd03215 138 GAKA 141
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-174 |
1.26e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 62.53 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 2 LIQLDQV--GRMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKmPGKvGYSAETVRQH 79
Cdd:PRK11160 338 SLTLNNVsfTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQ-PIA-DYSEAALRQA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 80 IGFVShsllekfqegERVidVVISGAFKS---IGVYQDIDDEVrneaHQLLKLVGMSAKAQQ------YIG----YLSTG 146
Cdd:PRK11160 416 ISVVS----------QRV--HLFSATLRDnllLAAPNASDEAL----IEVLQQVGLEKLLEDdkglnaWLGeggrQLSGG 479
|
170 180
....*....|....*....|....*...
gi 686428090 147 EKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:PRK11160 480 EQRRLGIARALLHDAPLLLLDEPTEGLD 507
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
18-174 |
1.74e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 62.29 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 18 LKNISWQINGGDKWILYGLNGAGKTTLLNILN-AYEPaTTGSVNLFGKMPGKVgySAETVRQHIGFVshsllekFQEG-- 94
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQrVFDP-QSGRILIDGTDIRTV--TRASLRRNIAVV-------FQDAgl 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 95 -ERVIDVVISgafksIGVYQDIDDEV-----RNEAHQLL--KLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLIL 166
Cdd:PRK13657 421 fNRSIEDNIR-----VGRPDATDEEMraaaeRAQAHDFIerKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILIL 495
|
....*...
gi 686428090 167 DEPAAGLD 174
Cdd:PRK13657 496 DEATSALD 503
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
18-178 |
1.93e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 61.67 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 18 LKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKVGYSAET--VRQHIGFVShslleKFQEGE 95
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIkpVRKKVGVVF-----QFPESQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 96 RVIDVVISG-AF--KSIGVYQDiddEVRNEAHQLLKLVGMSAKAQQYIGY-LSTGEKQRVMIARALMGQPQVLILDEPAA 171
Cdd:PRK13643 97 LFEETVLKDvAFgpQNFGIPKE---KAEKIAAEKLEMVGLADEFWEKSPFeLSGGQMRRVAIAGILAMEPEVLVLDEPTA 173
|
....*..
gi 686428090 172 GLDFIAR 178
Cdd:PRK13643 174 GLDPKAR 180
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
20-178 |
2.17e-11 |
|
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: 62.13 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 20 NISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNL-----FGKMPGKVGYSAETVRQHIGFVshsllekFQE- 93
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdeWVDMTKPGPDGRGRAKRYIGIL-------HQEy 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 94 GERVIDVVISGAFKSIGVyqDIDDEV-RNEAHQLLKLVGMSAKA-----QQYIGYLSTGEKQRVMIARALMGQPQVLILD 167
Cdd:TIGR03269 375 DLYPHRTVLDNLTEAIGL--ELPDELaRMKAVITLKMVGFDEEKaeeilDKYPDELSEGERHRVALAQVLIKEPRIVILD 452
|
170
....*....|.
gi 686428090 168 EPAAGLDFIAR 178
Cdd:TIGR03269 453 EPTGTMDPITK 463
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-179 |
2.21e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 61.22 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 15 KTILKNISWQINGGDKWILYGLNGAGKTTLLNILN----AYEPA--TTGSVNLFGKMPGKVgySAETVRQHIGFV----- 83
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNrlieIYDSKikVDGKVLYFGKDIFQI--DAIKLRKEVGMVfqqpn 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 84 ----------------SHSLLEKfqegeRVIDVVISGAFKSIGVYQDIDDEVRNEAHQLlklvgmsakaqqyigylSTGE 147
Cdd:PRK14246 101 pfphlsiydniayplkSHGIKEK-----REIKKIVEECLRKVGLWKEVYDRLNSPASQL-----------------SGGQ 158
|
170 180 190
....*....|....*....|....*....|..
gi 686428090 148 KQRVMIARALMGQPQVLILDEPAAGLDFIARE 179
Cdd:PRK14246 159 QQRLTIARALALKPKVLLMDEPTSMIDIVNSQ 190
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
35-178 |
2.75e-11 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 61.95 E-value: 2.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 35 GLNGAGKTTLLNILNAYEPATTGSVNLFGKmpgKVGYSAETVRQHIGFV-SHSLLekFQEGERVIDVVISGAFKsiGVYQ 113
Cdd:TIGR01257 963 GHNGAGKTTTLSILTGLLPPTSGTVLVGGK---DIETNLDAVRQSLGMCpQHNIL--FHHLTVAEHILFYAQLK--GRSW 1035
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 686428090 114 DiddEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDEPAAGLDFIAR 178
Cdd:TIGR01257 1036 E---EAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSR 1097
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
18-174 |
2.80e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 61.26 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 18 LKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVN--LFGKMPGKVGYSAETVRQHIgFVSHSLLEKFQ--- 92
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwiFKDEKNKKKTKEKEKVLEKL-VIQKTRFKKIKkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 93 EGERVIDVVISGA----FKSIgVYQDI----------DDEVRNEAHQLLKLVGMSAKAQQYIGY-LSTGEKQRVMIARAL 157
Cdd:PRK13651 102 EIRRRVGVVFQFAeyqlFEQT-IEKDIifgpvsmgvsKEEAKKRAAKYIELVGLDESYLQRSPFeLSGGQKRRVALAGIL 180
|
170
....*....|....*..
gi 686428090 158 MGQPQVLILDEPAAGLD 174
Cdd:PRK13651 181 AMEPDFLVFDEPTAGLD 197
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
8-175 |
3.36e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.97 E-value: 3.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 8 VGRMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILnayepattgsvnlFGKMPGKVGYSAETVRQhigfvshsl 87
Cdd:COG2401 36 VELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLL-------------AGALKGTPVAGCVDVPD--------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 88 lEKFQEGERVIDvvisgafkSIGVYQDIDDEVRneahqLLKLVGMSaKAQQYI---GYLSTGEKQRVMIARALMGQPQVL 164
Cdd:COG2401 94 -NQFGREASLID--------AIGRKGDFKDAVE-----LLNAVGLS-DAVLWLrrfKELSTGQKFRFRLALLLAERPKLL 158
|
170
....*....|.
gi 686428090 165 ILDEPAAGLDF 175
Cdd:COG2401 159 VIDEFCSHLDR 169
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
15-174 |
3.45e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 60.77 E-value: 3.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 15 KTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMpgkvgYSAETV---RQHIGFVshsllekF 91
Cdd:PRK13632 22 NNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGIT-----ISKENLkeiRKKIGII-------F 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 92 QE------GERVIDVVisgAF----KSIGvYQDIDDEVRNEAHQllklVGMSAKAQQYIGYLSTGEKQRVMIARALMGQP 161
Cdd:PRK13632 90 QNpdnqfiGATVEDDI---AFglenKKVP-PKKMKDIIDDLAKK----VGMEDYLDKEPQNLSGGQKQRVAIASVLALNP 161
|
170
....*....|...
gi 686428090 162 QVLILDEPAAGLD 174
Cdd:PRK13632 162 EIIIFDESTSMLD 174
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
15-177 |
3.67e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 60.56 E-value: 3.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 15 KTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAY-----EPATTGSVNLFGKMPgkvgYSAET----VRQHIGFVSH 85
Cdd:PRK14239 18 KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNI----YSPRTdtvdLRKEIGMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 86 -------SLLEKFQEGER--------VIDVVISGAFKSIGVYqdidDEVRNEAHQllklvgmSAkaqqyIGyLSTGEKQR 150
Cdd:PRK14239 94 qpnpfpmSIYENVVYGLRlkgikdkqVLDEAVEKSLKGASIW----DEVKDRLHD-------SA-----LG-LSGGQQQR 156
|
170 180
....*....|....*....|....*..
gi 686428090 151 VMIARALMGQPQVLILDEPAAGLDFIA 177
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPIS 183
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
13-174 |
3.68e-11 |
|
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: 61.30 E-value: 3.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 13 QGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNL------------FGKMpgkVGY---SAE--- 74
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLdgadlsqwdreeLGRH---IGYlpqDVElfd 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 75 -TVRQHIGfvshslleKFQEG--ERVIDvvisgAFKSIGVyqdiddevrneaHQL-LKL-------VGMSAKAqqyigyL 143
Cdd:COG4618 420 gTIAENIA--------RFGDAdpEKVVA-----AAKLAGV------------HEMiLRLpdgydtrIGEGGAR------L 468
|
170 180 190
....*....|....*....|....*....|.
gi 686428090 144 STGEKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:COG4618 469 SGGQRQRIGLARALYGDPRLVVLDEPNSNLD 499
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
33-174 |
4.35e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 60.66 E-value: 4.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 33 LYGLNGAGKTTLLNILNAYEPATTGSVNLfgkmPGKVGYSAE------TVRQHIGFVshsllekFQEGE-----RVIDVV 101
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVL----NGRVLFDAEkgiclpPEKRRIGYV-------FQDARlfphyKVRGNL 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 686428090 102 ISGAFKSIGVYQDiddevrneahQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:PRK11144 98 RYGMAKSMVAQFD----------KIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
3-174 |
4.47e-11 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 59.85 E-value: 4.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 3 IQLDQV---GRmkqgktiLKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPAtTGSVNLFGKMPGkvGYSAETVRQH 79
Cdd:COG4138 1 LQLNDVavaGR-------LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLS--DWSAAELARH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 80 IGFVSHSLLEKFQegervidvvisgafksIGVYQDI---------DDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQR 150
Cdd:COG4138 71 RAYLSQQQSPPFA----------------MPVFQYLalhqpagasSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQR 134
|
170 180 190
....*....|....*....|....*....|.
