|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-221 |
7.08e-125 |
|
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: 353.42 E-value: 7.08e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQET----HALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQ 76
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 77 QQQMGMVFQHYNLLENLKIYDNVALPLKLL---KEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPK 153
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAgvpKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488289759 154 WLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIGEF-----LNNPQ 221
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGtveevFANPQ 233
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-222 |
3.27e-108 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 315.09 E-value: 3.27e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVY----QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQ 76
Cdd:COG1135 1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 77 QQQMGMVFQHYNLLENLKIYDNVALPLKLL---KEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPK 153
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVALPLEIAgvpKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488289759 154 WLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI-----GEFLNNPQQ 222
Cdd:COG1135 161 VLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVeqgpvLDVFANPQS 234
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-222 |
3.43e-95 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 282.07 E-value: 3.43e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQ----ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQ 76
Cdd:PRK11153 1 MIELKNISKVFPqggrTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 77 QQQMGMVFQHYNLLENLKIYDNVALPLKLL---KEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPK 153
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVALPLELAgtpKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488289759 154 WLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI-----GEFLNNPQQ 222
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVeqgtvSEVFSHPKH 234
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-215 |
7.71e-85 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 251.89 E-value: 7.71e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQ----ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQ- 75
Cdd:COG1136 4 LLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 76 QQQQMGMVFQHYNLLENLKIYDNVALPLKLLKEKQPEKIER---LLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNP 152
Cdd:COG1136 84 RRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERareLLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488289759 153 KWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELEtVKRLCNRILVMEKGQLIGE 215
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPE-LAARADRVIRLRDGRIVSD 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-212 |
4.27e-84 |
|
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: 249.71 E-value: 4.27e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQ----ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKE-VRQQ 76
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 77 QQQMGMVFQHYNLLENLKIYDNVALPLKLLKEKQPEKIER---LLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPK 153
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERaeeLLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488289759 154 WLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELEtVKRLCNRILVMEKGQL 212
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPE-LAEYADRIIELRDGKI 218
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-222 |
1.78e-82 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 246.06 E-value: 1.78e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVqTFSKKEVRQQQQQM 80
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINKLRRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 81 GMVFQHYNLLENLKIYDNVAL-PLKLLKEKQPEKIER---LLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLL 156
Cdd:COG1126 80 GMVFQQFNLFPHLTVLENVTLaPIKVKKMSKAEAEERameLLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVML 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488289759 157 CDEATSSLDEENT---ESVVRLLHKTHQefrpTIFFVSHELETVKRLCNRILVMEKGQLI-----GEFLNNPQQ 222
Cdd:COG1126 160 FDEPTSALDPELVgevLDVMRDLAKEGM----TMVVVTHEMGFAREVADRVVFMDGGRIVeegppEEFFENPQH 229
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-213 |
5.92e-78 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 234.18 E-value: 5.92e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQETH-ALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQQQQ 79
Cdd:COG2884 1 MIRFENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 80 MGMVFQHYNLLENLKIYDNVALPLKLLKEKQPE---KIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLL 156
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEirrRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488289759 157 CDEATSSLDEENTESVVRLLHKTHQEfRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-213 |
3.39e-77 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 233.03 E-value: 3.39e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQ-ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQQQQ 79
Cdd:COG3638 2 MLELRNLSKRYPgGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 80 MGMVFQHYNLLENLKIYDNV---ALP--------LKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARAL 148
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVlagRLGrtstwrslLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARAL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 149 SRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:COG3638 162 VQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVV 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-222 |
5.66e-76 |
|
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: 238.26 E-value: 5.66e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVY-----QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQ 75
Cdd:COG1123 260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 76 QQQQMGMVFQHYN--LLENLKIYDNVALPLKLL----KEKQPEKIERLLTFVDM-AHKAEAYPAQLSGGEKQRVSIARAL 148
Cdd:COG1123 340 LRRRVQMVFQDPYssLNPRMTVGDIIAEPLRLHgllsRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488289759 149 SRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI-----GEFLNNPQQ 222
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVedgptEEVFANPQH 498
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-215 |
7.58e-72 |
|
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: 219.08 E-value: 7.58e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQQQQM 80
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 81 GMVFQHYNLLENLKIYDNVALPLKLLKEKQPEKIERL----LTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLL 156
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVAFPLREHTDLSEAEIRELvlekLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488289759 157 CDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIGE 215
Cdd:COG1127 165 YDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAE 223
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-216 |
2.83e-71 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 218.42 E-value: 2.83e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQ----ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGrnvqtfskKEVRQQ 76
Cdd:COG1116 7 ALELRGVSKRFPtgggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG--------KPVTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 77 QQQMGMVFQHYNLLENLKIYDNVALPLKLL---KEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPK 153
Cdd:COG1116 79 GPDRGVVFQEPALLPWLTVLDNVALGLELRgvpKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488289759 154 WLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHEL-ETVkRLCNRILVMEK--GQLIGEF 216
Cdd:COG1116 159 VLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVdEAV-FLADRVVVLSArpGRIVEEI 223
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-212 |
5.18e-71 |
|
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: 216.24 E-value: 5.18e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVqTFSKKEVRQQQQQMG 81
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TDDKKNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 82 MVFQHYNLLENLKIYDNVAL-PLKLLKEKQPEKIER---LLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLC 157
Cdd:cd03262 80 MVFQQFNLFPHLTVLENITLaPIKVKGMSKAEAEERaleLLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488289759 158 DEATSSLDEENTESVVRL---LHKTHQefrpTIFFVSHELETVKRLCNRILVMEKGQL 212
Cdd:cd03262 160 DEPTSALDPELVGEVLDVmkdLAEEGM----TMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-213 |
2.31e-68 |
|
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: 209.30 E-value: 2.31e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTfskkeVRQQQQQMG 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTG-----VPPERRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 82 MVFQHYNLLENLKIYDNVALPLKLLKEKQPEKIER---LLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCD 158
Cdd:cd03259 76 MVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARvreLLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 159 EATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:cd03259 156 EPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-215 |
4.28e-67 |
|
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: 206.97 E-value: 4.28e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQQQQMG 81
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 82 MVFQHYNLLENLKIYDNVALPL----KLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLC 157
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLrehtRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488289759 158 DEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIGE 215
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAE 218
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-213 |
1.48e-66 |
|
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: 205.88 E-value: 1.48e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVY-QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQQQQM 80
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 81 GMVFQHYNLLENLKIYDNV---ALP--------LKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALS 149
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVlsgRLGrrstwrslFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488289759 150 RNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-216 |
1.77e-66 |
|
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: 205.81 E-value: 1.77e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVY----QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVqtfSKKEVRQQ 76
Cdd:COG1124 1 MLEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPV---TRRRRKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 77 QQQMGMVFQHYNLLEN--LKIYDNVALPLKLLKEKQPEK-IERLLTFVDM-AHKAEAYPAQLSGGEKQRVSIARALSRNP 152
Cdd:COG1124 78 RRRVQMVFQDPYASLHprHTVDRILAEPLRIHGLPDREErIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488289759 153 KWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIGEF 216
Cdd:COG1124 158 ELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEEL 221
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-213 |
2.62e-66 |
|
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: 204.87 E-value: 2.62e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQ-ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQqqqM 80
Cdd:COG1122 1 IELENLSFSYPgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRK---V 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 81 GMVFQHY-NLLENLKIYDNVA---LPLKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLL 156
Cdd:COG1122 78 GLVFQNPdDQLFAPTVEEDVAfgpENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488289759 157 CDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:COG1122 158 LDEPTAGLDPRGRRELLELLKRLNKEGK-TVIIVTHDLDLVAELADRVIVLDDGRIV 213
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-216 |
8.58e-66 |
|
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: 203.09 E-value: 8.58e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQ----ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGrnvqtfskKEVRQQQ 77
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG--------EPVTGPG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 78 QQMGMVFQHYNLLENLKIYDNVALPLKL---LKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKW 154
Cdd:cd03293 73 PDRGYVFQQDALLPWLTVLDNVALGLELqgvPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488289759 155 LLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEK--GQLIGEF 216
Cdd:cd03293 153 LLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAEV 216
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-211 |
1.45e-65 |
|
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: 200.88 E-value: 1.45e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSkKEVRQQQQQMG 81
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLE-DELPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 82 MVFQHYNLLENLKIYDNVALPlkllkekqpekierlltfvdmahkaeaypaqLSGGEKQRVSIARALSRNPKWLLCDEAT 161
Cdd:cd03229 80 MVFQDFALFPHLTVLENIALG-------------------------------LSGGQQQRVALARALAMDPDVLLLDEPT 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488289759 162 SSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQ 211
Cdd:cd03229 129 SALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-211 |
1.48e-65 |
|
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: 202.31 E-value: 1.48e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 3 ELVNVSKVY--QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQqqqM 80
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRK---V 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 81 GMVFQHYNL-LENLKIYDNVALPLKLL---KEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLL 156
Cdd:cd03225 78 GLVFQNPDDqFFGPTVEEEVAFGLENLglpEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 157 CDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQ 211
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAEGK-TIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-221 |
2.06e-63 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 201.14 E-value: 2.06e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVqtFSKKEVRQQQqqMG 81
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL--FTNLPPRERR--VG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 82 MVFQHYNLLENLKIYDNVA--LP-LKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCD 158
Cdd:COG1118 79 FVFQHYALFPHMTVAENIAfgLRvRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488289759 159 EATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQL--IG---EFLNNPQ 221
Cdd:COG1118 159 EPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIeqVGtpdEVYDRPA 226
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-213 |
8.21e-63 |
|
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: 195.80 E-value: 8.21e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQE----THALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQ 76
Cdd:cd03257 1 LLEVKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 77 QQQMGMVFQHYNLLEN--LKIYDNVALPLKLL-----KEKQPEKIERLLTFVDMAHK-AEAYPAQLSGGEKQRVSIARAL 148
Cdd:cd03257 81 RKEIQMVFQDPMSSLNprMTIGEQIAEPLRIHgklskKEARKEAVLLLLVGVGLPEEvLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 149 SRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-213 |
2.36e-62 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 198.78 E-value: 2.36e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQtfskkEVRQQQQQM 80
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT-----GLPPEKRNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 81 GMVFQHYNLLENLKIYDNVALPLKLL---KEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLC 157
Cdd:COG3842 80 GMVFQDYALFPHLTVAENVAFGLRMRgvpKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488289759 158 DEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:COG3842 160 DEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIE 215
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-213 |
1.21e-61 |
|
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: 192.78 E-value: 1.21e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLM-----EQPSEGEIRIDGRNV--QTFSKKEVR 74
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIydLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 75 qqqQQMGMVFQHYNLLeNLKIYDNVALPLKL----LKEKQPEKIERLLTFVDMAH--KAEAYPAQLSGGEKQRVSIARAL 148
Cdd:cd03260 81 ---RRVGMVFQKPNPF-PGSIYDNVAYGLRLhgikLKEELDERVEEALRKAALWDevKDRLHALGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 149 SRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFrpTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLV 219
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-215 |
1.28e-61 |
|
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: 193.03 E-value: 1.28e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQ----ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKE---V 73
Cdd:COG4181 8 IIELRGLTKTVGtgagELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDArarL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 74 RQQQqqMGMVFQHYNLLENLKIYDNVALPLKLLKEKQPEKI-ERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNP 152
Cdd:COG4181 88 RARH--VGFVFQSFQLLPTLTALENVMLPLELAGRRDARARaRALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488289759 153 KWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRlCNRILVMEKGQLIGE 215
Cdd:COG4181 166 AILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVED 227
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-213 |
4.40e-60 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 189.12 E-value: 4.40e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSkKEVRqqqQQMG 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDP-AEVR---RRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 82 MVFQHYNLLENLKIYDNVALPLKLL---KEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCD 158
Cdd:COG1131 77 YVPQEPALYPDLTVRENLRFFARLYglpRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 159 EATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:COG1131 157 EPTSGLDPEARRELWELLRELAAEGK-TVLLSTHYLEEAERLCDRVAIIDKGRIV 210
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-212 |
1.23e-59 |
|
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: 187.23 E-value: 1.23e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVY-QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQQQQM 80
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 81 GMVFQHYNLLENLKIYDNVALPLKLLKEKQ---PEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLC 157
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPreiRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 158 DEATSSLDEENTESVVRLLHKTHQEfRPTIFFVSHELETVKRLCNRILVMEKGQL 212
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-220 |
3.87e-59 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 190.28 E-value: 3.87e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQtfskkEVRQQQQQM 80
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVT-----DLPPKDRNI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 81 GMVFQHYNLLENLKIYDNVALPLKLLKEKQPE---KIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLC 157
Cdd:COG3839 78 AMVFQSYALYPHMTVYENIAFPLKLRKVPKAEidrRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488289759 158 DEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQL--IG---EFLNNP 220
Cdd:COG3839 158 DEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIqqVGtpeELYDRP 225
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-212 |
5.69e-59 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 185.40 E-value: 5.69e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQqqqMG 81
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQ---VA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 82 MVFQHYNLLENlKIYDNVALPLKLLKEK-QPEKIERLLTFVDMAHKAEAYPA-QLSGGEKQRVSIARALSRNPKWLLCDE 159
Cdd:COG4619 78 YVPQEPALWGG-TVRDNLPFPFQLRERKfDRERALELLERLGLPPDILDKPVeRLSGGERQRLALIRALLLQPDVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488289759 160 ATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQL 212
Cdd:COG4619 157 PTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-213 |
2.97e-58 |
|
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: 184.86 E-value: 2.97e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRqqqQQM 80
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELA---RRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 81 GMVFQHYNLLENLKIYDNVAL-------PLKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPK 153
Cdd:COG1120 78 AYVPQEPPAPFGLTVRELVALgryphlgLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 154 WLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:COG1120 158 LLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIV 217
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-220 |
5.65e-57 |
|
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: 181.34 E-value: 5.65e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETH-ALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQqqqM 80
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRK---I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 81 GMVFQHYNLLENLKIYDNVALPLKLLKEKQPEKIER---LLTFVDM--AHKAEAYPAQLSGGEKQRVSIARALSRNPKWL 155
Cdd:cd03295 78 GYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERadeLLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 156 LCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI-----GEFLNNP 220
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVqvgtpDEILRSP 227
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-221 |
8.98e-57 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 180.98 E-value: 8.98e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNV---QTFSKKEVRQQQQ 78
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 79 QMGMVFQHYNLLENLKIYDN-VALPLKLL---KEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKW 154
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENlIEAPCKVLglsKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488289759 155 LLCDEATSSLDEENTESVVRLLHKThQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI----GEFLNNPQ 221
Cdd:COG4161 163 LLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYMEKGRIIeqgdASHFTQPQ 232
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
14-221 |
1.00e-56 |
|
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: 181.69 E-value: 1.00e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 14 THALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQ-QQQQMGMVFQHYNLLEN 92
Cdd:cd03294 37 TVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElRRKKISMVFQSFALLPH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 93 LKIYDNVALPLKLL---KEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLD---- 165
Cdd:cd03294 117 RTVLENVAFGLEVQgvpRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDplir 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488289759 166 EENTESVVRLlhktHQEFRPTIFFVSHELETVKRLCNRILVMEKGQL--IG---EFLNNPQ 221
Cdd:cd03294 197 REMQDELLRL----QAELQKTIVFITHDLDEALRLGDRIAIMKDGRLvqVGtpeEILTNPA 253
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-220 |
5.00e-56 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 178.75 E-value: 5.00e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTfSKKEVRQQQQQM 80
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVND-PKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 81 GMVFQHYNLLENLKIYDNVAL-PLKL--LKEKQPEKIER-LLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLL 156
Cdd:PRK09493 80 GMVFQQFYLFPHLTALENVMFgPLRVrgASKEEAEKQAReLLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLML 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488289759 157 CDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLI-----GEFLNNP 220
Cdd:PRK09493 160 FDEPTSALDPELRHEVLKVMQDLAEEGM-TMVIVTHEIGFAEKVASRLIFIDKGRIAedgdpQVLIKNP 227
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-211 |
6.16e-56 |
|
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: 176.42 E-value: 6.16e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETH--ALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQqqq 79
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 80 MGMVFQHYNLLeNLKIYDNValplkllkekqpekierlltfvdmahkaeaypaqLSGGEKQRVSIARALSRNPKWLLCDE 159
Cdd:cd03228 78 IAYVPQDPFLF-SGTIRENI----------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488289759 160 ATSSLDEENTESVVRLLHKTHQEfrPTIFFVSHELETVKRlCNRILVMEKGQ 211
Cdd:cd03228 123 ATSALDPETEALILEALRALAKG--KTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-229 |
2.67e-55 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 180.66 E-value: 2.67e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEvrqqqQQMG 81
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD-----RKVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 82 MVFQHYNLLENLKIYDNVALPLKLL-KEKQP------EKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKW 154
Cdd:PRK10851 78 FVFQHYALFRHMTVFDNIAFGLTVLpRRERPnaaaikAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 155 LLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLigEFLNNPQQYEEEPLS 229
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI--EQAGTPDQVWREPAT 230
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-221 |
3.23e-55 |
|
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: 179.09 E-value: 3.23e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQ----ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLR-LLNLMEQP--SEGEIRIDGRNVQTFSKKEV 73
Cdd:COG0444 1 LLEVRNLKVYFPtrrgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARaILGLLPPPgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 74 RQ-QQQQMGMVFQH-YNLLeN--LKIYDNVALPLKLL----KEKQPEKIERLLTFVDMAHKAE---AYPAQLSGGEKQRV 142
Cdd:COG0444 81 RKiRGREIQMIFQDpMTSL-NpvMTVGDQIAEPLRIHgglsKAEARERAIELLERVGLPDPERrldRYPHELSGGMRQRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 143 SIARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI-----GEFL 217
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVeegpvEELF 239
|
....
gi 488289759 218 NNPQ 221
Cdd:COG0444 240 ENPR 243
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-227 |
1.74e-54 |
|
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: 174.73 E-value: 1.74e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQtfskkEVRQQQQQMG 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT-----NLPPHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 82 MVFQHYNLLENLKIYDNVALPLKLLKEKQPE---KIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCD 158
Cdd:cd03300 76 TVFQNYALFPHLTVFENIAFGLRLKKLPKAEikeRVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488289759 159 EATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLigEFLNNPQQYEEEP 227
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKI--QQIGTPEEIYEEP 222
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-213 |
8.45e-54 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 173.28 E-value: 8.45e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNV---QTFSKKEVRQQQQ 78
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 79 QMGMVFQHYNLLENLKIYDN-VALPLKLL---KEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKW 154
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNlIEAPCRVLglsKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488289759 155 LLCDEATSSLDEENTESVVRLLHKThQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIV 220
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-229 |
1.60e-53 |
|
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: 172.52 E-value: 1.60e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVqtfSKKEVrqQQQQMG 81
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA---TDVPV--QERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 82 MVFQHYNLLENLKIYDNVALPLKLLKEKQP-------EKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKW 154
Cdd:cd03296 78 FVFQHYALFRHMTVFDNVAFGLRVKPRSERppeaeirAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 155 LLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLigEFLNNPQQYEEEPLS 229
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRI--EQVGTPDEVYDHPAS 230
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-212 |
1.98e-53 |
|
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: 171.28 E-value: 1.98e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEvrqqqQQMG 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD-----RDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 82 MVFQHYNLLENLKIYDNVALPLKLLKEKQPE---KIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCD 158
Cdd:cd03301 76 MVFQNYALYPHMTVYDNIAFGLKLRKVPKDEideRVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488289759 159 EATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQL 212
Cdd:cd03301 156 EPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-227 |
4.31e-53 |
|
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: 178.56 E-value: 4.31e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVY--QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLN-LMEQPSE--GEIRIDGRNVQTFSkkeVRQ 75
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMgLLPHGGRisGEVLLDGRDLLELS---EAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 76 QQQQMGMVFQHY-NLLENLKIYDNVALPLKLL---KEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRN 151
Cdd:COG1123 81 RGRRIGMVFQDPmTQLNPVTVGDQIAEALENLglsRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 152 PKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI-----GEFLNNPQQYEEE 226
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVedgppEEILAAPQALAAV 240
|
.
