|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
15-206 |
1.90e-54 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 173.31 E-value: 1.90e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 15 TILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKISfsNYNSTQ--ELRRLYFGYIFQDS-LIN 91
Cdd:COG1136 22 TALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIS--SLSERElaRLRRRHIGFVFQFFnLLP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 92 ERqDLIRNILCSVDYS--LQNNRRHLVNHFLSVVGLSSRTES-ASVLSGGEKQRLALARALIKKPKILLADEPTASLDRE 168
Cdd:COG1136 100 EL-TALENVALPLLLAgvSRKERRERARELLERVGLGDRLDHrPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSK 178
|
170 180 190
....*....|....*....|....*....|....*....
gi 1372031259 169 NKEKIMDIFKKFTNEGG-TVVMVTHDLELIDEKIQVIRL 206
Cdd:COG1136 179 TGEEVLELLRELNRELGtTIVMVTHDPELAARADRVIRL 217
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
8-206 |
1.05e-51 |
|
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: 165.48 E-value: 1.05e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 8 KKEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKISFSNYNSTQELRRLYFGYIFQD 87
Cdd:TIGR03608 5 SKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREKLGYLFQN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 88 SLINERQDLIRNILCSVDYSLQN--NRRHLVNHFLSVVGLSSRTES-ASVLSGGEKQRLALARALIKKPKILLADEPTAS 164
Cdd:TIGR03608 85 FALIENETVEENLDLGLKYKKLSkkEKREKKKEALEKVGLNLKLKQkIYELSGGEQQRVALARAILKPPPLILADEPTGS 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1372031259 165 LDRENKEKIMDIFKKFTNEGGTVVMVTHDLELIDEKIQVIRL 206
Cdd:TIGR03608 165 LDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAKQADRVIEL 206
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
14-206 |
1.36e-50 |
|
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: 163.04 E-value: 1.36e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 14 KTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKISFSNYNSTQELRRLYFGYIFQDSLINER 93
Cdd:cd03255 17 VQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFRRRHIGFVFQSFNLLPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 94 QDLIRNIL--CSVDYSLQNNRRHLVNHFLSVVGLSSR-TESASVLSGGEKQRLALARALIKKPKILLADEPTASLDRENK 170
Cdd:cd03255 97 LTALENVElpLLLAGVPKKERRERAEELLERVGLGDRlNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETG 176
|
170 180 190
....*....|....*....|....*....|....*..
gi 1372031259 171 EKIMDIFKKFTNEGG-TVVMVTHDLELIDEKIQVIRL 206
Cdd:cd03255 177 KEVMELLRELNKEAGtTIVVVTHDPELAEYADRIIEL 213
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-208 |
1.82e-47 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 155.21 E-value: 1.82e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 1 MISLY-INKKEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLD----GdfdgnyifydkKISFSNYNSTQ- 74
Cdd:COG2884 1 MIRFEnVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEErptsG-----------QVLVNGQDLSRl 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 75 ------ELRRlYFGYIFQD-SLINERqdlirNILCSVDYSLQ------NNRRHLVNHFLSVVGLSSRTES-ASVLSGGEK 140
Cdd:COG2884 70 krreipYLRR-RIGVVFQDfRLLPDR-----TVYENVALPLRvtgksrKEIRRRVREVLDLVGLSDKAKAlPHELSGGEQ 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1372031259 141 QRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLELIDE-KIQVIRLNN 208
Cdd:COG2884 144 QRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRmPKRVLELED 212
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
10-209 |
7.05e-45 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 148.04 E-value: 7.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 10 EFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNyIFYDKKiSFSNYNSTqELRRLyFGYIFQDSL 89
Cdd:COG4619 9 RVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGE-IYLDGK-PLSAMPPP-EWRRQ-VAYVPQEPA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 90 INErqDLIRNILcSVDYSLQNNR--RHLVNHFLSVVGLSSRTESASV--LSGGEKQRLALARALIKKPKILLADEPTASL 165
Cdd:COG4619 85 LWG--GTVRDNL-PFPFQLRERKfdRERALELLERLGLPPDILDKPVerLSGGERQRLALIRALLLQPDVLLLDEPTSAL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1372031259 166 DRENKEKIMDIFKKF-TNEGGTVVMVTHDLELIDEKI-QVIRLNNH 209
Cdd:COG4619 162 DPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVAdRVLTLEAG 207
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
12-209 |
3.59e-41 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 138.75 E-value: 3.59e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 12 RDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKIsfsNYNSTQELRRlYFGYIFQDSlin 91
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDL---TKLSLKELRR-KVGLVFQNP--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 92 ERQDLIRNILCSVDYSLQNN------RRHLVNHFLSVVGLSS-RTESASVLSGGEKQRLALARALIKKPKILLADEPTAS 164
Cdd:cd03225 85 DDQFFGPTVEEEVAFGLENLglpeeeIEERVEEALELVGLEGlRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAG 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1372031259 165 LDRENKEKIMDIFKKFTNEGGTVVMVTHDLELIDEKI-QVIRLNNH 209
Cdd:cd03225 165 LDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELAdRVIVLEDG 210
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
13-209 |
7.93e-40 |
|
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: 135.92 E-value: 7.93e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 13 DKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLDGDfDGNYIFYDKKISFSNynsTQELRRLyFGYIFQDS--- 88
Cdd:COG1122 13 GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLnGLLKPT-SGEVLVDGKDITKKN---LRELRRK-VGLVFQNPddq 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 89 LINE--RQDlirnilcsVDYSLQN------NRRHLVNHFLSVVGLSS-RTESASVLSGGEKQRLALARALIKKPKILLAD 159
Cdd:COG1122 88 LFAPtvEED--------VAFGPENlglpreEIRERVEEALELVGLEHlADRPPHELSGGQKQRVAIAGVLAMEPEVLVLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1372031259 160 EPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLELIDEKI-QVIRLNNH 209
Cdd:COG1122 160 EPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELAdRVIVLDDG 210
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
16-198 |
1.32e-39 |
|
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: 134.68 E-value: 1.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 16 ILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKISFSNYNSTQELRRlYFGYIFQDSLINERQD 95
Cdd:TIGR02673 17 ALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLRR-RIGVVFQDFRLLPDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 96 LIRNILCS--VDYSLQNNRRHLVNHFLSVVGLSSRTES-ASVLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEK 172
Cdd:TIGR02673 96 VYENVALPleVRGKKEREIQRRVGAALRQVGLEHKADAfPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLDPDLSER 175
|
170 180
....*....|....*....|....*.
gi 1372031259 173 IMDIFKKFTNEGGTVVMVTHDLELID 198
Cdd:TIGR02673 176 ILDLLKRLNKRGTTVIVATHDLSLVD 201
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
13-197 |
4.38e-38 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 131.54 E-value: 4.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 13 DKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLDGDfDGNYIFYDKKISFSNYNSTQELRRlYFGYIFQDSLIN 91
Cdd:cd03256 13 GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLnGLVEPT-SGSVLIDGTDINKLKGKALRQLRR-QIGMIFQQFNLI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 92 ERQDLIRNILCS-VDYSlqNNRRHLVNHF-----------LSVVGLSSRTES-ASVLSGGEKQRLALARALIKKPKILLA 158
Cdd:cd03256 91 ERLSVLENVLSGrLGRR--STWRSLFGLFpkeekqralaaLERVGLLDKAYQrADQLSGGQQQRVAIARALMQQPKLILA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1372031259 159 DEPTASLDRENKEKIMDIFKKFTNEGG-TVVMVTHDLELI 197
Cdd:cd03256 169 DEPVASLDPASSRQVMDLLKRINREEGiTVIVSLHQVDLA 208
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
1-195 |
7.43e-37 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 127.91 E-value: 7.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 1 MISLYINKKEFRDKTI----LSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKISFSNYNSTQEL 76
Cdd:NF038007 1 MLNMQNAEKCYITKTIktkvLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 77 RRLYFGYIFQDSLINERQDLIRNILCSVDYS--LQNNRRHLVNHFLSVVGLSSRTESASV-LSGGEKQRLALARALIKKP 153
Cdd:NF038007 81 RRELIGYIFQSFNLIPHLSIFDNVALPLKYRgvAKKERIERVNQVLNLFGIDNRRNHKPMqLSGGQQQRVAIARAMVSNP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1372031259 154 KILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLE 195
Cdd:NF038007 161 ALLLADEPTGNLDSKNARAVLQQLKYINQKGTTIIMVTHSDE 202
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
17-208 |
3.59e-36 |
|
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: 125.98 E-value: 3.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 17 LSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKISFSNYNSTQELRRlYFGYIFQDSLINERQDL 96
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRR-KIGVVFQDFRLLPDRNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 97 IRNILCSVDYSLQNNR--RHLVNHFLSVVGLSSRTES-ASVLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKI 173
Cdd:cd03292 96 YENVAFALEVTGVPPReiRKRVPAALELVGLSHKHRAlPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEI 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 1372031259 174 MDIFKKFTNEGGTVVMVTHDLELIDE-KIQVIRLNN 208
Cdd:cd03292 176 MNLLKKINKAGTTVVVATHAKELVDTtRHRVIALER 211
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
9-208 |
4.88e-36 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 123.89 E-value: 4.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 9 KEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKISfsnyNSTQELRRLYFGYIFQds 88
Cdd:cd00267 7 FRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIA----KLPLEELRRRIGYVPQ-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 89 linerqdlirnilcsvdyslqnnrrhlvnhflsvvglssrtesasvLSGGEKQRLALARALIKKPKILLADEPTASLDRE 168
Cdd:cd00267 81 ----------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA 114
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1372031259 169 NKEKIMDIFKKFTNEGGTVVMVTHDLELIDEKIQ-VIRLNN 208
Cdd:cd00267 115 SRERLLELLRELAEEGRTVIIVTHDPELAELAADrVIVLKD 155
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
11-209 |
1.49e-35 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 125.20 E-value: 1.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 11 FRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLL---DGdfdgnyifydkKISFSNYNSTQELRRLyfGYIFQ 86
Cdd:COG1121 16 YGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAIlGLLpptSG-----------TVRLFGKPPRRARRRI--GYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 87 DSLINER-----QDLI-------RNILCSvdysLQNNRRHLVNHFLSVVGLSS-RTESASVLSGGEKQRLALARALIKKP 153
Cdd:COG1121 83 RAEVDWDfpitvRDVVlmgrygrRGLFRR----PSRADREAVDEALERVGLEDlADRPIGELSGGQQQRVLLARALAQDP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1372031259 154 KILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLELIDEKI-QVIRLNNH 209
Cdd:COG1121 159 DLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFdRVLLLNRG 215
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
12-208 |
5.43e-35 |
|
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: 121.72 E-value: 5.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 12 RDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLDGDfDGNYIFYDKKISFSNynsTQELRRLyFGYIFQDSLI 90
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLlRLYDPT-SGEILIDGVDLRDLD---LESLRKN-IAYVPQDPFL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 91 nerqdlirnilcsVDYSLQNNrrhlvnhflsvvglssrtesasVLSGGEKQRLALARALIKKPKILLADEPTASLDRENK 170
Cdd:cd03228 88 -------------FSGTIREN----------------------ILSGGQRQRIAIARALLRDPPILILDEATSALDPETE 132
|
170 180 190
....*....|....*....|....*....|....*...
gi 1372031259 171 EKIMDIFKKFTnEGGTVVMVTHDLELIDEKIQVIRLNN 208
Cdd:cd03228 133 ALILEALRALA-KGKTVIVIAHRLSTIRDADRIIVLDD 169
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
9-209 |
1.08e-34 |
|
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: 121.82 E-value: 1.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 9 KEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLDgDFDGNyIFYDKKisfsNYNSTQELRRLYFGYIFQD 87
Cdd:COG4133 10 CRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILaGLLP-PSAGE-VLWNGE----PIRDAREDYRRRLAYLGHA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 88 SLINERQDLIRNILCSVDYSLQNNRRHLVNHFLSVVGLSSRTES-ASVLSGGEKQRLALARALIKKPKILLADEPTASLD 166
Cdd:COG4133 84 DGLKPELTVRENLRFWAALYGLRADREAIDEALEAVGLAGLADLpVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1372031259 167 RENKEKIMDIFKKFTNEGGTVVMVTHDLELIDEkIQVIRLNNH 209
Cdd:COG4133 164 AAGVALLAELIAAHLARGGAVLLTTHQPLELAA-ARVLDLGDF 205
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
12-198 |
2.13e-33 |
|
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: 119.91 E-value: 2.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 12 RDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKISFSNynsTQELRRLyFGYIFQDSL-- 89
Cdd:COG1124 16 RRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRR---RKAFRRR-VQMVFQDPYas 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 90 INERQdlirnilcSVDYSL--------QNNRRHLVNHFLSVVGLSS--RTESASVLSGGEKQRLALARALIKKPKILLAD 159
Cdd:COG1124 92 LHPRH--------TVDRILaeplrihgLPDREERIAELLEQVGLPPsfLDRYPHQLSGGQRQRVAIARALILEPELLLLD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1372031259 160 EPTASLDRENKEKIMDIFKKFTNEGG-TVVMVTHDLELID 198
Cdd:COG1124 164 EPTSALDVSVQAEILNLLKDLREERGlTYLFVSHDLAVVA 203
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
9-206 |
4.66e-33 |
|
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: 118.44 E-value: 4.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 9 KEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLDGDF----DGNYIFYDKKISFSNYNSTqELRRlYFGY 83
Cdd:cd03260 8 VYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnRLNDLIPgapdEGEVLLDGKDIYDLDVDVL-ELRR-RVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 84 IFQdslineRQDLIR-NILCSVDYSLQ----NNRRHL---VNHFLSVVGLS---SRTESASVLSGGEKQRLALARALIKK 152
Cdd:cd03260 86 VFQ------KPNPFPgSIYDNVAYGLRlhgiKLKEELderVEEALRKAALWdevKDRLHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1372031259 153 PKILLADEPTASLDRENKEKIMDIFKKFTNEgGTVVMVTHDLElidekiQVIRL 206
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQ------QAARV 206
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
13-195 |
6.17e-33 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 119.04 E-value: 6.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 13 DKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKIsfsnynsTQELRRLyfGYIFQDSLine 92
Cdd:COG1116 23 GVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV-------TGPGPDR--GVVFQEPA--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 93 rqdL------IRNILcsvdYSLQNN------RRHLVNHFLSVVGLSSRtESA--SVLSGGEKQRLALARALIKKPKILLA 158
Cdd:COG1116 91 ---LlpwltvLDNVA----LGLELRgvpkaeRRERARELLELVGLAGF-EDAypHQLSGGMRQRVAIARALANDPEVLLM 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1372031259 159 DEPTASLD---REN-KEKIMDIFKKftnEGGTVVMVTHDLE 195
Cdd:COG1116 163 DEPFGALDaltRERlQDELLRLWQE---TGKTVLFVTHDVD 200
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
12-199 |
7.14e-33 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 123.47 E-value: 7.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 12 RDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLDGDfDGNYIFYDKKISFSNYNSTQELRRlYFGYIFQD--S 88
Cdd:COG1123 276 GGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLlGLLRPT-SGSILFDGKDLTKLSRRSLRELRR-RVQMVFQDpyS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 89 LINERQdlirNILCSVDYSLQNN-------RRHLVNHFLSVVGLSSRTESASV--LSGGEKQRLALARALIKKPKILLAD 159
Cdd:COG1123 354 SLNPRM----TVGDIIAEPLRLHgllsraeRRERVAELLERVGLPPDLADRYPheLSGGQRQRVAIARALALEPKLLILD 429
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1372031259 160 EPTASLDRENKEKIMDIFKKFTNEGG-TVVMVTHDLELIDE 199
Cdd:COG1123 430 EPTSALDVSVQAQILNLLRDLQRELGlTYLFISHDLAVVRY 470
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
8-199 |
1.12e-32 |
|
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: 117.22 E-value: 1.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 8 KKEFRDK----TILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLDGDfDGNYIFYDKKISfSNYNSTQELRRLYFG 82
Cdd:cd03257 8 SVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAIlGLLKPT-SGSIIFDGKDLL-KLSRRLRKIRRKEIQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 83 YIFQDSL--IN-----ERQ--DLIRNILCSVDYSLQNNRRHLVnhfLSVVGLSSRTESA--SVLSGGEKQRLALARALIK 151
Cdd:cd03257 86 MVFQDPMssLNprmtiGEQiaEPLRIHGKLSKKEARKEAVLLL---LVGVGLPEEVLNRypHELSGGQRQRVAIARALAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1372031259 152 KPKILLADEPTASLDRENKEKIMDIFKKFTNEGG-TVVMVTHDLELIDE 199
Cdd:cd03257 163 NPKLLIADEPTSALDVSVQAQILDLLKKLQEELGlTLLFITHDLGVVAK 211
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
13-209 |
2.75e-32 |
|
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: 122.17 E-value: 2.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 13 DKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLDGD-----FDGnyifydkkISFSNYNSTQELRRL-YFG--- 82
Cdd:COG4988 349 GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLlGFLPPYsgsilING--------VDLSDLDPASWRRQIaWVPqnp 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 83 YIFQDSLINerqdlirNI-LCSVDYS----LQNNRRHLVNHFLSVV--GLSSR-TESASVLSGGEKQRLALARALIKKPK 154
Cdd:COG4988 421 YLFAGTIRE-------NLrLGRPDASdeelEAALEAAGLDEFVAALpdGLDTPlGEGGRGLSGGQAQRLALARALLRDAP 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1372031259 155 ILLADEPTASLDRENKEKIMDIFKKFTnEGGTVVMVTHDLELIDEKIQVIRLNNH 209
Cdd:COG4988 494 LLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLAQADRILVLDDG 547
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
11-209 |
4.03e-32 |
|
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: 115.32 E-value: 4.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 11 FRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLN-IIGLLDGDFdgNYIFYDKKisfsnynsTQELRRLYFGYIFQDSL 89
Cdd:cd03235 9 YGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKaILGLLKPTS--GSIRVFGK--------PLEKERKRIGYVPQRRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 90 IN-ERQDLIRNILCSVDYS-------LQNNRRHLVNHFLSVVGLSS-RTESASVLSGGEKQRLALARALIKKPKILLADE 160
Cdd:cd03235 79 IDrDFPISVRDVVLMGLYGhkglfrrLSKADKAKVDEALERVGLSElADRQIGELSGGQQQRVLLARALVQDPDLLLLDE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1372031259 161 PTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLELIDEKI-QVIRLNNH 209
Cdd:cd03235 159 PFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFdRVLLLNRT 208
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
12-208 |
8.31e-32 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 114.50 E-value: 8.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 12 RDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLN-IIGLLDGDF--DGNYIFYDKKISFSNynstQELRRLyfGYIFQDS 88
Cdd:COG4136 12 GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSPAFsaSGEVLLNGRRLTALP----AEQRRI--GILFQDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 89 LINERQDLIRNILCSVDYSLQ-NNRRHLVNHFLSVVGLSSRTES--ASvLSGGEKQRLALARALIKKPKILLADEPTASL 165
Cdd:COG4136 86 LLFPHLSVGENLAFALPPTIGrAQRRARVEQALEEAGLAGFADRdpAT-LSGGQRARVALLRALLAEPRALLLDEPFSKL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1372031259 166 DRENKEKIMD-IFKKFTNEGGTVVMVTHDLELIDEKIQVIRLNN 208
Cdd:COG4136 165 DAALRAQFREfVFEQIRQRGIPALLVTHDEEDAPAAGRVLDLGN 208
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
14-195 |
2.61e-31 |
|
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: 113.72 E-value: 2.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 14 KTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNyifydkkISFSNYNSTQELRRLyfGYIFQDSLiner 93
Cdd:cd03293 17 VTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGE-------VLVDGEPVTGPGPDR--GYVFQQDA---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 94 qdLI--RNILCSVDYSLQNN------RRHLVNHFLSVVGLSSrTESA--SVLSGGEKQRLALARALIKKPKILLADEPTA 163
Cdd:cd03293 84 --LLpwLTVLDNVALGLELQgvpkaeARERAEELLELVGLSG-FENAypHQLSGGMRQRVALARALAVDPDVLLLDEPFS 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 1372031259 164 SLD---REN-KEKIMDIFKKftnEGGTVVMVTHDLE 195
Cdd:cd03293 161 ALDaltREQlQEELLDIWRE---TGKTVLLVTHDID 193
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
9-197 |
2.61e-31 |
|
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: 112.28 E-value: 2.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 9 KEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKISFSNYNSTQELRRLyfGYIFQDS 88
Cdd:cd03229 8 KRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRI--GMVFQDF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 89 LINERQDLIRNIlcsvdyslqnnrrhlvnhflsvvglssrtesASVLSGGEKQRLALARALIKKPKILLADEPTASLDRE 168
Cdd:cd03229 86 ALFPHLTVLENI-------------------------------ALGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPI 134
|
170 180 190
....*....|....*....|....*....|
gi 1372031259 169 NKEKIMDIFKK-FTNEGGTVVMVTHDLELI 197
Cdd:cd03229 135 TRREVRALLKSlQAQLGITVVLVTHDLDEA 164
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
15-206 |
5.87e-31 |
|
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: 112.91 E-value: 5.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 15 TILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLD----GD--FDGNyifydkkiSFSNYNSTQ--ELRRLYFGYIFQ 86
Cdd:COG4181 26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDrptsGTvrLAGQ--------DLFALDEDAraRLRARHVGFVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 87 DSLinerqdLIRNiLCSVDY-----SLQNNR--RHLVNHFLSVVGLSSRTESA-SVLSGGEKQRLALARALIKKPKILLA 158
Cdd:COG4181 98 SFQ------LLPT-LTALENvmlplELAGRRdaRARARALLERVGLGHRLDHYpAQLSGGEQQRVALARAFATEPAILFA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1372031259 159 DEPTASLDRENKEKIMD-IFKKFTNEGGTVVMVTHDLELIDEKIQVIRL 206
Cdd:COG4181 171 DEPTGNLDAATGEQIIDlLFELNRERGTTLVLVTHDPALAARCDRVLRL 219
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-197 |
6.02e-31 |
|
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: 113.06 E-value: 6.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 1 MISLYINKKEFRDK----TILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKISFSNYNSTQEL 76
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 77 RRlYFGYIFQD-SLINERqdlirNILCSVDYSLQ------NNRRHLVNHFLSVVGLSSRTES-ASVLSGGEKQRLALARA 148
Cdd:cd03258 81 RR-RIGMIFQHfNLLSSR-----TVFENVALPLEiagvpkAEIEERVLELLELVGLEDKADAyPAQLSGGQKQRVGIARA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1372031259 149 LIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGG-TVVMVTHDLELI 197
Cdd:cd03258 155 LANNPKVLLCDEATSALDPETTQSILALLRDINRELGlTIVLITHEMEVV 204
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
11-196 |
8.09e-31 |
|
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: 113.21 E-value: 8.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 11 FRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLDGDfDGNyIFYDKKiSFSNYnSTQELRRLyFGYIFQDSL 89
Cdd:COG1120 11 YGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALaGLLKPS-SGE-VLLDGR-DLASL-SRRELARR-IAYVPQEPP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 90 INER---QDLI---RNILCSVDYSLQNNRRHLVNHFLSVVGLSS-RTESASVLSGGEKQRLALARALIKKPKILLADEPT 162
Cdd:COG1120 86 APFGltvRELValgRYPHLGLFGRPSAEDREAVEEALERTGLEHlADRPVDELSGGERQRVLIARALAQEPPLLLLDEPT 165
|
170 180 190
....*....|....*....|....*....|....*
gi 1372031259 163 ASLDRENKEKIMDIFKKFTNEGG-TVVMVTHDLEL 196
Cdd:COG1120 166 SHLDLAHQLEVLELLRRLARERGrTVVMVLHDLNL 200
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
16-193 |
1.03e-29 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 115.21 E-value: 1.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 16 ILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKISFSNYNSTQELRRLYFGYIFQDSLINERQD 95
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRREHFGFIFQRYHLLSHLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 96 LIRNILCSVDY--SLQNNRRHLVNHFLSVVGLSSRTE-SASVLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEK 172
Cdd:PRK10535 103 AAQNVEVPAVYagLERKQRLLRAQELLQRLGLEDRVEyQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEE 182
|
170 180
....*....|....*....|.
gi 1372031259 173 IMDIFKKFTNEGGTVVMVTHD 193
Cdd:PRK10535 183 VMAILHQLRDRGHTVIIVTHD 203
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
11-196 |
1.58e-29 |
|
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: 107.91 E-value: 1.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 11 FRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLDgdFDGNYIFYDKKiSFSNYnSTQELRRLyFGYIFQdsl 89
Cdd:cd03214 9 YGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLaGLLK--PSSGEILLDGK-DLASL-SPKELARK-IAYVPQ--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 90 inerqdlirnilcsvdyslqnnrrhlvnhFLSVVGLSS-RTESASVLSGGEKQRLALARALIKKPKILLADEPTASLDRE 168
Cdd:cd03214 81 -----------------------------ALELLGLAHlADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIA 131
|
170 180
....*....|....*....|....*....
gi 1372031259 169 NKEKIMDIFKKFTNEGG-TVVMVTHDLEL 196
Cdd:cd03214 132 HQIELLELLRRLARERGkTVVMVLHDLNL 160
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
9-205 |
2.90e-29 |
|
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: 107.99 E-value: 2.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 9 KEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLDGDfDGnyifydkKISFSNYNSTQ---ELRRLyfGYI 84
Cdd:cd03259 8 KTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIaGLERPD-SG-------EILIDGRDVTGvppERRNI--GMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 85 FQDSLINERQDLIRNILcsvdYSLQN------NRRHLVNHFLSVVGLSS-RTESASVLSGGEKQRLALARALIKKPKILL 157
Cdd:cd03259 78 FQDYALFPHLTVAENIA----FGLKLrgvpkaEIRARVRELLELVGLEGlLNRYPHELSGGQQQRVALARALAREPSLLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1372031259 158 ADEPTASLDRENKEKIMDIFKKFTNEGG-TVVMVTHDLE---LIDEKIQVIR 205
Cdd:cd03259 154 LDEPLSALDAKLREELREELKELQRELGiTTIYVTHDQEealALADRIAVMN 205
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
12-197 |
3.27e-29 |
|
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: 113.78 E-value: 3.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 12 RDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLDgDFDGNyIFYDKkISFSNYNsTQELRRlYFGYIFQDSLI 90
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLlGLYE-PTSGR-ILIDG-IDLRQID-PASLRR-QIGVVLQDVFL 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 91 NERqDLIRNI-LCSVDYSLQNnrrhlVNHFLSVVGLSSR------------TESASVLSGGEKQRLALARALIKKPKILL 157
Cdd:COG2274 561 FSG-TIRENItLGDPDATDEE-----IIEAARLAGLHDFiealpmgydtvvGEGGSNLSGGQRQRLAIARALLRNPRILI 634
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1372031259 158 ADEPTASLDRENKEKIMDIFKKFTNeGGTVVMVTHDLELI 197
Cdd:COG2274 635 LDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTI 673
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
8-197 |
2.16e-28 |
|
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: 106.60 E-value: 2.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 8 KKEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLL-NIIGLLDGDfDGNYIFYDKKISFSNYNSTQELRRlYFGYIFQ 86
Cdd:COG1127 12 TKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLkLIIGLLRPD-SGEILVDGQDITGLSEKELYELRR-RIGMLFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 87 -----DSL---------INERQDLIRNIlcsvdyslqnnRRHLVNHFLSVVGLSsrtESA----SVLSGGEKQRLALARA 148
Cdd:COG1127 90 ggalfDSLtvfenvafpLREHTDLSEAE-----------IRELVLEKLELVGLP---GAAdkmpSELSGGMRKRVALARA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1372031259 149 LIKKPKILLADEPTASLDRENKEKIMDIFKKFTNE-GGTVVMVTHDLELI 197
Cdd:COG1127 156 LALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSA 205
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
9-199 |
2.72e-28 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 106.30 E-value: 2.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 9 KEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLDGDfDGNYIFYDKKISfsnyNSTQELRRLyFGYIFQD 87
Cdd:COG1131 8 KRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLlGLLRPT-SGEVRVLGEDVA----RDPAEVRRR-IGYVPQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 88 SLINERQDLIRNI-----LCSVDYSLQNNRrhlVNHFLSVVGLSSRTES-ASVLSGGEKQRLALARALIKKPKILLADEP 161
Cdd:COG1131 82 PALYPDLTVRENLrffarLYGLPRKEARER---IDELLELFGLTDAADRkVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 1372031259 162 TASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLELIDE 199
Cdd:COG1131 159 TSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAER 196
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
9-195 |
2.73e-28 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 108.65 E-value: 2.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 9 KEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLDGDfDGNYIFYDKKISfsnyNSTQELRRlyFGYIFQD 87
Cdd:COG3842 13 KRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIaGFETPD-SGRILLDGRDVT----GLPPEKRN--VGMVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 88 slinerqdlirnilcsvdYSL-------QN-------------NRRHLVNHFLSVVGLSSRTE-SASVLSGGEKQRLALA 146
Cdd:COG3842 86 ------------------YALfphltvaENvafglrmrgvpkaEIRARVAELLELVGLEGLADrYPHQLSGGQQQRVALA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1372031259 147 RALIKKPKILLADEPTASLDRENKEK----IMDIFKKFtneGGTVVMVTHDLE 195
Cdd:COG3842 148 RALAPEPRVLLLDEPLSALDAKLREEmreeLRRLQREL---GITFIYVTHDQE 197
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
9-195 |
9.88e-28 |
|
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: 104.51 E-value: 9.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 9 KEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLL-NIIGLLDGD-----FDGNYIFYDKKISFsnynstQELRRLyFG 82
Cdd:cd03261 8 KSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLrLIVGLLRPDsgevlIDGEDISGLSEAEL------YRLRRR-MG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 83 YIFQ-----DSL---------INERQDLIRNILcsvdyslqnnrRHLVNHFLSVVGLSSRTES-ASVLSGGEKQRLALAR 147
Cdd:cd03261 81 MLFQsgalfDSLtvfenvafpLREHTRLSEEEI-----------REIVLEKLEAVGLRGAEDLyPAELSGGMKKRVALAR 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1372031259 148 ALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNE-GGTVVMVTHDLE 195
Cdd:cd03261 150 ALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLD 198
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
16-196 |
2.04e-27 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 103.74 E-value: 2.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 16 ILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKISFSNYNSTQELRRLYFGYIFQ-DSLI---N 91
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQfHHLLpdfT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 92 ERQDLIRNILCSVDYSLQNNRRHLvnHFLSVVGLSSRTE-SASVLSGGEKQRLALARALIKKPKILLADEPTASLDRENK 170
Cdd:PRK11629 104 ALENVAMPLLIGKKKPAEINSRAL--EMLAAVGLEHRANhRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNA 181
|
170 180
....*....|....*....|....*..