gi 686428090 151 VMIARALM-------GQPQVLILDEPAAGLD 174
Cdd:COG4138 135 VRLAAVLLqvwptinPEGQLLLLDEPMNSLD 165
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
14-174 |
5.19e-11 |
|
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: 61.08 E-value: 5.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 14 GKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEpATTGSVNLFGKMPGKVgySAETVRQHIGFVSHSLLekfqe 93
Cdd:TIGR01271 1231 GRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWNSV--TLQTWRKAFGVIPQKVF----- 1302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 94 gervidvVISGAF-KSIGVYQDIDDEvrnEAHQLLKLVGMSAKAQQYI----------GY-LSTGEKQRVMIARALMGQP 161
Cdd:TIGR01271 1303 -------IFSGTFrKNLDPYEQWSDE---EIWKVAEEVGLKSVIEQFPdkldfvlvdgGYvLSNGHKQLMCLARSILSKA 1372
|
170
....*....|...
gi 686428090 162 QVLILDEPAAGLD 174
Cdd:TIGR01271 1373 KILLLDEPSAHLD 1385
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-177 |
9.94e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 59.28 E-value: 9.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 15 KTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAY-----EPATTGSVNLFGKMPGKVGYSAETVRQHIGFV------ 83
Cdd:PRK14258 20 QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIYERRVNLNRLRRQVSMVhpkpnl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 84 -SHSLLEKFQEGERVI--------DVVISGAFKSigvyQDIDDEVRNEAHQllklvgmSAKAqqyigyLSTGEKQRVMIA 154
Cdd:PRK14258 100 fPMSVYDNVAYGVKIVgwrpkleiDDIVESALKD----ADLWDEIKHKIHK-------SALD------LSGGQQQRLCIA 162
|
170 180
....*....|....*....|...
gi 686428090 155 RALMGQPQVLILDEPAAGLDFIA 177
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIA 185
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
28-178 |
1.09e-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: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 28 GDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKmpgKVGYSAETVRQHIGFVShslleKFQegerVIDVVISGAfK 107
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGK---SILTNISDVHQNMGYCP-----QFD----AIDDLLTGR-E 2031
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 686428090 108 SIGVYQDI----DDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDEPAAGLDFIAR 178
Cdd:TIGR01257 2032 HLYLYARLrgvpAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQAR 2106
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
35-174 |
1.19e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 59.94 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 35 GLNGAGKTTLLN-ILNAYEPATTGSVNLFGKmPGKVGYSAETVRQHIGFVS-----HSLLEKFQEGERvIDVVISGAFKS 108
Cdd:PRK13549 295 GLVGAGRTELVQcLFGAYPGRWEGEIFIDGK-PVKIRNPQQAIAQGIAMVPedrkrDGIVPVMGVGKN-ITLAALDRFTG 372
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 686428090 109 IGVyqdIDD--EVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:PRK13549 373 GSR---IDDaaELKTILESIQRLKVKTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
16-172 |
1.20e-10 |
|
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: 58.69 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 16 TILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFG----KMPgkvgySAETVRQHIGFVSH------ 85
Cdd:TIGR03410 14 HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGeditKLP-----PHERARAGIAYVPQgreifp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 86 --SLLEKFQegervidvviSGAFKSIGVYQDIDDEVRN---EAHQLLKLVGmsakaqqyiGYLSTGEKQRVMIARALMGQ 160
Cdd:TIGR03410 89 rlTVEENLL----------TGLAALPRRSRKIPDEIYElfpVLKEMLGRRG---------GDLSGGQQQQLAIARALVTR 149
|
170
....*....|..
gi 686428090 161 PQVLILDEPAAG 172
Cdd:TIGR03410 150 PKLLLLDEPTEG 161
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
18-174 |
1.25e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 59.21 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 18 LKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKmpGKVGYSAETV---RQHIGFVshsllekFQ-- 92
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQ--DLLKADPEAQkllRQKIQIV-------FQnp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 93 --------------EGERVIDVVISGAfksigvyqdiddEVRNEAHQLLKLVGMsaKAQQYIGY---LSTGEKQRVMIAR 155
Cdd:PRK11308 102 ygslnprkkvgqilEEPLLINTSLSAA------------ERREKALAMMAKVGL--RPEHYDRYphmFSGGQRQRIAIAR 167
|
170
....*....|....*....
gi 686428090 156 ALMGQPQVLILDEPAAGLD 174
Cdd:PRK11308 168 ALMLDPDVVVADEPVSALD 186
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-174 |
1.35e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 58.44 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 24 QINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKVGYSAETVrqhigfvshSLLekFQEgervidvviS 103
Cdd:PRK10771 21 TVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPV---------SML--FQE---------N 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 104 GAFKSIGVYQDI----------DDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDEPAAGL 173
Cdd:PRK10771 81 NLFSHLTVAQNIglglnpglklNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSAL 160
|
.
gi 686428090 174 D 174
Cdd:PRK10771 161 D 161
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
17-174 |
1.36e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 59.27 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 17 ILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKVgysaETVRQHIGFV--SHSLLEKFQEG 94
Cdd:PRK11000 18 ISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDV----PPAERGVGMVfqSYALYPHLSVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 95 ERV-IDVVISGAFKSigvyqDIDDEVRNEAH--QLLKLVGMSAKAqqyigyLSTGEKQRVMIARALMGQPQVLILDEPAA 171
Cdd:PRK11000 94 ENMsFGLKLAGAKKE-----EINQRVNQVAEvlQLAHLLDRKPKA------LSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
|
...
gi 686428090 172 GLD 174
Cdd:PRK11000 163 NLD 165
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
117-174 |
1.56e-10 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 58.97 E-value: 1.56e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 686428090 117 DEVRNEAHQLLKLVGMSAK-AQQYIGYLSTGEKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:COG4608 131 AERRERVAELLELVGLRPEhADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
15-179 |
1.58e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 59.04 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 15 KTILKNISWQINGGDKWILYGLNGAGKTT---LLNILNAYEPATTGSVNLFGkmpgkVGYSAET---VRQHIGFVSHSLL 88
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDG-----ITLTAKTvwdIREKVGIVFQNPD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 89 EKFQeGERVIDVVISGaFKSIGVYQDiddEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDE 168
Cdd:PRK13640 95 NQFV-GATVGDDVAFG-LENRAVPRP---EMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDE 169
|
170
....*....|.
gi 686428090 169 PAAGLDFIARE 179
Cdd:PRK13640 170 STSMLDPAGKE 180
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
15-168 |
1.96e-10 |
|
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: 57.93 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 15 KTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKVGYSAE-----TVRQHIGFVsHSLL- 88
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGGGfnpelTGRENIYLN-GRLLg 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 89 EKFQEGERVIDVVIsgAFKSIGvyQDIDDEVRNeahqllklvgmsakaqqyigyLSTGEKQRVMIARALMGQPQVLILDE 168
Cdd:cd03220 114 LSRKEIDEKIDEII--EFSELG--DFIDLPVKT---------------------YSSGMKARLAFAIATALEPDILLIDE 168
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
20-174 |
2.86e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 57.12 E-value: 2.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 20 NISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKVGysaETVRQHIGFVSHsllekfQEGervID 99
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQR---DEYHQDLLYLGH------QPG---IK 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 686428090 100 VVISgAFKSIGVYQDIDDEVRNEA-HQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:PRK13538 87 TELT-ALENLRFYQRLHGPGDDEAlWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
14-174 |
4.13e-10 |
|
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: 56.77 E-value: 4.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 14 GKTILKNISWQINGGDKWILYGLNGAGKTTLLNIL---NAYEPaTTGSVNLFGK----MPgkvgySAETVRQHIgFVShs 86
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImghPKYEV-TEGEILFKGEditdLP-----PEERARLGI-FLA-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 87 llekFQEGERvidvvISGafksigvyqdiddeVRNEahQLLKLVGMSakaqqyigyLSTGEKQRVMIARALMGQPQVLIL 166
Cdd:cd03217 83 ----FQYPPE-----IPG--------------VKNA--DFLRYVNEG---------FSGGEKKRNEILQLLLLEPDLAIL 128
|
....*...