gi 488289759 227 P 227
Cdd:COG1123 241 P 241
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-213 |
1.74e-52 |
|
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: 180.42 E-value: 1.74e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVY--QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRqqqQQ 79
Cdd:COG2274 474 IELENVSFRYpgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLR---RQ 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 80 MGMVFQHYNLLENlKIYDNVALPLKLLKEkqpEKIERLLTFVDMAHKAEAYP-----------AQLSGGEKQRVSIARAL 148
Cdd:COG2274 551 IGVVLQDVFLFSG-TIRENITLGDPDATD---EEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIARAL 626
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488289759 149 SRNPKWLLCDEATSSLDEENTESVVRLLhktHQEFRP-TIFFVSHELETVkRLCNRILVMEKGQLI 213
Cdd:COG2274 627 LRNPRILILDEATSALDAETEAIILENL---RRLLKGrTVIIIAHRLSTI-RLADRIIVLDKGRIV 688
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-211 |
4.49e-52 |
|
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: 165.88 E-value: 4.49e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 3 ELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQqqqMGM 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRR---IGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 83 VFQhynllenlkiydnvalplkllkekqpekierlltfvdmahkaeaypaqLSGGEKQRVSIARALSRNPKWLLCDEATS 162
Cdd:cd00267 78 VPQ------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488289759 163 SLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQ 211
Cdd:cd00267 110 GLDPASRERLLELLRELAEEGR-TVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-212 |
9.25e-52 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 167.96 E-value: 9.25e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLR-LLNLMeQPSEGEIRIDGRNVqtfskkevRQQQQQ 79
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKaILGLL-PPTSGTVRLFGKPP--------RRARRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 80 MGMVFQHYNLLENLKI--YDNVAL-------PLKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSR 150
Cdd:COG1121 77 IGYVPQRAEVDWDFPItvRDVVLMgrygrrgLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488289759 151 NPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQL 212
Cdd:COG1121 157 DPDLLLLDEPFAGVDAATEEALYELLRELRREGK-TILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-212 |
1.10e-51 |
|
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: 165.65 E-value: 1.10e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVqtfsKKEVRQQQQQMG 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI----KKEPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 82 MVFQHYNLLENLKIYDNValplkllkekqpekierlltfvdmahkaeaypaQLSGGEKQRVSIARALSRNPKWLLCDEAT 161
Cdd:cd03230 77 YLPEEPSLYENLTVRENL---------------------------------KLSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488289759 162 SSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQL 212
Cdd:cd03230 124 SGLDPESRREFWELLRELKKEGK-TILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-226 |
1.75e-51 |
|
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: 167.34 E-value: 1.75e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQtfskKEVRQQQQQM 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR----KEPREARRQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 81 GMVFQHYNLLENLKIYDNVAL--PLKLLKEKQ-PEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLC 157
Cdd:COG4555 77 GVLPDERGLYDRLTVRENIRYfaELYGLFDEElKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488289759 158 DEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLIgeFLNNPQQYEEE 226
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRALKKEGK-TVLFSSHIMQEVEALCDRVVILHKGKVV--AQGSLDELREE 222
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-210 |
5.60e-51 |
|
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: 165.01 E-value: 5.60e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 3 ELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLR-LLNLMeQPSEGEIRIDGrnvqtfskKEVRQQQQQMG 81
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKaILGLL-KPTSGSIRVFG--------KPLEKERKRIG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 82 MVFQHYNLLEN--LKIYDNVAL-------PLKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNP 152
Cdd:cd03235 72 YVPQRRSIDRDfpISVRDVVLMglyghkgLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488289759 153 KWLLCDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKG 210
Cdd:cd03235 152 DLLLLDEPFAGVDPKTQEDIYELLRELRREGM-TILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-215 |
2.48e-50 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 172.66 E-value: 2.48e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQ-ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLN-LMEqPSEGEIRIDGRNVQTFSKKEVRqqqQQ 79
Cdd:COG1132 340 IEFENVSFSYPgDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLrFYD-PTSGRILIDGVDIRDLTLESLR---RQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 80 MGMVFQHYNLLeNLKIYDNVALPlklLKEKQPEKIERLLTFVDMAHKAEAYP-----------AQLSGGEKQRVSIARAL 148
Cdd:COG1132 416 IGVVPQDTFLF-SGTIRENIRYG---RPDATDEEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARAL 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488289759 149 SRNPKWLLCDEATSSLDEEnTEsvvRLLHKTHQEFRP--TIFFVSHELETVKRlCNRILVMEKGQLIGE 215
Cdd:COG1132 492 LKDPPILILDEATSALDTE-TE---ALIQEALERLMKgrTTIVIAHRLSTIRN-ADRILVLDDGRIVEQ 555
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
15-207 |
1.45e-49 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 164.90 E-value: 1.45e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 15 HALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQQQQMGMVFQH-YNLLeN- 92
Cdd:COG4608 32 KAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLRRRMQMVFQDpYASL-Np 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 93 -LKIYDNVALPLK---LLKEKQP-EKIERLLTFVDM--AHkAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLD 165
Cdd:COG4608 111 rMTVGDIIAEPLRihgLASKAERrERVAELLELVGLrpEH-ADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488289759 166 EENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVM 207
Cdd:COG4608 190 VSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVM 231
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-213 |
1.63e-49 |
|
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: 162.98 E-value: 1.63e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVY--QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNvqTFSKKEVRQQQQQ 79
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLD--TLDEENLWEIRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 80 MGMVFQhyNL----------------LENLKIydnvalPLKLLKEKqpekIERLLTFVDMAHKAEAYPAQLSGGEKQRVS 143
Cdd:TIGR04520 79 VGMVFQ--NPdnqfvgatveddvafgLENLGV------PREEMRKR----VDEALKLVGMEDFRDREPHLLSGGQKQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 144 IARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVkRLCNRILVMEKGQLI 213
Cdd:TIGR04520 147 IAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIV 215
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-233 |
1.37e-48 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 160.30 E-value: 1.37e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIR-----IDGRNVQTFSKKEVRQ 75
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRvgditIDTARSLSQQKGLIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 76 QQQQMGMVFQHYNLLENLKIYDNVAL-PLKLLKEKQPEKIER---LLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRN 151
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHRTVLENIIEgPVIVKGEPKEEATARareLLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 152 PKWLLCDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLI-----GEFLNNPQQyeEE 226
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVeqgpaKALFADPQQ--PR 239
|
....*..
gi 488289759 227 PLSYLEK 233
Cdd:PRK11264 240 TRQFLEK 246
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-214 |
5.33e-48 |
|
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: 157.46 E-value: 5.33e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 27 GEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKK-EVRQQQQQMGMVFQHYNLLENLKIYDNVALPLKL 105
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKiNLPPQQRKIGLVFQQYALFPHLNVRENLAFGLKR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 106 lKEKQPEKI--ERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEF 183
Cdd:cd03297 103 -KRNREDRIsvDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNL 181
|
170 180 190
....*....|....*....|....*....|.
gi 488289759 184 RPTIFFVSHELETVKRLCNRILVMEKGQLIG 214
Cdd:cd03297 182 NIPVIFVTHDLSEAEYLADRIVVMEDGRLQY 212
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-213 |
6.21e-48 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 157.99 E-value: 6.21e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQETHalKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVqtfSKKEVrqQQQQM 80
Cdd:COG3840 1 MLRLDDLTYRYGDFP--LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL---TALPP--AERPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 81 GMVFQHYNLLENLKIYDNVAL---P-LKlLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLL 156
Cdd:COG3840 74 SMLFQENNLFPHLTVAQNIGLglrPgLK-LTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488289759 157 CDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:COG3840 153 LDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIA 209
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-215 |
1.06e-47 |
|
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: 157.21 E-value: 1.06e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRqqqqQMG 81
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIA----RLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 82 MV--FQHYNLLENLKIYDNVALPLKLLK-------------EKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIAR 146
Cdd:cd03219 77 IGrtFQIPRLFPELTVLENVMVAAQARTgsglllararreeREARERAEELLERVGLADLADRPAGELSYGQQRRLEIAR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488289759 147 ALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLIGE 215
Cdd:cd03219 157 ALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGI-TVLLVEHDMDVVMSLADRVTVLDQGRVIAE 224
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
6-215 |
2.35e-47 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 156.51 E-value: 2.35e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 6 NVSKVYQE----THALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFS---KKEVRQQQq 78
Cdd:PRK11629 10 NLCKRYQEgsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaaKAELRNQK- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 79 qMGMVFQHYNLLENLKIYDNVALPLKLLKEKQPEKIER---LLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWL 155
Cdd:PRK11629 89 -LGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRaleMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 156 LCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLcNRILVMEKGQLIGE 215
Cdd:PRK11629 168 LADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTAE 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-162 |
3.31e-47 |
|
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: 153.19 E-value: 3.31e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRqqqQQMGMVFQHYNLLENLKIY 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLR---KEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488289759 97 DNVALPL---KLLKEKQPEKIERLLTFVDMAHKAE----AYPAQLSGGEKQRVSIARALSRNPKWLLCDEATS 162
Cdd:pfam00005 78 ENLRLGLllkGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-221 |
1.23e-46 |
|
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: 155.20 E-value: 1.23e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRqqqqQM 80
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIA----RL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 81 GMV--FQHYNLLENLKIYDNVALP-------------LKLLKEKQPE-----KIERLLTFVDMAHKAEAYPAQLSGGEKQ 140
Cdd:COG0411 80 GIArtFQNPRLFPELTVLENVLVAaharlgrgllaalLRLPRARREEreareRAEELLERVGLADRADEPAGNLSYGQQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 141 RVSIARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI-----GE 215
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIaegtpAE 239
|
....*.