gi 1372031259 171 EKIMDIFKKFTNEGGTV-VMVTHDLEL 196
Cdd:PRK11629 182 DSIFQLLGELNRLQGTAfLVVTHDLQL 208
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
32-208 |
2.31e-27 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 103.42 E-value: 2.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 32 ITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKISFSNYNSTQELRRlYFGYIFQDS-LINERQ--DLIRNILCSVDYSL 108
Cdd:PRK10908 33 LTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRR-QIGMIFQDHhLLMDRTvyDNVAIPLIIAGASG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 109 QNNRRHlVNHFLSVVGLSSRTESASV-LSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGTV 187
Cdd:PRK10908 112 DDIRRR-VSAALDKVGLLDKAKNFPIqLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTV 190
|
170 180
....*....|....*....|..
gi 1372031259 188 VMVTHDLELIDEK-IQVIRLNN 208
Cdd:PRK10908 191 LMATHDIGLISRRsYRMLTLSD 212
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
8-194 |
3.00e-27 |
|
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: 102.99 E-value: 3.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 8 KKEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKISFSNYNSTqELRRlYFGYIFQD 87
Cdd:cd03262 7 HKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNIN-ELRQ-KVGMVFQQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 88 SLINERQDLIRNILCSVDYSLQNNRRHLVNH---FLSVVGLSSR-TESASVLSGGEKQRLALARALIKKPKILLADEPTA 163
Cdd:cd03262 85 FNLFPHLTVLENITLAPIKVKGMSKAEAEERaleLLEKVGLADKaDAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTS 164
|
170 180 190
....*....|....*....|....*....|.
gi 1372031259 164 SLDRENKEKIMDIFKKFTNEGGTVVMVTHDL 194
Cdd:cd03262 165 ALDPELVGEVLDVMKDLAEEGMTMVVVTHEM 195
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
9-195 |
5.85e-27 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 102.86 E-value: 5.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 9 KEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLL----DGDF--DGnyifydkkISFSNYNSTQELRRLYFG 82
Cdd:PRK09493 9 KHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLeeitSGDLivDG--------LKVNDPKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 83 YIFQDSLINERQDLIRNIL---CSVDYSLQNNRRHLVNHFLSVVGLSSRTES-ASVLSGGEKQRLALARALIKKPKILLA 158
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMfgpLRVRGASKEEAEKQARELLAKVGLAERAHHyPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 1372031259 159 DEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLE 195
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIG 197
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
9-208 |
1.62e-26 |
|
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: 99.78 E-value: 1.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 9 KEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLDGDfDGNyIFYDKKisfsNYNSTQELRRLYFGYIFQD 87
Cdd:cd03230 8 KRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIIlGLLKPD-SGE-IKVLGK----DIKKEPEEVKRRIGYLPEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 88 SLINERQDLIRNILcsvdyslqnnrrhlvnhflsvvglssrtesasvLSGGEKQRLALARALIKKPKILLADEPTASLDR 167
Cdd:cd03230 82 PSLYENLTVRENLK---------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDP 128
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1372031259 168 ENKEKIMDIFKKFTNEGGTVVMVTHDLELIdEKI--QVIRLNN 208
Cdd:cd03230 129 ESRREFWELLRELKKEGKTILLSSHILEEA-ERLcdRVAILNN 170
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-197 |
1.93e-26 |
|
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: 100.41 E-value: 1.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 6 INKKEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLDGdfdgnyifYDKKISFSNYNSTQELRRLYFGYI 84
Cdd:cd03226 5 ISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILaGLIKE--------SSGSILLNGKPIKAKERRKSIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 85 FQDSlinERQDLIRNILCSVDYSLQN--NRRHLVNHFLSVVGLSSRTES-ASVLSGGEKQRLALARALIKKPKILLADEP 161
Cdd:cd03226 77 MQDV---DYQLFTDSVREELLLGLKEldAGNEQAETVLKDLDLYALKERhPLSLSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
170 180 190
....*....|....*....|....*....|....*.
gi 1372031259 162 TASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLELI 197
Cdd:cd03226 154 TSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFL 189
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
13-208 |
1.96e-26 |
|
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: 105.62 E-value: 1.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 13 DKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLDGDfDGNYIFYDKKISfsNYnSTQELRRLyFGYIFQDS-LI 90
Cdd:COG4987 347 GRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLlRFLDPQ-SGSITLGGVDLR--DL-DEDDLRRR-IAVVPQRPhLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 91 NErqdlirnilcsvdySLQNNRRhLVN---------HFLSVVGLSS--RT----------ESASVLSGGEKQRLALARAL 149
Cdd:COG4987 422 DT--------------TLRENLR-LARpdatdeelwAALERVGLGDwlAAlpdgldtwlgEGGRRLSGGERRRLALARAL 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 150 IKKPKILLADEPTASLDRENKEKIM-DIFKkfTNEGGTVVMVTHDLELIDEKIQVIRLNN 208
Cdd:COG4987 487 LRDAPILLLDEPTEGLDAATEQALLaDLLE--ALAGRTVLLITHRLAGLERMDRILVLED 544
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
12-199 |
2.09e-26 |
|
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: 105.37 E-value: 2.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 12 RDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLN-IIGLLD--GDFDGNYIFYDKKISfsnyNSTQELRRLYFGYIFQD- 87
Cdd:COG1123 17 GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALaLMGLLPhgGRISGEVLLDGRDLL----ELSEALRGRRIGMVFQDp 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 88 -------SLINERQDLIRNILCSVDyslqnNRRHLVNHFLSVVGLSSRTESA-SVLSGGEKQRLALARALIKKPKILLAD 159
Cdd:COG1123 93 mtqlnpvTVGDQIAEALENLGLSRA-----EARARVLELLEAVGLERRLDRYpHQLSGGQRQRVAIAMALALDPDLLIAD 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1372031259 160 EPTASLDRENKEKIMDIFKKFTNEGG-TVVMVTHDLELIDE 199
Cdd:COG1123 168 EPTTALDVTTQAEILDLLRELQRERGtTVLLITHDLGVVAE 208
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
16-196 |
3.43e-26 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 100.86 E-value: 3.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 16 ILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKISFS---NYNSTQELRRlYFGYIFQDSLINE 92
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSqkpSEKAIRLLRQ-KVGMVFQQYNLWP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 93 RQDLIRNIL---CSVdysLQNNRRHLV---NHFLSVVGLSSRTESASV-LSGGEKQRLALARALIKKPKILLADEPTASL 165
Cdd:COG4161 96 HLTVMENLIeapCKV---LGLSKEQARekaMKLLARLRLTDKADRFPLhLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170 180 190
....*....|....*....|....*....|.
gi 1372031259 166 DRENKEKIMDIFKKFTNEGGTVVMVTHDLEL 196
Cdd:COG4161 173 DPEITAQVVEIIRELSQTGITQVIVTHEVEF 203
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
23-209 |
5.10e-26 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 102.49 E-value: 5.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 23 EIIEGGFYVITGPSGVGKSSLLNII-GLLDGDfDGnYIFYDKKISFSNYNSTQ---ELRRLyfGYIFQDSLINERQDLIR 98
Cdd:COG4148 21 TLPGRGVTALFGPSGSGKTTLLRAIaGLERPD-SG-RIRLGGEVLQDSARGIFlppHRRRI--GYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 99 NILCSVDYSLQNNRRHLVNHFLSVVGLS---SRTESAsvLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMD 175
Cdd:COG4148 97 NLLYGRKRAPRAERRISFDEVVELLGIGhllDRRPAT--LSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILP 174
|
170 180 190
....*....|....*....|....*....|....*
gi 1372031259 176 IFKKFTNEGGT-VVMVTHDLeliDEkiqVIRLNNH 209
Cdd:COG4148 175 YLERLRDELDIpILYVSHSL---DE---VARLADH 203
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
25-205 |
5.26e-26 |
|
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: 99.68 E-value: 5.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 25 IEGGFYVITGPSGVGKSSLLNIIGLLDgDFDGNYIFYDKKISFS---NYNSTQELRRLyfGYIFQDSLINERQDLIRNIL 101
Cdd:cd03297 21 LNEEVTGIFGASGAGKSTLLRCIAGLE-KPDGGTIVLNGTVLFDsrkKINLPPQQRKI--GLVFQQYALFPHLNVRENLA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 102 CSVDYSLQNNRRHLVNHFLSVVGLSSRTESASV-LSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKF 180
Cdd:cd03297 98 FGLKRKRNREDRISVDELLDLLGLDHLLNRYPAqLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQI 177
|
170 180
....*....|....*....|....*....
gi 1372031259 181 -TNEGGTVVMVTHDL---ELIDEKIQVIR 205
Cdd:cd03297 178 kKNLNIPVIFVTHDLseaEYLADRIVVME 206
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
3-195 |
9.98e-26 |
|
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: 99.33 E-value: 9.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 3 SLYINKKEFRdktiLSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLDGDfDGNYIFYDKKISfsnyNSTQELRRlyF 81
Cdd:cd03299 5 NLSKDWKEFK----LKNVSLEVERGDYFVILGPTGSGKSVLLETIaGFIKPD-SGKILLNGKDIT----NLPPEKRD--I 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 82 GYIFQDSLINERQDLIRNIlcsvDYSLQNNRR---------HLVNHFLSVVGLSSRteSASVLSGGEKQRLALARALIKK 152
Cdd:cd03299 74 SYVPQNYALFPHMTVYKNI----AYGLKKRKVdkkeierkvLEIAEMLGIDHLLNR--KPETLSGGEQQRVAIARALVVN 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1372031259 153 PKILLADEPTASLDRENKEKIMDIFKKFTNEGG-TVVMVTHDLE 195
Cdd:cd03299 148 PKILLLDEPFSALDVRTKEKLREELKKIRKEFGvTVLHVTHDFE 191
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
13-208 |
3.95e-25 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 96.13 E-value: 3.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 13 DKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GL---------LDGdfdgnyifydkkISFSNYNSTQelRRLYFG 82
Cdd:cd03246 14 EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLIlGLlrptsgrvrLDG------------ADISQWDPNE--LGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 83 YIFQDslinerqdlirnilcsvdyslqnnrrhlvnhflsvVGLSSRTESASVLSGGEKQRLALARALIKKPKILLADEPT 162
Cdd:cd03246 80 YLPQD-----------------------------------DELFSGSIAENILSGGQRQRLGLARALYGNPRILVLDEPN 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1372031259 163 ASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLELIDEKIQVIRLNN 208
Cdd:cd03246 125 SHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVLED 170
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
26-163 |
6.02e-25 |
|
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: 95.02 E-value: 6.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 26 EGGFYVITGPSGVGKSSLLNII-GLLDGDfdGNYIFYDKKiSFSNYNSTQELRRLyfGYIFQDSLINERQDLIRNI---- 100
Cdd:pfam00005 10 PGEILALVGPNGAGKSTLLKLIaGLLSPT--EGTILLDGQ-DLTDDERKSLRKEI--GYVFQDPQLFPRLTVRENLrlgl 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1372031259 101 -LCSVDYSLQNNRRHLVNHFLSVVGLSSRT--ESASVLSGGEKQRLALARALIKKPKILLADEPTA 163
Cdd:pfam00005 85 lLKGLSKREKDARAEEALEKLGLGDLADRPvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
16-196 |
6.05e-25 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 97.78 E-value: 6.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 16 ILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKISFSNYNSTQELRRLY--FGYIFQDsliner 93
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDKAIRELRrnVGMVFQQ------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 94 qdlirnilcsvdYSL-------QNnrrhLVNHFLSVVGLSSR---------------TESASV----LSGGEKQRLALAR 147
Cdd:PRK11124 91 ------------YNLwphltvqQN----LIEAPCRVLGLSKDqalaraekllerlrlKPYADRfplhLSGGQQQRVAIAR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1372031259 148 ALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLEL 196
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEV 203
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
34-196 |
6.75e-25 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 97.16 E-value: 6.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 34 GPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKISFSNYNSTQELRRLYFGYIFQDSLINERQDLIRNILCSVDYSLQNNR- 112
Cdd:PRK10584 43 GESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRq 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 113 -RHLVNHFLSVVGLSSRTES-ASVLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMD-IFKKFTNEGGTVVM 189
Cdd:PRK10584 123 sRNGAKALLEQLGLGKRLDHlPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADlLFSLNREHGTTLIL 202
|
....*..
gi 1372031259 190 VTHDLEL 196
Cdd:PRK10584 203 VTHDLQL 209
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
8-195 |
1.25e-24 |
|
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: 96.54 E-value: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 8 KKEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKISFSNYNSTQelrrlyFGYIFQD 87
Cdd:cd03300 7 SKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRP------VNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 88 SLINERQDLIRNI-----LCSVDYSLQNNRrhlVNHFLSVVGLSS-RTESASVLSGGEKQRLALARALIKKPKILLADEP 161
Cdd:cd03300 81 YALFPHLTVFENIafglrLKKLPKAEIKER---VAEALDLVQLEGyANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEP 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 1372031259 162 TASLD---REN-KEKIMDIFKKFtneGGTVVMVTHDLE 195
Cdd:cd03300 158 LGALDlklRKDmQLELKRLQKEL---GITFVFVTHDQE 192
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
4-209 |
1.42e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 96.32 E-value: 1.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 4 LYINKKEFR--DKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKISfsnyNSTQELRRLYF 81
Cdd:PRK10247 8 LQLQNVGYLagDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIS----TLKPEIYRQQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 82 GYIFQ----------DSLINERQdlIRNIlcsvdyslQNNRRHLVNhFLSVVGLSSRTESASV--LSGGEKQRLALARAL 149
Cdd:PRK10247 84 SYCAQtptlfgdtvyDNLIFPWQ--IRNQ--------QPDPAIFLD-DLERFALPDTILTKNIaeLSGGEKQRISLIRNL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1372031259 150 IKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVM-VTHDLELIDEKIQVIRLNNH 209
Cdd:PRK10247 153 QFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLwVTHDKDEINHADKVITLQPH 213
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-193 |
1.85e-24 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 96.67 E-value: 1.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 2 ISLYINK--KEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKISfsnynSTQELRRL 79
Cdd:PRK11247 11 TPLLLNAvsKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLA-----EAREDTRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 80 yfgyIFQDSLINERQDLIRNilcsVDYSLQNNRRHLVNHFLSVVGLSSR-TESASVLSGGEKQRLALARALIKKPKILLA 158
Cdd:PRK11247 86 ----MFQDARLLPWKKVIDN----VGLGLKGQWRDAALQALAAVGLADRaNEWPAALSGGQKQRVALARALIHRPGLLLL 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 1372031259 159 DEPTASLDRENKEKIMDIFKKFTNEGG-TVVMVTHD 193
Cdd:PRK11247 158 DEPLGALDALTRIEMQDLIESLWQQHGfTVLLVTHD 193
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
16-197 |
2.33e-24 |
|
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: 94.80 E-value: 2.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 16 ILSDTCIEIIEGGFYVITGPSGVGKSSLL-NIIGLLDGD-----FDGNYIFYDKKisfsnynSTQELRRlYFGYIFQDSl 89
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLlHLNGLLRPQsgavlIDGEPLDYSRK-------GLLERRQ-RVGLVFQDP- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 90 inERQDLIRNILCSVDYSLQN------NRRHLVNHFLSVVGLSS-RTESASVLSGGEKQRLALARALIKKPKILLADEPT 162
Cdd:TIGR01166 78 --DDQLFAADVDQDVAFGPLNlglseaEVERRVREALTAVGASGlRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPT 155
|
170 180 190
....*....|....*....|....*....|....*
gi 1372031259 163 ASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLELI 197
Cdd:TIGR01166 156 AGLDPAGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-199 |
5.42e-24 |
|
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: 94.84 E-value: 5.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 17 LSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKIS---------FSNYnstqelrrlyfgyifqd 87
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITepgpdrmvvFQNY----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 88 SLI---NERQdlirNILCSVDYSL----QNNRRHLVNHFLSVVGLSSRTES-ASVLSGGEKQRLALARALIKKPKILLAD 159
Cdd:TIGR01184 64 SLLpwlTVRE----NIALAVDRVLpdlsKSERRAIVEEHIALVGLTEAADKrPGQLSGGMKQRVAIARALSIRPKVLLLD 139
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1372031259 160 EPTASLDRENKEKIMDIFKKFTNEGG-TVVMVTHDlelIDE 199
Cdd:TIGR01184 140 EPFGALDALTRGNLQEELMQIWEEHRvTVLMVTHD---VDE 177
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
8-194 |
2.14e-23 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 93.52 E-value: 2.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 8 KKEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLL----DGD--FDGNYIFYDKKisfsnynSTQELRRlYF 81
Cdd:COG1126 8 HKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLeepdSGTitVDGEDLTDSKK-------DINKLRR-KV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 82 GYIFQD-SLINERqdlirnilcSVdysLQN-----------NR---RHLVNHFLSVVGLSSRTES-ASVLSGGEKQRLAL 145
Cdd:COG1126 80 GMVFQQfNLFPHL---------TV---LENvtlapikvkkmSKaeaEERAMELLERVGLADKADAyPAQLSGGQQQRVAI 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1372031259 146 ARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDL 194
Cdd:COG1126 148 ARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEM 196
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
9-199 |
2.79e-23 |
|
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: 93.38 E-value: 2.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 9 KEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLDGDfDGnyifydkKISFSNYNSTQE----LRRLyfGY 83
Cdd:COG4555 9 KKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLaGLLKPD-SG-------SILIDGEDVRKEpreaRRQI--GV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 84 IFQDSLINERQDLIRNI-LCSVDYSLQNNRRHL-VNHFLSVVGLSS-RTESASVLSGGEKQRLALARALIKKPKILLADE 160
Cdd:COG4555 79 LPDERGLYDRLTVRENIrYFAELYGLFDEELKKrIEELIELLGLEEfLDRRVGELSTGMKKKVALARALVHDPKVLLLDE 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 1372031259 161 PTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLELIDE 199
Cdd:COG4555 159 PTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEA 197
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
3-195 |
2.97e-23 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 95.21 E-value: 2.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 3 SLYIN--KKEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLDGD-----FDGNYIFYDKkisfsnynSTQ 74
Cdd:COG1118 2 SIEVRniSKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIaGLETPDsgrivLNGRDLFTNL--------PPR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 75 ElRRLyfGYIFQDSLinerqdLIR------NILC--SVDYSLQNNRRHLVNHFLSVVGLSS---RTESAsvLSGGEKQRL 143
Cdd:COG1118 74 E-RRV--GFVFQHYA------LFPhmtvaeNIAFglRVRPPSKAEIRARVEELLELVQLEGladRYPSQ--LSGGQRQRV 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1372031259 144 ALARALIKKPKILLADEPTASLD----RENKEKIMDIFKKFtneGGTVVMVTHDLE 195
Cdd:COG1118 143 ALARALAVEPEVLLLDEPFGALDakvrKELRRWLRRLHDEL---GGTTVFVTHDQE 195
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
27-206 |
4.88e-23 |
|
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: 95.82 E-value: 4.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 27 GGFYVITGPSGVGKSSLLNII-GLLDGDfDGNYIFYDKKISFSNYNSTQElRRLYFG---YIFQDSLINerqdlirNIL- 101
Cdd:TIGR02857 348 GERVALVGPSGAGKSTLLNLLlGFVDPT-EGSIAVNGVPLADADADSWRD-QIAWVPqhpFLFAGTIAE-------NIRl 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 102 ----CSVDYSLQNNRRHLVNHFLSVVGLSSRT---ESASVLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIM 174
Cdd:TIGR02857 419 arpdASDAEIREALERAGLDEFVAALPQGLDTpigEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVL 498
|
170 180 190
....*....|....*....|....*....|..
gi 1372031259 175 DIFKKFTnEGGTVVMVTHDLELIDEKIQVIRL 206
Cdd:TIGR02857 499 EALRALA-QGRTVLLVTHRLALAALADRIVVL 529
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
26-198 |
5.70e-23 |
|
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: 92.11 E-value: 5.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 26 EGGFYVITGPSGVGKSSLLNIIglldgdfdgnyifydkkisFSNYNSTQelrrlyfGYIF---QDSLIN-----ERQDL- 96
Cdd:COG4778 36 AGECVALTGPSGAGKSTLLKCI-------------------YGNYLPDS-------GSILvrhDGGWVDlaqasPREILa 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 97 IRnilcsvdyslqnnRRHL--VNHFLSVV----------------GLS---SRTESASVL-----------------SGG 138
Cdd:COG4778 90 LR-------------RRTIgyVSQFLRVIprvsaldvvaepllerGVDreeARARARELLarlnlperlwdlppatfSGG 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 139 EKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLELID 198
Cdd:COG4778 157 EQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVRE 216
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
9-199 |
7.17e-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: 92.02 E-value: 7.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 9 KEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKISfsnynsTQELRRLYFGYIFQDS 88
Cdd:cd03296 10 KRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAT------DVPVQERNVGFVFQHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 89 LINERQDLIRNILCSVDYSLQNNR------RHLVNHFLSVVGLSSRTES-ASVLSGGEKQRLALARALIKKPKILLADEP 161
Cdd:cd03296 84 ALFRHMTVFDNVAFGLRVKPRSERppeaeiRAKVHELLKLVQLDWLADRyPAQLSGGQRQRVALARALAVEPKVLLLDEP 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1372031259 162 TASLDRENKEKIMDIFKKFTNEGG-TVVMVTHD----LELIDE 199
Cdd:cd03296 164 FGALDAKVRKELRRWLRRLHDELHvTTVFVTHDqeeaLEVADR 206
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-193 |
9.17e-23 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 93.60 E-value: 9.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 1 MISLYINK--KEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLDGDfDGNYIFYDKKIsfsNYNSTQElR 77
Cdd:COG3839 1 MASLELENvsKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIaGLEDPT-SGEILIGGRDV---TDLPPKD-R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 78 RLyfGYIFQD-------SLineRQdlirNILcsvdYSLQNNR------RHLVNHFLSVVGLSS---RTESAsvLSGGEKQ 141
Cdd:COG3839 76 NI--AMVFQSyalyphmTV---YE----NIA----FPLKLRKvpkaeiDRRVREAAELLGLEDlldRKPKQ--LSGGQRQ 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1372031259 142 RLALARALIKKPKILLADEPTASLD---REN-KEKIMDIFKKFtneGGTVVMVTHD 193
Cdd:COG3839 141 RVALGRALVREPKVFLLDEPLSNLDaklRVEmRAEIKRLHRRL---GTTTIYVTHD 193
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
12-208 |
1.50e-22 |
|
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: 91.13 E-value: 1.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 12 RDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNyIFYD----KKISFSnynstqELRRLyFGYIFQD 87
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQ-ILIDgidiRDISRK------SLRSM-IGVVLQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 88 SLInerqdLIRNILCSVDYSLQNNRRHLVNHFLSVVGL------------SSRTESASVLSGGEKQRLALARALIKKPKI 155
Cdd:cd03254 86 TFL-----FSGTIMENIRLGRPNATDEEVIEAAKEAGAhdfimklpngydTVLGENGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1372031259 156 LLADEPTASLDRENKEKIMDIFKKfTNEGGTVVMVTHDLELIDEKIQVIRLNN 208
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEK-LMKGRTSIIIAHRLSTIKNADKILVLDD 212
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
9-197 |
2.36e-22 |
|
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: 90.57 E-value: 2.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 9 KEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLDGDfDGNYIFYDKKISFSnynSTQELRRLYFGYIFQD 87
Cdd:cd03219 8 KRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLIsGFLRPT-SGSVLFDGEDITGL---PPHEIARLGIGRTFQI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 88 SLINERQDLIRNILC------SVDYSLQNNRRHL------VNHFLSVVGLSS-RTESASVLSGGEKQRLALARALIKKPK 154
Cdd:cd03219 84 PRLFPELTVLENVMVaaqartGSGLLLARARREErearerAEELLERVGLADlADRPAGELSYGQQRRLEIARALATDPK 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1372031259 155 ILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLELI 197
Cdd:cd03219 164 LLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVV 206
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
9-195 |
3.08e-22 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 90.84 E-value: 3.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 9 KEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLL-NIIGLLDGD--------FDGNYIFYDKKISfsnynstQELR-- 77
Cdd:PRK09984 12 KTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLrHLSGLITGDksagshieLLGRTVQREGRLA-------RDIRks 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 78 RLYFGYIFQDSLINERQDLIRNIL------------CSVDYSLQNNRRHLvnHFLSVVGLSSRT-ESASVLSGGEKQRLA 144
Cdd:PRK09984 85 RANTGYIFQQFNLVNRLSVLENVLigalgstpfwrtCFSWFTREQKQRAL--QALTRVGMVHFAhQRVSTLSGGQQQRVA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1372031259 145 LARALIKKPKILLADEPTASLDRENKEKIMDIFKKFT-NEGGTVVMVTHDLE 195
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINqNDGITVVVTLHQVD 214
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
9-194 |
6.66e-22 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 89.81 E-value: 6.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 9 KEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKISFSNYNSTQE--LRRL--YFGYI 84
Cdd:PRK11264 11 KKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKglIRQLrqHVGFV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 85 FQDSLINERQDLIRNIL---CSVDYSLQNNRRHLVNHFLSVVGLSSRTES-ASVLSGGEKQRLALARALIKKPKILLADE 160
Cdd:PRK11264 91 FQNFNLFPHRTVLENIIegpVIVKGEPKEEATARARELLAKVGLAGKETSyPRRLSGGQQQRVAIARALAMRPEVILFDE 170
|
170 180 190
....*....|....*....|....*....|....