gi 686428090 167 DEPAAGLD 174
Cdd:cd03217 129 DEPDSGLD 136
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-174 |
4.99e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 57.16 E-value: 4.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 17 ILKNISWQINGGDKWILYGLNGAGKTTLLNILNAY-----EPATTGSVNLFGKMPGKVGYSAETVRQHIGFVSHS----- 86
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDPIEVRREVGMVFQYpnpfp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 87 ------------LLEKFQEGERVIDVVISGAFKSIGVYqdidDEVRNeahqllklvgmsaKAQQYIGYLSTGEKQRVMIA 154
Cdd:PRK14267 99 hltiydnvaigvKLNGLVKSKKELDERVEWALKKAALW----DEVKD-------------RLNDYPSNLSGGQRQRLVIA 161
|
170 180
....*....|....*....|
gi 686428090 155 RALMGQPQVLILDEPAAGLD 174
Cdd:PRK14267 162 RALAMKPKILLMDEPTANID 181
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
3-174 |
5.43e-10 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 57.02 E-value: 5.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 3 IQLDQVGRMKQGKTILKNISWQI-NGGdkwI--LYGLNGAGKTTLLNILNAYEPATTGSVNLFGK----MPGKVgySAET 75
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIpKGG---ItaLIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLdvatTPSRE--LAKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 76 V---RQHIGFVShslleKFqegeRVIDVVISGAFK-SIGVYQDIDDEVRNEAHQLLKLVGMsakAQQYIGYLSTGEKQRV 151
Cdd:COG4604 77 LailRQENHINS-----RL----TVRELVAFGRFPySKGRLTAEDREIIDEAIAYLDLEDL---ADRYLDELSGGQRQRA 144
|
170 180
....*....|....*....|...
gi 686428090 152 MIARALMGQPQVLILDEPAAGLD 174
Cdd:COG4604 145 FIAMVLAQDTDYVLLDEPLNNLD 167
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
18-178 |
5.69e-10 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 57.74 E-value: 5.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 18 LKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKVGYSA--ETVRQHIGFVSHSLleKFQEGE 95
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrEVRRKKIAMVFQSF--ALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 96 RVIDVVISGaFKSIGVYQDiddEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDEPAAGLDF 175
Cdd:PRK10070 122 TVLDNTAFG-MELAGINAE---ERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
|
...
gi 686428090 176 IAR 178
Cdd:PRK10070 198 LIR 200
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
15-174 |
7.26e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 56.92 E-value: 7.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 15 KTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKvgYSAETVRQHIGFVSHSLLekfQEG 94
Cdd:PRK10253 20 YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQH--YASKEVARRIGLLAQNAT---TPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 95 E-RVIDVVISGAFKSIGVYQDIDDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDEPAAGL 173
Cdd:PRK10253 95 DiTVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
.
gi 686428090 174 D 174
Cdd:PRK10253 175 D 175
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
18-179 |
7.26e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 57.61 E-value: 7.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 18 LKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKmPGKVGYSAETVRQHIGFVshsllekFQEGERV 97
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ-EMRFASTTAALAAGVAII-------YQELHLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 98 IDVVIS-----GAF-KSIGVyqdIDD-EVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDEPA 170
Cdd:PRK11288 92 PEMTVAenlylGQLpHKGGI---VNRrLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPT 168
|
....*....
gi 686428090 171 AGLDfiARE 179
Cdd:PRK11288 169 SSLS--ARE 175
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
18-177 |
7.99e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 56.71 E-value: 7.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 18 LKNISWQINGGDKWILYGLNGAGKTTLL---NILNAYEPA--TTGSVNLFGKMPGKVGYSAETVRQHIGFV-------SH 85
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILrcfNRLNDLIPGfrVEGKVTFHGKNLYAPDVDPVEVRRRIGMVfqkpnpfPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 86 SLLEKFQEGERV------IDVVISGAFKSIGVYqdidDEVRNEahqlLKLVGMSakaqqyigyLSTGEKQRVMIARALMG 159
Cdd:PRK14243 106 SIYDNIAYGARIngykgdMDELVERSLRQAALW----DEVKDK----LKQSGLS---------LSGGQQQRLCIARAIAV 168
|
170
....*....|....*...
gi 686428090 160 QPQVLILDEPAAGLDFIA 177
Cdd:PRK14243 169 QPEVILMDEPCSALDPIS 186
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
18-178 |
8.34e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 56.72 E-value: 8.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 18 LKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVnLFGKMP---GKVGYSAETVRQHIGFVSHSLLEKfQEG 94
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGEL-LIDDHPlhfGDYSYRSQRIRMIFQDPSTSLNPR-QRI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 95 ERVIDVvisgafkSIGVYQDIDDEVRNEA-HQLLKLVGMSAK-AQQYIGYLSTGEKQRVMIARALMGQPQVLILDEPAAG 172
Cdd:PRK15112 107 SQILDF-------PLRLNTDLEPEQREKQiIETLRQVGLLPDhASYYPHMLAPGQKQRLGLARALILRPKVIIADEALAS 179
|
....*.
gi 686428090 173 LDFIAR 178
Cdd:PRK15112 180 LDMSMR 185
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
2-173 |
8.77e-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: 57.14 E-value: 8.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 2 LIQLDQVGRMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATT--GSVnLFGKMPGKVGYSAETVRQH 79
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEI-YWSGSPLKASNIRDTERAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 80 IGFVsHSLLEKFQEGERVIDVVISGAFKSIGVYQDiDDEVRNEAHQLLKLVGMSA-KAQQYIGYLSTGEKQRVMIARALM 158
Cdd:TIGR02633 80 IVII-HQELTLVPELSVAENIFLGNEITLPGGRMA-YNAMYLRAKNLLRELQLDAdNVTRPVGDYGGGQQQLVEIAKALN 157
|
170
....*....|....*
gi 686428090 159 GQPQVLILDEPAAGL 173
Cdd:TIGR02633 158 KQARLLILDEPSSSL 172
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
15-168 |
9.16e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 56.24 E-value: 9.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 15 KTILKNISWQINGGDKWILYGLNGAGKTTLLNILN-AYEPaTTGSVNLFGKMPGKVGYSA----E-TVRQHIGFVSHSLL 88
Cdd:COG1134 39 FWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAgILEP-TSGRVEVNGRVSALLELGAgfhpElTGRENIYLNGRLLG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 89 EKFQEGERVIDVVIsgAFKSIGVYqdIDDEVRNeahqllklvgmsakaqqYigylSTGEKQRVMIARALMGQPQVLILDE 168
Cdd:COG1134 118 LSRKEIDEKFDEIV--EFAELGDF--IDQPVKT-----------------Y----SSGMRARLAFAVATAVDPDILLVDE 172
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
17-174 |
1.09e-09 |
|
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: 55.55 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 17 ILKNISWQINGGDKWILYGLNGAGKTTLLN-ILNayE-PATTGSVNlfgkMPGKVGYSA-------ETVRQHIGFvshsl 87
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLG--ElEKLSGSVS----VPGSIAYVSqepwiqnGTIRENILF----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 88 LEKFQEgERVIDVVisgafksigvyqdiddevrnEAHQLLK-LVGMSAKAQQYIG----YLSTGEKQRVMIARALMGQPQ 162
Cdd:cd03250 89 GKPFDE-ERYEKVI--------------------KACALEPdLEILPDGDLTEIGekgiNLSGGQKQRISLARAVYSDAD 147
|
170
....*....|..
gi 686428090 163 VLILDEPAAGLD 174
Cdd:cd03250 148 IYLLDDPLSAVD 159
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2-173 |
1.36e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.60 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 2 LIQLDQVGRMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGK-----MPGKVG------ 70
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcarlTPAKAHqlgiyl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 71 -------YSAETVRQHIGFVshslLEKFQEGERVIDvvisgafksigvyqdiddevrneahQLLKLVGMSAKAQQYIGYL 143
Cdd:PRK15439 91 vpqepllFPNLSVKENILFG----LPKRQASMQKMK-------------------------QLLAALGCQLDLDSSAGSL 141
|
170 180 190
....*....|....*....|....*....|
gi 686428090 144 STGEKQRVMIARALMGQPQVLILDEPAAGL 173
Cdd:PRK15439 142 EVADRQIVEILRGLMRDSRILILDEPTASL 171
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
15-174 |
1.48e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 55.86 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 15 KTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKmpgKVGYSAETVR-QHIGFVshsllekFQe 93
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGK---DVTKLPEYKRaKYIGRV-------FQ- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 94 gerviDVVISGAF---------------KSIGVYQDIDDEVRNEAHQLLKLVG------MSAKaqqyIGYLSTGEKQRVM 152
Cdd:COG1101 88 -----DPMMGTAPsmtieenlalayrrgKRRGLRRGLTKKRRELFRELLATLGlglenrLDTK----VGLLSGGQRQALS 158
|
170 180
....*....|....*....|..
gi 686428090 153 IARALMGQPQVLILDEPAAGLD 174
Cdd:COG1101 159 LLMATLTKPKLLLLDEHTAALD 180
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
17-174 |
1.67e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 55.24 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 17 ILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKmPGKvgySAETVRqHIGFVSH--------SLL 88
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK-TAT---RGDRSR-FMAYLGHlpglkadlSTL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 89 EKFQ-----EGERVidvvisgafksigvyqdiddevRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQV 163
Cdd:PRK13543 101 ENLHflcglHGRRA----------------------KQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPL 158
|
170
....*....|.
gi 686428090 164 LILDEPAAGLD 174
Cdd:PRK13543 159 WLLDEPYANLD 169
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
13-177 |
1.88e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 56.43 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 13 QGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPAT--TGSVNLFGKMPGK-----VGYSAE--------TVR 77
Cdd:PLN03211 79 QERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKqilkrTGFVTQddilyphlTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 78 QHIGFVSHSLLEKF---QEGERVIDVVISgafkSIGvyqdiddevrneahqlLKLVGMSAKAQQYIGYLSTGEKQRVMIA 154
Cdd:PLN03211 159 ETLVFCSLLRLPKSltkQEKILVAESVIS----ELG----------------LTKCENTIIGNSFIRGISGGERKRVSIA 218
|
170 180
....*....|....*....|...