gi 488289759 216 FLNNPQ 221
Cdd:COG0411 240 VRADPR 245
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-213 |
1.39e-46 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 152.59 E-value: 1.39e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 3 ELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRqqqQQMGM 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELA---RKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 83 VFQhynllenlkiydnvalplkllkekqpekierLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATS 162
Cdd:cd03214 78 VPQ-------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488289759 163 SLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:cd03214 127 HLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-210 |
2.76e-46 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 154.63 E-value: 2.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVY----QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEvrqq 76
Cdd:COG4525 3 MLTVRHVSVRYpgggQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 77 qqqmGMVFQHYNLLENLKIYDNVALPLKL--LKEKQPEKI-ERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPK 153
Cdd:COG4525 79 ----GVVFQKDALLPWLNVLDNVAFGLRLrgVPKAERRARaEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488289759 154 WLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKG 210
Cdd:COG4525 155 FLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPG 211
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-215 |
8.20e-46 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 152.34 E-value: 8.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVY-QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQQQQ 79
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 80 MGMVFQHYNLLENLKIYDNVALPLkLLKEKQPEKIER----LLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWL 155
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPL-IIAGASGDDIRRrvsaALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488289759 156 LCDEATSSLDEENTESVVRLLhkthQEFRP---TIFFVSHELETVKRLCNRILVMEKGQLIGE 215
Cdd:PRK10908 160 LADEPTGNLDDALSEGILRLF----EEFNRvgvTVLMATHDIGLISRRSYRMLTLSDGHLHGG 218
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
9-222 |
9.74e-46 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 159.46 E-value: 9.74e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 9 KVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLR-LLNLmeQPSEGEIRIDGRNVQTFSKKEVRQQQQQMGMVFQH- 86
Cdd:COG4172 294 RTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLaLLRL--IPSEGEIRFDGQDLDGLSRRALRPLRRRMQVVFQDp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 87 YNLLeN--LKIYDNVALPLKLL-----KEKQPEKIERLLTFV----DMAHKaeaYPAQLSGGEKQRVSIARALSRNPKWL 155
Cdd:COG4172 372 FGSL-SprMTVGQIIAEGLRVHgpglsAAERRARVAEALEEVgldpAARHR---YPHEFSGGQRQRIAIARALILEPKLL 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488289759 156 LCDEATSSLDeentESV----VRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI-----GEFLNNPQQ 222
Cdd:COG4172 448 VLDEPTSALD----VSVqaqiLDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVeqgptEQVFDAPQH 519
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-224 |
2.21e-45 |
|
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: 151.33 E-value: 2.21e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETHaLKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEvrqqqQQMG 81
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK-----RDIS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 82 MVFQHYNLLENLKIYDNVALPLKLLKEKQPEKIERLLT---FVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCD 158
Cdd:cd03299 75 YVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEiaeMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488289759 159 EATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI-----GEFLNNPQQYE 224
Cdd:cd03299 155 EPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIqvgkpEEVFKKPKNEF 225
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-215 |
2.09e-44 |
|
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: 156.46 E-value: 2.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVY-QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQqqqM 80
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQ---I 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 81 GMVFQHYNLL-----ENLKIYDNVAlplkllkekQPEKIERLLTFVDMAHKAEAYP-----------AQLSGGEKQRVSI 144
Cdd:COG4988 414 AWVPQNPYLFagtirENLRLGRPDA---------SDEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLAL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488289759 145 ARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEfRpTIFFVSHELETVKRlCNRILVMEKGQLIGE 215
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKG-R-TVILITHRLALLAQ-ADRILVLDDGRIVEQ 552
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-215 |
7.36e-44 |
|
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: 145.26 E-value: 7.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQQqqMG 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAG--IA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 82 MVFQhynllenlkiydnvalplkllkekqpekierlltfvdmahkaeaypaqLSGGEKQRVSIARALSRNPKWLLCDEAT 161
Cdd:cd03216 79 MVYQ------------------------------------------------LSVGERQMVEIARALARNARLLILDEPT 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488289759 162 SSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLIGE 215
Cdd:cd03216 111 AALTPAEVERLFKVIRRLRAQGV-AVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-222 |
1.05e-43 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 147.88 E-value: 1.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLM--EQPS---EGEIRIDGRNVqtFSKK----E 72
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGarvEGEILLDGEDI--YDPDvdvvE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 73 VRqqqQQMGMVFQHYNLLeNLKIYDNVALPLKLLKEKQP----EKIERLLTFV----DMAHKAEAYPAQLSGGEKQRVSI 144
Cdd:COG1117 90 LR---RRVGMVFQKPNPF-PKSIYDNVAYGLRLHGIKSKseldEIVEESLRKAalwdEVKDRLKKSALGLSGGQQQRLCI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 145 ARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFrpTIFFVSHELETVKRLCNRILVMEKGQLIgEF------LN 218
Cdd:COG1117 166 ARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGELV-EFgpteqiFT 242
|
....
gi 488289759 219 NPQQ 222
Cdd:COG1117 243 NPKD 246
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-213 |
1.74e-43 |
|
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: 146.11 E-value: 1.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVY--QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTfskkEVRQQQQQ 79
Cdd:cd03263 1 LQIRNLTKTYkkGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT----DRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 80 MGMVFQHYNLLENLKIYDNVAL--PLKLLKEKQ-PEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLL 156
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLRFyaRLKGLPKSEiKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488289759 157 CDEATSSLDEENTESVVRLLHKTHQEfrPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVRKG--RSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
6-215 |
2.17e-43 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 147.53 E-value: 2.17e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 6 NVSKVYQE-----THA----LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQ 76
Cdd:PRK10419 8 GLSHHYAHgglsgKHQhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 77 QQQMGMVFQHYNLLENLK--IYDNVALPLKLL----KEKQPEKIERLLTFVDMAHK-AEAYPAQLSGGEKQRVSIARALS 149
Cdd:PRK10419 88 RRDIQMVFQDSISAVNPRktVREIIREPLRHLlsldKAERLARASEMLRAVDLDDSvLDKRPPQLSGGQLQRVCLARALA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488289759 150 RNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIGE 215
Cdd:PRK10419 168 VEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVET 233
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-227 |
2.43e-43 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 150.10 E-value: 2.43e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQtfskkEVRQQQQQMG 81
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT-----HVPAENRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 82 MVFQHYNLLENLKIYDNVALPLKLLKEKQPEKIERL---LTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCD 158
Cdd:PRK09452 90 TVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVmeaLRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488289759 159 EATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLigEFLNNPQQYEEEP 227
Cdd:PRK09452 170 ESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRI--EQDGTPREIYEEP 236
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-216 |
2.73e-43 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 152.48 E-value: 2.73e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVrqQQQQM 80
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDA--QAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 81 GMVFQHYNLLENLKIYDNVAL---PLKLL---KEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKW 154
Cdd:COG1129 82 AIIHQELNLVPNLSVAENIFLgrePRRGGlidWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488289759 155 LLCDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLIGEF 216
Cdd:COG1129 162 LILDEPTASLTEREVERLFRIIRRLKAQGV-AIIYISHRLDEVFEIADRVTVLRDGRLVGTG 222
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-221 |
1.23e-42 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 145.11 E-value: 1.23e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNV----------QTFSKK 71
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlKVADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 72 EVRQQQQQMGMVFQHYNLLENLKIYDNV-ALPLKLL---KEKQPEKIERLLTFVDMAHKAEA-YPAQLSGGEKQRVSIAR 146
Cdd:PRK10619 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVmEAPIQVLglsKQEARERAVKYLAKVGIDERAQGkYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 147 ALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQL-----IGEFLNNPQ 221
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSSHVIFLHQGKIeeegaPEQLFGNPQ 244
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
19-213 |
2.99e-42 |
|
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: 146.78 E-value: 2.99e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 19 NIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQ-----TFSKKEVRQqqqqMGMVFQHYNLLENL 93
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQdsargIFLPPHRRR----IGYVFQEARLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 94 KIYDNVALPLK-LLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTESV 172
Cdd:COG4148 93 SVRGNLLYGRKrAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEI 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488289759 173 VRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:COG4148 173 LPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVV 213
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-213 |
3.25e-42 |
|
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: 150.69 E-value: 3.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVY--QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRqqqQQ 79
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLR---RR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 80 MGMVFQHY-----NLLENLKIydnvALPlkllkEKQPEKIERLLTFVDMAHKAEAYP-----------AQLSGGEKQRVS 143
Cdd:COG4987 411 IAVVPQRPhlfdtTLRENLRL----ARP-----DATDEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLA 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 144 IARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEfRpTIFFVSHELETVKRlCNRILVMEKGQLI 213
Cdd:COG4987 482 LARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAG-R-TVLLITHRLAGLER-MDRILVLEDGRIV 548
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-215 |
3.54e-42 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 149.41 E-value: 3.54e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRqqQQQM 80
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAI--ALGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 81 GMVFQHYNLLENLKIYDNVAL---PLKLLKEKQPEKIERLLTF-------VDmahkAEAYPAQLSGGEKQRVSIARALSR 150
Cdd:COG3845 83 GMVHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARARIRELserygldVD----PDAKVEDLSVGEQQRVEILKALYR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 151 NPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLIGE 215
Cdd:COG3845 159 GARILILDEPTAVLTPQEADELFEILRRLAAEGK-SIIFITHKLREVMAIADRVTVLRRGKVVGT 222
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-212 |
3.64e-42 |
|
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: 141.20 E-value: 3.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETHA--LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRqqqQQ 79
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELG---DH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 80 MGMVFQHYNLLENlKIYDNValplkllkekqpekierlltfvdmahkaeaypaqLSGGEKQRVSIARALSRNPKWLLCDE 159
Cdd:cd03246 78 VGYLPQDDELFSG-SIAENI----------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488289759 160 ATSSLDEENTESVVRLLhKTHQEFRPTIFFVSHELETVKRlCNRILVMEKGQL 212
Cdd:cd03246 123 PNSHLDVEGERALNQAI-AALKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-220 |
1.85e-41 |
|
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: 141.06 E-value: 1.85e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQtfskkevRQQQQQMgMVFQHYNLLENLKIY 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQIT-------EPGPDRM-VVFQNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 97 DNVALPLK-----LLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTES 171