gi 1372031259 161 PTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDL 194
Cdd:PRK11264 171 PTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEM 204
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
13-206 |
8.55e-22 |
|
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: 89.37 E-value: 8.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 13 DKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIG------------LLDGDFDGNYIFydkkisfsnynstqELRRLy 80
Cdd:COG1119 15 GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITgdlpptygndvrLFGERRGGEDVW--------------ELRKR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 81 FGYI---FQDSLinERQDLIRNILCS---------VDYSLQNnrRHLVNHFLSVVGLSSRTESA-SVLSGGEKQRLALAR 147
Cdd:COG1119 80 IGLVspaLQLRF--PRDETVLDVVLSgffdsiglyREPTDEQ--RERARELLELLGLAHLADRPfGTLSQGEQRRVLIAR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1372031259 148 ALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGG-TVVMVTHDLELIDEKI-QVIRL 206
Cdd:COG1119 156 ALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGApTLVLVTHHVEEIPPGItHVLLL 216
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
19-195 |
9.69e-22 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 89.63 E-value: 9.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 19 DTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLDGDFdGNYIFYDKKISFSNYNSTQELRRLYFGYIFQD-SLINERqdl 96
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCInRLIEPTS-GKVLIDGQDIAAMSRKELRELRRKKISMVFQSfALLPHR--- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 97 irNILCSVDYSLQ------NNRRHLVNHFLSVVGLSSRTES-ASVLSGGEKQRLALARALIKKPKILLADEPTASLD--- 166
Cdd:cd03294 118 --TVLENVAFGLEvqgvprAEREERAAEALELVGLEGWEHKyPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDpli 195
|
170 180 190
....*....|....*....|....*....|
gi 1372031259 167 -RENKEKIMDIFKKFtneGGTVVMVTHDLE 195
Cdd:cd03294 196 rREMQDELLRLQAEL---QKTIVFITHDLD 222
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
12-192 |
1.99e-21 |
|
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: 86.44 E-value: 1.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 12 RDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYdkkisfsnynstqELRRLYF----GYIFQD 87
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMP-------------EGEDLLFlpqrPYLPLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 88 SLinerqdliRNILCsvdYSLQnnrrhlvnhflsvvglssrtesaSVLSGGEKQRLALARALIKKPKILLADEPTASLDR 167
Cdd:cd03223 79 TL--------REQLI---YPWD-----------------------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDE 124
|
170 180
....*....|....*....|....*
gi 1372031259 168 ENKEKIMDIFKKftnEGGTVVMVTH 192
Cdd:cd03223 125 ESEDRLYQLLKE---LGITVISVGH 146
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
12-195 |
3.02e-21 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 88.38 E-value: 3.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 12 RDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLL---DGD--FDGNYIfydkkisfsnynSTQELRRlyfGYIF 85
Cdd:COG4525 18 QPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIaGFLapsSGEitLDGVPV------------TGPGADR---GVVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 86 QDSLINERQDLIRNilcsVDYSLQ------NNRRHLVNHFLSVVGLSSrTESASV--LSGGEKQRLALARALIKKPKILL 157
Cdd:COG4525 83 QKDALLPWLNVLDN----VAFGLRlrgvpkAERRARAEELLALVGLAD-FARRRIwqLSGGMRQRVGIARALAADPRFLL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1372031259 158 ADEPTASLD---REN-KEKIMDIFKKftnEGGTVVMVTHDLE 195
Cdd:COG4525 158 MDEPFGALDaltREQmQELLLDVWQR---TGKGVFLITHSVE 196
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
17-209 |
5.61e-21 |
|
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: 89.02 E-value: 5.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 17 LSDTCIEI---IEG-GFYVITGPSGVGKSSLLNII-GLLDGDfdGNYIFYDKKISFSNYNSTQ---ELRRlyFGYIFQDS 88
Cdd:TIGR02142 9 LGDFSLDAdftLPGqGVTAIFGRSGSGKTTLIRLIaGLTRPD--EGEIVLNGRTLFDSRKGIFlppEKRR--IGYVFQEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 89 LINERQDLIRNILCSVDYSLQNNRRHLVNHFLSVVGLSSRTES-ASVLSGGEKQRLALARALIKKPKILLADEPTASLDR 167
Cdd:TIGR02142 85 RLFPHLSVRGNLRYGMKRARPSERRISFERVIELLGIGHLLGRlPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1372031259 168 ENKEKIMDIFKKFTNEGGT-VVMVTHDLElidekiQVIRLNNH 209
Cdd:TIGR02142 165 PRKYEILPYLERLHAEFGIpILYVSHSLQ------EVLRLADR 201
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
9-204 |
6.48e-21 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 86.09 E-value: 6.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 9 KEFRDKTILSDTCIEIiEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKISfsnyNSTQELRRLyFGYIFQDS 88
Cdd:cd03264 8 KRYGKKRALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL----KQPQKLRRR-IGYLPQEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 89 LINERqdlIRNILCsVDYS--LQN----NRRHLVNHFLSVVGLS-SRTESASVLSGGEKQRLALARALIKKPKILLADEP 161
Cdd:cd03264 82 GVYPN---FTVREF-LDYIawLKGipskEVKARVDEVLELVNLGdRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1372031259 162 TASLDRENKEKIMDIFKKFTnEGGTVVMVTH---DLELIDEKIQVI 204
Cdd:cd03264 158 TAGLDPEERIRFRNLLSELG-EDRIVILSTHiveDVESLCNQVAVL 202
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-205 |
7.32e-21 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 88.21 E-value: 7.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 1 MISLyIN-KKEFRDK----TILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLD----GDfdgnyIFYDKKiSFSNYn 71
Cdd:COG1135 1 MIEL-ENlSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLErptsGS-----VLVDGV-DLTAL- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 72 STQELR--RLYFGYIFQ-DSLINERqdlirNILCSVDYSLQ------NNRRHLVNHFLSVVGLSSRTES-ASVLSGGEKQ 141
Cdd:COG1135 73 SERELRaaRRKIGMIFQhFNLLSSR-----TVAENVALPLEiagvpkAEIRKRVAELLELVGLSDKADAyPSQLSGGQKQ 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1372031259 142 RLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKfTNE--GGTVVMVTHDLElidekiqVIR 205
Cdd:COG1135 148 RVGIARALANNPKVLLCDEATSALDPETTRSILDLLKD-INRelGLTIVLITHEMD-------VVR 205
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
9-193 |
1.40e-20 |
|
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: 85.38 E-value: 1.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 9 KEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLDGDfDGNYIFYDKKIsfsNYNSTQElRRLyfGYIFQD 87
Cdd:cd03301 8 KRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIaGLEEPT-SGRIYIGGRDV---TDLPPKD-RDI--AMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 88 SLINERQDLIRNI-----LCSVDYSLQNNRRHLVNHFLSVVGLSSRTESAsvLSGGEKQRLALARALIKKPKILLADEPT 162
Cdd:cd03301 81 YALYPHMTVYDNIafglkLRKVPKDEIDERVREVAELLQIEHLLDRKPKQ--LSGGQRQRVALGRAIVREPKVFLMDEPL 158
|
170 180 190
....*....|....*....|....*....|..
gi 1372031259 163 ASLDRENKEKIMDIFKKFTNE-GGTVVMVTHD 193
Cdd:cd03301 159 SNLDAKLRVQMRAELKRLQQRlGTTTIYVTHD 190
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
14-195 |
1.54e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 86.29 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 14 KTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLDGDfDGNYIFYDKKISfsnyNSTQELRRLYFGYIFQD----- 87
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIaGSLPPD-SGSILIDGKDVT----KLPEYKRAKYIGRVFQDpmmgt 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 88 ------------------------SLINERQDLIRNILCSVDYSLQnnrrhlvNHFLSVVGLssrtesasvLSGGEKQRL 143
Cdd:COG1101 94 apsmtieenlalayrrgkrrglrrGLTKKRRELFRELLATLGLGLE-------NRLDTKVGL---------LSGGQRQAL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1372031259 144 ALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGG-TVVMVTHDLE 195
Cdd:COG1101 158 SLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNlTTLMVTHNME 210
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
9-203 |
2.09e-20 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 85.43 E-value: 2.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 9 KEFRD-KTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKISfsNYNSTqELRRlYFGYIFQD 87
Cdd:cd03295 8 KRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIR--EQDPV-ELRR-KIGYVIQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 88 SLINERQDLIRNI--LCSVDYSLQNNRRHLVNHFLSVVGLSSRTESA---SVLSGGEKQRLALARALIKKPKILLADEPT 162
Cdd:cd03295 84 IGLFPHMTVEENIalVPKLLKWPKEKIRERADELLALVGLDPAEFADrypHELSGGQQQRVGVARALAADPPLLLMDEPF 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1372031259 163 ASLDRENKEKIMDIFKKFTNE-GGTVVMVTHDlelIDEKIQV 203
Cdd:cd03295 164 GALDPITRDQLQEEFKRLQQElGKTIVFVTHD---IDEAFRL 202
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-192 |
2.11e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 85.73 E-value: 2.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 8 KKEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLL---------DGD--FDGNYIFydkKISFSnynstqEL 76
Cdd:PRK14247 10 KVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypearvSGEvyLDGQDIF---KMDVI------EL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 77 RRlYFGYIFQDSLINERQDLIRNILCSVDYS-LQNNRRHL---VNHFLSVVGLSSRTES-----ASVLSGGEKQRLALAR 147
Cdd:PRK14247 81 RR-RVQMVFQIPNPIPNLSIFENVALGLKLNrLVKSKKELqerVRWALEKAQLWDEVKDrldapAGKLSGGQQQRLCIAR 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1372031259 148 ALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEgGTVVMVTH 192
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTH 203
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
13-208 |
2.66e-20 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 83.90 E-value: 2.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 13 DKTILSDTCIEIIEGGFYVITGPSGVGKSSLLniiGLLDGDFDGNYifydkkisfsnynstqelrrlyfGYI-FQDSLIN 91
Cdd:cd03247 14 EQQVLKNLSLELKQGEKIALLGRSGSGKSTLL---QLLTGDLKPQQ-----------------------GEItLDGVPVS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 92 ERQDLIRNILCSVdyslqNNRRHLVNHFLsvvglssRTESASVLSGGEKQRLALARALIKKPKILLADEPTASLDRENKE 171
Cdd:cd03247 68 DLEKALSSLISVL-----NQRPYLFDTTL-------RNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITER 135
|
170 180 190
....*....|....*....|....*....|....*..
gi 1372031259 172 KIMDIFKKFTnEGGTVVMVTHDLELIDEKIQVIRLNN 208
Cdd:cd03247 136 QLLSLIFEVL-KDKTLIWITHHLTGIEHMDKILFLEN 171
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
34-197 |
2.96e-20 |
|
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: 86.65 E-value: 2.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 34 GPSGVGKSSL-LNIIGLLD--GDFDGNYIFYDKKI-SFSNynstQELRRLY---FGYIFQD---SLiNERQDlIRNILCS 103
Cdd:COG0444 38 GESGSGKSTLaRAILGLLPppGITSGEILFDGEDLlKLSE----KELRKIRgreIQMIFQDpmtSL-NPVMT-VGDQIAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 104 VdysLQNNR-------RHLVNHFLSVVGLSSRTESASV----LSGGEKQRLALARALIKKPKILLADEPTASLDRENKEK 172
Cdd:COG0444 112 P---LRIHGglskaeaRERAIELLERVGLPDPERRLDRypheLSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQ 188
|
170 180
....*....|....*....|....*.
gi 1372031259 173 IMDIFKKFTNEGG-TVVMVTHDLELI 197
Cdd:COG0444 189 ILNLLKDLQRELGlAILFITHDLGVV 214
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
13-192 |
5.00e-20 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 87.14 E-value: 5.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 13 DKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLDGDfDGNyIFYD----KKISfsnynsTQELRRLyFGYIFQD 87
Cdd:COG1132 352 DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLlRFYDPT-SGR-ILIDgvdiRDLT------LESLRRQ-IGVVPQD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 88 S-LINerqDLIR-NILCSV-DYSLQNNRR--HLVN--HFL--------SVVGlssrtESASVLSGGEKQRLALARALIKK 152
Cdd:COG1132 423 TfLFS---GTIReNIRYGRpDATDEEVEEaaKAAQahEFIealpdgydTVVG-----ERGVNLSGGQRQRIAIARALLKD 494
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1372031259 153 PKILLADEPTASLDRENKEKIMDIFKKFTnEGGTVVMVTH 192
Cdd:COG1132 495 PPILILDEATSALDTETEALIQEALERLM-KGRTTIVIAH 533
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
14-196 |
8.02e-20 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 84.40 E-value: 8.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 14 KTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLDGDfDGNYIFYDKKIS-FSnynsTQEL--RR--------LYF 81
Cdd:COG4559 14 RTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLtGELTPS-SGEVRLNGRPLAaWS----PWELarRRavlpqhssLAF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 82 GYIFQD----------SLINERQDLIRNILCSVDyslqnnrrhlvnhflsVVGLSSRteSASVLSGGEKQRLALARALI- 150
Cdd:COG4559 89 PFTVEEvvalgraphgSSAAQDRQIVREALALVG----------------LAHLAGR--SYQTLSGGEQQRVQLARVLAq 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1372031259 151 ------KKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLEL 196
Cdd:COG4559 151 lwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNL 202
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
23-195 |
8.24e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 86.82 E-value: 8.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 23 EIIEGGFYVITGPSGVGKSSLLN-IIGLLDgdfdgnyifYDKKISFSNynstQELRRL-------YFGYIFQDSLINErQ 94
Cdd:PRK11174 372 TLPAGQRIALVGPSGAGKTSLLNaLLGFLP---------YQGSLKING----IELRELdpeswrkHLSWVGQNPQLPH-G 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 95 DLIRNILCS--------VDYSLQNNRrhlVNHFLSVV--GLSSRT-ESASVLSGGEKQRLALARALIKKPKILLADEPTA 163
Cdd:PRK11174 438 TLRDNVLLGnpdasdeqLQQALENAW---VSEFLPLLpqGLDTPIgDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTA 514
|
170 180 190
....*....|....*....|....*....|..
gi 1372031259 164 SLDRENKEKIMDIFKKFTNeGGTVVMVTHDLE 195
Cdd:PRK11174 515 SLDAHSEQLVMQALNAASR-RQTTLMVTHQLE 545
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
12-206 |
8.92e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 86.40 E-value: 8.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 12 RDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLldgdfdgnYIFYDKKISFsnynstQELRRLYF----GYIFQ 86
Cdd:COG4178 374 DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIaGL--------WPYGSGRIAR------PAGARVLFlpqrPYLPL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 87 DSLinerqdliRNILC----SVDYSLQNnrrhlVNHFLSVVGLSSRTES-------ASVLSGGEKQRLALARALIKKPKI 155
Cdd:COG4178 440 GTL--------REALLypatAEAFSDAE-----LREALEAVGLGHLAERldeeadwDQVLSLGEQQRLAFARLLLHKPDW 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1372031259 156 LLADEPTASLDRENKEKIMDIFKKfTNEGGTVVMVTHDLELIDEKIQVIRL 206
Cdd:COG4178 507 LFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGHRSTLAAFHDRVLEL 556
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
9-199 |
9.16e-20 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 81.34 E-value: 9.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 9 KEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKkisfsnynstqelrrLYFGYIFQds 88
Cdd:cd03221 8 KTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST---------------VKIGYFEQ-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 89 linerqdlirnilcsvdyslqnnrrhlvnhflsvvglssrtesasvLSGGEKQRLALARALIKKPKILLADEPTASLDRE 168
Cdd:cd03221 71 ----------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLE 104
|
170 180 190
....*....|....*....|....*....|.
gi 1372031259 169 NKEKIMDIFKKFTnegGTVVMVTHDLELIDE 199
Cdd:cd03221 105 SIEALEEALKEYP---GTVILVSHDRYFLDQ 132
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
8-196 |
1.06e-19 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 84.25 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 8 KKEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKISFSNYNSTQ---------ELRR 78
Cdd:PRK10619 12 HKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQlkvadknqlRLLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 79 LYFGYIFQDSLINERQDLIRNILCS----VDYSLQNNRRHLVnHFLSVVGLSSRTESA--SVLSGGEKQRLALARALIKK 152
Cdd:PRK10619 92 TRLTMVFQHFNLWSHMTVLENVMEApiqvLGLSKQEARERAV-KYLAKVGIDERAQGKypVHLSGGQQQRVSIARALAME 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1372031259 153 PKILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLEL 196
Cdd:PRK10619 171 PEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGF 214
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
15-206 |
1.23e-19 |
|
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: 82.41 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 15 TILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLDGDfDGNYIFYDKKISFSNYNSTQELrrLYFGYifqdsliner 93
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILaGLLRPD-SGEVRWNGTPLAEQRDEPHENI--LYLGH---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 94 QDLIRNILcSVDYSLQNNRRHLVNHFLSV------VGLSSRTES-ASVLSGGEKQRLALARALIKKPKILLADEPTASLD 166
Cdd:TIGR01189 81 LPGLKPEL-SALENLHFWAAIHGGAQRTIedalaaVGLTGFEDLpAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1372031259 167 RENKEKIMDIFKKFTNEGGTVVMVTHdLELIDEKIQVIRL 206
Cdd:TIGR01189 160 KAGVALLAGLLRAHLARGGIVLLTTH-QDLGLVEARELRL 198
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-195 |
1.28e-19 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 85.14 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 2 ISLYINK--KEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKISfsnynsTQELRRL 79
Cdd:PRK10851 1 MSIEIANikKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVS------RLHARDR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 80 YFGYIFQDSLINERQDLIRNILCSVDYSLQNNR------RHLVNHFLSVVGLSSRTES-ASVLSGGEKQRLALARALIKK 152
Cdd:PRK10851 75 KVGFVFQHYALFRHMTVFDNIAFGLTVLPRRERpnaaaiKAKVTQLLEMVQLAHLADRyPAQLSGGQKQRVALARALAVE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1372031259 153 PKILLADEPTASLDRENKEKIMDIFKKFTNE-GGTVVMVTHDLE 195
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQE 198
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
17-192 |
1.95e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 83.64 E-value: 1.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 17 LSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKISFSNYNSTQELRRLYFGYIFQdslINERQDL 96
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQ---FPESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 97 IRNILCSVDYSLQN------NRRHLVNHFLSVVGLSS--RTESASVLSGGEKQRLALARALIKKPKILLADEPTASLDRE 168
Cdd:PRK13649 100 EETVLKDVAFGPQNfgvsqeEAEALAREKLALVGISEslFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPK 179
|
170 180
....*....|....*....|....
gi 1372031259 169 NKEKIMDIFKKFTNEGGTVVMVTH 192
Cdd:PRK13649 180 GRKELMTLFKKLHQSGMTIVLVTH 203
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
32-194 |
3.19e-19 |
|
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: 85.10 E-value: 3.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 32 ITGPSGVGKSSLLNII-GLLDGDfDGNYIFYDKKISFSNYNstqELRRLYfgyifqdSLINERQDLIrnilcsvDYSLQN 110
Cdd:TIGR02868 366 ILGPSGSGKSTLLATLaGLLDPL-QGEVTLDGVPVSSLDQD---EVRRRV-------SVCAQDAHLF-------DTTVRE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 111 NRR--------HLVNHFLSVVGL------------SSRTESASVLSGGEKQRLALARALIKKPKILLADEPTASLDRENK 170
Cdd:TIGR02868 428 NLRlarpdatdEELWAALERVGLadwlralpdgldTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETA 507
|
170 180
....*....|....*....|....*
gi 1372031259 171 EKIM-DIFKkfTNEGGTVVMVTHDL 194
Cdd:TIGR02868 508 DELLeDLLA--ALSGRTVVLITHHL 530
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
13-208 |
3.23e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 81.46 E-value: 3.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 13 DKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKISFSNYNStqelRRLYFGYifQDSLINE 92
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAE----ACHYLGH--RNAMKPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 93 ---RQDLI--RNILcsvdyslqNNRRHLVNHFLSVVGLSSRTE-SASVLSGGEKQRLALARALIKKPKILLADEPTASLD 166
Cdd:PRK13539 88 ltvAENLEfwAAFL--------GGEELDIAAALEAVGLAPLAHlPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1372031259 167 RENKEKIMDIFKKFTNEGGTVVMVTH-DLELidEKIQVIRLNN 208
Cdd:PRK13539 160 AAAVALFAELIRAHLAQGGIVIAATHiPLGL--PGARELDLGP 200
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
13-194 |
3.41e-19 |
|
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: 82.20 E-value: 3.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 13 DKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII----GLLDGD--FDGNYIfydkkisfSNYNStQELRRLyFGYIFQ 86
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLerfyDPTSGEilLDGVDI--------RDLNL-RWLRSQ-IGLVSQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 87 DSLINERQdlIR-NILCSVDYSLQNNRRH-------------LVNHFLSVVGlssrtESASVLSGGEKQRLALARALIKK 152
Cdd:cd03249 85 EPVLFDGT--IAeNIRYGKPDATDEEVEEaakkanihdfimsLPDGYDTLVG-----ERGSQLSGGQKQRIAIARALLRN 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1372031259 153 PKILLADEPTASLDRENKEKIMDIFKKFTnEGGTVVMVTHDL 194
Cdd:cd03249 158 PKILLLDEATSALDAESEKLVQEALDRAM-KGRTTIVIAHRL 198
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
13-195 |
3.75e-19 |
|
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: 82.48 E-value: 3.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 13 DKTILSDTCIEIIEGGFYVITGPSGVGKSSL-LNIIGLLD---GD--FDGnyifydkkISFSNYNSTQELRRLyFGYIFQ 86
Cdd:TIGR04520 14 EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLaKLLNGLLLptsGKvtVDG--------LDTLDEENLWEIRKK-VGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 87 DSlinERQdlirnILCS-----VDYSLQNNR------RHLVNHFLSVVGLSS-RTESASVLSGGEKQRLALARALIKKPK 154
Cdd:TIGR04520 85 NP---DNQ-----FVGAtveddVAFGLENLGvpreemRKRVDEALKLVGMEDfRDREPHLLSGGQKQRVAIAGVLAMRPD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1372031259 155 ILLADEPTASLDRENKEKIMDIFKKFTNEGG-TVVMVTHDLE 195
Cdd:TIGR04520 157 IIILDEATSMLDPKGRKEVLETIRKLNKEEGiTVISITHDME 198
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
2-192 |
4.60e-19 |
|
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: 81.06 E-value: 4.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 2 ISLYINKKEFRD-KTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIglldgdfdgnyifydkkisfSNYNSTQELRrly 80
Cdd:cd03213 9 LTVTVKSSPSKSgKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNAL--------------------AGRRTGLGVS--- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 81 fGYIfqdsLINERQDLIRNILCSVDYSLQNNRRHL---VNHFLSVvglssrteSA--SVLSGGEKQRLALARALIKKPKI 155
Cdd:cd03213 66 -GEV----LINGRPLDKRSFRKIIGYVPQDDILHPtltVRETLMF--------AAklRGLSGGERKRVSIALELVSNPSL 132
|
170 180 190
....*....|....*....|....*....|....*..
gi 1372031259 156 LLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTH 192
Cdd:cd03213 133 LFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIH 169
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
8-199 |
5.74e-19 |
|
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: 81.17 E-value: 5.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 8 KKEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLDGDfDGNYIFYDKKISFSNYNST---QELRRLYFGY 83
Cdd:cd03269 7 TKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMIlGIILPD-SGEVLFDGKPLDIAARNRIgylPEERGLYPKM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 84 IFQDSLI--NERQDL-IRNILCSVDYSLqnNRRHLVNHflsvvgLSSRTESasvLSGGEKQRLALARALIKKPKILLADE 160
Cdd:cd03269 86 KVIDQLVylAQLKGLkKEEARRRIDEWL--ERLELSEY------ANKRVEE---LSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 1372031259 161 PTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLELIDE 199
Cdd:cd03269 155 PFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEE 193
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
32-195 |
7.51e-19 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 81.34 E-value: 7.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 32 ITGPSGVGKSSLLNIIG----------LLDG-DFDGNYIfYDKKISFsnynstqelrrlyfgyIFQD-----SLinerqD 95
Cdd:COG3840 30 ILGPSGAGKSTLLNLIAgflppdsgriLWNGqDLTALPP-AERPVSM----------------LFQEnnlfpHL-----T 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 96 LIRNILCSVDYSLQNNR--RHLVNHFLSVVGLS---SRTESAsvLSGGEKQRLALARALIKKPKILLADEPTASLDRENK 170
Cdd:COG3840 88 VAQNIGLGLRPGLKLTAeqRAQVEQALERVGLAgllDRLPGQ--LSGGQRQRVALARCLVRKRPILLLDEPFSALDPALR 165
|
170 180
....*....|....*....|....*.
gi 1372031259 171 EKIMDIFKKFTNEGG-TVVMVTHDLE 195
Cdd:COG3840 166 QEMLDLVDELCRERGlTVLMVTHDPE 191
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
14-196 |
9.18e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 81.36 E-value: 9.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 14 KTILSDTCIEIIEGGFYVITGPSGVGKSSLLniiGLLDGDFDGnyifYDKKISFSNYN----STQEL--RR--------L 79
Cdd:PRK13548 15 RTLLDDVSLTLRPGEVVAILGPNGAGKSTLL---RALSGELSP----DSGEVRLNGRPladwSPAELarRRavlpqhssL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 80 YF-----------GYIFQDSLInERQDLIRNILCSVDyslqnnrrhlvnhflsVVGLSSRteSASVLSGGEKQRLALARA 148
Cdd:PRK13548 88 SFpftveevvamgRAPHGLSRA-EDDALVAAALAQVD----------------LAHLAGR--DYPQLSGGEQQRVQLARV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1372031259 149 LI------KKPKILLADEPTASLDRENKEKIMDIFKKFTNE-GGTVVMVTHDLEL 196
Cdd:PRK13548 149 LAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHErGLAVIVVLHDLNL 203
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
3-208 |
9.35e-19 |
|
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: 80.21 E-value: 9.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 3 SLYINKKEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLN-IIG---LLDGDfdgnyIFYDKKISFSnynsTQElrr 78
Cdd:cd03250 7 SFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGeleKLSGS-----VSVPGSIAYV----SQE--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 79 lyfGYIFQDSLINerqdlirNIL----------------CSVDYSLQNnrrhLVNHFLSVVGlssrtESASVLSGGEKQR 142
Cdd:cd03250 75 ---PWIQNGTIRE-------NILfgkpfdeeryekvikaCALEPDLEI----LPDGDLTEIG-----EKGINLSGGQKQR 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1372031259 143 LALARALIKKPKILLADEPTASLDRENKEKIMD-IFKKFTNEGGTVVMVTHDLELIDEKIQVIRLNN 208
Cdd:cd03250 136 ISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEnCILGLLLNNKTRILVTHQLQLLPHADQIVVLDN 202
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
32-209 |
1.23e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 82.23 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 32 ITGPSGVGKSSLLNIIGLLDGDFDGnYIFYDKKISF---SNYNSTQELRRLyfGYIFQDS-LINErqdlirnilcsvdYS 107
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKG-RIVLNGRVLFdaeKGICLPPEKRRI--GYVFQDArLFPH-------------YK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 108 LQNN-----RRHLVNHFLSVVG------LSSRTESAsvLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDI 176
Cdd:PRK11144 93 VRGNlrygmAKSMVAQFDKIVAllgiepLLDRYPGS--LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPY 170
|
170 180 190
....*....|....*....|....*....|....
gi 1372031259 177 FKKFTNEGGT-VVMVTHDLeliDEkiqVIRLNNH 209
Cdd:PRK11144 171 LERLAREINIpILYVSHSL---DE---ILRLADR 198
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
113-206 |
1.94e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 79.20 E-value: 1.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 113 RHLVNHFLSVVGLSS-RTESASVLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVT 191
Cdd:NF040873 97 RAAVDDALERVGLADlAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVT 176
|
90
....*....|....*
gi 1372031259 192 HDLELIDEKIQVIRL 206
Cdd:NF040873 177 HDLELVRRADPCVLL 191
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
12-197 |
2.68e-18 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 81.39 E-value: 2.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 12 RDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKI-SFSNynstQELR--RLYFGYIFQD- 87
Cdd:PRK11153 16 RTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtALSE----KELRkaRRQIGMIFQHf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 88 SLINERQdLIRNI-----LCSVDYSLQNNRrhlVNHFLSVVGLSSRTES-ASVLSGGEKQRLALARALIKKPKILLADEP 161
Cdd:PRK11153 92 NLLSSRT-VFDNValpleLAGTPKAEIKAR---VTELLELVGLSDKADRyPAQLSGGQKQRVAIARALASNPKVLLCDEA 167
|
170 180 190
....*....|....*....|....*....|....*..