gi 686428090 155 RALMGQPQVLILDEPAAGLDFIA 177
Cdd:PLN03211 219 HEMLINPSLLILDEPTSGLDATA 241
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
7-174 |
2.52e-09 |
|
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: 54.56 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 7 QVGRMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPA--TTGSVNLFGKmPGKvgysaETVRQHIGFVS 84
Cdd:cd03232 12 TVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGR-PLD-----KNFQRSTGYVE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 85 HsllekfqegervIDVVISGAfksigvyqdiddEVRnEAHQLlklvgmSAkaqqYIGYLSTGEKQRVMIARALMGQPQVL 164
Cdd:cd03232 86 Q------------QDVHSPNL------------TVR-EALRF------SA----LLRGLSVEQRKRLTIGVELAAKPSIL 130
|
170
....*....|
gi 686428090 165 ILDEPAAGLD 174
Cdd:cd03232 131 FLDEPTSGLD 140
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
120-174 |
3.01e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 55.87 E-value: 3.01e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 686428090 120 RNEAHQLLKLVGMSAKAQQYIGY---LSTGEKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:PRK15134 131 RGEILNCLDRVGIRQAAKRLTDYphqLSGGERQRVMIAMALLTRPELLIADEPTTALD 188
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
14-175 |
3.12e-09 |
|
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: 54.80 E-value: 3.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 14 GKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKVgySAETVRQHIGFV-------SHS 86
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALA--DPAWLRRQVGVVlqenvlfNRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 87 LLEKFQEG------ERVIDVV-ISGAFKSIgvyqdidDEVRNEAHQLLKLVGMSakaqqyigyLSTGEKQRVMIARALMG 159
Cdd:cd03252 92 IRDNIALAdpgmsmERVIEAAkLAGAHDFI-------SELPEGYDTIVGEQGAG---------LSGGQRQRIAIARALIH 155
|
170
....*....|....*.
gi 686428090 160 QPQVLILDEPAAGLDF 175
Cdd:cd03252 156 NPRILIFDEATSALDY 171
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-179 |
3.16e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 55.09 E-value: 3.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 18 LKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKvgYSAETVRQhIGFVshsllekFqeGER- 96
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFK--RRKEFARR-IGVV-------F--GQRs 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 97 -------VIDvvisgAFKSIGVYQDIDDEV-RNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDE 168
Cdd:COG4586 106 qlwwdlpAID-----SFRLLKAIYRIPDAEyKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDE 180
|
170
....*....|.
gi 686428090 169 PAAGLDFIARE 179
Cdd:COG4586 181 PTIGLDVVSKE 191
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
14-177 |
3.33e-09 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 54.66 E-value: 3.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 14 GKTILKNISWQINggDKWI--LYGLNGAGKTTLL---NILNAYEP--ATTGSVNLFGKMPGKVGYSAETVRQHIGFVshs 86
Cdd:COG1117 23 DKQALKDINLDIP--ENKVtaLIGPSGCGKSTLLrclNRMNDLIPgaRVEGEILLDGEDIYDPDVDVVELRRRVGMV--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 87 llekFQE-------------------GER---VIDVVISGAFKSIGVYqdidDEVRNEAHQllklvgmSAKAqqyigyLS 144
Cdd:COG1117 98 ----FQKpnpfpksiydnvayglrlhGIKsksELDEIVEESLRKAALW----DEVKDRLKK-------SALG------LS 156
|
170 180 190
....*....|....*....|....*....|...
gi 686428090 145 TGEKQRVMIARALMGQPQVLILDEPAAGLDFIA 177
Cdd:COG1117 157 GGQQQRLCIARALAVEPEVLLMDEPTSALDPIS 189
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-174 |
4.00e-09 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 54.63 E-value: 4.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 1 MLIQLDQVGRMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKvgYSAETVRQHI 80
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISM--LSSRQLARRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 81 GFVSHSLLEKfqEGERVIDVVISGAFKSIGVYQDIDDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQ 160
Cdd:PRK11231 79 ALLPQHHLTP--EGITVRELVAYGRSPWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQD 156
|
170
....*....|....
gi 686428090 161 PQVLILDEPAAGLD 174
Cdd:PRK11231 157 TPVVLLDEPTTYLD 170
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
12-174 |
4.09e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 54.83 E-value: 4.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 12 KQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNayepattgsvnlfGKMPGKVGYSAETVRQHIGFVSHSL---- 87
Cdd:PRK13547 11 RRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALA-------------GDLTGGGAPRGARVTGDVTLNGEPLaaid 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 88 ---LEKF-----QEGER-----VIDVVISGAFKSIGVYQDIDDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIA 154
Cdd:PRK13547 78 aprLARLravlpQAAQPafafsAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFA 157
|
170 180
....*....|....*....|....*....
gi 686428090 155 RAL---------MGQPQVLILDEPAAGLD 174
Cdd:PRK13547 158 RVLaqlwpphdaAQPPRYLLLDEPTAALD 186
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
11-176 |
4.24e-09 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 54.86 E-value: 4.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 11 MKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLN----ILNayepaTTGSVNLFGKMPGKVgySAETVRQHIGFVSHS 86
Cdd:cd03289 13 TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSaflrLLN-----TEGDIQIDGVSWNSV--PLQKWRKAFGVIPQK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 87 LLekfqegervidvVISGAF-KSIGVYQDIDDEvrnEAHQLLKLVGMSAKAQQYIG-----------YLSTGEKQRVMIA 154
Cdd:cd03289 86 VF------------IFSGTFrKNLDPYGKWSDE---EIWKVAEEVGLKSVIEQFPGqldfvlvdggcVLSHGHKQLMCLA 150
|
170 180
....*....|....*....|..
gi 686428090 155 RALMGQPQVLILDEPAAGLDFI 176
Cdd:cd03289 151 RSVLSKAKILLLDEPSAHLDPI 172
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
13-174 |
4.54e-09 |
|
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: 53.31 E-value: 4.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 13 QGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNlfgkMPGkvgysaetvRQHIGFVS-HSLLekf 91
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG----MPE---------GEDLLFLPqRPYL--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 92 qegervidvvISGAFKSIGVY--QDIddevrneahqllklvgmsakaqqyigyLSTGEKQRVMIARALMGQPQVLILDEP 169
Cdd:cd03223 76 ----------PLGTLREQLIYpwDDV---------------------------LSGGEQQRLAFARLLLHKPKFVFLDEA 118
|
....*
gi 686428090 170 AAGLD 174
Cdd:cd03223 119 TSALD 123
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-174 |
4.64e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 55.10 E-value: 4.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 15 KTILKNISWQINGGDKWILYGLNGAGKTT----LLNILNAyepatTGSVnLFGKMPGKvGYSAET---VRQHIGFVSH-- 85
Cdd:PRK15134 299 NVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEI-WFDGQPLH-NLNRRQllpVRHRIQVVFQdp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 86 --------SLLEKFQEGERVIDVVISGAfksigvyqdiddEVRNEAHQLLKLVGMSAKAQQ-YIGYLSTGEKQRVMIARA 156
Cdd:PRK15134 372 nsslnprlNVLQIIEEGLRVHQPTLSAA------------QREQQVIAVMEEVGLDPETRHrYPAEFSGGQRQRIAIARA 439
|
170
....*....|....*...
gi 686428090 157 LMGQPQVLILDEPAAGLD 174
Cdd:PRK15134 440 LILKPSLIILDEPTSSLD 457
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-174 |
5.86e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 54.15 E-value: 5.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 17 ILKNISWQINGGDKWILYGLNGAGKTTLLNILNAY-----EPATTGSVNLFGKMPGKVGYSAETVRQHIGFV------SH 85
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIELRRRVQMVFQipnpipNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 86 SLLEKFQEGERVIDVVISGAFKSIGVYQDID-----DEVRNEahqllklvgMSAKAqqyiGYLSTGEKQRVMIARALMGQ 160
Cdd:PRK14247 98 SIFENVALGLKLNRLVKSKKELQERVRWALEkaqlwDEVKDR---------LDAPA----GKLSGGQQQRLCIARALAFQ 164
|
170
....*....|....
gi 686428090 161 PQVLILDEPAAGLD 174
Cdd:PRK14247 165 PEVLLADEPTANLD 178
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
14-174 |
7.97e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.57 E-value: 7.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 14 GKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMpgKVGYsaetvrqhigFVSH-------- 85
Cdd:PRK11147 331 GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKL--EVAY----------FDQHraeldpek 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 86 SLLEKFQEGERviDVVISGAFKSI-GVYQDIddevrneahqLLKlvgmSAKAQQYIGYLSTGEKQRVMIARALMGQPQVL 164
Cdd:PRK11147 399 TVMDNLAEGKQ--EVMVNGRPRHVlGYLQDF----------LFH----PKRAMTPVKALSGGERNRLLLARLFLKPSNLL 462
|
170
....*....|
gi 686428090 165 ILDEPAAGLD 174
Cdd:PRK11147 463 ILDEPTNDLD 472
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
19-178 |
8.14e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 54.29 E-value: 8.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 19 KNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMpgkvgYSAETVRQHI--GFVShsLLEKFQEGER 96
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKE-----INALSTAQRLarGLVY--LPEDRQSSGL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 97 VIDV-----VISGAFKSIGVYQDIDDE--VRNEAHQLL--KLvgmsAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILD 167
Cdd:PRK15439 353 YLDAplawnVCALTHNRRGFWIKPAREnaVLERYRRALniKF----NHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVD 428
|
170
....*....|.