Cdd:TIGR01184 73 ENIALAVDrvlpdLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488289759 172 VVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKG--QLIGEFLNNP 220
Cdd:TIGR01184 153 LQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGpaANIGQILEVP 203
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
2-213 |
5.71e-41 |
|
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: 139.55 E-value: 5.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQEThalkNIHFSVQL--GEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVqTFSKKEVRQqqqq 79
Cdd:cd03298 1 VRLDKIRFSYGEQ----PMHFDLTFaqGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV-TAAPPADRP---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 80 MGMVFQHYNLLENLKIYDNVAL---PLKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLL 156
Cdd:cd03298 72 VSMLFQENNLFAHLTVEQNVGLglsPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488289759 157 CDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:cd03298 152 LDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-213 |
6.30e-41 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 143.32 E-value: 6.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKkevrqQQQQMG 81
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSI-----QQRDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 82 MVFQHYNLLENLKIYDNVALPLKLLKEKQPEKIERL---LTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCD 158
Cdd:PRK11432 82 MVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVkeaLELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 159 EATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:PRK11432 162 EPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIM 216
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
14-237 |
7.34e-41 |
|
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: 142.94 E-value: 7.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 14 THALKnIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKK-EVRQQQQQMGMVFQHYNLLEN 92
Cdd:TIGR02142 11 DFSLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGiFLPPEKRRIGYVFQEARLFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 93 LKIYDNVALPLKLLKEKQ----PEKIERLLtfvDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEEN 168
Cdd:TIGR02142 90 LSVRGNLRYGMKRARPSErrisFERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 169 TESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIGEflNNPQQYEEEP-LSYLEKVERS 237
Cdd:TIGR02142 167 KYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAA--GPIAEVWASPdLPWLAREDQG 234
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-215 |
8.74e-41 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 140.92 E-value: 8.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVY--QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRnvqTFSKKEVRQQQQQ 79
Cdd:PRK13635 6 IRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 80 MGMVFQHY-NLLENLKIYDNVALPLKLLKEKQPEKIERL---LTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWL 155
Cdd:PRK13635 83 VGMVFQNPdNQFVGATVQDDVAFGLENIGVPREEMVERVdqaLRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 156 LCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRlCNRILVMEKGQLIGE 215
Cdd:PRK13635 163 ILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEE 221
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-213 |
1.30e-40 |
|
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: 138.90 E-value: 1.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETH-ALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRqqqQQM 80
Cdd:cd03254 3 IEFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLR---SMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 81 GMVFQHYNLL-----ENLKIYDNVAlplKLLKEKQPEKIERLLTFVDmaHKAEAYPAQ-------LSGGEKQRVSIARAL 148
Cdd:cd03254 80 GVVLQDTFLFsgtimENIRLGRPNA---TDEEVIEAAKEAGAHDFIM--KLPNGYDTVlgenggnLSQGERQLLAIARAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 149 SRNPKWLLCDEATSSLDEEnTESVV-----RLLHKThqefrpTIFFVSHELETVKRlCNRILVMEKGQLI 213
Cdd:cd03254 155 LRDPKILILDEATSNIDTE-TEKLIqealeKLMKGR------TSIIIAHRLSTIKN-ADKILVLDDGKII 216
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-234 |
2.58e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 139.80 E-value: 2.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQ-----ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVqTFSKKEVRQQ 76
Cdd:PRK13637 3 IKIENLTHIYMegtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDI-TDKKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 77 QQQMGMVFQH--YNLLENlKIYDNVALPLKLLKEKQPEKIERL--------LTFVDMAHKAeayPAQLSGGEKQRVSIAR 146
Cdd:PRK13637 82 RKKVGLVFQYpeYQLFEE-TIEKDIAFGPINLGLSEEEIENRVkramnivgLDYEDYKDKS---PFELSGGQKRRVAIAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 147 ALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLigEFLNNPQQYEEE 226
Cdd:PRK13637 158 VVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKC--ELQGTPREVFKE 235
|
....*...
gi 488289759 227 pLSYLEKV 234
Cdd:PRK13637 236 -VETLESI 242
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-213 |
4.74e-40 |
|
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: 137.34 E-value: 4.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVY--QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRqqqQQ 79
Cdd:cd03245 3 IEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLR---RN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 80 MGMVFQHYNLLeNLKIYDNVALPLKLLKEkqpEKIERLLTFVDMAHKAEAYP-----------AQLSGGEKQRVSIARAL 148
Cdd:cd03245 80 IGYVPQDVTLF-YGTLRDNITLGAPLADD---ERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488289759 149 SRNPKWLLCDEATSSLDEENTEsvvRLLHKTHQEFRP-TIFFVSHELeTVKRLCNRILVMEKGQLI 213
Cdd:cd03245 156 LNDPPILLLDEPTSAMDMNSEE---RLKERLRQLLGDkTLIIITHRP-SLLDLVDRIIVMDSGRIV 217
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-213 |
4.98e-40 |
|
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: 137.62 E-value: 4.98e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQ--ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRqqqQQ 79
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLR---RQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 80 MGMVFQHyNLLENLKIYDNVALPLKLLKEKQPEKIERLLTFVDMAHK-AEAYP-------AQLSGGEKQRVSIARALSRN 151
Cdd:cd03252 78 VGVVLQE-NVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISElPEGYDtivgeqgAGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488289759 152 PKWLLCDEATSSLDEENTESVVRLLHKTHQEfrPTIFFVSHELETVKRlCNRILVMEKGQLI 213
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICAG--RTVIIIAHRLSTVKN-ADRIIVMEKGRIV 215
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-215 |
7.01e-40 |
|
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: 136.73 E-value: 7.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVqtfsKKEVRQQQQQMG 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV----VREPREVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 82 MVFQHYNLLENLKIYDNVALPLKLL---KEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCD 158
Cdd:cd03265 77 IVFQDLSVDDELTGWENLYIHARLYgvpGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488289759 159 EATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIGE 215
Cdd:cd03265 157 EPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAE 213
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-229 |
1.41e-39 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 140.36 E-value: 1.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQtfskkEVRQQQQQM 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS-----HVPPYQRPI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 81 GMVFQHYNLLENLKIYDNVALPLK---LLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLC 157
Cdd:PRK11607 94 NMMFQSYALFPHMTVEQNIAFGLKqdkLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488289759 158 DEATSSLDEENTE----SVVRLLHKTHQefrpTIFFVSHELETVKRLCNRILVMEKGQL--IGEflnnPQQYEEEPLS 229
Cdd:PRK11607 174 DEPMGALDKKLRDrmqlEVVDILERVGV----TCVMVTHDQEEAMTMAGRIAIMNRGKFvqIGE----PEEIYEHPTT 243
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
14-213 |
1.67e-39 |
|
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: 135.46 E-value: 1.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 14 THALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTfskkevRQQQQQMGMVFQH--YNLLE 91
Cdd:cd03226 13 TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA------KERRKSIGYVMQDvdYQLFT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 92 NlKIYDNVALPLKLLKEKqPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTES 171
Cdd:cd03226 87 D-SVREELLLGLKELDAG-NEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMER 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488289759 172 VVRLLhKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:cd03226 165 VGELI-RELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-227 |
1.87e-39 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 143.71 E-value: 1.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQ----ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQ- 75
Cdd:PRK10535 4 LLELKDIRRSYPsgeeQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 76 QQQQMGMVFQHYNLLENLKIYDNVALPL---KLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNP 152
Cdd:PRK10535 84 RREHFGFIFQRYHLLSHLTAAQNVEVPAvyaGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 153 KWLLCDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHElETVKRLCNRILVMEKGQLIGeflNNPQQYEEEP 227
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQLRDRGH-TVIIVTHD-PQVAAQAERVIEIRDGEIVR---NPPAQEKVNV 233
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-222 |
9.34e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 135.63 E-value: 9.34e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVY---QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGrnvQTFSKKEVRQQQ 77
Cdd:PRK13650 4 IIEVKNLTFKYkedQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG---DLLTEENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 78 QQMGMVFQHY-NLLENLKIYDNVA-------LPLKLLKEKqpekIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALS 149
Cdd:PRK13650 81 HKIGMVFQNPdNQFVGATVEDDVAfglenkgIPHEEMKER----VNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488289759 150 RNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKrLCNRILVMEKGQLigEFLNNPQQ 222
Cdd:PRK13650 157 MRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQV--ESTSTPRE 226
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-213 |
1.04e-38 |
|
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: 134.44 E-value: 1.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEG-EIRIDGRnvqTFSKKEVRQQQQQ 79
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGE---RRGGEDVWELRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 80 MGMV--FQHYNLLENLKI--------YDNVALPLKLlKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALS 149
Cdd:COG1119 80 IGLVspALQLRFPRDETVldvvlsgfFDSIGLYREP-TDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488289759 150 RNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:COG1119 159 KDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVV 222
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-221 |
1.93e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 134.73 E-value: 1.93e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVY--QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGrnvQTFSKKEVRQQQQ 78
Cdd:PRK13632 7 MIKVENVSFSYpnSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDG---ITISKENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 79 QMGMVFQHY-NLLENLKIYDNVALPL---KLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKW 154
Cdd:PRK13632 84 KIGIIFQNPdNQFIGATVEDDIAFGLenkKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488289759 155 LLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKrLCNRILVMEKGQLIG-----EFLNNPQ 221
Cdd:PRK13632 164 IIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAqgkpkEILNNKE 234
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-213 |
2.00e-38 |
|
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: 133.51 E-value: 2.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETH--ALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQqqq 79
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQ--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 80 MGMVFQHyNLLENLKIYDNVALPLKllkEKQPEKIErlltfvDMAHKAEAYP-----------------AQLSGGEKQRV 142
Cdd:cd03251 78 IGLVSQD-VFLFNDTVAENIAYGRP---GATREEVE------EAARAANAHEfimelpegydtvigergVKLSGGQRQRI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488289759 143 SIARALSRNPKWLLCDEATSSLDEENTESVVRLLHKThQEFRpTIFFVSHELETVKRlCNRILVMEKGQLI 213
Cdd:cd03251 148 AIARALLKDPPILILDEATSALDTESERLVQAALERL-MKNR-TTFVIAHRLSTIEN-ADRIVVLEDGKIV 215
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-231 |
2.19e-38 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 134.37 E-value: 2.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLM---EQPSEGEIRIDGRNVQTFSK--KEVRQ 75
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRlaRDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 76 QQQQMGMVFQHYNLLENLKIYDNVALP-----------LKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSI 144
Cdd:PRK09984 84 SRANTGYIFQQFNLVNRLSVLENVLIGalgstpfwrtcFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 145 ARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIgeFLNNPQQYE 224
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVF--YDGSSQQFD 241
|
....*..