gi 1372031259 162 TASLDRENKEKIMDIFKKFTNEGG-TVVMVTHDLELI 197
Cdd:PRK11153 168 TSALDPATTRSILELLKDINRELGlTIVLITHEMDVV 204
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
17-199 |
3.00e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 80.64 E-value: 3.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 17 LSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKISFSNYN-STQELRRlYFGYIFQdslINERQD 95
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNkNLKKLRK-KVSLVFQ---FPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 96 LIRNILCSVDYSLQN------NRRHLVNHFLSVVGLSSRTESASV--LSGGEKQRLALARALIKKPKILLADEPTASLDR 167
Cdd:PRK13641 99 FENTVLKDVEFGPKNfgfsedEAKEKALKWLKKVGLSEDLISKSPfeLSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178
|
170 180 190
....*....|....*....|....*....|..
gi 1372031259 168 ENKEKIMDIFKKFTNEGGTVVMVTHDLELIDE 199
Cdd:PRK13641 179 EGRKEMMQLFKDYQKAGHTVILVTHNMDDVAE 210
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
10-208 |
3.68e-18 |
|
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: 79.58 E-value: 3.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 10 EFRD--------KTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIglldgdfdgnYIFYDK---KISFSNY---NSTQE 75
Cdd:cd03253 2 EFENvtfaydpgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLL----------FRFYDVssgSILIDGQdirEVTLD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 76 LRRLYFGYIFQDS-LINerqDLIR-NI-----------------LCSVDYSLQNnrrhLVNHFLSVVGlssrtESASVLS 136
Cdd:cd03253 72 SLRRAIGVVPQDTvLFN---DTIGyNIrygrpdatdeevieaakAAQIHDKIMR----FPDGYDTIVG-----ERGLKLS 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1372031259 137 GGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNeGGTVVMVTHDLELIDEKIQVIRLNN 208
Cdd:cd03253 140 GGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLSTIVNADKIIVLKD 210
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-199 |
3.94e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 81.65 E-value: 3.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 9 KEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLDGDfDGNyIFYDKKIS--------FSNYNST------ 73
Cdd:COG0488 6 KSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILaGELEPD-SGE-VSIPKGLRigylpqepPLDDDLTvldtvl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 74 ----------QELRRLYFGYIFQDSLInERQDLIRNILCSVD-YSLQNNRRHLvnhfLSVVGLSSRTESASV--LSGGEK 140
Cdd:COG0488 84 dgdaelraleAELEELEAKLAEPDEDL-ERLAELQEEFEALGgWEAEARAEEI----LSGLGFPEEDLDRPVseLSGGWR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1372031259 141 QRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTnegGTVVMVTHDLELIDE 199
Cdd:COG0488 159 RRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYP---GTVLVVSHDRYFLDR 214
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
16-208 |
6.14e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 81.41 E-value: 6.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 16 ILSDTCIEIIEGGFYVITGPSGVGKSSLLNiigLLDGDFD---GNYIFYDKKISfsNYNSTQeLR--------RLYfgyI 84
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQ---LLTRAWDpqqGEILLNGQPIA--DYSEAA-LRqaisvvsqRVH---L 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 85 FQDSLineRQDLIRNILCSVDYSLQnnrrhlvnHFLSVVGLSSRTESAS-----------VLSGGEKQRLALARALIKKP 153
Cdd:PRK11160 426 FSATL---RDNLLLAAPNASDEALI--------EVLQQVGLEKLLEDDKglnawlgeggrQLSGGEQRRLGIARALLHDA 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1372031259 154 KILLADEPTASLDRENKEKIMDIFKKFTnEGGTVVMVTHDLELIDEKIQVIRLNN 208
Cdd:PRK11160 495 PLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITHRLTGLEQFDRICVMDN 548
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
9-195 |
6.28e-18 |
|
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: 77.08 E-value: 6.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 9 KEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLDGDfDGNYIFYDKKISFsnyNSTQELRRLYFGYIFQd 87
Cdd:cd03216 8 KRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILsGLYKPD-SGEILVDGKEVSF---ASPRDARRAGIAMVYQ- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 88 slinerqdlirnilcsvdyslqnnrrhlvnhflsvvglssrtesasvLSGGEKQRLALARALIKKPKILLADEPTASLDR 167
Cdd:cd03216 83 -----------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTP 115
|
170 180
....*....|....*....|....*...
gi 1372031259 168 ENKEKIMDIFKKFTNEGGTVVMVTHDLE 195
Cdd:cd03216 116 AEVERLFKVIRRLRAQGVAVIFISHRLD 143
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-193 |
9.63e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 78.94 E-value: 9.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 4 LYINkkefrDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLdgdfdgnYIFYDKKISFSNynstqelRRLYFGY 83
Cdd:PRK14246 18 LYIN-----DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRL-------IEIYDSKIKVDG-------KVLYFGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 84 -IFQDSLINERQDLIR-----------NILCSVDYSLQNNR-------RHLVNHFLSVVGL----SSRTES-ASVLSGGE 139
Cdd:PRK14246 79 dIFQIDAIKLRKEVGMvfqqpnpfphlSIYDNIAYPLKSHGikekreiKKIVEECLRKVGLwkevYDRLNSpASQLSGGQ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1372031259 140 KQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEgGTVVMVTHD 193
Cdd:PRK14246 159 QQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHN 211
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
10-195 |
1.06e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 78.59 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 10 EFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGlldgdfdgNYIFYDK-KISFSNYN-STQELRRlyfGYIFQD 87
Cdd:PRK11248 10 DYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIA--------GFVPYQHgSITLDGKPvEGPGAER---GVVFQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 88 slinerQDLI--RNILCSVDYSLQ------NNRRHLVNHFLSVVGLSSrTESASV--LSGGEKQRLALARALIKKPKILL 157
Cdd:PRK11248 79 ------EGLLpwRNVQDNVAFGLQlagvekMQRLEIAHQMLKKVGLEG-AEKRYIwqLSGGQRQRVGIARALAANPQLLL 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 1372031259 158 ADEPTASLDRENKEKIMDIFKKFTNEGGT-VVMVTHDLE 195
Cdd:PRK11248 152 LDEPFGALDAFTREQMQTLLLKLWQETGKqVLLITHDIE 190
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
13-194 |
1.09e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 78.52 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 13 DKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKISfsNYNSTQELRRLYFgyIFQDSLINE 92
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPIS--MLSSRQLARRLAL--LPQHHLTPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 93 R---QDLI---RNILCSVDYSLQNNRRHLVNHFLSVVGLSSRTES-ASVLSGGEKQRLALARALIKKPKILLADEPTASL 165
Cdd:PRK11231 90 GitvRELVaygRSPWLSLWGRLSAEDNARVNQAMEQTRINHLADRrLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYL 169
|
170 180
....*....|....*....|....*....
gi 1372031259 166 DRENKEKIMDIFKKFTNEGGTVVMVTHDL 194
Cdd:PRK11231 170 DINHQVELMRLMRELNTQGKTVVTVLHDL 198
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
32-195 |
1.89e-17 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 77.15 E-value: 1.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 32 ITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKISFSnynstqELRRLYFGYIFQDSLINERQDLIRNILCSVDYSLQNN 111
Cdd:cd03298 29 IVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAA------PPADRPVSMLFQENNLFAHLTVEQNVGLGLSPGLKLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 112 --RRHLVNHFLSVVGLSSRTES-ASVLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGG-TV 187
Cdd:cd03298 103 aeDRQAIEVALARVGLAGLEKRlPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKmTV 182
|
....*...
gi 1372031259 188 VMVTHDLE 195
Cdd:cd03298 183 LMVTHQPE 190
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-195 |
1.90e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 78.59 E-value: 1.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 2 ISLYINKKEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSL---LNIIgLLDGDFDGNYIFYDKKI-----SFSNYNST 73
Cdd:PRK13651 8 IVKIFNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFiehLNAL-LLPDTGTIEWIFKDEKNkkktkEKEKVLEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 74 QELRRLYF-------------GYIFQ-------DSLINErqDLIrniLCSVDYSLQNNR-RHLVNHFLSVVGL--SSRTE 130
Cdd:PRK13651 87 LVIQKTRFkkikkikeirrrvGVVFQfaeyqlfEQTIEK--DII---FGPVSMGVSKEEaKKRAAKYIELVGLdeSYLQR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1372031259 131 SASVLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLE 195
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLD 226
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
27-206 |
1.95e-17 |
|
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: 76.76 E-value: 1.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 27 GGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKISFSNYNSTQELrrLYFGYifqdslinerQDLIRNILcSVDY 106
Cdd:cd03231 26 GEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGL--LYLGH----------APGIKTTL-SVLE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 107 SLQ----NNRRHLVNHFLSVVGLSSrTESASV--LSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKF 180
Cdd:cd03231 93 NLRfwhaDHSDEQVEEALARVGLNG-FEDRPVaqLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGH 171
|
170 180
....*....|....*....|....*..
gi 1372031259 181 TNEGGTVVMVTH-DLELIDEKIQVIRL 206
Cdd:cd03231 172 CARGGMVVLTTHqDLGLSEAGARELDL 198
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
9-195 |
2.29e-17 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 79.11 E-value: 2.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 9 KEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIG----------LLDGDFDGNYIFYDKKIS--FSNY----NS 72
Cdd:PRK11607 27 KSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAgfeqptagqiMLDGVDLSHVPPYQRPINmmFQSYalfpHM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 73 TQElRRLYFGyIFQDSL----INERqdlirnilcsvdyslqnnrrhlVNHFLSVVGLSS-RTESASVLSGGEKQRLALAR 147
Cdd:PRK11607 107 TVE-QNIAFG-LKQDKLpkaeIASR----------------------VNEMLGLVHMQEfAKRKPHQLSGGQRQRVALAR 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1372031259 148 ALIKKPKILLADEPTASLDRENKEK----IMDIFKKFtneGGTVVMVTHDLE 195
Cdd:PRK11607 163 SLAKRPKLLLLDEPMGALDKKLRDRmqleVVDILERV---GVTCVMVTHDQE 211
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
9-193 |
2.98e-17 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 78.61 E-value: 2.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 9 KEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNyIFYDKKISfsNYNSTQElRRLYFgyIFQDS 88
Cdd:PRK11432 14 KRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQ-IFIDGEDV--THRSIQQ-RDICM--VFQSY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 89 LINERQDLIRNilcsVDYSLQ------NNRRHLVNHFLSVVGLSSrTESASV--LSGGEKQRLALARALIKKPKILLADE 160
Cdd:PRK11432 88 ALFPHMSLGEN----VGYGLKmlgvpkEERKQRVKEALELVDLAG-FEDRYVdqISGGQQQRVALARALILKPKVLLFDE 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 1372031259 161 PTASLD----RENKEKIMDIFKKFtneGGTVVMVTHD 193
Cdd:PRK11432 163 PLSNLDanlrRSMREKIRELQQQF---NITSLYVTHD 196
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
10-198 |
3.50e-17 |
|
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: 76.39 E-value: 3.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 10 EFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLD---GD--FDGNYIFYDKKisfsnynstQELRRLyfGY 83
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLtGELRptsGTayINGYSIRTDRK---------AARQSL--GY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 84 IFQDSLINER---QDLIRnILCSVDYSLQNNRRHLVNHFLSVVGLSS-RTESASVLSGGEKQRLALARALIKKPKILLAD 159
Cdd:cd03263 80 CPQFDALFDEltvREHLR-FYARLKGLPKSEIKEEVELLLRVLGLTDkANKRARTLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 1372031259 160 EPTASLDRENKEKIMDIFKKFTnEGGTVVMVTHDLELID 198
Cdd:cd03263 159 EPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAE 196
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-198 |
3.70e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.95 E-value: 3.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 9 KEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLDGDfDGNyIFYDKKISFSNYnsTQElrrlyfgyifQD 87
Cdd:COG0488 323 KSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLaGELEPD-SGT-VKLGETVKIGYF--DQH----------QE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 88 SLiNERQDLIRNIlcsVDYSLQNNRRHLVNhFLSVVGLSSR--TESASVLSGGEKQRLALARALIKKPKILLADEPTASL 165
Cdd:COG0488 389 EL-DPDKTVLDEL---RDGAPGGTEQEVRG-YLGRFLFSGDdaFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHL 463
|
170 180 190
....*....|....*....|....*....|...
gi 1372031259 166 DRENKEKIMDIFKKFTnegGTVVMVTHDLELID 198
Cdd:COG0488 464 DIETLEALEEALDDFP---GTVLLVSHDRYFLD 493
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
130-205 |
5.31e-17 |
|
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: 78.64 E-value: 5.31e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1372031259 130 ESASVLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLELIDE--KIQVIR 205
Cdd:COG4618 463 EGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAAvdKLLVLR 540
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
11-199 |
7.14e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 76.58 E-value: 7.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 11 FRDKTILSDTCIEIIEGGFYVITGPSGVGKSSL-LNIIGLLDGDfDGNYIFYDKKISFSNyNSTQELRRlYFGYIFQDSl 89
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLfMNLSGLLRPQ-KGAVLWQGKPLDYSK-RGLLALRQ-QVATVFQDP- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 90 inERQDLIRNILCSVDYSLQN--------NRRhlVNHFLSVVGLSS-RTESASVLSGGEKQRLALARALIKKPKILLADE 160
Cdd:PRK13638 87 --EQQIFYTDIDSDIAFSLRNlgvpeaeiTRR--VDEALTLVDAQHfRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDE 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 1372031259 161 PTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLELIDE 199
Cdd:PRK13638 163 PTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYE 201
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
8-204 |
8.27e-17 |
|
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: 75.51 E-value: 8.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 8 KKEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLDGDfDGNYIFYDKKIS---FSNYNSTQELRRLYFGY 83
Cdd:TIGR03740 7 SKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMItGILRPT-SGEIIFDGHPWTrkdLHKIGSLIESPPLYENL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 84 IFQDSLinerqdLIRNILCSVDYSLqnnrrhlVNHFLSVVGLS-SRTESASVLSGGEKQRLALARALIKKPKILLADEPT 162
Cdd:TIGR03740 86 TARENL------KVHTTLLGLPDSR-------IDEVLNIVDLTnTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPT 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1372031259 163 ASLDRENKEKIMDIFKKFTNEGGTVVMVTHDL---ELIDEKIQVI 204
Cdd:TIGR03740 153 NGLDPIGIQELRELIRSFPEQGITVILSSHILsevQQLADHIGII 197
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
17-204 |
1.21e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 76.18 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 17 LSDTCIEIIEGGFYVITGPSGVGKSSL-LNIIGLLDGDfDGNYIFydKKISFSNYNSTQELRRLyFGYIFQDSlinERQD 95
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLaLHLNGLLRPQ-KGKVLV--SGIDTGDFSKLQGIRKL-VGIVFQNP---ETQF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 96 LIRNILCSVDYSLQN------NRRHLVNHFLSVVGLSS-RTESASVLSGGEKQRLALARALIKKPKILLADEPTASLDRE 168
Cdd:PRK13644 91 VGRTVEEDLAFGPENlclppiEIRKRVDRALAEIGLEKyRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPD 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 1372031259 169 NKEKIMDIFKKFTNEGGTVVMVTHDLELIDEKIQVI 204
Cdd:PRK13644 171 SGIAVLERIKKLHEKGKTIVYITHNLEELHDADRII 206
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
5-195 |
1.55e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 75.89 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 5 YINKKEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNyiFYDKKISFSNYNSTQELRRLYfGYI 84
Cdd:PRK13633 14 YESNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGK--VYVDGLDTSDEENLWDIRNKA-GMV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 85 FQdsliNERQDLIRNILCS-VDYSLQN------NRRHLVNHFLSVVGLSS-RTESASVLSGGEKQRLALARALIKKPKIL 156
Cdd:PRK13633 91 FQ----NPDNQIVATIVEEdVAFGPENlgippeEIRERVDESLKKVGMYEyRRHAPHLLSGGQKQRVAIAGILAMRPECI 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1372031259 157 LADEPTASLDRENKEKIMDIFKKFTNEGG-TVVMVTHDLE 195
Cdd:PRK13633 167 IFDEPTAMLDPSGRREVVNTIKELNKKYGiTIILITHYME 206
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
22-194 |
1.87e-16 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 74.50 E-value: 1.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 22 IEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNyIFYDKKISFSNynstqelrRLYFGYIFQdslineRQDLIRNIL 101
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGT-VKVAGASPGKG--------WRHIGYVPQ------RHEFAWDFP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 102 CSVDYSLQNNR-RHL-------------VNHFLSVVGLSS-RTESASVLSGGEKQRLALARALIKKPKILLADEPTASLD 166
Cdd:TIGR03771 66 ISVAHTVMSGRtGHIgwlrrpcvadfaaVRDALRRVGLTElADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLD 145
|
170 180
....*....|....*....|....*...
gi 1372031259 167 RENKEKIMDIFKKFTNEGGTVVMVTHDL 194
Cdd:TIGR03771 146 MPTQELLTELFIELAGAGTAILMTTHDL 173
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
32-197 |
2.21e-16 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 75.26 E-value: 2.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 32 ITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKISFSNYNSTQELRRLyfgyIFQD---SLiNERQDlIRNILcsvDYSL 108
Cdd:COG4167 44 IIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCKHIRM----IFQDpntSL-NPRLN-IGQIL---EEPL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 109 QNN-------RRHLVNHFLSVVGLssRTESASV----LSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIF 177
Cdd:COG4167 115 RLNtdltaeeREERIFATLRLVGL--LPEHANFyphmLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLM 192
|
170 180
....*....|....*....|.
gi 1372031259 178 KKFTNEGG-TVVMVTHDLELI 197
Cdd:COG4167 193 LELQEKLGiSYIYVSQHLGIV 213
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
14-197 |
2.52e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 75.11 E-value: 2.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 14 KTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKISFSNYNSTQELRRlYFGYIFQDSL--IN 91
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRR-DIQMVFQDSIsaVN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 92 ERQDlIRNI-------LCSVDyslQNNRRHLVNHFLSVVGLssRTESAS----VLSGGEKQRLALARALIKKPKILLADE 160
Cdd:PRK10419 104 PRKT-VREIireplrhLLSLD---KAERLARASEMLRAVDL--DDSVLDkrppQLSGGQLQRVCLARALAVEPKLLILDE 177
|
170 180 190
....*....|....*....|....*....|....*...
gi 1372031259 161 PTASLDRENKEKIMDIFKKFTNEGGTV-VMVTHDLELI 197
Cdd:PRK10419 178 AVSNLDLVLQAGVIRLLKKLQQQFGTAcLFITHDLRLV 215
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
14-208 |
2.54e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 75.22 E-value: 2.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 14 KTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLDGDFDGNyifydKKISFSNYNSTQELR---RLYFGYIFQDSl 89
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLInGLLLPDDNPN-----SKITVDGITLTAKTVwdiREKVGIVFQNP- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 90 inERQDLIRNILCSVDYSLQNNR------RHLVNHFLSVVGLSSRTES-ASVLSGGEKQRLALARALIKKPKILLADEPT 162
Cdd:PRK13640 94 --DNQFVGATVGDDVAFGLENRAvprpemIKIVRDVLADVGMLDYIDSePANLSGGQKQRVAIAGILAVEPKIIILDEST 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1372031259 163 ASLDRENKEKIMDIFKKFTNEGG-TVVMVTHDLELIDEKIQVIRLNN 208
Cdd:PRK13640 172 SMLDPAGKEQILKLIRKLKKKNNlTVISITHDIDEANMADQVLVLDD 218
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
120-197 |
2.83e-16 |
|
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: 74.69 E-value: 2.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 120 LSVVGLSSRT-ESASVLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGG-TVVMVTHDLELI 197
Cdd:COG0411 137 LERVGLADRAdEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGiTILLIEHDMDLV 216
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
9-199 |
3.31e-16 |
|
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: 76.38 E-value: 3.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 9 KEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLDGDFDGNYIFYD------------------------- 62
Cdd:TIGR03269 8 KKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrGMDQYEPTSGRIIYHvalcekcgyverpskvgepcpvcgg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 63 --KKISFSNYNSTQELRRLYFGYI---FQDSL-INERQDLIRNILCSVD---YSLQNNRRHLVNhFLSVVGLSSR-TESA 132
Cdd:TIGR03269 88 tlEPEEVDFWNLSDKLRRRIRKRIaimLQRTFaLYGDDTVLDNVLEALEeigYEGKEAVGRAVD-LIEMVQLSHRiTHIA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1372031259 133 SVLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKK-FTNEGGTVVMVTHDLELIDE 199
Cdd:TIGR03269 167 RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEaVKASGISMVLTSHWPEVIED 234
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
13-206 |
4.70e-16 |
|
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: 73.66 E-value: 4.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 13 DKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIG----------LLDG----DFDGNYifYDKKISFSnynsTQElrR 78
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLEnfyqpqggqvLLDGkpisQYEHKY--LHSKVSLV----GQE--P 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 79 LYFGYIFQDSLINERQDlirnilCSVDYSLQNNRRHLVNHFLSVVGLSSRT---ESASVLSGGEKQRLALARALIKKPKI 155
Cdd:cd03248 98 VLFARSLQDNIAYGLQS------CSFECVKEAAQKAHAHSFISELASGYDTevgEKGSQLSGGQKQRVAIARALIRNPQV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1372031259 156 LLADEPTASLDRENKEKIMDIFKKfTNEGGTVVMVTHDLELIDEKIQVIRL 206
Cdd:cd03248 172 LILDEATSALDAESEQQVQQALYD-WPERRTVLVIAHRLSTVERADQILVL 221
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
17-192 |
4.71e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 74.77 E-value: 4.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 17 LSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKISFSNYNSTQELRRLYFGYIFQdslINERQDL 96
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQ---FPESQLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 97 IRNILCSVDYSLQN------NRRHLVNHFLSVVGLSSR--TESASVLSGGEKQRLALARALIKKPKILLADEPTASLDRE 168
Cdd:PRK13643 99 EETVLKDVAFGPQNfgipkeKAEKIAAEKLEMVGLADEfwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK 178
|
170 180
....*....|....*....|....
gi 1372031259 169 NKEKIMDIFKKFTNEGGTVVMVTH 192
Cdd:PRK13643 179 ARIEMMQLFESIHQSGQTVVLVTH 202
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
17-195 |
7.08e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 74.29 E-value: 7.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 17 LSDTCIEIIEGGFYVITGPSGVGKSSLL-NIIGLLDGDfDGNYIFYDKKISFSNYNstQELRRL--YFGYIFQdslINER 93
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLqHLNGLLQPT-SGTVTIGERVITAGKKN--KKLKPLrkKVGIVFQ---FPEH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 94 QDLIRNILCSVDYSLQN------NRRHLVNHFLSVVGLSS--RTESASVLSGGEKQRLALARALIKKPKILLADEPTASL 165
Cdd:PRK13634 97 QLFEETVEKDICFGPMNfgvseeDAKQKAREMIELVGLPEelLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGL 176
|
170 180 190
....*....|....*....|....*....|.
gi 1372031259 166 DRENKEKIMDIFKKFTNEGG-TVVMVTHDLE 195
Cdd:PRK13634 177 DPKGRKEMMEMFYKLHKEKGlTTVLVTHSME 207
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-197 |
8.56e-16 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 73.29 E-value: 8.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 16 ILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIF--YDKKISFSNYnstqeLRRlYFGYIFQDSLINER 93
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVdgHDLALADPAW-----LRR-QVGVVLQENVLFNR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 94 QdlIRNILCSVDYSLQNNR--------------RHLVNHFLSVVGlssrtESASVLSGGEKQRLALARALIKKPKILLAD 159
Cdd:cd03252 91 S--IRDNIALADPGMSMERvieaaklagahdfiSELPEGYDTIVG-----EQGAGLSGGQRQRIAIARALIHNPRILIFD 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 1372031259 160 EPTASLDRENKEKIMDIFKKFTnEGGTVVMVTHDLELI 197
Cdd:cd03252 164 EATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTV 200
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
32-195 |
1.04e-15 |
|
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: 71.69 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 32 ITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKISFSnynSTQELRRLYFGYIFQDslinerqdliRnilcsvdyslqnn 111
Cdd:cd03215 31 IAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRR---SPRDAIRAGIAYVPED----------R------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 112 RRHLVNHFLSV---VGLSSRtesasvLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGTVV 188
Cdd:cd03215 85 KREGLVLDLSVaenIALSSL------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVL 158
|
....*..
gi 1372031259 189 MVTHDLE 195
Cdd:cd03215 159 LISSELD 165
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
31-195 |
1.22e-15 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 72.69 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 31 VITGPSGVGKSSLLNII-GLLDGDfdGNYIFydkkISFSNYNSTQELRRLyFGYIFQD----SLINERQdlirNILCSVD 105
Cdd:PRK10771 29 AILGPSGAGKSTLLNLIaGFLTPA--SGSLT----LNGQDHTTTPPSRRP-VSMLFQEnnlfSHLTVAQ----NIGLGLN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 106 YSLQNN--RRHLVNHFLSVVGLS---SRTESAsvLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKF 180
Cdd:PRK10771 98 PGLKLNaaQREKLHAIARQMGIEdllARLPGQ--LSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQV 175
|
170
....*....|....*.
gi 1372031259 181 TNEGG-TVVMVTHDLE 195
Cdd:PRK10771 176 CQERQlTLLMVSHSLE 191
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
10-196 |
1.23e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 74.49 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 10 EFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLDGDfDGNYIFYDKKISfsNYNSTQELRRLyfGYIFQDS 88
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAInGTLTPT-AGTVLVAGDDVE--ALSARAASRRV--ASVPQDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 89 LINERQDlIRNI--------LCSVDYSLQNNRRhLVNHFLSVVGLSSRTE-SASVLSGGEKQRLALARALIKKPKILLAD 159
Cdd:PRK09536 87 SLSFEFD-VRQVvemgrtphRSRFDTWTETDRA-AVERAMERTGVAQFADrPVTSLSGGERQRVLLARALAQATPVLLLD 164
|
170 180 190
....*....|....*....|....*....|....*..
gi 1372031259 160 EPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLEL 196
Cdd:PRK09536 165 EPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDL 201
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
17-198 |
2.01e-15 |
|
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: 71.85 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 17 LSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLldgdfdgnYIFYDKKISFSNYNSTQ----ELRRLYfGYIFQDS-LI 90
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLaGL--------YKPTSGSVLLDGTDIRQldpaDLRRNI-GYVPQDVtLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 91 NERqdlIR-NILCSVDYS-----LQNNRRHLVNHFL--SVVGLSSRT-ESASVLSGGEKQRLALARALIKKPKILLADEP 161
Cdd:cd03245 91 YGT---LRdNITLGAPLAdderiLRAAELAGVTDFVnkHPNGLDLQIgERGRGLSGGQRQAVALARALLNDPPILLLDEP 167
|
170 180 190
....*....|....*....|....*....|....*..