gi 686428090 168 EPAAGLDFIAR 178
Cdd:PRK15439 429 EPTRGVDVSAR 439
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-173 |
1.05e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 54.24 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 2 LIQLDQVGRMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKmpgKVGYSAETVRQHIG 81
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGK---EVTFNGPKSSQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 82 F-VSHSLLEKFQEGERVIDVVISGAFKSIgvYQDID-DEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMG 159
Cdd:PRK10762 81 IgIIHQELNLIPQLTIAENIFLGREFVNR--FGRIDwKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSF 158
|
170
....*....|....
gi 686428090 160 QPQVLILDEPAAGL 173
Cdd:PRK10762 159 ESKVIIMDEPTDAL 172
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
18-173 |
1.81e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.39 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 18 LKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPattgsvnlFGKMPGKVGYSAETVR-QHIgfvshsllekfQEGER 96
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYP--------HGTYEGEIIFEGEELQaSNI-----------RDTER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 97 VIDVVISGAF---KSIGVYQDI-------------DDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQ 160
Cdd:PRK13549 82 AGIAIIHQELalvKELSVLENIflgneitpggimdYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQ 161
|
170
....*....|...
gi 686428090 161 PQVLILDEPAAGL 173
Cdd:PRK13549 162 ARLLILDEPTASL 174
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
21-179 |
1.95e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 52.63 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 21 ISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATtGSVNLFGKMPGkvGYSAETVRQHIGFVSHSllekfqegervidv 100
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGS-GSIQFAGQPLE--AWSAAELARHRAYLSQQ-------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 101 vISGAFkSIGVYQDID---------DEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIA-------RALMGQPQVL 164
Cdd:PRK03695 78 -QTPPF-AMPVFQYLTlhqpdktrtEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLL 155
|
170
....*....|....*
gi 686428090 165 ILDEPAAGLDfIARE 179
Cdd:PRK03695 156 LLDEPMNSLD-VAQQ 169
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
16-174 |
1.95e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 52.93 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 16 TILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLfgkMPGKVGYSAETVRQHIGFVSHSLlEKFQEGE 95
Cdd:PRK13631 40 VALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQV---GDIYIGDKKNNHELITNPYSKKI-KNFKELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 96 RVIDVVISgaFKSIGVYQD-IDDEV----------RNEAHQLLK--LVGMSAKaQQYIGY----LSTGEKQRVMIARALM 158
Cdd:PRK13631 116 RRVSMVFQ--FPEYQLFKDtIEKDImfgpvalgvkKSEAKKLAKfyLNKMGLD-DSYLERspfgLSGGQKRRVAIAGILA 192
|
170
....*....|....*.
gi 686428090 159 GQPQVLILDEPAAGLD 174
Cdd:PRK13631 193 IQPEILIFDEPTAGLD 208
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
14-174 |
2.08e-08 |
|
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: 53.18 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 14 GKTILKNISWQINGGDKWILYGLNGAGKTTLLNIL-NAYEPaTTGSVnLFGKMPGKvGYSAETVRQHIGFVSHSLlekFQ 92
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIpRFYEP-DSGQI-LLDGHDLA-DYTLASLRRQVALVSQDV---VL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 93 EGERVIDVVISGAFKSIGvyqdiDDEVRN--EAHQLLKLV-GMSAKAQQYIG----YLSTGEKQRVMIARALMGQPQVLI 165
Cdd:TIGR02203 418 FNDTIANNIAYGRTEQAD-----RAEIERalAAAYAQDFVdKLPLGLDTPIGengvLLSGGQRQRLAIARALLKDAPILI 492
|
....*....
gi 686428090 166 LDEPAAGLD 174
Cdd:TIGR02203 493 LDEATSALD 501
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
14-174 |
2.56e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.97 E-value: 2.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 14 GKTILKNISWQINGGDKWILYGLNGAGKTTLLNIL-NAYEPaTTGSVNLFGKmpGKVGYSAEtvrqhigfvSHSllEKFQ 92
Cdd:PRK15064 331 NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLvGELEP-DSGTVKWSEN--ANIGYYAQ---------DHA--YDFE 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 93 EGERVIDVVisGAFKSIGvyqdiDDE--VRNEAHQLL---KLVGMSAKAqqyigyLSTGEKQRVMIARALMGQPQVLILD 167
Cdd:PRK15064 397 NDLTLFDWM--SQWRQEG-----DDEqaVRGTLGRLLfsqDDIKKSVKV------LSGGEKGRMLFGKLMMQKPNVLVMD 463
|
....*..
gi 686428090 168 EPAAGLD 174
Cdd:PRK15064 464 EPTNHMD 470
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-178 |
2.65e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 52.90 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 20 NISWQINGGDKWILYGLNGAGKTTLLN-ILNAYEPATTGSVNLFGKmPGKVGYSAETVRQHIGFV-----SHSLLEKFQE 93
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGK-PVDIRNPAQAIRAGIAMVpedrkRHGIVPILGV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 94 GERVIDVVISgAFKSIGVyqdIDDEVR----NEAHQLLKLvgMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDEP 169
Cdd:TIGR02633 357 GKNITLSVLK-SFCFKMR---IDAAAElqiiGSAIQRLKV--KTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEP 430
|
....*....
gi 686428090 170 AAGLDFIAR 178
Cdd:TIGR02633 431 TRGVDVGAK 439
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
14-174 |
2.65e-08 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 52.26 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 14 GKTILKNISWQINGGDKWILYGLNGAGKTTLLNIL---NAYEpATTGSVNLFGKMPGKVgySAETvRQHIG-FVShslle 89
Cdd:TIGR01978 12 DKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIaghPSYE-VTSGTILFKGQDLLEL--EPDE-RARAGlFLA----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 90 kFQEGERVIDV-------VISGAFKSIGVYQDID-DEVRNEAHQLLKLVGMSAK-AQQYIGY-LSTGEKQRVMIARALMG 159
Cdd:TIGR01978 83 -FQYPEEIPGVsnleflrSALNARRSARGEEPLDlLDFEKLLKEKLALLDMDEEfLNRSVNEgFSGGEKKRNEILQMALL 161
|
170
....*....|....*
gi 686428090 160 QPQVLILDEPAAGLD 174
Cdd:TIGR01978 162 EPKLAILDEIDSGLD 176
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
33-178 |
2.89e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.61 E-value: 2.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 33 LYGLNGAGKTTLLNILNAYEPATTGSVNLFGKmPGKVGYSAETVRQHI----------GFVS-HSLLEKfqegervIDVV 101
Cdd:PRK11288 284 LFGLVGAGRSELMKLLYGATRRTAGQVYLDGK-PIDIRSPRDAIRAGImlcpedrkaeGIIPvHSVADN-------INIS 355
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 686428090 102 ISGAFKSIGVYQDIDDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDEPAAGLDFIAR 178
Cdd:PRK11288 356 ARRHHLRAGCLINNRWEAENADRFIRSLNIKTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAK 432
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
16-174 |
3.81e-08 |
|
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: 52.51 E-value: 3.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 16 TILKNISWQINGGDKWILYGLNGAGKTTLLNIL-NAYEPaTTGSVNLFGKMPGKVgySAETVRQHIGFVShsllekfQeg 94
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLfRFYDV-TSGRILIDGQDIRDV--TQASLRAAIGIVP-------Q-- 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 95 erviDVVIsgaFK-SIgvYQDI--------DDEVRnEAHQLLKLVGMSAKAQQyiGY----------LSTGEKQRVMIAR 155
Cdd:COG5265 440 ----DTVL---FNdTI--AYNIaygrpdasEEEVE-AAARAAQIHDFIESLPD--GYdtrvgerglkLSGGEKQRVAIAR 507
|
170
....*....|....*....
gi 686428090 156 ALMGQPQVLILDEPAAGLD 174
Cdd:COG5265 508 TLLKNPPILIFDEATSALD 526
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
116-174 |
5.41e-08 |
|
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: 51.99 E-value: 5.41e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 116 DDEVRNEAHQLLKLVGMSAKAQQ-YIGYLSTGEKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:COG4172 398 AAERRARVAEALEEVGLDPAARHrYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD 457
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
13-179 |
5.93e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 50.72 E-value: 5.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 13 QGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKvgySAETVRQHIGFVSHSllekfq 92
Cdd:PRK13540 12 HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK---DLCTYQKQLCFVGHR------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 93 egervidvviSGAFKSIGV----YQDIDDEVRN-EAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILD 167
Cdd:PRK13540 83 ----------SGINPYLTLrencLYDIHFSPGAvGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLD 152
|
170
....*....|..