gi 488289759 225 EEPLSYL 231
Cdd:PRK09984 242 NERFDHL 248
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-213 |
4.42e-38 |
|
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: 132.74 E-value: 4.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQ-ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRqqqQQM 80
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLR---RAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 81 GMVFQHyNLLENLKIYDNVAL--PlkllkEKQPEKIERLLTFVDMAHKAEAYPAQ-----------LSGGEKQRVSIARA 147
Cdd:cd03253 78 GVVPQD-TVLFNDTIGYNIRYgrP-----DATDEEVIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488289759 148 LSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEfRPTIfFVSHELETVKRlCNRILVMEKGQLI 213
Cdd:cd03253 152 ILKNPPILLLDEATSALDTHTEREIQAALRDVSKG-RTTI-VIAHRLSTIVN-ADKIIVLKDGRIV 214
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
16-220 |
5.46e-38 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 136.70 E-value: 5.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 16 ALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQ-QQQQMGMVFQHYNLLENLK 94
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvRRKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 95 IYDNVALPLKLL---KEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLD----EE 167
Cdd:PRK10070 123 VLDNTAFGMELAginAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDplirTE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488289759 168 NTESVVRLLHKtHQEfrpTIFFVSHELETVKRLCNRILVMEKGQLI-----GEFLNNP 220
Cdd:PRK10070 203 MQDELVKLQAK-HQR---TIVFISHDLDEAMRIGDRIAIMQNGEVVqvgtpDEILNNP 256
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-216 |
1.26e-37 |
|
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: 131.08 E-value: 1.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETH--ALKNIHFSVQLGEIVGIVGKSGSGKSTL-LRLLNLMEqPSEGEIRIDGRNVQTFSKKEVRqqqQ 78
Cdd:cd03244 3 IEFKNVSLRYRPNLppVLKNISFSIKPGEKVGIVGRTGSGKSSLlLALFRLVE-LSSGSILIDGVDISKIGLHDLR---S 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 79 QMGMVFQHYNLL-----ENLKIYD-------NVALPLKLLKE---KQPEKIErlltfvdmaHKAEAYPAQLSGGEKQRVS 143
Cdd:cd03244 79 RISIIPQDPVLFsgtirSNLDPFGeysdeelWQALERVGLKEfveSLPGGLD---------TVVEEGGENLSVGQRQLLC 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488289759 144 IARALSRNPKWLLCDEATSSLDEENTESVVRLLhktHQEFR-PTIFFVSHELETVKRlCNRILVMEKGQLIgEF 216
Cdd:cd03244 150 LARALLRKSKILVLDEATASVDPETDALIQKTI---REAFKdCTVLTIAHRLDTIID-SDRILVLDKGRVV-EF 218
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
2-222 |
1.28e-37 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 132.27 E-value: 1.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVY---------QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTfskKE 72
Cdd:COG4167 5 LEVRNLSKTFkyrtglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEY---GD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 73 VRQQQQQMGMVFQHYN--LLENLKIYDNVALPLKL---LKEKQ-PEKIERLLTFVDM-AHKAEAYPAQLSGGEKQRVSIA 145
Cdd:COG4167 82 YKYRCKHIRMIFQDPNtsLNPRLNIGQILEEPLRLntdLTAEErEERIFATLRLVGLlPEHANFYPHMLSSGQKQRVALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 146 RALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI-----GEFLNNP 220
Cdd:COG4167 162 RALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVeygktAEVFANP 241
|
..
gi 488289759 221 QQ 222
Cdd:COG4167 242 QH 243
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-213 |
1.65e-37 |
|
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: 131.12 E-value: 1.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVY---QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQqq 78
Cdd:cd03249 1 IEFKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQ-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 79 qMGMVFQHYNLLENlKIYDNVALPLKLLKEKQPEKIerlltfvdmAHKAEAYP-----------------AQLSGGEKQR 141
Cdd:cd03249 79 -IGLVSQEPVLFDG-TIAENIRYGKPDATDEEVEEA---------AKKANIHDfimslpdgydtlvgergSQLSGGQKQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488289759 142 VSIARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFrpTIFFVSHELETVKRlCNRILVMEKGQLI 213
Cdd:cd03249 148 IAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGR--TTIVIAHRLSTIRN-ADLIAVLQNGQVV 216
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-200 |
3.02e-37 |
|
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: 129.52 E-value: 3.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQtfskKEVRQQQQQM 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIR----DAREDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 81 GMVFqHYNLL-ENLKIYDNVALPLKLLKEKQP-EKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCD 158
Cdd:COG4133 78 AYLG-HADGLkPELTVRENLRFWAALYGLRADrEAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488289759 159 EATSSLDEENTESVVRLLHKtHQEFRPTIFFVSH---ELETVKRL 200
Cdd:COG4133 157 EPFTALDAAGVALLAELIAA-HLARGGAVLLTTHqplELAAARVL 200
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-213 |
1.84e-36 |
|
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: 127.69 E-value: 1.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETHALKNIHFSVQLGeIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVqtfsKKEVRQQQQQMG 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV----LKQPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 82 MVFQHYNLLENLKIYDNVALpLKLLKE----KQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLC 157
Cdd:cd03264 76 YLPQEFGVYPNFTVREFLDY-IAWLKGipskEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488289759 158 DEATSSLDEENTESVVRLLHKTHQEfrpTIFFVS-HELETVKRLCNRILVMEKGQLI 213
Cdd:cd03264 155 DEPTAGLDPEERIRFRNLLSELGED---RIVILStHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-214 |
3.01e-36 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 128.64 E-value: 3.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 6 NVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIrIDGRNVQTFSKKEVRqqqqqmgMVFQ 85
Cdd:PRK11247 17 AVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLAEAREDTR-------LMFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 86 HYNLLENLKIYDNVALPlklLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLD 165
Cdd:PRK11247 89 DARLLPWKKVIDNVGLG---LKGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488289759 166 E----ENTESVVRLLhkthQEFRPTIFFVSHELETVKRLCNRILVMEKGQlIG 214
Cdd:PRK11247 166 AltriEMQDLIESLW----QQHGFTVLLVTHDVSEAVAMADRVLLIEEGK-IG 213
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
4-210 |
3.29e-36 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 131.31 E-value: 3.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 4 LVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQtfskkEVRQQQQQMGMV 83
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN-----DVPPAERGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 84 FQHYNLLENLKIYDNVALPLKLLKEKQPE---KIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEA 160
Cdd:PRK11000 81 FQSYALYPHLSVAENMSFGLKLAGAKKEEinqRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 161 TSSLDeenteSVVRL-----LHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKG 210
Cdd:PRK11000 161 LSNLD-----AALRVqmrieISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAG 210
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-211 |
3.63e-36 |
|
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: 127.55 E-value: 3.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVY-------QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQT-FSKKE 72
Cdd:COG4778 4 LLEVENLSKTFtlhlqggKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVdLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 73 VRQ----QQQQMGMVFQHYNLLENLKIYDNVALPLKLL---KEKQPEKIERLLTFVDMAHK-AEAYPAQLSGGEKQRVSI 144
Cdd:COG4778 84 PREilalRRRTIGYVSQFLRVIPRVSALDVVAEPLLERgvdREEARARARELLARLNLPERlWDLPPATFSGGEQQRVNI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488289759 145 ARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQ 211
Cdd:COG4778 164 ARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGT-AIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
15-210 |
3.95e-36 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 130.08 E-value: 3.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 15 HALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQQQQMGMVFQH-YNLLE-N 92
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKIQIVFQNpYGSLNpR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 93 LKIYDNVALPL----KLLKEKQPEKIERLLTFVDM-AHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEE 167
Cdd:PRK11308 109 KKVGQILEEPLlintSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVS 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488289759 168 NTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVM------EKG 210
Cdd:PRK11308 189 VQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMylgrcvEKG 237
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-222 |
5.27e-36 |
|
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: 133.27 E-value: 5.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 12 QETHALKNIHFSVQLGEIVGIVGKSGSGKS-TLLRLLNLMEQPS---EGEIRIDGRNVQTFSKKEVRQ-QQQQMGMVFQh 86
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPAahpSGSILFDGQDLLGLSERELRRiRGNRIAMIFQ- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 87 ynllE-----N--LKIYDNVALPLKL---LKEKQP-EKIERLLTFV---DMAHKAEAYPAQLSGGEKQRVSIARALSRNP 152
Cdd:COG4172 100 ----EpmtslNplHTIGKQIAEVLRLhrgLSGAAArARALELLERVgipDPERRLDAYPHQLSGGQRQRVMIAMALANEP 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 153 KWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI-----GEFLNNPQQ 222
Cdd:COG4172 176 DLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVeqgptAELFAAPQH 250
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
16-216 |
2.62e-35 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 132.01 E-value: 2.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 16 ALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRqqqQQMGMVFQHYNLLeNLKI 95
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLR---RNIAVVFQDAGLF-NRSI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 96 YDNvalpLKLLKEKQpekierllTFVDMAHKAEAYPA--------------------QLSGGEKQRVSIARALSRNPKWL 155
Cdd:PRK13657 426 EDN----IRVGRPDA--------TDEEMRAAAERAQAhdfierkpdgydtvvgergrQLSGGERQRLAIARALLKDPPIL 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488289759 156 LCDEATSSLDEEnTESVVRLLHKTHQEFRpTIFFVSHELETVkRLCNRILVMEKGQLI--GEF 216
Cdd:PRK13657 494 ILDEATSALDVE-TEAKVKAALDELMKGR-TTFIIAHRLSTV-RNADRILVFDNGRVVesGSF 553
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-215 |
4.47e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 125.96 E-value: 4.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQE-THALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQtFSKKEVRQQQQQ 79
Cdd:PRK13639 1 ILETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 80 MGMVFQHY-NLLENLKIYDNVA---LPLKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWL 155
Cdd:PRK13639 80 VGIVFQNPdDQLFAPTVEEDVAfgpLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEII 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 156 LCDEATSSLDEENTESVVRLLHKTHQEfRPTIFFVSHELETVKRLCNRILVMEKGQLIGE 215
Cdd:PRK13639 160 VLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKE 218
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-210 |
5.35e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 125.63 E-value: 5.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQ--ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQqq 78
Cdd:PRK13648 7 IIVFKNVSFQYQsdASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKH-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 79 qMGMVFQH--YNLLENLKIYD------NVALPLKLLKEKQPEKIERlltfVDMAHKAEAYPAQLSGGEKQRVSIARALSR 150
Cdd:PRK13648 85 -IGIVFQNpdNQFVGSIVKYDvafgleNHAVPYDEMHRRVSEALKQ----VDMLERADYEPNALSGGQKQRVAIAGVLAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488289759 151 NPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHEL-ETVKrlCNRILVMEKG 210
Cdd:PRK13648 160 NPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLsEAME--ADHVIVMNKG 218
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-216 |
5.61e-35 |
|
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: 123.87 E-value: 5.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKevrqqQQQMG 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA-----LRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 82 MVFQHYNLLENLKIYDNVALPLKLLKEKQpEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEAT 161
Cdd:cd03268 76 ALIEAPGFYPNLTARENLRLLARLLGIRK-KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 162 SSLDEENTESVVRLLHKtHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIGEF 216
Cdd:cd03268 155 NGLDPDGIKELRELILS-LRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-213 |
8.39e-35 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 124.88 E-value: 8.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKkevRQQQQQM 80
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSP---AELARRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 81 GMVFQHYNLLENLKIYDNVAL---PLKLLKEKQPEKIERLLTFVDMAHKAE-AYPaQLSGGEKQRVSIARAL------SR 150
Cdd:PRK13548 79 AVLPQHSSLSFPFTVEEVVAMgraPHGLSRAEDDALVAAALAQVDLAHLAGrDYP-QLSGGEQQRVQLARVLaqlwepDG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488289759 151 NPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:PRK13548 158 PPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLV 220
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
9-229 |
3.54e-34 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 128.28 E-value: 3.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 9 KVYQETHALKNIHFSVQLGEIVGIVGKSGSGKST----LLRLLNlmeqpSEGEIRIDGRNVQTFSKKEVRQQQQQMGMVF 84
Cdd:PRK15134 294 RTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQLLPVRHRIQVVF 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 85 QHYN--LLENLKIYDNVALPLK-----LLKEKQPEKIERLLTFVDM-AHKAEAYPAQLSGGEKQRVSIARALSRNPKWLL 156
Cdd:PRK15134 369 QDPNssLNPRLNVLQIIEEGLRvhqptLSAAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLII 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488289759 157 CDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIGE-----FLNNPQQ-YEEEPLS 229
Cdd:PRK15134 449 LDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQgdcerVFAAPQQeYTRQLLA 527
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
14-213 |
6.20e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 123.03 E-value: 6.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 14 THALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQtFSKKEVRQQQQQMGMVFQHY-NLLEN 92
Cdd:PRK13636 19 THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID-YSRKGLMKLRESVGMVFQDPdNQLFS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 93 LKIYDNV---ALPLKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENT 169
Cdd:PRK13636 98 ASVYQDVsfgAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGV 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488289759 170 ESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:PRK13636 178 SEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI 221
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-213 |
9.68e-34 |
|
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: 127.53 E-value: 9.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVY--QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQqqq 79
Cdd:TIGR02203 331 VEFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQ--- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 80 MGMVFQHYNLLeNLKIYDNVALplKLLKEKQPEKIER------LLTFVDMAHKAEAYP-----AQLSGGEKQRVSIARAL 148
Cdd:TIGR02203 408 VALVSQDVVLF-NDTIANNIAY--GRTEQADRAEIERalaaayAQDFVDKLPLGLDTPigengVLLSGGQRQRLAIARAL 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 149 SRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEfRPTIfFVSHELETVKRlCNRILVMEKGQLI 213
Cdd:TIGR02203 485 LKDAPILILDEATSALDNESERLVQAALERLMQG-RTTL-VIAHRLSTIEK-ADRIVVMDDGRIV 546
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-213 |
1.03e-33 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 121.76 E-value: 1.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKkevRQQQQQM 80
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSP---WELARRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 81 GMVFQHYNLLENLKIYDNVAL---PLKLLKEKQPEKIERLLTFVDMAHKAE-AYPaQLSGGEKQRVSIARAL-------S 149
Cdd:COG4559 78 AVLPQHSSLAFPFTVEEVVALgraPHGSSAAQDRQIVREALALVGLAHLAGrSYQ-TLSGGEQQRVQLARVLaqlwepvD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 150 RNPKWLLCDEATSSLDEENTESVVRLLHK-THQEFrpTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:COG4559 157 GGPRWLFLDEPTSALDLAHQHAVLRLARQlARRGG--GVVAVLHDLNLAAQYADRILLLHQGRLV 219
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-213 |
1.24e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 121.49 E-value: 1.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLM-----EQPSEGEIRIDGRNVqtFSKK----E 72
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNI--YSPDvdpiE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 73 VRQQqqqMGMVFQHYNLLENLKIYDNVALPLKL-----LKEKQPEKIERLLT----FVDMAHKAEAYPAQLSGGEKQRVS 143
Cdd:PRK14267 83 VRRE---VGMVFQYPNPFPHLTIYDNVAIGVKLnglvkSKKELDERVEWALKkaalWDEVKDRLNDYPSNLSGGQRQRLV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 144 IARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFrpTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLI 227
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
12-212 |
1.25e-33 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 121.04 E-value: 1.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 12 QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQ-QQQQMGMVFQHYNLL 90
Cdd:PRK10584 21 HELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKlRAKHVGFVFQSFMLI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 91 ENLKIYDNVALPLKLLKEKQPEKIER---LLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEE 167
Cdd:PRK10584 101 PTLNALENVELPALLRGESSRQSRNGakaLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQ 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488289759 168 NTESVVRLLHKTHQEFRPTIFFVSHELETVKRlCNRILVMEKGQL 212
Cdd:PRK10584 181 TGDKIADLLFSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQL 224
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-214 |
1.63e-33 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 123.80 E-value: 1.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQ-ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEvrqqqQQ 79
Cdd:PRK11650 3 GLKLQAVRKSYDgKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD-----RD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 80 MGMVFQHYNLLENLKIYDNVALPLKLLKEKQPEKIERlltfVDMAHKA---EAY----PAQLSGGEKQRVSIARALSRNP 152
Cdd:PRK11650 78 IAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEER----VAEAARIlelEPLldrkPRELSGGQRQRVAMGRAIVREP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488289759 153 KWLLCDEATSSLDeentesvVRL-------LHKTHQEFRPTIFFVSH-ELETVKrLCNRILVMEKGQL--IG 214
Cdd:PRK11650 154 AVFLFDEPLSNLD-------AKLrvqmrleIQRLHRRLKTTSLYVTHdQVEAMT-LADRVVVMNGGVAeqIG 217
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-195 |
2.13e-33 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 120.96 E-value: 2.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEvrqqqqqm 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 81 GMVFQHYNLLENLKIYDNVALPLKLL---KEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLC 157
Cdd:PRK11248 73 GVVFQNEGLLPWRNVQDNVAFGLQLAgveKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 488289759 158 DEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELE 195
Cdd:PRK11248 153 DEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIE 190
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-215 |
2.27e-33 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 119.78 E-value: 2.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQ----ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQtfskKEVRQQ 76
Cdd:cd03266 1 MITADALTKRFRdvkkTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV----KEPAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 77 QQQMGMVFQHYNLLENLKIYDNVALPLKL--LKEKQPE-KIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPK 153
Cdd:cd03266 77 RRRLGFVSDSTGLYDRLTARENLEYFAGLygLKGDELTaRLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488289759 154 WLLCDEATSSLDEENTESVVRLLhKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIGE 215
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFI-RQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
16-212 |
2.38e-33 |
|
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: 118.69 E-value: 2.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 16 ALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQqqqmGMVF-----QHYNLL 90
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRA----GIAYvpedrKREGLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 91 ENLKIYDNVALPlkllkekqpekierlltfvdmahkaeaypAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTE 170
Cdd:cd03215 91 LDLSVAENIALS-----------------------------SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488289759 171 SVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQL 212
Cdd:cd03215 142 EIYRLIRELADAGK-AVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-213 |
2.55e-33 |
|