gi 1372031259 162 TASLDRENKEKIMDIFKKFTnEGGTVVMVTHDLELID 198
Cdd:cd03245 168 TSAMDMNSEERLKERLRQLL-GDKTLIIITHRPSLLD 203
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
24-208 |
2.86e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 72.08 E-value: 2.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 24 IIEGGFYVITGPSGVGKSSLL---NIIGLLDgdfDGNYIFYDKKISFSNynsTQELRRLyFGYIFQDSlinERQDLIRNI 100
Cdd:PRK13647 28 IPEGSKTALLGPNGAGKSTLLlhlNGIYLPQ---RGRVKVMGREVNAEN---EKWVRSK-VGLVFQDP---DDQVFSSTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 101 LCSVDYSLQN--------NRRhlVNHFLSVVGLSSRTESASV-LSGGEKQRLALARALIKKPKILLADEPTASLDRENKE 171
Cdd:PRK13647 98 WDDVAFGPVNmgldkdevERR--VEEALKAVRMWDFRDKPPYhLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQE 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 1372031259 172 KIMDIFKKFTNEGGTVVMVTHDLELIDE-KIQVIRLNN 208
Cdd:PRK13647 176 TLMEILDRLHNQGKTVIVATHDVDLAAEwADQVIVLKE 213
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
32-176 |
3.24e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 72.13 E-value: 3.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 32 ITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKISFSNYN-STQELRrlyfgYIFQDSL--INERQDlIRNILcsvDYSL 108
Cdd:PRK15112 44 IIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSyRSQRIR-----MIFQDPStsLNPRQR-ISQIL---DFPL 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1372031259 109 QNN-------RRHLVNHFLSVVGLssRTESAS----VLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDI 176
Cdd:PRK15112 115 RLNtdlepeqREKQIIETLRQVGL--LPDHASyyphMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINL 191
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
13-194 |
3.63e-15 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 71.61 E-value: 3.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 13 DKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLD--------GD--FDGNYIfYDKKISfsnynsTQELRRlYF 81
Cdd:COG1117 23 DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnRMNDlipgarveGEilLDGEDI-YDPDVD------VVELRR-RV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 82 GYIFQ----------DslinerqdlirNILcsvdYSLQ----NNRRHL---VNHFLSVVGL----SSR-TESASVLSGGE 139
Cdd:COG1117 95 GMVFQkpnpfpksiyD-----------NVA----YGLRlhgiKSKSELdeiVEESLRKAALwdevKDRlKKSALGLSGGQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1372031259 140 KQRLALARALIKKPKILLADEPTASLDRENKEKIMDIF----KKFtneggTVVMVTHDL 194
Cdd:COG1117 160 QQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELIlelkKDY-----TIVIVTHNM 213
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
115-196 |
3.89e-15 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 71.77 E-value: 3.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 115 LVNHFLSVVGLSS-RTESASVLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHD 193
Cdd:TIGR03873 117 VVDRALARTELSHlADRDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDVRAQLETLALVRELAATGVTVVAALHD 196
|
...
gi 1372031259 194 LEL 196
Cdd:TIGR03873 197 LNL 199
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-192 |
5.57e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 71.03 E-value: 5.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 11 FRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLL-----DGDFDGNYIFYDKKISFSNYNSTQELRRLyfGYIF 85
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDPIEVRREV--GMVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 86 QDSLINERQDLIRNILCSVDYS-LQNNRRHL---VNHFLSVVGLSSRTES-----ASVLSGGEKQRLALARALIKKPKIL 156
Cdd:PRK14267 92 QYPNPFPHLTIYDNVAIGVKLNgLVKSKKELderVEWALKKAALWDEVKDrlndyPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 1372031259 157 LADEPTASLDRENKEKIMDIFKKFTNEgGTVVMVTH 192
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTH 206
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
9-193 |
6.40e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 71.98 E-value: 6.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 9 KEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKIsfsnyNSTQELRRlYFGYIFQDS 88
Cdd:PRK11000 11 KAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRM-----NDVPPAER-GVGMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 89 LINERQDLIRNI-----LCSVDYSLQNNRRHLVNHFLSVVGLSSRTESAsvLSGGEKQRLALARALIKKPKILLADEPTA 163
Cdd:PRK11000 85 ALYPHLSVAENMsfglkLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKA--LSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
|
170 180 190
....*....|....*....|....*....|....
gi 1372031259 164 SLDR----ENKEKIMDIFKKFtneGGTVVMVTHD 193
Cdd:PRK11000 163 NLDAalrvQMRIEISRLHKRL---GRTMIYVTHD 193
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
32-194 |
6.66e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 71.92 E-value: 6.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 32 ITGPSGVGKSSLLNIIGLLDGDFDGNyIFYDKKISFSNYNSTQELRRLYFGYIFQD---SLiNERQDlIRNILcsvDYSL 108
Cdd:PRK11308 46 VVGESGCGKSTLARLLTMIETPTGGE-LYYQGQDLLKADPEAQKLLRQKIQIVFQNpygSL-NPRKK-VGQIL---EEPL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 109 QNN-------RRHLVNHFLSVVGLssRTESAS----VLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIF 177
Cdd:PRK11308 120 LINtslsaaeRREKALAMMAKVGL--RPEHYDryphMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLM 197
|
170
....*....|....*...
gi 1372031259 178 KKFTNEGGTV-VMVTHDL 194
Cdd:PRK11308 198 MDLQQELGLSyVFISHDL 215
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
8-205 |
6.83e-15 |
|
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: 69.94 E-value: 6.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 8 KKEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLDgdFDGNYIFYDKKISFSNYNSTQELRRLYFGYIFQ 86
Cdd:cd03268 7 TKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIIlGLIK--PDSGEITFDGKSYQKNIEALRRIGALIEAPGFY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 87 DSLiNERQDLIRNilcSVDYSLQNNRrhlVNHFLSVVGLSSRT-ESASVLSGGEKQRLALARALIKKPKILLADEPTASL 165
Cdd:cd03268 85 PNL-TARENLRLL---ARLLGIRKKR---IDEVLDVVGLKDSAkKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1372031259 166 DRENKEKIMDIFKKFTNEGGTVVMVTH---DLELIDEKIQVIR 205
Cdd:cd03268 158 DPDGIKELRELILSLRDQGITVLISSHllsEIQKVADRIGIIN 200
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
8-199 |
9.05e-15 |
|
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: 70.09 E-value: 9.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 8 KKEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLDGDFDGNYIFydkkiSFSNYNSTQELRRlYFGYIFQ 86
Cdd:cd03265 7 VKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLtTLLKPTSGRATVA-----GHDVVREPREVRR-RIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 87 DSLINERQDLIRNILCSVD-YSLQNN-RRHLVNHFLSVVGL-SSRTESASVLSGGEKQRLALARALIKKPKILLADEPTA 163
Cdd:cd03265 81 DLSVDDELTGWENLYIHARlYGVPGAeRRERIDELLDFVGLlEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 1372031259 164 SLDRENKEKIMDIFKKFTNEGG-TVVMVTHDLELIDE 199
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEFGmTILLTTHYMEEAEQ 197
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
17-207 |
1.07e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 70.55 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 17 LSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKISFSNYnstQELRRlYFGYIFQDSlinERQDL 96
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNF---EKLRK-HIGIVFQNP---DNQFV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 97 IRNILCSVDYSLQNNR------RHLVNHFLSVVGLSSRTES-ASVLSGGEKQRLALARALIKKPKILLADEPTASLDREN 169
Cdd:PRK13648 98 GSIVKYDVAFGLENHAvpydemHRRVSEALKQVDMLERADYePNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDA 177
|
170 180 190
....*....|....*....|....*....|....*....
gi 1372031259 170 KEKIMDIFKKFTNEGG-TVVMVTHDLELIDEKIQVIRLN 207
Cdd:PRK13648 178 RQNLLDLVRKVKSEHNiTIISITHDLSEAMEADHVIVMN 216
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
17-197 |
1.08e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 70.65 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 17 LSDTCIEIIEGGFYVITGPSGVGKSSLL-NIIGLLDGDfDGNYIFYDKKISFSNyNSTQELRRlYFGYIFQDSlinERQD 95
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFqNLNGILKPS-SGRILFDGKPIDYSR-KGLMKLRE-SVGMVFQDP---DNQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 96 LIRNILCSVDYSLQNNR------RHLVNHFLSVVGLSS-RTESASVLSGGEKQRLALARALIKKPKILLADEPTASLDRE 168
Cdd:PRK13636 96 FSASVYQDVSFGAVNLKlpedevRKRVDNALKRTGIEHlKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPM 175
|
170 180 190
....*....|....*....|....*....|
gi 1372031259 169 NKEKIMDIFKKFTNEGG-TVVMVTHDLELI 197
Cdd:PRK13636 176 GVSEIMKLLVEMQKELGlTIIIATHDIDIV 205
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
8-195 |
1.27e-14 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 71.13 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 8 KKEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKISfsnyNSTQELRRLyfGYIFQD 87
Cdd:PRK09452 21 SKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT----HVPAENRHV--NTVFQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 88 SLINERQDLIRNilcsVDYSLQNNR------RHLVNHFLSVVGLSSRTES-ASVLSGGEKQRLALARALIKKPKILLADE 160
Cdd:PRK09452 95 YALFPHMTVFEN----VAFGLRMQKtpaaeiTPRVMEALRMVQLEEFAQRkPHQLSGGQQQRVAIARAVVNKPKVLLLDE 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 1372031259 161 PTASLDRENKEKIMDIFKKFTNEGG-TVVMVTHDLE 195
Cdd:PRK09452 171 SLSALDYKLRKQMQNELKALQRKLGiTFVFVTHDQE 206
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
26-204 |
1.28e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 70.49 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 26 EGGFYVITGPSGVGKSSL-LNIIGLLDGD-----FDGNYIFYDKKisfsnynSTQELRRLyFGYIFQDSlinERQDLIRN 99
Cdd:PRK13639 27 KGEMVALLGPNGAGKSTLfLHFNGILKPTsgevlIKGEPIKYDKK-------SLLEVRKT-VGIVFQNP---DDQLFAPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 100 ILCSVDYSLQN--------NRRhlVNHFLSVVGLSSRTESASV-LSGGEKQRLALARALIKKPKILLADEPTASLDRENK 170
Cdd:PRK13639 96 VEEDVAFGPLNlglskeevEKR--VKEALKAVGMEGFENKPPHhLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGA 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 1372031259 171 EKIMDIFKKFTNEGGTVVMVTHDLELID---EKIQVI 204
Cdd:PRK13639 174 SQIMKLLYDLNKEGITIIISTHDVDLVPvyaDKVYVM 210
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
2-195 |
1.41e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 70.19 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 2 ISLYINKKEfrdktILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLdGDFDGNY-----IFYDKKISFSNYNSTQEL 76
Cdd:PRK14239 11 LSVYYNKKK-----ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRM-NDLNPEVtitgsIVYNGHNIYSPRTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 77 RRlYFGYIFQdslinERQDLIRNILCSVDYSLQNN---RRHLVNHFL--SVVGLSSRTE-------SASVLSGGEKQRLA 144
Cdd:PRK14239 85 RK-EIGMVFQ-----QPNPFPMSIYENVVYGLRLKgikDKQVLDEAVekSLKGASIWDEvkdrlhdSALGLSGGQQQRVC 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1372031259 145 LARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEgGTVVMVTHDLE 195
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQ 208
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
34-197 |
1.48e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 71.27 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 34 GPSGVGKSS----LLNIIGLlDGD--FDGNyifydkkiSFSNYNSTQEL---RRLYFgyIFQD--SLINERQdlirNILC 102
Cdd:PRK15134 319 GESGSGKSTtglaLLRLINS-QGEiwFDGQ--------PLHNLNRRQLLpvrHRIQV--VFQDpnSSLNPRL----NVLQ 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 103 SVDYSLQNNRRHL--------VNHFLSVVGLS--SRTESASVLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEK 172
Cdd:PRK15134 384 IIEEGLRVHQPTLsaaqreqqVIAVMEEVGLDpeTRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQ 463
|
170 180
....*....|....*....|....*.
gi 1372031259 173 IMDIFKKFTNEGG-TVVMVTHDLELI 197
Cdd:PRK15134 464 ILALLKSLQQKHQlAYLFISHDLHVV 489
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
17-208 |
1.58e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 70.43 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 17 LSDTCIEIIEGGFYVITGPSGVGKSSLL-NIIGLLDGDfDGNYIFYDKKISFSNynsTQELRRlYFGYIFQDSlinERQD 95
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAkLLNGLLLPE-AGTITVGGMVLSEET---VWDVRR-QVGMVFQNP---DNQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 96 LIRNILCSVDYSLQNN--------RRhlVNHFLSVVGLSS-RTESASVLSGGEKQRLALARALIKKPKILLADEPTASLD 166
Cdd:PRK13635 95 VGATVQDDVAFGLENIgvpreemvER--VDQALRQVGMEDfLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1372031259 167 RENKEKIMDIFKKFTNEGG-TVVMVTHDLELIDEKIQVIRLNN 208
Cdd:PRK13635 173 PRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQADRVIVMNK 215
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
9-192 |
1.69e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 71.45 E-value: 1.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 9 KEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLDGD-FDGNYIFYDKKISfsnynsTQELRRLyfGYIFQ 86
Cdd:PLN03211 76 RQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALaGRIQGNnFTGTILANNRKPT------KQILKRT--GFVTQ 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 87 DSLI----NERQDLIRNILCSVDYSLQNNRRHLV-NHFLSVVGLSsRTESASV-------LSGGEKQRLALARALIKKPK 154
Cdd:PLN03211 148 DDILyphlTVRETLVFCSLLRLPKSLTKQEKILVaESVISELGLT-KCENTIIgnsfirgISGGERKRVSIAHEMLINPS 226
|
170 180 190
....*....|....*....|....*....|....*...
gi 1372031259 155 ILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTH 192
Cdd:PLN03211 227 LLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMH 264
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
9-195 |
1.87e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 70.63 E-value: 1.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 9 KEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLDGDfDGNYIFYDKKISfsnynSTQELRRLYFGYIFQ- 86
Cdd:PRK13536 49 KSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMIlGMTSPD-AGKITVLGVPVP-----ARARLARARIGVVPQf 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 87 DSLinERQDLIR-NILCSVDYSLQNNRR--HLVNHFLSVVGLSSRTES-ASVLSGGEKQRLALARALIKKPKILLADEPT 162
Cdd:PRK13536 123 DNL--DLEFTVReNLLVFGRYFGMSTREieAVIPSLLEFARLESKADArVSDLSGGMKRRLTLARALINDPQLLILDEPT 200
|
170 180 190
....*....|....*....|....*....|...
gi 1372031259 163 ASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLE 195
Cdd:PRK13536 201 TGLDPHARHLIWERLRSLLARGKTILLTTHFME 233
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
30-201 |
2.33e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 70.26 E-value: 2.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 30 YVITGPSGVGKSSLLN-IIGLLD---GDFDGNYIFYDKKISFSNYNST---------QELRRLyFGYIFQDSLINERQDL 96
Cdd:PRK13631 55 YFIIGNSGSGKSTLVThFNGLIKskyGTIQVGDIYIGDKKNNHELITNpyskkiknfKELRRR-VSMVFQFPEYQLFKDT 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 97 IRNILCSVDYSL---QNNRRHLVNHFLSVVGLSSR--TESASVLSGGEKQRLALARALIKKPKILLADEPTASLDRENKE 171
Cdd:PRK13631 134 IEKDIMFGPVALgvkKSEAKKLAKFYLNKMGLDDSylERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEH 213
|
170 180 190
....*....|....*....|....*....|....
gi 1372031259 172 KIMDIFKKFTNEGGTVVMVTHD----LELIDEKI 201
Cdd:PRK13631 214 EMMQLILDAKANNKTVFVITHTmehvLEVADEVI 247
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
13-193 |
3.04e-14 |
|
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: 70.35 E-value: 3.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 13 DKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDkkisfsNYNstqelrrlyFGYIFQDSLINE 92
Cdd:TIGR03719 17 KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQP------GIK---------VGYLPQEPQLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 93 RQDLIRNILCSVdyslqNNRRHLVNHFLSVVG------------------------------LSSRTESA---------- 132
Cdd:TIGR03719 82 TKTVRENVEEGV-----AEIKDALDRFNEISAkyaepdadfdklaaeqaelqeiidaadawdLDSQLEIAmdalrcppwd 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1372031259 133 ---SVLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTnegGTVVMVTHD 193
Cdd:TIGR03719 157 advTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYP---GTVVAVTHD 217
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
16-190 |
3.07e-14 |
|
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: 68.61 E-value: 3.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 16 ILSDTCIEIIEGGFYVITGPSGVGKSSLLN-IIGLLDGdFDGNYIFYDKKISFSnynSTQELRRLYFGYIFQDslinerq 94
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKtIMGLLPP-RSGSIRFDGRDITGL---PPHERARAGIGYVPEG------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 95 dliRNILcsvdyslqnnrrhlvnHFLSV-----VGLSSRTES-----------------------ASVLSGGEKQRLALA 146
Cdd:cd03224 84 ---RRIF----------------PELTVeenllLGAYARRRAkrkarlervyelfprlkerrkqlAGTLSGGEQQMLAIA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1372031259 147 RALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMV 190
Cdd:cd03224 145 RALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLV 188
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
9-209 |
3.16e-14 |
|
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: 70.62 E-value: 3.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 9 KEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLL--DGDFDGNYIFYDKKISFSNYNSTQelrRLYFGYIFQ 86
Cdd:TIGR02633 9 KTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNIRDTE---RAGIVIIHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 87 DSLINERQDLIRNILCSVDYSLQNNRRHL------VNHFLSVVGLSSRTESASV--LSGGEKQRLALARALIKKPKILLA 158
Cdd:TIGR02633 86 ELTLVPELSVAENIFLGNEITLPGGRMAYnamylrAKNLLRELQLDADNVTRPVgdYGGGQQQLVEIAKALNKQARLLIL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1372031259 159 DEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLE---LIDEKIQVIRLNNH 209
Cdd:TIGR02633 166 DEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNevkAVCDTICVIRDGQH 219
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
12-206 |
3.17e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 68.29 E-value: 3.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 12 RDKTIL-SDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLDGDfDGNyIFYDKkisfsnynstQELRR---------LY 80
Cdd:PRK13538 11 RDERILfSGLSFTLNAGELVQIEGPNGAGKTSLLRILaGLARPD-AGE-VLWQG----------EPIRRqrdeyhqdlLY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 81 FGY---IfqDSLINERQDLirNILCSVDYSLQNNRRHlvnHFLSVVGLSSRTE-SASVLSGGEKQRLALARALIKKPKIL 156
Cdd:PRK13538 79 LGHqpgI--KTELTALENL--RFYQRLHGPGDDEALW---EALAQVGLAGFEDvPVRQLSAGQQRRVALARLWLTRAPLW 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1372031259 157 LADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTH-DLELIDEKIQVIRL 206
Cdd:PRK13538 152 ILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTHqDLPVASDKVRKLRL 202
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
37-195 |
3.47e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 70.43 E-value: 3.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 37 GVGKSSLLNIIGlldgdfdGNY------IFYD-KKISFSnynSTQELRRLYFGYIFQD-SLINERqdlirnilcSVdysL 108
Cdd:COG1129 40 GAGKSTLMKILS-------GVYqpdsgeILLDgEPVRFR---SPRDAQAAGIAIIHQElNLVPNL---------SV---A 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 109 QN-------NRRHLVNH---------FLSVVGL--SSRTESASvLSGGEKQRLALARALIKKPKILLADEPTASLDRENK 170
Cdd:COG1129 98 ENiflgrepRRGGLIDWramrrrareLLARLGLdiDPDTPVGD-LSVAQQQLVEIARALSRDARVLILDEPTASLTEREV 176
|
170 180
....*....|....*....|....*
gi 1372031259 171 EKIMDIFKKFTNEGGTVVMVTHDLE 195
Cdd:COG1129 177 ERLFRIIRRLKAQGVAIIYISHRLD 201
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-209 |
4.04e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.60 E-value: 4.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 1 MISLYINKKEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLDGDfdgnyifydkkisfsnYNSTQELRRL 79
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVlGLVAPD----------------EGVIKRNGKL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 80 YFGYIFQD-------SLINERQDLIR------NILCSVDyslQNNRRHLVNHFLSVvglssrtesasvLSGGEKQRLALA 146
Cdd:PRK09544 68 RIGYVPQKlyldttlPLTVNRFLRLRpgtkkeDILPALK---RVQAGHLIDAPMQK------------LSGGETQRVLLA 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1372031259 147 RALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNE-GGTVVMVTHDLELIDEKI-QVIRLNNH 209
Cdd:PRK09544 133 RALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTdEVLCLNHH 197
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
12-204 |
4.67e-14 |
|
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: 70.13 E-value: 4.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 12 RDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIG----------LLDGDFDGNYIFYDKKISFSNYnsTQELrrlyf 81
Cdd:TIGR02203 343 RDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPrfyepdsgqiLLDGHDLADYTLASLRRQVALV--SQDV----- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 82 gYIFQDSLIN-----ERQDL----IRNILcsVDYSLQNNRRHLVNHFLSVVGlssrtESASVLSGGEKQRLALARALIKK 152
Cdd:TIGR02203 416 -VLFNDTIANniaygRTEQAdraeIERAL--AAAYAQDFVDKLPLGLDTPIG-----ENGVLLSGGQRQRLAIARALLKD 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1372031259 153 PKILLADEPTASLDRENKEKIMDIFKKFTnEGGTVVMVTHDLELIDEKIQVI 204
Cdd:TIGR02203 488 APILILDEATSALDNESERLVQAALERLM-QGRTTLVIAHRLSTIEKADRIV 538
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
13-208 |
5.34e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 68.60 E-value: 5.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 13 DKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLDGDfDGNYIFYDKKISFSNynsTQELRRLyFGYIFQDSlin 91
Cdd:PRK13650 19 EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIdGLLEAE-SGQIIIDGDLLTEEN---VWDIRHK-IGMVFQNP--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 92 ERQDLIRNILCSVDYSLQN------NRRHLVNHFLSVVGLSS-RTESASVLSGGEKQRLALARALIKKPKILLADEPTAS 164
Cdd:PRK13650 91 DNQFVGATVEDDVAFGLENkgipheEMKERVNEALELVGMQDfKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSM 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1372031259 165 LDRENKEKIMDIFKKFTNEGG-TVVMVTHDLELIDEKIQVIRLNN 208
Cdd:PRK13650 171 LDPEGRLELIKTIKGIRDDYQmTVISITHDLDEVALSDRVLVMKN 215
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
14-198 |
5.39e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 68.06 E-value: 5.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 14 KTILSDTCIEIIEGGFYVITGPSGVGKSSLLN-IIGLLDGDFDgnyifydkkisfsnyNSTQELRRLYFGyifQDSLINE 92
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRlLAGALKGTPV---------------AGCVDVPDNQFG---REASLID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 93 RQDLIRNILCSVDyslqnnrrhlvnhFLSVVGLSS----RTeSASVLSGGEKQRLALARALIKKPKILLADEPTASLDRE 168
Cdd:COG2401 105 AIGRKGDFKDAVE-------------LLNAVGLSDavlwLR-RFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180 190
....*....|....*....|....*....|.
gi 1372031259 169 NKEKIMDIFKKFTNEGG-TVVMVTHDLELID 198
Cdd:COG2401 171 TAKRVARNLQKLARRAGiTLVVATHHYDVID 201
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
14-192 |
8.85e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 69.31 E-value: 8.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 14 KTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDG---DFDGNYIFYDKKISfsnynsTQELRRLYfGYIFQDSL- 89
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNGMPID------AKEMRAIS-AYVQQDDLf 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 90 ---INERQDLIRNILCSVDYSL-QNNRRHLVNHFLSVVGLSS----RTESAS---VLSGGEKQRLALARALIKKPKILLA 158
Cdd:TIGR00955 111 iptLTVREHLMFQAHLRMPRRVtKKEKRERVDEVLQALGLRKcantRIGVPGrvkGLSGGERKRLAFASELLTDPPLLFC 190
|
170 180 190
....*....|....*....|....*....|....
gi 1372031259 159 DEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTH 192
Cdd:TIGR00955 191 DEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIH 224
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
34-195 |
1.25e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 67.50 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 34 GPSGVGKSSLL---NIIGLLDGDF--DGNYIFYDKKISFSNYNSTQELRRLyfGYIFQdslinERQDLIRNILCSVDYS- 107
Cdd:PRK14243 43 GPSGCGKSTILrcfNRLNDLIPGFrvEGKVTFHGKNLYAPDVDPVEVRRRI--GMVFQ-----KPNPFPKSIYDNIAYGa 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 108 ----LQNNRRHLVNHFLSVVGLSSRT-----ESASVLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFK 178
Cdd:PRK14243 116 ringYKGDMDELVERSLRQAALWDEVkdklkQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMH 195
|
170
....*....|....*..
gi 1372031259 179 KFtNEGGTVVMVTHDLE 195
Cdd:PRK14243 196 EL-KEQYTIIIVTHNMQ 211
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
8-192 |
1.57e-13 |
|
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: 66.91 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 8 KKEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLDGDfdgnYIFYDKkISFSNYNSTQELRRLYFGYIFQ 86
Cdd:cd03234 14 KNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsGRVEGG----GTTSGQ-ILFNGQPRKPDQFQKCVAYVRQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 87 D----SLINERQDLIRNILCSVDYSLQNNRRHLVNHF--LSVVGLSS-RTESASVLSGGEKQRLALARALIKKPKILLAD 159
Cdd:cd03234 89 DdillPGLTVRETLTYTAILRLPRKSSDAIRKKRVEDvlLRDLALTRiGGNLVKGISGGERRRVSIAVQLLWDPKVLILD 168
|
170 180 190
....*....|....*....|....*....|...
gi 1372031259 160 EPTASLDRENKEKIMDIFKKFTNEGGTVVMVTH 192
Cdd:cd03234 169 EPTSGLDSFTALNLVSTLSQLARRNRIVILTIH 201
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
16-197 |
1.61e-13 |
|
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: 66.87 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 16 ILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLldgdfdgnyiFYD---KKISFSNYN----STQELRRlYFGYIFQDS 88
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPR----------FYDvdsGRILIDGHDvrdyTLASLRR-QIGLVSQDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 89 -LINerqDLIRNilcSVDYSLQNNRRHLVNH-----------------FLSVVGlssrtESASVLSGGEKQRLALARALI 150
Cdd:cd03251 86 fLFN---DTVAE---NIAYGRPGATREEVEEaaraanahefimelpegYDTVIG-----ERGVKLSGGQRQRIAIARALL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1372031259 151 KKPKILLADEPTASLDRENKEKIMDIFKKFTnEGGTVVMVTHDLELI 197
Cdd:cd03251 155 KDPPILILDEATSALDTESERLVQAALERLM-KNRTTFVIAHRLSTI 200
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
32-205 |
1.96e-13 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 68.17 E-value: 1.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 32 ITGPSGVGKSSL-LNIIGLLDgdFDGNYIFYDKKISFSNYNSTQELRRlYFGYIFQD---SLiNERQ---DLIRNILCSV 104
Cdd:COG4172 317 LVGESGSGKSTLgLALLRLIP--SEGEIRFDGQDLDGLSRRALRPLRR-RMQVVFQDpfgSL-SPRMtvgQIIAEGLRVH 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 105 DYSLQ-NNRRHLVNHFLSVVGLSSRT------EsasvLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIF 177
Cdd:COG4172 393 GPGLSaAERRARVAEALEEVGLDPAArhryphE----FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLL 468
|
170 180
....*....|....*....|....*....
gi 1372031259 178 KKFTNEGG-TVVMVTHDLelidekiQVIR 205
Cdd:COG4172 469 RDLQREHGlAYLFISHDL-------AVVR 490
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
32-199 |
2.17e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 67.14 E-value: 2.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 32 ITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKISFSNynsTQELRRlYFGYIFQDSlinerQDLIRNILCSVDYSL--- 108
Cdd:PRK13652 35 VIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEN---IREVRK-FVGLVFQNP-----DDQIFSPTVEQDIAFgpi 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 109 -----QNNRRHLVNHFLSVVGLSS-RTESASVLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTN 182
Cdd:PRK13652 106 nlgldEETVAHRVSSALHMLGLEElRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPE 185
|
170
....*....|....*...
gi 1372031259 183 E-GGTVVMVTHDLELIDE 199
Cdd:PRK13652 186 TyGMTVIFSTHQLDLVPE 203
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
118-194 |
2.68e-13 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 66.36 E-value: 2.68e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1372031259 118 HFLSVVGLSSRTES-ASVLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDL 194
Cdd:COG4598 137 ALLAKVGLADKRDAyPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEM 214
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
5-206 |
2.70e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 66.96 E-value: 2.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 5 YINKKEFRDKTiLSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKISfSNYNSTQELRRLY--FG 82
Cdd:PRK13645 16 YAKKTPFEFKA-LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIP-ANLKKIKEVKRLRkeIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 83 YIFQDSLINERQDLIRNILCSVDYSLQNNRRHL---VNHFLSVVGLSSR--TESASVLSGGEKQRLALARALIKKPKILL 157
Cdd:PRK13645 94 LVFQFPEYQLFQETIEKDIAFGPVNLGENKQEAykkVPELLKLVQLPEDyvKRSPFELSGGQKRRVALAGIIAMDGNTLV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1372031259 158 ADEPTASLDRENKEKIMDIFKKFT-NEGGTVVMVTHDLElidekiQVIRL 206
Cdd:PRK13645 174 LDEPTGGLDPKGEEDFINLFERLNkEYKKRIIMVTHNMD------QVLRI 217
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
32-173 |
2.71e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 67.68 E-value: 2.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 32 ITGPSGVGKSSLLNiigLLDGDFD--GNYIFYD----KKISFsnynstQELRRlYFGYIFQDSLINER--QDLIRniLCS 103
Cdd:PRK13657 366 IVGPTGAGKSTLIN---LLQRVFDpqSGRILIDgtdiRTVTR------ASLRR-NIAVVFQDAGLFNRsiEDNIR--VGR 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 104 VDYSLQNNRRHLV------------NHFLSVVGlssrtESASVLSGGEKQRLALARALIKKPKILLADEPTASLDRENKE 171
Cdd:PRK13657 434 PDATDEEMRAAAEraqahdfierkpDGYDTVVG-----ERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEA 508
|
..