gi 686428090 168 EPAAGLDFIARE 179
Cdd:PRK13540 153 EPLVALDELSLL 164
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
3-174 |
6.54e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 51.55 E-value: 6.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 3 IQLDQVGRMKQGKT-----ILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSvNLFG--KMPGKVGYSAET 75
Cdd:PRK13645 7 IILDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQ-TIVGdyAIPANLKKIKEV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 76 --VRQHIGFVSHslLEKFQEGERVIDVVIsgAFKSIGVYQDiDDEVRNEAHQLLKLVGMSAK-AQQYIGYLSTGEKQRVM 152
Cdd:PRK13645 86 krLRKEIGLVFQ--FPEYQLFQETIEKDI--AFGPVNLGEN-KQEAYKKVPELLKLVQLPEDyVKRSPFELSGGQKRRVA 160
|
170 180
....*....|....*....|..
gi 686428090 153 IARALMGQPQVLILDEPAAGLD 174
Cdd:PRK13645 161 LAGIIAMDGNTLVLDEPTGGLD 182
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
3-174 |
7.71e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 51.56 E-value: 7.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 3 IQLDQVGRMKQGKTI--LKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKvgYSAETVRQHI 80
Cdd:PRK11176 342 IEFRNVTFTYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRD--YTLASLRNQV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 81 GFVShsllekfQEGERVIDVV---ISGAFKSIGVYQDIDDEVRnEAHQLLKLVGMSAKAQQYIG----YLSTGEKQRVMI 153
Cdd:PRK11176 420 ALVS-------QNVHLFNDTIannIAYARTEQYSREQIEEAAR-MAYAMDFINKMDNGLDTVIGengvLLSGGQRQRIAI 491
|
170 180
....*....|....*....|.
gi 686428090 154 ARALMGQPQVLILDEPAAGLD 174
Cdd:PRK11176 492 ARALLRDSPILILDEATSALD 512
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
35-178 |
9.76e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 51.28 E-value: 9.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 35 GLNGAGKTTLLNILNAYEPATTGSVNLFGKmpgKVGYSAETVRQHIGFVSH--SLLekfqeGErvidvvisgafksIGVY 112
Cdd:NF033858 299 GSNGCGKSTTMKMLTGLLPASEGEAWLFGQ---PVDAGDIATRRRVGYMSQafSLY-----GE-------------LTVR 357
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 686428090 113 QDID----------DEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDEPAAGLDFIAR 178
Cdd:NF033858 358 QNLElharlfhlpaAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVAR 433
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
7-174 |
1.73e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.88 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 7 QVGRMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNayEPATTGSVNLFGKMpgkVGYSA--ETVRQHIGFVS 84
Cdd:TIGR00956 768 EVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTGVITGGDRL---VNGRPldSSFQRSIGYVQ 842
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 85 ----HSllekfqEGERVIDVVISGAF----KSIGVYQDID--DEVrneahqlLKLVGMSAKAQQYIGY----LSTGEKQR 150
Cdd:TIGR00956 843 qqdlHL------PTSTVRESLRFSAYlrqpKSVSKSEKMEyvEEV-------IKLLEMESYADAVVGVpgegLNVEQRKR 909
|
170 180
....*....|....*....|....*
gi 686428090 151 VMIARALMGQPQVLI-LDEPAAGLD 174
Cdd:TIGR00956 910 LTIGVELVAKPKLLLfLDEPTSGLD 934
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-174 |
1.76e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.58 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 32 ILyGLNGAGKTTLLNILnayepatTGSV--NLfGKMPGKVGYSaETVRQHIGFVSHSLLEKFQEGErvIDVV-------- 101
Cdd:PRK13409 104 IL-GPNGIGKTTAVKIL-------SGELipNL-GDYEEEPSWD-EVLKRFRGTELQNYFKKLYNGE--IKVVhkpqyvdl 171
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 686428090 102 ISGAFKsiGVYQDI---DDEvRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:PRK13409 172 IPKVFK--GKVRELlkkVDE-RGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
15-174 |
2.10e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 50.28 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 15 KTILKNISWQINGGDKWILYGLNGAGKTTLLNIL-NAYEPaTTGSVNLfgkMPG-KVGysaeTVRQhigfvshsllEKFQ 92
Cdd:PRK15064 14 KPLFENISVKFGGGNRYGLIGANGCGKSTFMKILgGDLEP-SAGNVSL---DPNeRLG----KLRQ----------DQFA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 93 -EGERVIDVVISGAFKSIGVYQDIDD------------------------------EVRneAHQLLKLVGMSakAQQYIG 141
Cdd:PRK15064 76 fEEFTVLDTVIMGHTELWEVKQERDRiyalpemseedgmkvadlevkfaemdgytaEAR--AGELLLGVGIP--EEQHYG 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 686428090 142 YLST---GEKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:PRK15064 152 LMSEvapGWKLRVLLAQALFSNPDILLLDEPTNNLD 187
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
9-174 |
2.10e-07 |
|
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: 49.18 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 9 GRMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILnayepatTGSVNLFGKMPGKVGYSaetvrqhiGFVSHSLL 88
Cdd:cd03233 14 GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKAL-------ANRTEGNVSVEGDIHYN--------GIPYKEFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 89 EKFQEgerviDVVISGA----FKSIGVYQDIDDEVRneahqllklvgmsAKAQQYIGYLSTGEKQRVMIARALMGQPQVL 164
Cdd:cd03233 79 EKYPG-----EIIYVSEedvhFPTLTVRETLDFALR-------------CKGNEFVRGISGGERKRVSIAEALVSRASVL 140
|
170
....*....|
gi 686428090 165 ILDEPAAGLD 174
Cdd:cd03233 141 CWDNSTRGLD 150
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
35-174 |
2.41e-07 |
|
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: 49.93 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 35 GLNGAGKTTLLNILNAYEPATTGSVnlfgkmpgKVGysaETVrqHIGFV--SHSLLEkfqeGERVIDVVISGAfksigvy 112
Cdd:TIGR03719 355 GPNGAGKSTLFRMITGQEQPDSGTI--------EIG---ETV--KLAYVdqSRDALD----PNKTVWEEISGG------- 410
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 113 QDI----DDEVRNEAHqllklVG----MSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:TIGR03719 411 LDIiklgKREIPSRAY-----VGrfnfKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
35-174 |
4.35e-07 |
|
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: 49.40 E-value: 4.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 35 GLNGAGKTTLLNILnayepattgSVNL---FGKMPGKVGYSaETVRQHIGFVSHSLLEKFQEGE-RV------IDVvISG 104
Cdd:COG1245 106 GPNGIGKSTALKIL---------SGELkpnLGDYDEEPSWD-EVLKRFRGTELQDYFKKLANGEiKVahkpqyVDL-IPK 174
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 686428090 105 AFKsiGVYQDI---DDEvRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:COG1245 175 VFK--GTVRELlekVDE-RGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
120-174 |
4.44e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 48.97 E-value: 4.44e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 686428090 120 RNEAHQLLKLVGMSAKAQQ---YIGYLSTGEKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:PRK11022 128 RQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALD 185
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
120-174 |
5.37e-07 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 48.75 E-value: 5.37e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 686428090 120 RNEAHQLLKLVG-------MSAKAQQyigyLSTGEKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:COG4170 133 KKRAIELLHRVGikdhkdiMNSYPHE----LTEGECQKVMIAMAIANQPRLLIADEPTNAME 190
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
144-174 |
9.41e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 48.18 E-value: 9.41e-07
10 20 30
....*....|....*....|....*....|.
gi 686428090 144 STGEKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALD 193
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
112-174 |
9.89e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.49 E-value: 9.89e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 686428090 112 YQDIDD-EVRNEAHQLLKLVGMSAKAQQY---IGY----LSTGEKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:PTZ00265 541 YQTIKDsEVVDVSKKVLIHDFVSALPDKYetlVGSnaskLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
35-174 |
1.05e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.19 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 35 GLNGAGKTTLLNILNAYEPATTGSVnlfgkmpgKVGysaETVrqHIGFV--SHSLLEkfqeGERVIDVVISGAfksigvy 112
Cdd:PRK11819 357 GPNGAGKSTLFKMITGQEQPDSGTI--------KIG---ETV--KLAYVdqSRDALD----PNKTVWEEISGG------- 412
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 686428090 113 QDIddevrneahqlLKL--VGMSAKA------------QQYIGYLSTGEKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:PRK11819 413 LDI-----------IKVgnREIPSRAyvgrfnfkggdqQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
15-177 |
2.07e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.47 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 15 KTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLfgkmPGKvgYSAETVRQHIGFVSHSLLE----- 89
Cdd:PRK10636 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTF----PGN--WQLAWVNQETPALPQPALEyvidg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 90 --KFQEGERVIDVV-----------ISGAFKSIGVYQdiddeVRNEAHQLLKLVGMS-AKAQQYIGYLSTGEKQRVMIAR 155
Cdd:PRK10636 88 drEYRQLEAQLHDAnerndghaiatIHGKLDAIDAWT-----IRSRAASLLHGLGFSnEQLERPVSDFSGGWRMRLNLAQ 162
|
170 180
....*....|....*....|..
gi 686428090 156 ALMGQPQVLILDEPAAGLDFIA 177
Cdd:PRK10636 163 ALICRSDLLLLDEPTNHLDLDA 184
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
17-174 |
2.24e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 47.25 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 17 ILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKM-------------PGKV-GYSAETVrQHIGf 82
Cdd:PRK11147 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLivarlqqdpprnvEGTVyDFVAEGI-EEQA- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 83 vshSLLEKFQEGERVIDVVISGA-FKSIGVYQDIDD-----EVRNEAHQLLKLVGMSAKAQqyIGYLSTGEKQRVMIARA 156
Cdd:PRK11147 96 ---EYLKRYHDISHLVETDPSEKnLNELAKLQEQLDhhnlwQLENRINEVLAQLGLDPDAA--LSSLSGGWLRKAALGRA 170
|
170
....*....|....*...