gi 1372031259 172 KI 173
Cdd:PRK13657 509 KV 510
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
26-204 |
2.95e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 67.07 E-value: 2.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 26 EGGFYVITGPSGVGKS-SLLNIIGLLDgdFDGNYIfyDKKISFSNYN----STQELRRLY---FGYIFQDSLINerqdli 97
Cdd:PRK11022 32 QGEVVGIVGESGSGKSvSSLAIMGLID--YPGRVM--AEKLEFNGQDlqriSEKERRNLVgaeVAMIFQDPMTS------ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 98 RNILCSVDYSL-----------QNNRRHLVNHFLSVVGLSSRTESASV----LSGGEKQRLALARALIKKPKILLADEPT 162
Cdd:PRK11022 102 LNPCYTVGFQImeaikvhqggnKKTRRQRAIDLLNQVGIPDPASRLDVyphqLSGGMSQRVMIAMAIACRPKLLIADEPT 181
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1372031259 163 ASLDRENKEKIMDIFKKFTN-EGGTVVMVTHDLELIDEKIQVI 204
Cdd:PRK11022 182 TALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKI 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
22-199 |
3.41e-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: 3.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 22 IEIIEGGFYVITGPSGVGKSSLLNII-GLLDGDfDGNYIFY--DKKISFSNYNSTQELR-RLYFGYIFQDSLINERQDLI 97
Cdd:TIGR03269 305 LEVKEGEIFGIVGTSGAGKTTLSKIIaGVLEPT-SGEVNVRvgDEWVDMTKPGPDGRGRaKRYIGILHQEYDLYPHRTVL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 98 RNILCSVDYSLQNN--RRHLVnHFLSVVGLSSRtESASVL-------SGGEKQRLALARALIKKPKILLADEPTASLDRE 168
Cdd:TIGR03269 384 DNLTEAIGLELPDElaRMKAV-ITLKMVGFDEE-KAEEILdkypdelSEGERHRVALAQVLIKEPRIVILDEPTGTMDPI 461
|
170 180 190
....*....|....*....|....*....|..
gi 1372031259 169 NKEKIMD-IFKKFTNEGGTVVMVTHDLELIDE 199
Cdd:TIGR03269 462 TKVDVTHsILKAREEMEQTFIIVSHDMDFVLD 493
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-194 |
3.41e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 66.66 E-value: 3.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 11 FRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKI---SFSNYNSTQELRRlYFGYIFQD 87
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLggrSIFNYRDVLEFRR-RVGMLFQR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 88 SliNE-RQDLIRNILCSVDYSLQNNR---RHLVNHFLSVVGL-----SSRTESASVLSGGEKQRLALARALIKKPKILLA 158
Cdd:PRK14271 110 P--NPfPMSIMDNVLAGVRAHKLVPRkefRGVAQARLTEVGLwdavkDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLL 187
|
170 180 190
....*....|....*....|....*....|....*.
gi 1372031259 159 DEPTASLDRENKEKIMDIFKKFTNEgGTVVMVTHDL 194
Cdd:PRK14271 188 DEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNL 222
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
133-193 |
3.63e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 67.45 E-value: 3.63e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1372031259 133 SVLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTnegGTVVMVTHD 193
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYP---GTVVAVTHD 219
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
8-166 |
3.77e-13 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 65.64 E-value: 3.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 8 KKEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLDGDfdgnyifyDKKISFSNYNSTQ----ELRRLYFG 82
Cdd:cd03218 7 SKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIvGLVKPD--------SGKILLDGQDITKlpmhKRARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 83 YIFQDSLINERQDLIRNILCSVD--YSLQNNRRHLVNHFLSVVGLSS-RTESASVLSGGEKQRLALARALIKKPKILLAD 159
Cdd:cd03218 79 YLPQEASIFRKLTVEENILAVLEirGLSKKEREEKLEELLEEFHITHlRKSKASSLSGGERRRVEIARALATNPKFLLLD 158
|
....*..
gi 1372031259 160 EPTASLD 166
Cdd:cd03218 159 EPFAGVD 165
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
13-205 |
3.98e-13 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 67.44 E-value: 3.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 13 DKTILSDTCIEIIEGGFYVITGPSGVGKSS----LLNIIG------LLDG----DFDGNYifYDKKISFSNynstQElrR 78
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTvaalLQNLYQptggqvLLDGvplvQYDHHY--LHRQVALVG----QE--P 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 79 LYFGYIFQDS----LINERQDLIRNI--LCSVDYSLQNnrrhLVNHFLSVVGlssrtESASVLSGGEKQRLALARALIKK 152
Cdd:TIGR00958 565 VLFSGSVRENiaygLTDTPDEEIMAAakAANAHDFIME----FPNGYDTEVG-----EKGSQLSGGQKQRIAIARALVRK 635
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1372031259 153 PKILLADEPTASLDRENkEKIMDIFKKFtnEGGTVVMVTHDLELID--EKIQVIR 205
Cdd:TIGR00958 636 PRVLILDEATSALDAEC-EQLLQESRSR--ASRTVLLIAHRLSTVEraDQILVLK 687
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
13-195 |
4.23e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 66.22 E-value: 4.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 13 DKTILSDTCIEIIEGGFYVITGPSGVGKSSLL-NIIGLLDGDfDGNYIFYDKKISFSNYNSTqELRRlYFGYIFQdslIN 91
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIqHLNGLLKPT-SGKIIIDGVDITDKKVKLS-DIRK-KVGLVFQ---YP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 92 ERQDLIRNILCSVDYSLQN--------NRRhlVNHFLSVVGLSSRT---ESASVLSGGEKQRLALARALIKKPKILLADE 160
Cdd:PRK13637 93 EYQLFEETIEKDIAFGPINlglseeeiENR--VKRAMNIVGLDYEDykdKSPFELSGGQKRRVAIAGVVAMEPKILILDE 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 1372031259 161 PTASLDRENKEKIMDIFKKFTNE-GGTVVMVTHDLE 195
Cdd:PRK13637 171 PTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSME 206
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
6-204 |
5.47e-13 |
|
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: 65.43 E-value: 5.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 6 INKKEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLL---DGDFD-GNYIFYDKKISFsnynstqeLRRly 80
Cdd:cd03267 26 LFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILsGLLqptSGEVRvAGLVPWKRRKKF--------LRR-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 81 FGYIFqdsliNERQDLIRNILCSVDYSL------------QNNRRHLVN-----HFLSVvglssrteSASVLSGGEKQRL 143
Cdd:cd03267 96 IGVVF-----GQKTQLWWDLPVIDSFYLlaaiydlpparfKKRLDELSElldleELLDT--------PVRQLSLGQRMRA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1372031259 144 ALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVT----HDLELIDEKIQVI 204
Cdd:cd03267 163 EIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTshymKDIEALARRVLVI 227
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
14-194 |
6.03e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 65.78 E-value: 6.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 14 KTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGnYIFYDKKiSFSNYNSTQELRRLyfGYIFQDSliNER 93
Cdd:PRK10253 20 YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHG-HVWLDGE-HIQHYASKEVARRI--GLLAQNA--TTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 94 QDL-IRNILCSVDYSLQ-------NNRRHLVNHFLSVVGLSS-RTESASVLSGGEKQRLALARALIKKPKILLADEPTAS 164
Cdd:PRK10253 94 GDItVQELVARGRYPHQplftrwrKEDEEAVTKAMQATGITHlADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190
....*....|....*....|....*....|.
gi 1372031259 165 LDRENKEKIMDIFKKFTNEGG-TVVMVTHDL 194
Cdd:PRK10253 174 LDISHQIDLLELLSELNREKGyTLAAVLHDL 204
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
6-195 |
6.11e-13 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 66.60 E-value: 6.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 6 INKKEFRDKTILS----DTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKISFSNYNSTQELRRLYF 81
Cdd:PRK10070 29 LSKEQILEKTGLSlgvkDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 82 GYIFQDSLINERQDLIRNILCSVDYS--LQNNRRHLVNHFLSVVGLSSRTES-ASVLSGGEKQRLALARALIKKPKILLA 158
Cdd:PRK10070 109 AMVFQSFALMPHMTVLDNTAFGMELAgiNAEERREKALDALRQVGLENYAHSyPDELSGGMRQRVGLARALAINPDILLM 188
|
170 180 190
....*....|....*....|....*....|....*...
gi 1372031259 159 DEPTASLDRENKEKIMDIFKKF-TNEGGTVVMVTHDLE 195
Cdd:PRK10070 189 DEAFSALDPLIRTEMQDELVKLqAKHQRTIVFISHDLD 226
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-208 |
6.76e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 65.44 E-value: 6.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 14 KTILSDTCIEIIEGGFYVITGPSGVGKSSL---LNIIGLLDGDF--DGNYIFYDKKISFSNYNsTQELRRlyfgyifQDS 88
Cdd:PRK14258 20 QKILEGVSMEIYQSKVTAIIGPSGCGKSTFlkcLNRMNELESEVrvEGRVEFFNQNIYERRVN-LNRLRR-------QVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 89 LINERQDLI-RNILCSVDYSLQNNRRH-------LVNHFLSVVGLSSRTE-----SASVLSGGEKQRLALARALIKKPKI 155
Cdd:PRK14258 92 MVHPKPNLFpMSVYDNVAYGVKIVGWRpkleiddIVESALKDADLWDEIKhkihkSALDLSGGQQQRLCIARALAVKPKV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1372031259 156 LLADEPTASLDRENKEKIMDIFKKFTNEGG-TVVMVTHDLElidekiQVIRLNN 208
Cdd:PRK14258 172 LLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNLH------QVSRLSD 219
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
135-194 |
1.01e-12 |
|
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: 66.00 E-value: 1.01e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 135 LSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTnEGGTVVMVTHDL 194
Cdd:COG5265 495 LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVA-RGRTTLVIAHRL 553
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
8-195 |
1.12e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 65.21 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 8 KKEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLN-IIGLLDGDfDGNYIFYDKKISfsnynSTQELRRLYFGYIFQ 86
Cdd:PRK13537 14 EKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRmLLGLTHPD-AGSISLCGEPVP-----SRARHARQRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 87 DSLINERQDLIRNILCSVDY---SLQNNRRhLVNHFLSVVGLSSRTES-ASVLSGGEKQRLALARALIKKPKILLADEPT 162
Cdd:PRK13537 88 FDNLDPDFTVRENLLVFGRYfglSAAAARA-LVPPLLEFAKLENKADAkVGELSGGMKRRLTLARALVNDPDVLVLDEPT 166
|
170 180 190
....*....|....*....|....*....|...
gi 1372031259 163 ASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLE 195
Cdd:PRK13537 167 TGLDPQARHLMWERLRSLLARGKTILLTTHFME 199
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
129-204 |
1.17e-12 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 64.05 E-value: 1.17e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1372031259 129 TESASVLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMD-IFKKFTNEggTVVMVTHDLE-LID-EKIQVI 204
Cdd:cd03244 134 EEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKtIREAFKDC--TVLTIAHRLDtIIDsDRILVL 210
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
34-194 |
1.33e-12 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 65.14 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 34 GPSGVGKSSLLN-IIGLLD---GD--FDGNYIFYdkkisfsnyNSTQELRRLY--FGYIFQD---SLiNERQdLIRNILc 102
Cdd:COG4608 51 GESGCGKSTLGRlLLRLEEptsGEilFDGQDITG---------LSGRELRPLRrrMQMVFQDpyaSL-NPRM-TVGDII- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 103 svDYSLQNN-------RRHLVNHFLSVVGLssRTESAS----VLSGGEKQRLALARALIKKPKILLADEPTASLDRENKE 171
Cdd:COG4608 119 --AEPLRIHglaskaeRRERVAELLELVGL--RPEHADryphEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQA 194
|
170 180
....*....|....*....|....
gi 1372031259 172 KIMDIFKKFTNEGG-TVVMVTHDL 194
Cdd:COG4608 195 QVLNLLEDLQDELGlTYLFISHDL 218
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
13-195 |
1.36e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 64.63 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 13 DKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKISFSNYNstqELRRlYFGYIFQDSlinE 92
Cdd:PRK13632 21 ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLK---EIRK-KIGIIFQNP---D 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 93 RQDLIRNILCSVDYSLQNNR------RHLVNHFLSVVGLSSRTE-SASVLSGGEKQRLALARALIKKPKILLADEPTASL 165
Cdd:PRK13632 94 NQFIGATVEDDIAFGLENKKvppkkmKDIIDDLAKKVGMEDYLDkEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSML 173
|
170 180 190
....*....|....*....|....*....|.
gi 1372031259 166 DRENKEKIMDIFKKFTNEGG-TVVMVTHDLE 195
Cdd:PRK13632 174 DPKGKREIKKIMVDLRKTRKkTLISITHDMD 204
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
4-199 |
1.56e-12 |
|
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: 63.11 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 4 LYINKKEFRDKTILSdtcIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGdfdgnyifydkkisfsnynstqelrrlyfgy 83
Cdd:cd03238 1 LTVSGANVHNLQNLD---VSIPLNVLVVVTGVSGSGKSTLVNEGLYASG------------------------------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 84 ifQDSLINERQDLIRNILCSVDySLQnnrrhlvnhFLSVVGLSSRT--ESASVLSGGEKQRLALARALIKKPK--ILLAD 159
Cdd:cd03238 47 --KARLISFLPKFSRNKLIFID-QLQ---------FLIDVGLGYLTlgQKLSTLSGGELQRVKLASELFSEPPgtLFILD 114
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1372031259 160 EPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLELIDE 199
Cdd:cd03238 115 EPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSS 154
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
136-194 |
2.65e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 64.36 E-value: 2.65e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 136 SGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGT-VVMVTHDL 194
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDL 222
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
32-194 |
2.65e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 63.71 E-value: 2.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 32 ITGPSGVGKSSLLNII-GLLDGDfdGNYIFYDKKISfsNYnSTQELRRL--Y-------------FGYI--FQDSLINER 93
Cdd:COG4138 27 LIGPNGAGKSTLLARMaGLLPGQ--GEILLNGRPLS--DW-SAAELARHraYlsqqqsppfampvFQYLalHQPAGASSE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 94 QDlirnilcsvdyslqnnrRHLVNHFLSVVGLSSR-TESASVLSGGEKQRLALARALIK-------KPKILLADEPTASL 165
Cdd:COG4138 102 AV-----------------EQLLAQLAEALGLEDKlSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSL 164
|
170 180
....*....|....*....|....*....
gi 1372031259 166 DRENKEKIMDIFKKFTNEGGTVVMVTHDL 194
Cdd:COG4138 165 DVAQQAALDRLLRELCQQGITVVMSSHDL 193
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
17-194 |
4.18e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 63.65 E-value: 4.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 17 LSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKISfsNYNSTQELR--RLYFGYIFQdslINERQ 94
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIT--HKTKDKYIRpvRKRIGMVFQ---FPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 95 DLIRNILCSVDYSLQNNRRHLVN------HFLSVVGLSSRTESAS--VLSGGEKQRLALARALIKKPKILLADEPTASLD 166
Cdd:PRK13646 98 LFEDTVEREIIFGPKNFKMNLDEvknyahRLLMDLGFSRDVMSQSpfQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180
....*....|....*....|....*....
gi 1372031259 167 RENKEKIMDIFKKF-TNEGGTVVMVTHDL 194
Cdd:PRK13646 178 PQSKRQVMRLLKSLqTDENKTIILVSHDM 206
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
8-192 |
4.47e-12 |
|
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: 63.06 E-value: 4.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 8 KKEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLN-IIGLLDGDfdgnyifyDKKISFSNYNST----QELRRLYFG 82
Cdd:TIGR04406 8 IKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYmIVGLVRPD--------AGKILIDGQDIThlpmHERARLGIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 83 YIFQDSLINERQDLIRNILCSVDYSL---QNNRRHLVNHFLSVVGLS-SRTESASVLSGGEKQRLALARALIKKPKILLA 158
Cdd:TIGR04406 80 YLPQEASIFRKLTVEENIMAVLEIRKdldRAEREERLEALLEEFQIShLRDNKAMSLSGGERRRVEIARALATNPKFILL 159
|
170 180 190
....*....|....*....|....*....|....
gi 1372031259 159 DEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTH 192
Cdd:TIGR04406 160 DEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDH 193
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
22-197 |
5.27e-12 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 63.02 E-value: 5.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 22 IEIIEGGFYVITGPSGVGKSSLLNII---GLldgdfdgNYIFYDKKISFSNYNSTQELRRLyfgyifqDSLINERQ---- 94
Cdd:cd03271 16 VDIPLGVLTCVTGVSGSGKSSLINDTlypAL-------ARRLHLKKEQPGNHDRIEGLEHI-------DKVIVIDQspig 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 95 --------------DLIRNILCSVDYSLQNNRRHL--------------------VNHFLSV------------VGLSSR 128
Cdd:cd03271 82 rtprsnpatytgvfDEIRELFCEVCKGKRYNRETLevrykgksiadvldmtveeaLEFFENIpkiarklqtlcdVGLGYI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1372031259 129 T--ESASVLSGGEKQRLALARALIKK---PKILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLELI 197
Cdd:cd03271 162 KlgQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVI 235
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
13-198 |
5.45e-12 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 62.16 E-value: 5.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 13 DKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGlldgdfdGN--YIFYDKKISFSNYN----STQELRRLYFGYIFQ 86
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIM-------GHpkYEVTEGEILFKGEDitdlPPEERARLGIFLAFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 87 DSlinERQDLIRNilcsvdyslqnnrrhlvNHFLSVVGLSsrtesasvLSGGEKQRLALARALIKKPKILLADEPTASLD 166
Cdd:cd03217 85 YP---PEIPGVKN-----------------ADFLRYVNEG--------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLD 136
|
170 180 190
....*....|....*....|....*....|..
gi 1372031259 167 RENKEKIMDIFKKFTNEGGTVVMVTHDLELID 198
Cdd:cd03217 137 IDALRLVAEVINKLREEGKSVLIITHYQRLLD 168
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
32-194 |
5.64e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 63.02 E-value: 5.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 32 ITGPSGVGKSSLLNII-GLLDGDfDGNYIFYDKKISFSNYN--STQELRRLY---FGYIFQDSL------------INER 93
Cdd:PRK11701 37 IVGESGSGKTTLLNALsARLAPD-AGEVHYRMRDGQLRDLYalSEAERRRLLrteWGFVHQHPRdglrmqvsaggnIGER 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 94 qdlirniLCSVDYSLQNNRRHLVNHFLSVVGL-SSRTESA-SVLSGGEKQRLALARALIKKPKILLADEPTASLDRENKE 171
Cdd:PRK11701 116 -------LMAVGARHYGDIRATAGDWLERVEIdAARIDDLpTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQA 188
|
170 180
....*....|....*....|....
gi 1372031259 172 KIMDIFKKFTNEGG-TVVMVTHDL 194
Cdd:PRK11701 189 RLLDLLRGLVRELGlAVVIVTHDL 212
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
135-195 |
1.52e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 62.74 E-value: 1.52e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1372031259 135 LSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLE 195
Cdd:COG3845 142 LSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLR 202
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
13-195 |
2.17e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 61.65 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 13 DKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKISFSNynsTQELRRlYFGYIFQDSlinE 92
Cdd:PRK13642 19 DVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAEN---VWNLRR-KIGMVFQNP---D 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 93 RQDLIRNILCSVDYSLQNN---RRHLVNH----FLSVVGLSSRTESASVLSGGEKQRLALARALIKKPKILLADEPTASL 165
Cdd:PRK13642 92 NQFVGATVEDDVAFGMENQgipREEMIKRvdeaLLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSML 171
|
170 180 190
....*....|....*....|....*....|.
gi 1372031259 166 DRENKEKIMDIFKKFTNEGG-TVVMVTHDLE 195
Cdd:PRK13642 172 DPTGRQEIMRVIHEIKEKYQlTVLSITHDLD 202
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
11-197 |
3.97e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.50 E-value: 3.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 11 FRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIG---LLDgdfDGNYIfYDKKISFSNYNstQELRRLYFGYIF-- 85
Cdd:PRK11147 13 FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNgevLLD---DGRII-YEQDLIVARLQ--QDPPRNVEGTVYdf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 86 -------QDSLINERQDLIRNILcsVDYS---------LQNNRRHL--------VNHFLSVVGLSSRTESASvLSGGEKQ 141
Cdd:PRK11147 87 vaegieeQAEYLKRYHDISHLVE--TDPSeknlnelakLQEQLDHHnlwqlenrINEVLAQLGLDPDAALSS-LSGGWLR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1372031259 142 RLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFtneGGTVVMVTHDLELI 197
Cdd:PRK11147 164 KAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTF---QGSIIFISHDRSFI 216
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
132-190 |
4.66e-11 |
|
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: 60.00 E-value: 4.66e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1372031259 132 ASVLSGGEKQRLALARALIKKPKILLADEPTASL-----DRenkekIMDIFKKFTNEGGTVVMV 190
Cdd:COG0410 134 AGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLaplivEE-----IFEIIRRLNREGVTILLV 192
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
9-194 |
5.43e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 59.91 E-value: 5.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 9 KEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSS-LLNIIGLLDGDfDGNYIFYDKKISFSnynSTQELRRLYFGYIFQD 87
Cdd:PRK10895 11 KAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTtFYMVVGIVPRD-AGNIIIDDEDISLL---PLHARARRGIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 88 SLINERQDLIRNILCSVDYS---LQNNRRHLVNHFLSVVGLSS-RTESASVLSGGEKQRLALARALIKKPKILLADEPTA 163
Cdd:PRK10895 87 ASIFRRLSVYDNLMAVLQIRddlSAEQREDRANELMEEFHIEHlRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190
....*....|....*....|....*....|.
gi 1372031259 164 SLDRENKEKIMDIFKKFTNEGGTVVMVTHDL 194
Cdd:PRK10895 167 GVDPISVIDIKRIIEHLRDSGLGVLITDHNV 197
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
135-208 |
5.66e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.20 E-value: 5.66e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1372031259 135 LSGGEKQRLALARALIKKPKILLADEPTASLDrENKEK-----IMDIFKKFTNeggTVVMVTHDLELIDEKIQVIRLNN 208
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLD-SNSEKliektIVDIKDKADK---TIITIAHRIASIKRSDKIVVFNN 1433
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-194 |
7.53e-11 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 59.71 E-value: 7.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 1 MISLY-INKKeFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIG-LLDGDfDGNyIFYDKKiSFSNYNSTQELRR 78
Cdd:COG4604 1 MIEIKnVSKR-YGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISrLLPPD-SGE-VLVDGL-DVATTPSRELAKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 79 LYfgyIF-QDSLINER---QDLI---RnilcsVDYS---LQNNRRHLVN---HFLSVVGLSSR--TEsasvLSGGEKQRL 143
Cdd:COG4604 77 LA---ILrQENHINSRltvRELVafgR-----FPYSkgrLTAEDREIIDeaiAYLDLEDLADRylDE----LSGGQRQRA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1372031259 144 ALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGG-TVVMVTHDL 194
Cdd:COG4604 145 FIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGkTVVIVLHDI 196
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
129-204 |
1.03e-10 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 58.58 E-value: 1.03e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1372031259 129 TESASVLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNeGGTVVMVTHDLE-LID-EKIQVI 204
Cdd:cd03369 120 SEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFT-NSTILTIAHRLRtIIDyDKILVM 196
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
135-197 |
1.21e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 60.10 E-value: 1.21e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1372031259 135 LSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNE-GGTVVMVTHDLELI 197
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIV 220
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
17-194 |
1.34e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 58.79 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 17 LSDTCI--EIIeggfYVItGPSGVGKSSLLN-IIGLLDGDfdGNYIFYDKkiSFSNYN-STQELRRLY------------ 80
Cdd:PRK03695 15 LSAEVRagEIL----HLV-GPNGAGKSTLLArMAGLLPGS--GSIQFAGQ--PLEAWSaAELARHRAYlsqqqtppfamp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 81 -FGY--IFQDSLINERQDlirnilcsvdyslqnnrRHLVNHFLSVVGLSSRTE-SASVLSGGEKQRLALARALIK----- 151
Cdd:PRK03695 86 vFQYltLHQPDKTRTEAV-----------------ASALNEVAEALGLDDKLGrSVNQLSGGEWQRVRLAAVVLQvwpdi 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1372031259 152 KP--KILLADEPTASLDREnKEKIMD-IFKKFTNEGGTVVMVTHDL 194
Cdd:PRK03695 149 NPagQLLLLDEPMNSLDVA-QQAALDrLLSELCQQGIAVVMSSHDL 193
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
10-196 |
1.54e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.04 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 10 EFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKISFSNYNSTQELrrlyfGYIFQDSL 89
Cdd:PRK13540 10 DYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQL-----CFVGHRSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 90 INERQDLIRNILCSVDYSLQNNRrhlVNHFLSVVGLSSRTE-SASVLSGGEKQRLALARALIKKPKILLADEPTASLDRE 168
Cdd:PRK13540 85 INPYLTLRENCLYDIHFSPGAVG---ITELCRLFSLEHLIDyPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDEL 161
|
170 180
....*....|....*....|....*....
gi 1372031259 169 NKEKIMDIFKKFTNEGGTVVMVTH-DLEL 196
Cdd:PRK13540 162 SLLTIITKIQEHRAKGGAVLLTSHqDLPL 190
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
135-198 |
1.61e-10 |
|
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: 59.80 E-value: 1.61e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1372031259 135 LSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVT-HDLELID 198
Cdd:COG1245 456 LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVdHDIYLID 520
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
27-195 |
1.79e-10 |
|
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: 58.15 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 27 GGFYVITGPSGVGKSSLLNII-GLLDGDfdgnyifyDKKISFSNYNSTQE----LRRLyfGYIFQDSLINERQDLIRNIL 101
Cdd:cd03266 31 GEVTGLLGPNGAGKTTTLRMLaGLLEPD--------AGFATVDGFDVVKEpaeaRRRL--GFVSDSTGLYDRLTARENLE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 102 CSVD-YSLQNNRRH-LVNHFLSVVG----LSSRTESasvLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMD 175
Cdd:cd03266 101 YFAGlYGLKGDELTaRLEELADRLGmeelLDRRVGG---FSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALRE 177
|
170 180
....*....|....*....|
gi 1372031259 176 IFKKFTNEGGTVVMVTHDLE 195
Cdd:cd03266 178 FIRQLRALGKCILFSTHIMQ 197
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
135-194 |
1.87e-10 |
|
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: 59.31 E-value: 1.87e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1372031259 135 LSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGT-VVMVTHDL 194
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMaLLLITHDL 217
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
12-199 |
1.99e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 59.35 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 12 RDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGlldgdfdGNYIFYDKKI-----SFSNYnSTQELRRlYFGYIFQ 86
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLM-------GYYPLTEGEIrldgrPLSSL-SHSVLRQ-GVAMVQQ 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 87 DSLINErQDLIRNILCSVDYSlqnnrRHLVNHFLSVV-----------GLSSRT-ESASVLSGGEKQRLALARALIKKPK 154
Cdd:PRK10790 423 DPVVLA-DTFLANVTLGRDIS-----EEQVWQALETVqlaelarslpdGLYTPLgEQGNNLSVGQKQLLALARVLVQTPQ 496
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1372031259 155 ILLADEPTASLDRENKEKIMDIFKKfTNEGGTVVMVTHDLELIDE 199
Cdd:PRK10790 497 ILILDEATANIDSGTEQAIQQALAA-VREHTTLVVIAHRLSTIVE 540
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
17-197 |
2.01e-10 |
|
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: 58.11 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 17 LSDTCIEIIEGGFYVITGPSGVGKSSLL-NIIGLLDgDFDGNYIFYDKKISFSNYNSTQELRRLYFGYIFQDS-LINERQ 94
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQ-TLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPwLLNATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 95 DliRNILCSVDYSLQnnRRHLVNHFLS------VVGLSSRTESASV---LSGGEKQRLALARALIKKPKILLADEPTASL 165
Cdd:cd03290 96 E--ENITFGSPFNKQ--RYKAVTDACSlqpdidLLPFGDQTEIGERginLSGGQRQRICVARALYQNTNIVFLDDPFSAL 171
|
170 180 190
....*....|....*....|....*....|....
gi 1372031259 166 DRENKEKIMD--IFKKFTNEGGTVVMVTHDLELI 197
Cdd:cd03290 172 DIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYL 205
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
135-198 |
2.03e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.19 E-value: 2.03e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1372031259 135 LSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIfkkFTNEGGTVVMVTHDLELID 198
Cdd:PRK11147 441 LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEEL---LDSYQGTVLLVSHDRQFVD 501
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
13-194 |
2.22e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 58.62 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 13 DKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIG-LLDGD-----FDGNYIfydKKISFSN-YNSTQELRRLY-FGYI 84
Cdd:PRK11831 19 NRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGgQIAPDhgeilFDGENI---PAMSRSRlYTVRKRMSMLFqSGAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 85 FQDslinerqdliRNILCSVDYSLqnnRRH----------LVNHFLSVVGLSSRTE-SASVLSGGEKQRLALARALIKKP 153
Cdd:PRK11831 96 FTD----------MNVFDNVAYPL---REHtqlpapllhsTVMMKLEAVGLRGAAKlMPSELSGGMARRAALARAIALEP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1372031259 154 KILLADEPTASLDrenkEKIMDIFKKFTNE-----GGTVVMVTHDL 194
Cdd:PRK11831 163 DLIMFDEPFVGQD----PITMGVLVKLISElnsalGVTCVVVSHDV 204
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
22-192 |
3.17e-10 |
|
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: 58.99 E-value: 3.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 22 IEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDG-------NYIFYdkkISFSNYNSTQELRRlyfGYIFQDSLINER- 93
Cdd:TIGR00954 473 FEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGrltkpakGKLFY---VPQRPYMTLGTLRD---QIIYPDSSEDMKr 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 94 -----QDLIRnILCSVD--YSLQNNrrhlvnhflsvVGLSSRTESASVLSGGEKQRLALARALIKKPKILLADEPTA--S 164
Cdd:TIGR00954 547 rglsdKDLEQ-ILDNVQltHILERE-----------GGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSavS 614
|
170 180
....*....|....*....|....*...
gi 1372031259 165 LDRENKekimdIFKKFTNEGGTVVMVTH 192
Cdd:TIGR00954 615 VDVEGY-----MYRLCREFGITLFSVSH 637
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
12-208 |
3.32e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.89 E-value: 3.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 12 RDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLL----DGDF---------DGNYIFYDKKIS--------FSN- 69
Cdd:PTZ00265 396 KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLydptEGDIiindshnlkDINLKWWRSKIGvvsqdpllFSNs 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 70 ------YN--STQELRRL--YFGYIFQDSLINERQDLIRNILCSVDYSLQNN--------------------------RR 113
Cdd:PTZ00265 476 iknnikYSlySLKDLEALsnYYNEDGNDSQENKNKRNSCRAKCAGDLNDMSNttdsneliemrknyqtikdsevvdvsKK 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 114 HLVNHFLSVVGLSSRT---ESASVLSGGEKQRLALARALIKKPKILLADEPTASLDRENK---EKIMDIFKKftNEGGTV 187
Cdd:PTZ00265 556 VLIHDFVSALPDKYETlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEylvQKTINNLKG--NENRIT 633
|
250 260
....*....|....*....|.
gi 1372031259 188 VMVTHDLELIDEKIQVIRLNN 208
Cdd:PTZ00265 634 IIIAHRLSTIRYANTIFVLSN 654
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
135-198 |
3.86e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 58.67 E-value: 3.86e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1372031259 135 LSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFT-NEGGTVVMVTHDLELID 198
Cdd:PRK13409 454 LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAeEREATALVVDHDIYMID 518
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
32-197 |
3.90e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 58.72 E-value: 3.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 32 ITGPSGVGKSSLLNIIGlldGDFdgnyifydKKISFSNYNSTQeLRRLYFGYIFQDSLINERQDLIRNILCSVDYSLQNN 111
Cdd:PLN03073 540 MVGPNGIGKSTILKLIS---GEL--------QPSSGTVFRSAK-VRMAVFSQHHVDGLDLSSNPLLYMMRCFPGVPEQKL 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 112 RRHLVNhfLSVVGlSSRTESASVLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFtnEGGtVVMVT 191
Cdd:PLN03073 608 RAHLGS--FGVTG-NLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLF--QGG-VLMVS 681
|
....*.
gi 1372031259 192 HDLELI 197
Cdd:PLN03073 682 HDEHLI 687
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
126-197 |
3.94e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 58.49 E-value: 3.94e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1372031259 126 SSRTESASVLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDL-ELI 197
Cdd:COG1129 386 PSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELpELL 458
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
16-207 |
5.30e-10 |
|
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: 58.21 E-value: 5.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 16 ILSDTCIEIIEGGFYVITGPSGVGKSSLLNiigLLDGDFDGNYifydKKISFSNYN----STQELRRlYFGYIFQDSLIN 91
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAK---LLVGFFQARS----GEILLNGFSlkdiDRHTLRQ-FINYLPQEPYIF 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 92 ErQDLIRNILcsvdysLQNNRRHLVNHFLSVVGL---------------SSRTESASVLSGGEKQRLALARALIKKPKIL 156
Cdd:TIGR01193 561 S-GSILENLL------LGAKENVSQDEIWAACEIaeikddienmplgyqTELSEEGSSISGGQKQRIALARALLTDSKVL 633
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1372031259 157 LADEPTASLDRENKEKIMDIFKKFTNEggTVVMVTHDLELIDEKIQVIRLN 207
Cdd:TIGR01193 634 ILDESTSNLDTITEKKIVNNLLNLQDK--TIIFVAHRLSVAKQSDKIIVLD 682
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
131-197 |
6.79e-10 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 57.73 E-value: 6.79e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1372031259 131 SASVLSGGEKQRLALARALIKKPK-----ILlaDEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLELI 197
Cdd:COG0178 823 PATTLSGGEAQRVKLASELSKRSTgktlyIL--DEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHNLDVI 892
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
13-199 |
7.06e-10 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 56.61 E-value: 7.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 13 DKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GlldgdfDGNYIFYDKKISFSNYN----STQELRRLYFGYIFQD 87
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmG------HPKYEVTSGSILLDGEDilelSPDERARAGIFLAFQY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 88 -------SLINerqdLIRNILCSVDYSLQNNR--RHLVNHFLSVVGLSSRTESASV---LSGGEKQRLALARALIKKPKI 155
Cdd:COG0396 86 pveipgvSVSN----FLRTALNARRGEELSARefLKLLKEKMKELGLDEDFLDRYVnegFSGGEKKRNEILQMLLLEPKL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1372031259 156 LLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLELIDE 199
Cdd:COG0396 162 AILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQRILDY 205
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
135-199 |
7.13e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 57.04 E-value: 7.13e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1372031259 135 LSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLELIDE 199
Cdd:COG4152 130 LSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEE 194
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
131-197 |
1.19e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.21 E-value: 1.19e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1372031259 131 SASVLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTnegGTVVMVTHDLELI 197
Cdd:PRK15064 435 SVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYE---GTLIFVSHDREFV 498
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
136-208 |
1.19e-09 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 56.64 E-value: 1.19e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1372031259 136 SGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGG-TVVMVTHDLEL---IDEKIQVIRLNN 208
Cdd:PRK15079 163 SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGlSLIFIAHDLAVvkhISDRVLVMYLGH 239
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
9-197 |
1.21e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.10 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 9 KEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKISFSNYNSTQELRrlyFGYIFQD- 87
Cdd:PRK09700 13 KSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLG---IGIIYQEl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 88 SLINERQdLIRNI---------LCSVDYSLQNNRRHLVNHFLSVVGLS-SRTESASVLSGGEKQRLALARALIKKPKILL 157
Cdd:PRK09700 90 SVIDELT-VLENLyigrhltkkVCGVNIIDWREMRVRAAMMLLRVGLKvDLDEKVANLSISHKQMLEIAKTLMLDAKVII 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1372031259 158 ADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLELI 197
Cdd:PRK09700 169 MDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEI 208
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
15-199 |
1.28e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 56.43 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 15 TILSDTCIEIIEGGFYVITGPSGVGKSSL----LNIIGLLDGDfdgnyifydkkISFSNYNSTQELRRLYFGYIFQdsli 90
Cdd:PRK15056 21 TALRDASFTVPGGSIAALVGVNGSGKSTLfkalMGFVRLASGK-----------ISILGQPTRQALQKNLVAYVPQ---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 91 NERQD-----LIRNILCSVDYS-------LQNNRRHLVNHFLSVVGLSS-RTESASVLSGGEKQRLALARALIKKPKILL 157
Cdd:PRK15056 86 SEEVDwsfpvLVEDVVMMGRYGhmgwlrrAKKRDRQIVTAALARVDMVEfRHRQIGELSGGQKKRVFLARAIAQQGQVIL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1372031259 158 ADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLELIDE 199
Cdd:PRK15056 166 LDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTE 207
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
119-204 |
1.45e-09 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 55.73 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 119 FLSVVGLS--SRTESASVLSGGEKQRLALARALIKKPK--ILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDL 194
Cdd:cd03270 120 FLVDVGLGylTLSRSAPTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDE 199
|
90
....*....|
gi 1372031259 195 ELIDEKIQVI 204
Cdd:cd03270 200 DTIRAADHVI 209
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
130-197 |
1.59e-09 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 56.95 E-value: 1.59e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1372031259 130 ESASVLSGGEKQRLALARALIKK---PKILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLELI 197
Cdd:TIGR00630 825 QPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVI 895
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
128-190 |
1.73e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 55.66 E-value: 1.73e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1372031259 128 RTESASVLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMV 190
Cdd:PRK11614 131 RIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLV 193
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
14-208 |
2.07e-09 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 54.29 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 14 KTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGdfdgnyifydkkisfsnYNSTQELRRLYFGyifqdsliner 93
Cdd:cd03227 8 PSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALG-----------------GAQSATRRRSGVK----------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 94 qdlIRNILCSVDYSLQnnrrhlvnhfLSVVGLSsrtesasvlsGGEKQRLALARALI---KKPKILLA-DEPTASLDREN 169
Cdd:cd03227 60 ---AGCIVAAVSAELI----------FTRLQLS----------GGEKELSALALILAlasLKPRPLYIlDEIDRGLDPRD 116
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1372031259 170 KEKIMDIFKKFTNEGGTVVMVTHDLELI---DEKIQVIRLNN 208
Cdd:cd03227 117 GQALAEAILEHLVKGAQVIVITHLPELAelaDKLIHIKKVIT 158
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
127-194 |
2.10e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.17 E-value: 2.10e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1372031259 127 SRTESASVLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDL 194
Cdd:PRK10762 388 SMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEM 455
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
118-204 |
2.43e-09 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 55.38 E-value: 2.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 118 HFLSVVGLSS-RTESASVLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGG-TVVMVTHDLE 195
Cdd:PRK11300 136 TWLERVGLLEhANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNvTVLLIEHDMK 215
|
90
....*....|..
gi 1372031259 196 L---IDEKIQVI 204
Cdd:PRK11300 216 LvmgISDRIYVV 227
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
135-198 |
3.60e-09 |
|
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: 54.72 E-value: 3.60e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1372031259 135 LSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFT-NEGGTVVMVTHDLELID 198
Cdd:cd03237 116 LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAeNNEKTAFVVEHDIIMID 180
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
32-206 |
3.64e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 55.63 E-value: 3.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 32 ITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDKKISFSNYNSTQELRRlYFGYIFQD--SLINERQDLIRNIL--CSVDYS 107
Cdd:PRK10261 355 LVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRR-DIQFIFQDpyASLDPRQTVGDSIMepLRVHGL 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 108 LQNNR-RHLVNHFLSVVGLssRTESA----SVLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTN 182
Cdd:PRK10261 434 LPGKAaAARVAWLLERVGL--LPEHAwrypHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQR 511
|
170 180
....*....|....*....|....*...
gi 1372031259 183 EGG-TVVMVTHDL---ELIDEKIQVIRL 206
Cdd:PRK10261 512 DFGiAYLFISHDMavvERISHRVAVMYL 539
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
13-170 |
3.78e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.41 E-value: 3.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 13 DKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIgllDGDFDGNY-----IF----------YD--KKISfsnYNSTQe 75
Cdd:PRK10938 272 DRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI---TGDHPQGYsndltLFgrrrgsgetiWDikKHIG---YVSSS- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 76 lrrLYFGYIFQDSlinerqdlIRNILCS-------VDYSLQNNRRHLVNHFLSVVGLSSRTESASV--LSGGEkQRLAL- 145
Cdd:PRK10938 345 ---LHLDYRVSTS--------VRNVILSgffdsigIYQAVSDRQQKLAQQWLDILGIDKRTADAPFhsLSWGQ-QRLALi 412
|
170 180
....*....|....*....|....*
gi 1372031259 146 ARALIKKPKILLADEPTASLDRENK 170
Cdd:PRK10938 413 VRALVKHPTLLILDEPLQGLDPLNR 437
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
133-198 |
4.84e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 55.18 E-value: 4.84e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1372031259 133 SVLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLELID 198
Cdd:COG1245 211 SELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDLAILD 276
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
135-198 |
6.63e-09 |
|
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: 53.34 E-value: 6.63e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1372031259 135 LSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGG-TVVMVTHDLELID 198
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKkTALVVEHDLAVLD 136
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
13-203 |
6.83e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.98 E-value: 6.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 13 DKTILSDTCIEIIEGGFYVITGPSGVGKSSLLN-IIGLLDGDFDGNYIF-----YDKKISFSnYNSTQElRRLYFGYIFQ 86
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIrgsvaYVPQVSWI-FNATVR-ENILFGSDFE 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 87 DSLINERQDLIrnilcsvdySLQNNRRHLVNHFLSVVGlssrtESASVLSGGEKQRLALARALIKKPKILLADEPTASLD 166
Cdd:PLN03232 707 SERYWRAIDVT---------ALQHDLDLLPGRDLTEIG-----ERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1372031259 167 RENKEKIMDIFKKFTNEGGTVVMVT---HDLELIDEKIQV 203
Cdd:PLN03232 773 AHVAHQVFDSCMKDELKGKTRVLVTnqlHFLPLMDRIILV 812
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-198 |
7.00e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 53.91 E-value: 7.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 26 EGGFYVITGPSGVGKSSLLNIiglLDGDFDGNYIFYDKKISF----SNYNSTqELRRlYFGYIFQDSL--INERQ--DLI 97
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKI---LAGKLKPNLGKFDDPPDWdeilDEFRGS-ELQN-YFTKLLEGDVkvIVKPQyvDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 98 --------RNILCSVDyslqnnRRHLVNHFLSVVGLSSRTESA-SVLSGGEKQRLALARALIKKPKILLADEPTASLDRE 168
Cdd:cd03236 100 pkavkgkvGELLKKKD------ERGKLDELVDQLELRHVLDRNiDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIK 173
|
170 180 190
....*....|....*....|....*....|
gi 1372031259 169 NKEKIMDIFKKFTNEGGTVVMVTHDLELID 198
Cdd:cd03236 174 QRLNAARLIRELAEDDNYVLVVEHDLAVLD 203
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
31-192 |
7.19e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 53.70 E-value: 7.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 31 VITGPSGVGKSSLLNII-GLLDGDfdgnyifyDKKISFSNYNSTQELRRLYFGYIfqDSLINERQDL--IRNI--LCSvd 105
Cdd:PRK13543 41 LVQGDNGAGKTTLLRVLaGLLHVE--------SGQIQIDGKTATRGDRSRFMAYL--GHLPGLKADLstLENLhfLCG-- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 106 ysLQNNR-RHLVNHFLSVVGLSSRTES-ASVLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNE 183
Cdd:PRK13543 109 --LHGRRaKQMPGSALAIVGLAGYEDTlVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHLRG 186
|
....*....
gi 1372031259 184 GGTVVMVTH 192
Cdd:PRK13543 187 GGAALVTTH 195
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
130-204 |
7.39e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 54.64 E-value: 7.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 130 ESASVLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKI---MDIFKKftneGGTVVMVTHDLELI---DEkIQV 203
Cdd:PRK11176 476 ENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIqaaLDELQK----NRTSLVIAHRLSTIekaDE-ILV 550
|
.
gi 1372031259 204 I 204
Cdd:PRK11176 551 V 551
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
135-206 |
7.49e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 7.49e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1372031259 135 LSGGEKQ------RLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLELIDEKIQVIRL 206
Cdd:PRK03918 789 LSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDEERRRKLVDIMERYLRKIPQVIIVSHDEELKDAADYVIRV 866
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
135-205 |
7.61e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.55 E-value: 7.61e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1372031259 135 LSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLELIDE---KIQVIR 205
Cdd:PRK13549 144 LGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAisdTICVIR 217
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
128-204 |
8.12e-09 |
|
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: 55.02 E-value: 8.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 128 RTESASVLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNeGGTVVMVTHDL---ELIDEKIQVI 204
Cdd:TIGR01257 1055 RNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMdeaDLLGDRIAII 1133
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
16-205 |
1.06e-08 |
|
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: 52.99 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 16 ILSDTCIEIIE--GGFYVITGPSGVGKSSLLNII-----GLLDGDFDGNyiFYDKKISFSNYNSTQElrRLYFgyifqdS 88
Cdd:cd03240 9 IRSFHERSEIEffSPLTLIVGQNGAGKTTIIEALkyaltGELPPNSKGG--AHDPKLIREGEVRAQV--KLAF------E 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 89 LINERQDLIR---NILCSVDYSLQNNRRHLVnhflsvvglssrTESASVLSGGEKQ------RLALARALIKKPKILLAD 159
Cdd:cd03240 79 NANGKKYTITrslAILENVIFCHQGESNWPL------------LDMRGRCSGGEKVlasliiRLALAETFGSNCGILALD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1372031259 160 EPTASLDRENKE-KIMDIFKKFTNEGG-TVVMVTHDLEL---IDEKIQVIR 205
Cdd:cd03240 147 EPTTNLDEENIEeSLAEIIEERKSQKNfQLIVITHDEELvdaADHIYRVEK 197
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
135-197 |
1.21e-08 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 53.76 E-value: 1.21e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1372031259 135 LSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFT-NEGGTVVMVTHDLELI 197
Cdd:COG4170 159 LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNqLQGTSILLISHDLESI 222
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
136-197 |
1.24e-08 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 53.16 E-value: 1.24e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1372031259 136 SGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLELI 197
Cdd:COG1134 148 SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAV 209
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
25-194 |
1.69e-08 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 52.32 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 25 IEGGFYVITGPSGVGKSSLLNIIGLL-------DGDFDGNYIFYDKK-----ISFSNYNSTQELRRLY------------ 80
Cdd:COG0419 21 FDDGLNLIVGPNGAGKSTILEAIRYAlygkarsRSKLRSDLINVGSEeasveLEFEHGGKRYRIERRQgefaefleakps 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 81 -----FGYIFQDSLINERQDLIRNILCSVDYSLQ--NNRRHLVNHFLSVVglsSRTESASVLSGGEKQRLALARALikkp 153
Cdd:COG0419 101 erkeaLKRLLGLEIYEELKERLKELEEALESALEelAELQKLKQEILAQL---SGLDPIETLSGGERLRLALADLL---- 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1372031259 154 kILLADepTASLDRENKEKIMDIFKKftneggtVVMVTHDL 194
Cdd:COG0419 174 -SLILD--FGSLDEERLERLLDALEE-------LAIITHVI 204
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
3-199 |
1.69e-08 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 53.56 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 3 SLYINKKEFR----DKTILSDTCIEIIEGGFYVITGPSGVGKSSLLniiGLLDGDFDgnyiFYDKKISFSNYNSTQ---- 74
Cdd:PRK10789 313 ELDVNIRQFTypqtDHPALENVNFTLKPGQMLGICGPTGSGKSTLL---SLIQRHFD----VSEGDIRFHDIPLTKlqld 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 75 ELR-RLYF----GYIFQDSLINE--------RQDLIRNI--LCSVDYSLQNnrrhLVNHFLSVVGlssrtESASVLSGGE 139
Cdd:PRK10789 386 SWRsRLAVvsqtPFLFSDTVANNialgrpdaTQQEIEHVarLASVHDDILR----LPQGYDTEVG-----ERGVMLSGGQ 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 140 KQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFtNEGGTVVMVTHDLELIDE 199
Cdd:PRK10789 457 KQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQW-GEGRTVIISAHRLSALTE 515
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
41-198 |
2.96e-08 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 52.78 E-value: 2.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 41 SSLLNIIGLLDGDFDGNYIFYDKKISFSNYNSTQELRRLYFGYIFQDSLINERQDLIR----------NILCSVDYSLQN 110
Cdd:pfam13304 133 SELSDLISGLLLLSIISPLSFLLLLDEGLLLEDWAVLDLAADLALFPDLKELLQRLVRglkladlnlsDLGEGIEKSLLV 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 111 NRRHLVNHFLSVVGLSSRTESASVLSGGEKQRLALARALI---KKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGTV 187
Cdd:pfam13304 213 DDRLRERGLILLENGGGGELPAFELSDGTKRLLALLAALLsalPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQL 292
|
170
....*....|.
gi 1372031259 188 VMVTHDLELID 198
Cdd:pfam13304 293 ILTTHSPLLLD 303
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-209 |
3.21e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 50.83 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 27 GGFYVITGPSGVGKSSLLNIIGlldgdfdgnyifydkkisfsnynstQELRRLYFGYIFQDSLINERQDLIRNILCSVDy 106
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALA-------------------------RELGPPGGGVIYIDGEDILEEVLDQLLLIIVG- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 107 slqnnrrhlvnhflsvvglssrtESASVLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDI------FKKF 180
Cdd:smart00382 56 -----------------------GKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrllLLLK 112
|
170 180
....*....|....*....|....*....
gi 1372031259 181 TNEGGTVVMVTHDLELIDEKIQVIRLNNH 209
Cdd:smart00382 113 SEKNLTVILTTNDEKDLGPALLRRRFDRR 141
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
119-197 |
3.21e-08 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 53.29 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 119 FLSVVGLSSRTESASV--LSGGEKQRLALAR----ALIKKPKILlaDEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTH 192
Cdd:PRK00635 459 ILIDLGLPYLTPERALatLSGGEQERTALAKhlgaELIGITYIL--DEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEH 536
|
....*
gi 1372031259 193 DLELI 197
Cdd:PRK00635 537 DEQMI 541
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
131-195 |
3.48e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 52.43 E-value: 3.48e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1372031259 131 SASVLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLE 195
Cdd:NF000106 141 AAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYME 205
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
135-197 |
4.07e-08 |
|
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: 51.76 E-value: 4.07e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1372031259 135 LSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLELI 197
Cdd:cd03220 143 YSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSI 205
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
135-199 |
6.11e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 52.17 E-value: 6.11e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1372031259 135 LSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGT-VVMVTHDLELIDE 199
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMgVIFITHDMGVVAE 234
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
9-205 |
7.41e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 51.71 E-value: 7.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 9 KEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLD-GDFDGNYIFYDKKISFSNYNST---------QELr 77
Cdd:NF040905 9 KTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLsGVYPhGSYEGEILFDGEVCRFKDIRDSealgiviihQEL- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 78 rlyfgyifqdSLI------------NERQDliRNIlcsVDYSLQNNR-RHLvnhfLSVVGLSsrtESASVLSG----GEK 140
Cdd:NF040905 88 ----------ALIpylsiaeniflgNERAK--RGV---IDWNETNRRaREL----LAKVGLD---ESPDTLVTdigvGKQ 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1372031259 141 QRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDL---ELIDEKIQVIR 205
Cdd:NF040905 146 QLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLneiRRVADSITVLR 213
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
129-197 |
8.07e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 51.71 E-value: 8.07e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1372031259 129 TESASVLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTnegGTVVMVTHDLELI 197
Cdd:PRK10636 425 TEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFE---GALVVVSHDRHLL 490
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
133-206 |
9.75e-08 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 51.75 E-value: 9.75e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1372031259 133 SVLSGGEKQRLALARALI---KKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLELIDEKIQVIRL 206
Cdd:PRK00635 808 SSLSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLEL 884
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
133-198 |
1.52e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.96 E-value: 1.52e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1372031259 133 SVLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTnEGGTVVMVTHDLELID 198
Cdd:PRK13409 211 SELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELA-EGKYVLVVEHDLAVLD 275
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
129-207 |
1.72e-07 |
|
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: 51.10 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 129 TESASVLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMD-IFKKFtnEGGTVVMVTHDLELIDEKIQVIRLN 207
Cdd:TIGR00957 1416 AEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQStIRTQF--EDCTVLTIAHRLNTIMDYTRVIVLD 1493
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
8-193 |
1.77e-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: 50.70 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 8 KKEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNYIFYDkkisfsnynsTQELrrlyfGYIFQ- 86
Cdd:TIGR03719 329 TKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGE----------TVKL-----AYVDQs 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 87 -DSL---------INERQDLIRniLCSVDYslqnNRRHLVNHFlSVVGlSSRTESASVLSGGEKQRLALARALIKKPKIL 156
Cdd:TIGR03719 394 rDALdpnktvweeISGGLDIIK--LGKREI----PSRAYVGRF-NFKG-SDQQKKVGQLSGGERNRVHLAKTLKSGGNVL 465
|
170 180 190
....*....|....*....|....*....|....*..
gi 1372031259 157 LADEPTASLDRENKEKIMDIFKKFtneGGTVVMVTHD 193
Cdd:TIGR03719 466 LLDEPTNDLDVETLRALEEALLNF---AGCAVVISHD 499
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
13-192 |
1.87e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 49.48 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 13 DKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIGLLDGDFDGNyIFYDKkisfsnyNSTQELRRLYFGYIFQDSLINE 92
Cdd:PRK13541 12 EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGN-IYYKN-------CNINNIAKPYCTYIGHNLGLKL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 93 RQDLIRNILCSVDYSLQNNRRHLVNHFLSVVGLSSrtESASVLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEK 172
Cdd:PRK13541 84 EMTVFENLKFWSEIYNSAETLYAAIHYFKLHDLLD--EKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDL 161
|
170 180
....*....|....*....|
gi 1372031259 173 IMDIFKKFTNEGGTVVMVTH 192
Cdd:PRK13541 162 LNNLIVMKANSGGIVLLSSH 181
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
132-195 |
2.71e-07 |
|
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: 50.40 E-value: 2.71e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1372031259 132 ASVLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLE 195
Cdd:TIGR01257 2068 AGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSME 2131
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
2-191 |
2.97e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.11 E-value: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 2 ISLYINKKEFRDKTILSDtCIEIIEGG-FYVITGPSGVGKSSLLNIIGlldGDFDGNYIFYDKKISFSNYnSTQELRRLY 80
Cdd:TIGR00956 62 FRKLKKFRDTKTFDILKP-MDGLIKPGeLTVVLGRPGSGCSTLLKTIA---SNTDGFHIGVEGVITYDGI-TPEEIKKHY 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 81 FGyifqDSLINERQDLIRNILcSVDYSLQ--------NNR----------RHLVNHFLSVVGLSsRTESASV-------L 135
Cdd:TIGR00956 137 RG----DVVYNAETDVHFPHL-TVGETLDfaarcktpQNRpdgvsreeyaKHIADVYMATYGLS-HTRNTKVgndfvrgV 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1372031259 136 SGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVT 191
Cdd:TIGR00956 211 SGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVA 266
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
119-204 |
3.25e-07 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 50.01 E-value: 3.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 119 FLSVVGLS--SRTESASVLSGGEKQRLALAR----ALIKKPKILlaDEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTH 192
Cdd:TIGR00630 471 FLIDVGLDylSLSRAAGTLSGGEAQRIRLATqigsGLTGVLYVL--DEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEH 548
|
90
....*....|..