gi 686428090 157 LMGQPQVLILDEPAAGLD 174
Cdd:PRK11147 171 LVSNPDVLLLDEPTNHLD 188
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
137-178 |
2.38e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.03 E-value: 2.38e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 686428090 137 QQYIGYLSTGEKQRVMIARALMGQPQVLILDEPAAGLDFIAR 178
Cdd:PRK10982 386 RTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAK 427
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-175 |
4.61e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 46.48 E-value: 4.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 17 ILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKVGYsaETVRQHIGFVSHSllekfqeger 96
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGL--HDLRFKITIIPQD---------- 1368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 97 viDVVISGAFK----SIGVYQDIDDEVRNEAHQLLKLV-----GMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILD 167
Cdd:TIGR00957 1369 --PVLFSGSLRmnldPFSQYSDEEVWWALELAHLKTFVsalpdKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLD 1446
|
....*...
gi 686428090 168 EPAAGLDF 175
Cdd:TIGR00957 1447 EATAAVDL 1454
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
143-174 |
4.72e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.56 E-value: 4.72e-06
10 20 30
....*....|....*....|....*....|..
gi 686428090 143 LSTGEKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLD 1390
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
107-174 |
5.47e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 46.00 E-value: 5.47e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 686428090 107 KSIGVYQDID-DEVRNEAHQLLKLVGM---SAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:PRK10261 129 ESIRLHQGASrEEAMVEAKRMLDQVRIpeaQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALD 200
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
33-173 |
7.69e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.55 E-value: 7.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 33 LYGLNGAGKTTLLNILNAYEPAttgsvnlfGKMPGKVGYSAETVR-------QHIGFVS-H---------SLLEK-FQEG 94
Cdd:NF040905 32 LCGENGAGKSTLMKVLSGVYPH--------GSYEGEILFDGEVCRfkdirdsEALGIVIiHqelalipylSIAENiFLGN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 95 ERvidvvisgafKSIGVyqdID-DEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDEPAAGL 173
Cdd:NF040905 104 ER----------AKRGV---IDwNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAAL 170
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
18-178 |
8.61e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 45.08 E-value: 8.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 18 LKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMpgkvgYSAETV---RQHIGFVSHSLLEKFQeG 94
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGEL-----LTAENVwnlRRKIGMVFQNPDNQFV-G 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 95 ERVIDVVISGaFKSIGVYQDiddEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:PRK13642 97 ATVEDDVAFG-MENQGIPRE---EMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLD 172
|
....
gi 686428090 175 FIAR 178
Cdd:PRK13642 173 PTGR 176
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
15-174 |
8.62e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 45.02 E-value: 8.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 15 KTILKNISWQINGGDKWILYGLNGAGKTTLLNILnAYEPA---TTGSVNLFGKmpgKVGYSAETVRQHIG-FVShsllek 90
Cdd:CHL00131 20 NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVI-AGHPAykiLEGDILFKGE---SILDLEPEERAHLGiFLA------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 91 FQegervIDVVISG---------AFKSIGVYQDIDD-------EVRNEAhqlLKLVGMSAKaqqyigYL--------STG 146
Cdd:CHL00131 90 FQ-----YPIEIPGvsnadflrlAYNSKRKFQGLPEldpleflEIINEK---LKLVGMDPS------FLsrnvnegfSGG 155
|
170 180
....*....|....*....|....*...
gi 686428090 147 EKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:CHL00131 156 EKKRNEILQMALLDSELAILDETDSGLD 183
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-174 |
9.12e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 45.05 E-value: 9.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 33 LYGLNGAGKTTLLNILnayepATTGSVNLfGKMPGKVGYSaETVRQHIGFVSHSLLEKFQEGErvIDVV--------ISG 104
Cdd:cd03236 31 LVGPNGIGKSTALKIL-----AGKLKPNL-GKFDDPPDWD-EILDEFRGSELQNYFTKLLEGD--VKVIvkpqyvdlIPK 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 686428090 105 AFK-SIGVYQDIDDEvRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:cd03236 102 AVKgKVGELLKKKDE-RGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-174 |
1.46e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 44.32 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 14 GKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSvnlfgKMPGKVGYSAETV---------RQHIGFVs 84
Cdd:PRK14271 33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGY-----RYSGDVLLGGRSIfnyrdvlefRRRVGML- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 85 hsllekFQEGE----RVIDVVISGAFKSIGVYQDiddEVRNEAHQLLKLVGMSAKAQQYIG----YLSTGEKQRVMIARA 156
Cdd:PRK14271 107 ------FQRPNpfpmSIMDNVLAGVRAHKLVPRK---EFRGVAQARLTEVGLWDAVKDRLSdspfRLSGGQQQLLCLART 177
|
170
....*....|....*...
gi 686428090 157 LMGQPQVLILDEPAAGLD 174
Cdd:PRK14271 178 LAVNPEVLLLDEPTSALD 195
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
10-178 |
2.53e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 44.08 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 10 RMKQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKV-GYSAETVRQHIGFVshsll 88
Cdd:PRK10261 332 RVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLsPGKLQALRRDIQFI----- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 89 ekFQEGERVID---VVISGAFKSIGVYQDID-DEVRNEAHQLLKLVGMSAK-AQQYIGYLSTGEKQRVMIARALMGQPQV 163
Cdd:PRK10261 407 --FQDPYASLDprqTVGDSIMEPLRVHGLLPgKAAAARVAWLLERVGLLPEhAWRYPHEFSGGQRQRICIARALALNPKV 484
|
170
....*....|....*
gi 686428090 164 LILDEPAAGLDFIAR 178
Cdd:PRK10261 485 IIADEAVSALDVSIR 499
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
12-174 |
2.74e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 44.34 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 12 KQGKTILKNISWQINGGDKWILYGLNGAGKTTLLN-ILNAYEPATTGSVNLfgkmPGKVGYSAE-------TVRQHIGFV 83
Cdd:PLN03130 627 KAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVI----RGTVAYVPQvswifnaTVRDNILFG 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 84 SHSLLEKFqegERVIDVVisgafksiGVYQDIDdevrneahqLLklvgmSAKAQQYIGY----LSTGEKQRVMIARALMG 159
Cdd:PLN03130 703 SPFDPERY---ERAIDVT--------ALQHDLD---------LL-----PGGDLTEIGErgvnISGGQKQRVSMARAVYS 757
|
170
....*....|....*
gi 686428090 160 QPQVLILDEPAAGLD 174
Cdd:PLN03130 758 NSDVYIFDDPLSALD 772
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
138-174 |
5.26e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 43.24 E-value: 5.26e-05
10 20 30
....*....|....*....|....*....|....*..
gi 686428090 138 QYIGYLSTGEKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:NF040905 400 QKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
15-176 |
5.39e-05 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 42.83 E-value: 5.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 15 KTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGK-MPGKVGYSAETVRQHIgfvshSLLekFQe 93
Cdd:PRK11831 20 RCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEnIPAMSRSRLYTVRKRM-----SML--FQ- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 94 gervidvviSGA-FKSIGVYQDIDDEVRNEAHQ---------LLKL--VGMSAKAQQYIGYLSTGEKQRVMIARALMGQP 161
Cdd:PRK11831 92 ---------SGAlFTDMNVFDNVAYPLREHTQLpapllhstvMMKLeaVGLRGAAKLMPSELSGGMARRAALARAIALEP 162
|
170
....*....|....*
gi 686428090 162 QVLILDEPAAGLDFI 176
Cdd:PRK11831 163 DLIMFDEPFVGQDPI 177
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
118-174 |
7.47e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 42.41 E-value: 7.47e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 686428090 118 EVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:NF000106 120 DARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLD 176
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
33-174 |
8.14e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.91 E-value: 8.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 33 LYGLNGAGKTTLLNILNAYEpatTGsvnlfGKMPGKVGYSA-----ETVRQHIGFVSHSLLEKFQEgeRVIDVVISGAF- 106
Cdd:PLN03140 911 LMGVSGAGKTTLMDVLAGRK---TG-----GYIEGDIRISGfpkkqETFARISGYCEQNDIHSPQV--TVRESLIYSAFl 980
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 686428090 107 ---KSIGvyqdiDDEVRNEAHQLLKLVGMSAKAQQYIGY-----LSTGEKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:PLN03140 981 rlpKEVS-----KEEKMMFVDEVMELVELDNLKDAIVGLpgvtgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
35-174 |
8.52e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 42.49 E-value: 8.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 35 GLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKVGY----SAETVRQhigfvshsLLEKfqegervidvvISGAFKSIG 110
Cdd:PRK13409 372 GPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQYikpdYDGTVED--------LLRS-----------ITDDLGSSY 432
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 686428090 111 VYQDIddevrNEAHQLLKLVgmsakaQQYIGYLSTGEKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:PRK13409 433 YKSEI-----IKPLQLERLL------DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
117-174 |
9.16e-05 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 42.00 E-value: 9.16e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 686428090 117 DEVRNEAHQLLKLVGMSAKA-QQYIGYLSTGEKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:PRK15079 135 QEVKDRVKAMMLKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
143-169 |
1.22e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 41.71 E-value: 1.22e-04
10 20
....*....|....*....|....*..