gi 1372031259 193 DLELIDEKIQVI 204
Cdd:TIGR00630 549 DEDTIRAADYVI 560
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
26-204 |
3.57e-07 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 48.80 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 26 EGGFYVITGPSGVGKSSLLNIIglldgdfdgNYIFYDKKISFSNYNSTqelrrlyfgyifqDSLINERQDLIRnilcsVD 105
Cdd:cd03279 27 NNGLFLICGPTGAGKSTILDAI---------TYALYGKTPRYGRQENL-------------RSVFAPGEDTAE-----VS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 106 YSLQ-NNRRHLV--------NHFLSVV----GLSSR--TESASVLSGGEK------QRLALARALIKKPKI----LLADE 160
Cdd:cd03279 80 FTFQlGGKKYRVersrgldyDQFTRIVllpqGEFDRflARPVSTLSGGETflaslsLALALSEVLQNRGGArleaLFIDE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1372031259 161 PTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLEL---IDEKIQVI 204
Cdd:cd03279 160 GFGTLDPEALEAVATALELIRTENRMVGVISHVEELkerIPQRLEVI 206
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
135-194 |
4.93e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.16 E-value: 4.93e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 135 LSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDL 194
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSEL 465
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
109-196 |
5.09e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 48.63 E-value: 5.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 109 QNNRRHlVNHFLSVVGLSSRTES-ASVLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGG-T 186
Cdd:PRK10575 122 AADREK-VEEAISLVGLKPLAHRlVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGlT 200
|
90
....*....|
gi 1372031259 187 VVMVTHDLEL 196
Cdd:PRK10575 201 VIAVLHDINM 210
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
131-197 |
5.10e-07 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 49.30 E-value: 5.10e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1372031259 131 SASVLSGGEKQRLALARALIKKPK-----ILlaDEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLELI 197
Cdd:PRK00349 827 PATTLSGGEAQRVKLAKELSKRSTgktlyIL--DEPTTGLHFEDIRKLLEVLHRLVDKGNTVVVIEHNLDVI 896
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
135-194 |
5.77e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 48.54 E-value: 5.77e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1372031259 135 LSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGT-VVMVTHDL 194
Cdd:PRK10418 141 MSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALgMLLVTHDM 201
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
132-166 |
5.94e-07 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 48.49 E-value: 5.94e-07
10 20 30
....*....|....*....|....*....|....*
gi 1372031259 132 ASVLSGGEKQRLALARALIKKPKILLADEPTASLD 166
Cdd:COG1137 134 AYSLSGGERRRVEIARALATNPKFILLDEPFAGVD 168
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
135-194 |
6.03e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 49.05 E-value: 6.03e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 135 LSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDL 194
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSEL 463
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
135-195 |
6.35e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 48.54 E-value: 6.35e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1372031259 135 LSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVT-HDLE 195
Cdd:COG4586 155 LSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTsHDMD 216
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
134-199 |
8.54e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 48.75 E-value: 8.54e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1372031259 134 VLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKK-FTNegGTVVMVTHDLELIDE 199
Cdd:TIGR01271 1353 VLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQsFSN--CTVILSEHRVEALLE 1417
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
13-194 |
9.17e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.58 E-value: 9.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 13 DKTILSDTCIEIIEGGFYVITGPSGVGKSSLLN-IIGLLDGDFDGNYIF-----YDKKISFSnYNSTqeLR-RLYFGYIF 85
Cdd:PLN03130 629 ERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIrgtvaYVPQVSWI-FNAT--VRdNILFGSPF 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 86 QDSLINERQDLIrnilcsvdySLQNNRRHLVNHFLSVVGlssrtESASVLSGGEKQRLALARALIKKPKILLADEPTASL 165
Cdd:PLN03130 706 DPERYERAIDVT---------ALQHDLDLLPGGDLTEIG-----ERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSAL 771
|
170 180
....*....|....*....|....*....
gi 1372031259 166 DRENKEKIMDIFKKFTNEGGTVVMVTHDL 194
Cdd:PLN03130 772 DAHVGRQVFDKCIKDELRGKTRVLVTNQL 800
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
34-192 |
9.79e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 48.69 E-value: 9.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 34 GPSGVGKSSLLNIiglLDGDFDGNYIFYDKKISfsNYNSTQELRRLYFGYIFQDSL----INERQDLIRNILCSVDYSLQ 109
Cdd:PLN03140 913 GVSGAGKTTLMDV---LAGRKTGGYIEGDIRIS--GFPKKQETFARISGYCEQNDIhspqVTVRESLIYSAFLRLPKEVS 987
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 110 NNRR-----------HLVNHFLSVVGLSSRTEsasvLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFK 178
Cdd:PLN03140 988 KEEKmmfvdevmelvELDNLKDAIVGLPGVTG----LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVR 1063
|
170
....*....|....
gi 1372031259 179 KFTNEGGTVVMVTH 192
Cdd:PLN03140 1064 NTVDTGRTVVCTIH 1077
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
135-204 |
1.20e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 47.87 E-value: 1.20e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1372031259 135 LSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFT-NEGGTVVMVTHDLELID---EKIQVI 204
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNqNNNTTILLISHDLQMLSqwaDKINVL 232
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
129-198 |
1.31e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.24 E-value: 1.31e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 129 TESASVLSGGEKQRLALARALIKKPKILLADEPTASLDRenkEKIMDIFKKFTNEGGTVVMVTHDLELID 198
Cdd:PRK10636 144 ERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDL---DAVIWLEKWLKSYQGTLILISHDRDFLD 210
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
23-166 |
1.61e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 47.53 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 23 EIIEGGFYVITGPSGVGKSSLLNII-GL---LDGDfdgnyifydkkisfsnynstqelrrLYFGyifqDSLINERQDLIR 98
Cdd:PRK11650 26 DVADGEFIVLVGPSGCGKSTLLRMVaGLeriTSGE-------------------------IWIG----GRVVNELEPADR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 99 NILC-----------SV----DYSLQN--------NRRhlVNHFLSVVGLSS---RTESAsvLSGGEKQRLALARALIKK 152
Cdd:PRK11650 77 DIAMvfqnyalyphmSVrenmAYGLKIrgmpkaeiEER--VAEAARILELEPlldRKPRE--LSGGQRQRVAMGRAIVRE 152
|
170
....*....|....
gi 1372031259 153 PKILLADEPTASLD 166
Cdd:PRK11650 153 PAVFLFDEPLSNLD 166
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
130-197 |
1.63e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 47.74 E-value: 1.63e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1372031259 130 ESASVLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLELI 197
Cdd:PRK15439 399 QAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEI 466
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-197 |
2.71e-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: 47.25 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 22 IEIIEGGFYVITGPSGVGKSSLLNIiglLDGDFDGnyifYDKKISFSNYnstqelrrlyFGYIFQDSLInERQDLIRNIL 101
Cdd:TIGR00957 659 FSIPEGALVAVVGQVGCGKSSLLSA---LLAEMDK----VEGHVHMKGS----------VAYVPQQAWI-QNDSLRENIL 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 102 csVDYSLQNNRRHLVNHF------LSVVGLSSRTESASV---LSGGEKQRLALARALIKKPKILLADEPTASLDRENKEK 172
Cdd:TIGR00957 721 --FGKALNEKYYQQVLEAcallpdLEILPSGDRTEIGEKgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKH 798
|
170 180
....*....|....*....|....*..
gi 1372031259 173 IMD--IFKKFTNEGGTVVMVTHDLELI 197
Cdd:TIGR00957 799 IFEhvIGPEGVLKNKTRILVTHGISYL 825
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
134-199 |
2.92e-06 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 46.77 E-value: 2.92e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1372031259 134 VLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKfTNEGGTVVMVTHDLELIDE 199
Cdd:cd03289 138 VLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQ-AFADCTVILSEHRIEAMLE 202
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
135-194 |
3.20e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 46.83 E-value: 3.20e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 135 LSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDL 194
Cdd:PRK11288 397 LSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDL 456
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
135-194 |
3.27e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 46.70 E-value: 3.27e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 135 LSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDL 194
Cdd:PRK09700 410 LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSEL 469
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
10-197 |
4.37e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 46.70 E-value: 4.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 10 EFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLniiGLLDGDFD--GNYIFYDKKISFSN-----YNSTQELRRLYFg 82
Cdd:PTZ00243 669 ELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLL---QSLLSQFEisEGRVWAERSIAYVPqqawiMNATVRGNILFF- 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 83 yifqDSLINER-QDLIRnilCSvdySLQNNRRHLVNHFLSVVGlssrtESASVLSGGEKQRLALARALIKKPKILLADEP 161
Cdd:PTZ00243 745 ----DEEDAARlADAVR---VS---QLEADLAQLGGGLETEIG-----EKGVNLSGGQKARVSLARAVYANRDVYLLDDP 809
|
170 180 190
....*....|....*....|....*....|....*..
gi 1372031259 162 TASLDRENKEKIM-DIFKKFTnEGGTVVMVTHDLELI 197
Cdd:PTZ00243 810 LSALDAHVGERVVeECFLGAL-AGKTRVLATHQVHVV 845
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
132-195 |
7.40e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 45.79 E-value: 7.40e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1372031259 132 ASVLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLE 195
Cdd:COG3845 400 ARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLD 463
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
133-206 |
1.24e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.20 E-value: 1.24e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1372031259 133 SVLSGGEKQRLALARALI---KKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLELIDEKIQVIRL 206
Cdd:PRK00635 1698 SSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDPALLKQADYLIEM 1774
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
5-191 |
1.25e-05 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 44.18 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 5 YINKKEFRDKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLDGdfdgnYIFYDKKISFSNYNSTQelrrlyFGY 83
Cdd:cd03233 11 FTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALaNRTEG-----NVSVEGDIHYNGIPYKE------FAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 84 IFQDSLINERQDLIRNILCSVDYSLQNNRRHLVNHFLSVVglssrtesasvlSGGEKQRLALARALIKKPKILLADEPTA 163
Cdd:cd03233 80 KYPGEIIYVSEEDVHFPTLTVRETLDFALRCKGNEFVRGI------------SGGERKRVSIAEALVSRASVLCWDNSTR 147
|
170 180
....*....|....*....|....*...
gi 1372031259 164 SLDRENKEKIMDIFKKFTNEGGTVVMVT 191
Cdd:cd03233 148 GLDSSTALEILKCIRTMADVLKTTTFVS 175
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
133-196 |
1.64e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 44.43 E-value: 1.64e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1372031259 133 SVLSGGEKQRLALARAL---------IKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGT-VVMVTHDLEL 196
Cdd:PRK13547 144 TTLSGGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHDPNL 217
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
13-198 |
1.75e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 44.25 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 13 DKTILSDTCIEIIEGGFYVITGPSGVGKSSLLNIIG------LLDGDFdgnyIFYDKKISfsnyNSTQELRR-----LYF 81
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAghpaykILEGDI----LFKGESIL----DLEPEERAhlgifLAF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 82 GYIFQDSLINErQDLIRNILCSVDYSLQNNRR------HLVNHFLSVVGLSSRTESASV---LSGGEKQRLALARALIKK 152
Cdd:CHL00131 91 QYPIEIPGVSN-ADFLRLAYNSKRKFQGLPELdpleflEIINEKLKLVGMDPSFLSRNVnegFSGGEKKRNEILQMALLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1372031259 153 PKILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLELID 198
Cdd:CHL00131 170 SELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLD 215
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
132-193 |
1.87e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 44.72 E-value: 1.87e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1372031259 132 ASVLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFtneGGTVVMVTHD 193
Cdd:PRK11819 443 VGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEF---PGCAVVISHD 501
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-208 |
2.36e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 44.52 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 16 ILSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLDGDfDGNyIFYDKKISFSNYNSTqelrrLYFGYIFQDSLINERQ 94
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMImGELEPS-EGK-IKHSGRISFSPQTSW-----IMPGTIKDNIIFGLSY 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 95 DLIRNILCSVDYSLQNNRRHLVNHFLSVVGlssrtESASVLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIM 174
Cdd:TIGR01271 514 DEYRYTSVIKACQLEEDIALFPEKDKTVLG-----EGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIF 588
|
170 180 190
....*....|....*....|....*....|....*.
gi 1372031259 175 D--IFKKFTNEggTVVMVTHDLELIDEKIQVIRLNN 208
Cdd:TIGR01271 589 EscLCKLMSNK--TRILVTSKLEHLKKADKILLLHE 622
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
32-204 |
2.57e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 44.58 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 32 ITGPSGVGKSSLLN----IIGLLDGdfdgnyifydkKISFSNYNSTQ----ELRRLYfgyifqdSLINERQDLIR-NILC 102
Cdd:PLN03232 1267 VVGRTGAGKSSMLNalfrIVELEKG-----------RIMIDDCDVAKfgltDLRRVL-------SIIPQSPVLFSgTVRF 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 103 SVDYSLQNNRRHLVN-----HFLSVVGLSSRTESASVLSGGE------KQRLALARALIKKPKILLADEPTASLDRENKE 171
Cdd:PLN03232 1329 NIDPFSEHNDADLWEaleraHIKDVIDRNPFGLDAEVSEGGEnfsvgqRQLLSLARALLRRSKILVLDEATASVDVRTDS 1408
|
170 180 190
....*....|....*....|....*....|....*.
gi 1372031259 172 KIM-DIFKKFtnEGGTVVMVTHDLE-LID-EKIQVI 204
Cdd:PLN03232 1409 LIQrTIREEF--KSCTMLVIAHRLNtIIDcDKILVL 1442
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
118-197 |
2.97e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 44.25 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 118 HFLSVVGLS----SRteSASVLSGGEKQRLALARALikk----pkILlaDEPTASL-DRENkEKIMDIFKKFTNEGGTVV 188
Cdd:COG0178 467 GFLVDVGLDyltlDR--SAGTLSGGEAQRIRLATQIgsglvgvlyVL--DEPSIGLhQRDN-DRLIETLKRLRDLGNTVI 541
|
....*....
gi 1372031259 189 MVTHDLELI 197
Cdd:COG0178 542 VVEHDEDTI 550
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
74-208 |
3.10e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 44.00 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 74 QELRRLyFGYIFQDSLINE---RQDlirnilcsVDYSLQNNRRHlVNHFLSVVGLSSRTESAS------VLSGG------ 138
Cdd:PTZ00243 1380 RELRRQ-FSMIPQDPVLFDgtvRQN--------VDPFLEASSAE-VWAALELVGLRERVASESegidsrVLEGGsnysvg 1449
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1372031259 139 EKQRLALARALIKK-PKILLADEPTAS----LDRENKEKIMDIFKKFtneggTVVMVTHDLELIDEKIQVIRLNN 208
Cdd:PTZ00243 1450 QRQLMCMARALLKKgSGFILMDEATANidpaLDRQIQATVMSAFSAY-----TVITIAHRLHTVAQYDKIIVMDH 1519
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-208 |
3.64e-05 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 43.31 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 16 ILSDTCIEIIEGGFYVITGPSGVGKSSLL-NIIGLLDGDfdGNYIFYDKKISFSNYnstqelrrlyFGYIFQDSlINErq 94
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLmLILGELEPS--EGKIKHSGRISFSSQ----------FSWIMPGT-IKE-- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 95 dlirNILCSVDY------------SLQNNRRHLVNHFLSVVGlssrtESASVLSGGEKQRLALARALIKKPKILLADEPT 162
Cdd:cd03291 117 ----NIIFGVSYdeyryksvvkacQLEEDITKFPEKDNTVLG-----EGGITLSGGQRARISLARAVYKDADLYLLDSPF 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1372031259 163 ASLDRENKEKIMD--IFKKFTNEggTVVMVTHDLELIDEKIQVIRLNN 208
Cdd:cd03291 188 GYLDVFTEKEIFEscVCKLMANK--TRILVTSKMEHLKKADKILILHE 233
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
128-166 |
4.45e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.70 E-value: 4.45e-05
10 20 30
....*....|....*....|....*....|....*....
gi 1372031259 128 RTESASVLSGGEKQRLALARALIKKPKILLADEPTASLD 166
Cdd:PLN03073 338 QVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
9-192 |
4.50e-05 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 42.45 E-value: 4.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 9 KEFRDKTILSdtcieiIEGGFYVITGPSGVGKSsllNII-------GLldgdfdgnyifydkkisfsnyNSTQELRRlyf 81
Cdd:cd03278 10 KSFADKTTIP------FPPGLTAIVGPNGSGKS---NIIdairwvlGE---------------------QSAKSLRG--- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 82 gyifqDSLinerQDLIRN--------ILCSVDYSLQNNrrhlvNHFLSVVG-------LSS---RTESASVLSGGEKQRL 143
Cdd:cd03278 57 -----EKM----SDVIFAgsetrkpaNFAEVTLTFDNS-----DGRYSIISqgdvseiIEApgkKVQRLSLLSGGEKALT 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1372031259 144 ALAR--ALIK-KPK---ILlaDEPTASLDRENKEKIMDIFKKFTNEGGTVVmVTH 192
Cdd:cd03278 123 ALALlfAIFRvRPSpfcVL--DEVDAALDDANVERFARLLKEFSKETQFIV-ITH 174
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
118-166 |
4.83e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 43.57 E-value: 4.83e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1372031259 118 HFLSVVGLSSRTESASVLSGGE------KQRLALARALIKKPKILLADEPTASLD 166
Cdd:PLN03130 1352 HLKDVIRRNSLGLDAEVSEAGEnfsvgqRQLLSLARALLRRSKILVLDEATAAVD 1406
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
34-162 |
7.33e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 42.80 E-value: 7.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 34 GPSGVGKSSLLNIIG-----------LLDGDFDgnyifyDK--------KISFSnynsTQEL-RRLY-----------FG 82
Cdd:NF033858 34 GPDGVGKSSLLSLIAgarkiqqgrveVLGGDMA------DArhrravcpRIAYM----PQGLgKNLYptlsvfenldfFG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 83 YIF-QDSLinERQDLIRNILCSVdyslqnnrrhlvnhflsvvGLSS-RTESASVLSGGEKQRLALARALIKKPKILLADE 160
Cdd:NF033858 104 RLFgQDAA--ERRRRIDELLRAT-------------------GLAPfADRPAGKLSGGMKQKLGLCCALIHDPDLLILDE 162
|
..
gi 1372031259 161 PT 162
Cdd:NF033858 163 PT 164
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
129-204 |
8.53e-05 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 42.20 E-value: 8.53e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1372031259 129 TESASVLSGGEKQRLALARALIKKPKILLADEPTASLDRENkEKIMD--IFKKFTNEggTVVMVTHDLELIDEKIQVI 204
Cdd:cd03288 151 TEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT-ENILQkvVMTAFADR--TVVTIAHRVSTILDADLVL 225
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
23-45 |
1.06e-04 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 41.61 E-value: 1.06e-04
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
135-199 |
1.24e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 42.21 E-value: 1.24e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1372031259 135 LSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLELIDE 199
Cdd:PRK11288 141 LSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFA 205
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
117-208 |
1.29e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 117 NHFLSVVGLSSRTESASVLSGGEK-Q-----RLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTnEGGTVVMV 190
Cdd:COG4717 541 DLSLKVDTEDGRTRPVEELSRGTReQlylalRLALAELLAGEPLPLILDDAFVNFDDERLRAALELLAELA-KGRQVIYF 619
|
90 100
....*....|....*....|..
gi 1372031259 191 THDLELID----EKIQVIRLNN 208
Cdd:COG4717 620 TCHEELVElfqeEGAHVIELES 641
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-205 |
2.53e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 41.14 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 17 LSDTCIEIIEGGFYVITGPSGVGKSSLLNII-GLLDGDfDGNYIFYDKKISFSNYNSTQELrrlyfGYifqdSLINERQD 95
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLtGIYTRD-AGSILYLGKEVTFNGPKSSQEA-----GI----GIIHQELN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 96 LIRNIlcsvdySLQNN---RRHLVNHF---------------LSVVGL--SSRTeSASVLSGGEKQRLALARALIKKPKI 155
Cdd:PRK10762 90 LIPQL------TIAENiflGREFVNRFgridwkkmyaeadklLARLNLrfSSDK-LVGELSIGEQQMVEIAKVLSFESKV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1372031259 156 LLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLELIDE---KIQVIR 205
Cdd:PRK10762 163 IIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEicdDVTVFR 215
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-204 |
3.38e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.77 E-value: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 1 MISLYINKKEFRdktiLSDT------CIEIIEGGFYVITGPSGVGKSSLLNIIG----LLDGDFdgnyifydkkisfsnY 70
Cdd:PRK10938 1 MSSLQISQGTFR----LSDTktlqlpSLTLNAGDSWAFVGANGSGKSALARALAgelpLLSGER---------------Q 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 71 NSTQELRRLYF-------GYIFQDS---LINERQD----LIRNILcsVDYSLQNNRRHLVNHFLSVVGLSSRteSASVLS 136
Cdd:PRK10938 62 SQFSHITRLSFeqlqklvSDEWQRNntdMLSPGEDdtgrTTAEII--QDEVKDPARCEQLAQQFGITALLDR--RFKYLS 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1372031259 137 GGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLELIDEKIQVI 204
Cdd:PRK10938 138 TGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFA 205
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
130-197 |
3.80e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.48 E-value: 3.80e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1372031259 130 ESASVLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDLELI 197
Cdd:PRK10982 130 AKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEI 197
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
135-204 |
4.05e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.48 E-value: 4.05e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1372031259 135 LSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDL-EL--IDEKIQVI 204
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMpELlgITDRILVM 464
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
34-205 |
4.16e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 40.42 E-value: 4.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 34 GPSGVGKSSLLNII-GLLDGDfDGNYIFYDKKISFSNYNSTQELRrLYFgyIFQDSLINERQDLIRNILCSVDYSLQNNR 112
Cdd:PRK15439 44 GGNGAGKSTLMKIIaGIVPPD-SGTLEIGGNPCARLTPAKAHQLG-IYL--VPQEPLLFPNLSVKENILFGLPKRQASMQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 113 RhlVNHFLSVVGLSSRTE-SASVLSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVT 191
Cdd:PRK15439 120 K--MKQLLAALGCQLDLDsSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFIS 197
|
170
....*....|....*..
gi 1372031259 192 HDL-EL--IDEKIQVIR 205
Cdd:PRK15439 198 HKLpEIrqLADRISVMR 214
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
34-192 |
4.82e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 40.48 E-value: 4.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 34 GPSGVGKSSLLNIiglLDGDFDGNYIFYDKKIS-FSNYNSTQElRRLyfGYIfqdslinERQDL------IRNILCSVDY 106
Cdd:TIGR00956 796 GASGAGKTTLLNV---LAERVTTGVITGGDRLVnGRPLDSSFQ-RSI--GYV-------QQQDLhlptstVRESLRFSAY 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 107 SLQNN------RRHLVNHFLSVVGLSSRTEsASVLSGGE------KQRLALARALIKKPKILL-ADEPTASLDRENKEKI 173
Cdd:TIGR00956 863 LRQPKsvskseKMEYVEEVIKLLEMESYAD-AVVGVPGEglnveqRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSI 941
|
170
....*....|....*....
gi 1372031259 174 MDIFKKFTNEGGTVVMVTH 192
Cdd:TIGR00956 942 CKLMRKLADHGQAILCTIH 960
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
138-166 |
5.42e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 40.49 E-value: 5.42e-04
10 20
....*....|....*....|....*....
gi 1372031259 138 GEKQRLALARALIKKPKILLADEPTASLD 166
Cdd:NF033858 401 GIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| RsgA |
COG1162 |
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis]; |
23-45 |
1.01e-03 |
|
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440776 [Multi-domain] Cd Length: 300 Bit Score: 38.94 E-value: 1.01e-03
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
94-205 |
1.11e-03 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 38.87 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 94 QDLIRNILCSVDYSLQN-------NRRHLVNHFLSVVGLSSRTESASVLSGGEKQRLALARALI---KKPKILLADEPTA 163
Cdd:COG1106 155 KEELLELLKIADPGIEDieveeeeIEDLVERKLIFKHKGGNVPLPLSEESDGTKRLLALAGALLdalAKGGVLLIDEIEA 234
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1372031259 164 SLDRENKEKIMDIFKKFTNEGGT-VVMVTHDLELIDEKIQVIR 205
Cdd:COG1106 235 SLHPSLLRKLLKLFLDLANKNNAqLIFTTHSTELLDAFLELLR 277
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
135-197 |
1.31e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.11 E-value: 1.31e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1372031259 135 LSGGEKQ------RLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGG---TVVMVTHDLELI 197
Cdd:PRK01156 802 LSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEYSLKDSSdipQVIMISHHRELL 873
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
135-197 |
1.35e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.00 E-value: 1.35e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1372031259 135 LSGGEKQRLALARALIKKPKILLADEPTASLDRENKEKIMDIFKKFTNEGGTVVMVTHDL-ELI 197
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELpELL 468
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
138-166 |
2.77e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 37.95 E-value: 2.77e-03
10 20
....*....|....*....|....*....
gi 1372031259 138 GEKQRLALARALIKKPKILLADEPTASLD 166
Cdd:PRK15064 159 GWKLRVLLAQALFSNPDILLLDEPTNNLD 187
|
|
| TIGR00157 |
TIGR00157 |
ribosome small subunit-dependent GTPase A; Members of this protein were designated YjeQ and ... |
22-47 |
2.80e-03 |
|
ribosome small subunit-dependent GTPase A; Members of this protein were designated YjeQ and are now designated RsgA (ribosome small subunit-dependent GTPase A). The strongest motif in the alignment of these proteins is GXSGVGKS[ST], a classic P-loop for nucleotide binding. This protein has been shown to cleave GTP and remain bound to GDP. A role as a regulator of translation has been suggested. The Aquifex aeolicus ortholog is split into consecutive open reading frames. Consequently, this model was build in fragment mode (-f option). [Protein synthesis, Translation factors]
Pssm-ID: 272934 [Multi-domain] Cd Length: 245 Bit Score: 37.78 E-value: 2.80e-03
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
131-179 |
3.70e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 35.29 E-value: 3.70e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1372031259 131 SASVLSGGEKQRL---ALARALI----------KKPKILLADEPTASLDRENKEKIMDIFKK 179
Cdd:pfam13558 29 RSGGLSGGEKQLLaylPLAAALAaqygsaegrpPAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| COG3911 |
COG3911 |
Predicted ATPase [General function prediction only]; |
29-45 |
4.27e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443117 Cd Length: 180 Bit Score: 36.72 E-value: 4.27e-03
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
25-45 |
5.35e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 36.37 E-value: 5.35e-03
|
| ATPase_2 |
pfam01637 |
ATPase domain predominantly from Archaea; This family contain a conserved P-loop motif that is ... |
23-79 |
6.66e-03 |
|
ATPase domain predominantly from Archaea; This family contain a conserved P-loop motif that is involved in binding ATP. There are eukaryote members as well as archaeal members in this family.
Pssm-ID: 376582 [Multi-domain] Cd Length: 222 Bit Score: 36.53 E-value: 6.66e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1372031259 23 EIIEGG---FYVITGPSGVGKSSLLN--IIGLLDGDFDGNYIFYDKKISFSNYNSTQELRRL 79
Cdd:pfam01637 13 EWAERGpnlIYVIYGPEGCGKTALLResIENLLDLGYYVIYYDPLRRYFISKLDRFEEVRRL 74
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
18-44 |
7.92e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 33.73 E-value: 7.92e-03
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
29-208 |
9.16e-03 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 35.75 E-value: 9.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 29 FYVITGPSGVGKSSLLNIIGLLDGDfdgnyifydkkisfsnynSTQELRRlyfgyifQDSLINERQDLIRNIL-CSVDYS 107
Cdd:cd03239 24 FNAIVGPNGSGKSNIVDAICFVLGG------------------KAAKLRR-------GSLLFLAGGGVKAGINsASVEIT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372031259 108 LQNNrrhlvnHFLSVVGLSSRtesasVLSGGEKQRLALARAL----IKKPKILLADEPTASLDRENKEKIMDIFKKFTNE 183
Cdd:cd03239 79 FDKS------YFLVLQGKVEQ-----ILSGGEKSLSALALIFalqeIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKH 147
|
170 180
....*....|....*....|....*...
gi 1372031259 184 GGTVVMVTHDLELI---DEKIQVIRLNN 208
Cdd:cd03239 148 TSQFIVITLKKEMFenaDKLIGVLFVHG 175
|
|
| |