gi 686428090 143 LSTGEKQRVMIARALMGQPQVLILDEP 169
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEP 185
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
140-179 |
1.49e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 41.55 E-value: 1.49e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 686428090 140 IGYLSTGEKQRVMIARALMGQPQVLILDEPAAGLDFIARE 179
Cdd:COG3845 400 ARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIE 439
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
35-174 |
1.51e-04 |
|
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: 41.69 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 35 GLNGAGKTTLLNILNAYEPATTGSVNlfgkMPGKVGY--------SAETVRQhigfvshsLLEKfqegervidvVISGAF 106
Cdd:COG1245 373 GPNGIGKTTFAKILAGVLKPDEGEVD----EDLKISYkpqyispdYDGTVEE--------FLRS----------ANTDDF 430
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 686428090 107 KSIGVYQDIDDEVrneahQLLKLVgmsakaQQYIGYLSTGEKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:COG1245 431 GSSYYKTEIIKPL-----GLEKLL------DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
14-179 |
2.32e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.38 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 14 GKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVnlfgkmpgkvgYSAETVRQHIgFVSHSLlekfqE 93
Cdd:PLN03073 521 GPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV-----------FRSAKVRMAV-FSQHHV-----D 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 94 GervIDVVISGAFKSIGVYQDIDdEVRNEAHqlLKLVGMSAK-AQQYIGYLSTGEKQRVMIARALMGQPQVLILDEPAAG 172
Cdd:PLN03073 584 G---LDLSSNPLLYMMRCFPGVP-EQKLRAH--LGSFGVTGNlALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNH 657
|
....*..
gi 686428090 173 LDFIARE 179
Cdd:PLN03073 658 LDLDAVE 664
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
35-174 |
2.34e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 40.28 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 35 GLNGAGKTTllnILNAYEPATTGSVNLFGKMpgkvgysaetvrqhiGFVSHSLlekFQEGERVIDVVIsgAFKSigvYQD 114
Cdd:cd03240 29 GQNGAGKTT---IIEALKYALTGELPPNSKG---------------GAHDPKL---IREGEVRAQVKL--AFEN---ANG 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 686428090 115 IDDEVRNEAHQLLKLV----GMSAK-AQQYIGYLSTGEKQ------RVMIARALMGQPQVLILDEPAAGLD 174
Cdd:cd03240 83 KKYTITRSLAILENVIfchqGESNWpLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLD 153
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
35-174 |
2.96e-04 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 40.29 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 35 GLNGAGKTTLLNILNAYEPATTGSV--NLFGKMPGKVGYSAETVRQHI-----GFVSHSLLEKFQE--------GERVID 99
Cdd:PRK11701 39 GESGSGKTTLLNALSARLAPDAGEVhyRMRDGQLRDLYALSEAERRRLlrtewGFVHQHPRDGLRMqvsaggniGERLMA 118
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 686428090 100 VvisgafksiGV--YQDIddevRNEAHQLLKLVGM-SAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:PRK11701 119 V---------GArhYGDI----RATAGDWLERVEIdAARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLD 183
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
14-168 |
3.19e-04 |
|
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: 40.89 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 14 GKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSV------NLFgKMPGKVGYSAETVRQHIGFvSHSL 87
Cdd:TIGR00954 464 GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLtkpakgKLF-YVPQRPYMTLGTLRDQIIY-PDSS 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 88 LEKFQEGERVIDVVisgafksigvyqDIDDEVRNEaHQLLKLVGMSAkAQQYIGYLSTGEKQRVMIARALMGQPQVLILD 167
Cdd:TIGR00954 542 EDMKRRGLSDKDLE------------QILDNVQLT-HILEREGGWSA-VQDWMDVLSGGEKQRIAMARLFYHKPQFAILD 607
|
.
gi 686428090 168 E 168
Cdd:TIGR00954 608 E 608
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
33-173 |
3.67e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.48 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 33 LYGLNGAGKTTLLNILNAYEPATTGSVNLFGKmPGKVGYSAETVRQHIGFVSHSLLEKFQEGerVIDVVISGAFKSIGVY 112
Cdd:PRK10982 29 LMGENGAGKSTLLKCLFGIYQKDSGSILFQGK-EIDFKSSKEALENGISMVHQELNLVLQRS--VMDNMWLGRYPTKGMF 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 686428090 113 QDiDDEVRNEAHQLLKLVGMSAKAQQYIGYLSTGEKQRVMIARALMGQPQVLILDEPAAGL 173
Cdd:PRK10982 106 VD-QDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-174 |
6.91e-04 |
|
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: 39.31 E-value: 6.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 25 INGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKmpgKVGYSAETVR-QHIGFVSHSLLEKFQegerviDVVIS 103
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELD---TVSYKPQYIKaDYEGTVRDLLSSITK------DFYTH 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 686428090 104 GAFKS-----IGVYQDIDDEVRNeahqllklvgmsakaqqyigyLSTGEKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:cd03237 93 PYFKTeiakpLQIEQILDREVPE---------------------LSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
1-52 |
8.31e-04 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 39.72 E-value: 8.31e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 686428090 1 MLIQLDQVgrmkQGKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYE 52
Cdd:COG4694 1 MITKIKKL----KNVGAFKDFGWLAFFKKLNLIYGENGSGKSTLSRILRSLE 48
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
91-174 |
1.30e-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: 37.94 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 91 FQEGERVIDVVISGAFKSIGVYQDIDDEVRNEAHQLLKLVGMSAKAQqYIGyLSTGEKQRVMIARALMGQPQVLILDEPA 170
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQ-YID-LSGGELQRVAIAAALLRNATFYLFDEPS 99
|
....
gi 686428090 171 AGLD 174
Cdd:cd03222 100 AYLD 103
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
143-177 |
1.55e-03 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 38.14 E-value: 1.55e-03
10 20 30
....*....|....*....|....*....|....*
gi 686428090 143 LSTGEKQRVMIARALMGQPQVLILDEPAAGLDFIA 177
Cdd:PRK10418 141 MSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVA 175
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
143-174 |
1.66e-03 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 38.29 E-value: 1.66e-03
10 20 30
....*....|....*....|....*....|..
gi 686428090 143 LSTGEKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:PRK11650 135 LSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| Arf_Arl |
cd00878 |
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ... |
32-76 |
1.69e-03 |
|
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl (Arf-like) small GTPases. Arf proteins are activators of phospholipase D isoforms. Unlike Ras proteins they lack cysteine residues at their C-termini and therefore are unlikely to be prenylated. Arfs are N-terminally myristoylated. Members of the Arf family are regulators of vesicle formation in intracellular traffic that interact reversibly with membranes of the secretory and endocytic compartments in a GTP-dependent manner. They depart from other small GTP-binding proteins by a unique structural device, interswitch toggle, that implements front-back communication from N-terminus to the nucleotide binding site. Arf-like (Arl) proteins are close relatives of the Arf, but only Arl1 has been shown to function in membrane traffic like the Arf proteins. Arl2 has an unrelated function in the folding of native tubulin, and Arl4 may function in the nucleus. Most other Arf family proteins are so far relatively poorly characterized. Thus, despite their significant sequence homologies, Arf family proteins may regulate unrelated functions.
Pssm-ID: 206644 [Multi-domain] Cd Length: 158 Bit Score: 37.56 E-value: 1.69e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 686428090 32 ILYGLNGAGKTTLLNILNAYEPATTgsvnlfgkMPgKVGYSAETV 76
Cdd:cd00878 3 LMLGLDGAGKTTILYKLKLGEVVTT--------IP-TIGFNVETV 38
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
138-176 |
1.74e-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: 1.74e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 686428090 138 QYIGYLSTGEKQRVMIARALMGQPQ--VLILDEPAAGLDFI 176
Cdd:cd03238 83 QKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQ 123
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
14-174 |
2.02e-03 |
|
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: 37.70 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 14 GKTILKNISWQINGGDKWILYGLNGAGKTTLLNILNAYEPATTGSVNLFGKMPGKVGYSAETVRQHiGFVSHSLLEKFQE 93
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNR-YSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686428090 94 GERVIDVVISGAFKSIGVYQDIDDEVRNEAH-QLLKLVGMSAKAQQYIGyLSTGEKQRVMIARALMGQPQVLILDEPAAG 172
Cdd:cd03290 92 NATVEENITFGSPFNKQRYKAVTDACSLQPDiDLLPFGDQTEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSA 170
|
..
gi 686428090 173 LD 174
Cdd:cd03290 171 LD 172
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
143-174 |
2.49e-03 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 38.15 E-value: 2.49e-03
10 20 30
....*....|....*....|....*....|..
gi 686428090 143 LSTGEKQRVMIARALMGQPQVLILDEPAAGLD 174
Cdd:PRK10789 452 LSGGQKQRISIARALLLNAEILILDDALSAVD 483
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
144-177 |
8.84e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 36.38 E-value: 8.84e-03
10 20 30
....*....|....*....|....*....|....
gi 686428090 144 STGEKQRVMIARALMGQPQVLILDEPAAGLDFIA 177
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHA 379
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|
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