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: 126.47 E-value: 2.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETHA-LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQqqqM 80
Cdd:COG5265 358 VRFENVSFGYDPERPiLKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAA---I 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 81 GMVFQHyNLLENLKIYDNVAL--PlkllkEKQPEKIER------LLTFVdmAHKAEAYPAQ-------LSGGEKQRVSIA 145
Cdd:COG5265 435 GIVPQD-TVLFNDTIAYNIAYgrP-----DASEEEVEAaaraaqIHDFI--ESLPDGYDTRvgerglkLSGGEKQRVAIA 506
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488289759 146 RALSRNPKWLLCDEATSSLD---EENTESVVRLLHKTHqefrpTIFFVSHELETVKRlCNRILVMEKGQLI 213
Cdd:COG5265 507 RTLLKNPPILIFDEATSALDsrtERAIQAALREVARGR-----TTLVIAHRLSTIVD-ADEILVLEAGRIV 571
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-222 |
5.30e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 120.02 E-value: 5.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLM-----EQPSEGEIRIDGRNVQTFSKKEVRQQ 76
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 77 QQqmgMVFQHYNLLENLKIYDNVALPLKL---------LKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARA 147
Cdd:PRK14247 84 VQ---MVFQIPNPIPNLSIFENVALGLKLnrlvkskkeLQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 148 LSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFrpTIFFVSHELETVKRLCNRILVMEKGQLI-----GEFLNNPQQ 222
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVewgptREVFTNPRH 238
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-207 |
9.08e-33 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 124.32 E-value: 9.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQ-ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRqqqQQM 80
Cdd:TIGR02857 322 LEFSGVSVAYPgRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWR---DQI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 81 GMVFQHYNLLENlKIYDNVALPlklLKEKQPEKIERLLTFVDMAHKAEAYP-----------AQLSGGEKQRVSIARALS 149
Cdd:TIGR02857 399 AWVPQHPFLFAG-TIAENIRLA---RPDASDAEIREALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLALARAFL 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488289759 150 RNPKWLLCDEATSSLDEEnTESVV----RLLHKTHqefrpTIFFVSHELETVkRLCNRILVM 207
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAE-TEAEVlealRALAQGR-----TVLLVTHRLALA-ALADRIVVL 529
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-213 |
9.62e-33 |
|
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: 118.15 E-value: 9.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTfskkevrQQQQQMG 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI-------AARNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 82 MVFQHYNLLENLKIYDNVAL--PLKLLKEKQPEK-IERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCD 158
Cdd:cd03269 74 YLPEERGLYPKMKVIDQLVYlaQLKGLKKEEARRrIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 159 EATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:cd03269 154 EPFSGLDPVNVELLKDVIRELARAGK-TVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-213 |
1.56e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 119.00 E-value: 1.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 3 ELVNVSKVY---QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRnVQTFSKKEVR----Q 75
Cdd:PRK14246 9 DVFNISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGK-VLYFGKDIFQidaiK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 76 QQQQMGMVFQHYNLLENLKIYDNVALPLKL--LKEKQP------EKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARA 147
Cdd:PRK14246 88 LRKEVGMVFQQPNPFPHLSIYDNIAYPLKShgIKEKREikkiveECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488289759 148 LSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFrpTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:PRK14246 168 LALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELV 231
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
16-221 |
2.00e-32 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 120.20 E-value: 2.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 16 ALKNIHFSVQLGEIVGIVGKSGSGKSTLLR-LLNLMEQpSEGEIRIDGRNVQTFSKKEVRQQQQQMGMVFQH--YNLLEN 92
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARaIIGLVKA-TDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQDplASLNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 93 LKIYDNVALPL-----KLLKEKQPEKIERLLTFVDM-AHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDE 166
Cdd:PRK15079 115 MTIGEIIAEPLrtyhpKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 167 ENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI-----GEFLNNPQ 221
Cdd:PRK15079 195 SIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVelgtyDEVYHNPL 254
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-212 |
3.38e-32 |
|
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: 117.19 E-value: 3.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQ---ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQqq 78
Cdd:cd03248 12 VKFQNVTFAYPtrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 79 qMGMVFQHYNLLENlKIYDNVALPLkllkekQPEKIERLLTFVDMAHKAEAYP--------------AQLSGGEKQRVSI 144
Cdd:cd03248 90 -VSLVGQEPVLFAR-SLQDNIAYGL------QSCSFECVKEAAQKAHAHSFISelasgydtevgekgSQLSGGQKQRVAI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488289759 145 ARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQefRPTIFFVSHELETVKRlCNRILVMEKGQL 212
Cdd:cd03248 162 ARALIRNPQVLILDEATSALDAESEQQVQQALYDWPE--RRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-215 |
4.51e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 118.17 E-value: 4.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQE-THALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSK-KEVRqqqQ 78
Cdd:PRK13644 1 MIRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIR---K 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 79 QMGMVFQH-------YNLLENLKI-YDNVALPlkllkekqPEKIERLltfVDMA---HKAEAY----PAQLSGGEKQRVS 143
Cdd:PRK13644 78 LVGIVFQNpetqfvgRTVEEDLAFgPENLCLP--------PIEIRKR---VDRAlaeIGLEKYrhrsPKTLSGGQGQCVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488289759 144 IARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVkRLCNRILVMEKGQLIGE 215
Cdd:PRK13644 147 LAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGK-TIVYITHNLEEL-HDADRIIVMDRGKIVLE 216
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-213 |
6.16e-32 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 122.24 E-value: 6.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVY--QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRqqqQQ 79
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALR---QA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 80 MGMVFQHYNLL-----ENLKIydnvALPlkllkEKQPEKIERLLTFVDMAHKAEAYPA----------QLSGGEKQRVSI 144
Cdd:PRK11160 416 ISVVSQRVHLFsatlrDNLLL----AAP-----NASDEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGI 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488289759 145 ARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEfrPTIFFVSHELETVKRLcNRILVMEKGQLI 213
Cdd:PRK11160 487 ARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQN--KTVLMITHRLTGLEQF-DRICVMDNGQII 552
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-211 |
1.82e-31 |
|
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: 115.22 E-value: 1.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQtfskkevRQQQQQ-- 79
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDIT-------GLPPHEra 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 80 ---MGMVFQHYNLLENLKIYDNVALPLKLL-KEKQPEKIERLLT-FVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKW 154
Cdd:cd03224 74 ragIGYVPEGRRIFPELTVEENLLLGAYARrRAKRKARLERVYElFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 155 LLCDEATSSLdeenTESVVRLLHKTHQEFRP---TIFFVSHELETVKRLCNRILVMEKGQ 211
Cdd:cd03224 154 LLLDEPSEGL----APKIVEEIFEAIRELRDegvTILLVEQNARFALEIADRAYVLERGR 209
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-213 |
3.13e-31 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 120.51 E-value: 3.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQ--ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRqqqQQ 79
Cdd:PRK11176 342 IEFRNVTFTYPgkEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLR---NQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 80 MGMVFQHYNLLeNLKIYDNVALPLKllKEKQPEKIERLLTfvdMAHKAEAYP--------------AQLSGGEKQRVSIA 145
Cdd:PRK11176 419 VALVSQNVHLF-NDTIANNIAYART--EQYSREQIEEAAR---MAYAMDFINkmdngldtvigengVLLSGGQRQRIAIA 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 146 RALSRNPKWLLCDEATSSLDeenTESvVRLLHKTHQEFRP--TIFFVSHELETVKRlCNRILVMEKGQLI 213
Cdd:PRK11176 493 RALLRDSPILILDEATSALD---TES-ERAIQAALDELQKnrTSLVIAHRLSTIEK-ADEILVVEDGEIV 557
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-213 |
4.55e-31 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 114.79 E-value: 4.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVY----------------------QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEI 58
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 59 RIDGRNVQTFSkkevrqqqqqMGMVFqHYNL--LENlkIYDNVALpLKLLKEKQPEKIER------LLTFVDMAHKaeAY 130
Cdd:COG1134 84 EVNGRVSALLE----------LGAGF-HPELtgREN--IYLNGRL-LGLSRKEIDEKFDEivefaeLGDFIDQPVK--TY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 131 paqlSGGEKQRVSIARALSRNPKWLLCDEATSSLDEentesvvRLLHKTHQEFR------PTIFFVSHELETVKRLCNRI 204
Cdd:COG1134 148 ----SSGMRARLAFAVATAVDPDILLVDEVLAVGDA-------AFQKKCLARIRelresgRTVIFVSHSMGAVRRLCDRA 216
|
....*....
gi 488289759 205 LVMEKGQLI 213
Cdd:COG1134 217 IWLEKGRLV 225
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-212 |
5.76e-31 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 113.91 E-value: 5.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQetHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKkevrqQQQQM 80
Cdd:PRK10771 1 MLKLTDITWLYH--HLPMRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPP-----SRRPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 81 GMVFQHYNLLENLKIYDNVAL---P-LKLlKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLL 156
Cdd:PRK10771 74 SMLFQENNLFSHLTVAQNIGLglnPgLKL-NAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488289759 157 CDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQL 212
Cdd:PRK10771 153 LDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-216 |
9.63e-31 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 118.48 E-value: 9.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 3 ELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVrqQQQQMGM 82
Cdd:PRK11288 6 SFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAA--LAAGVAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 83 VFQHYNLLENLKIYDNV---ALP-------LKLLKEKQPEKIERLLTFVDmahkAEAYPAQLSGGEKQRVSIARALSRNP 152
Cdd:PRK11288 84 IYQELHLVPEMTVAENLylgQLPhkggivnRRLLNYEAREQLEHLGVDID----PDTPLKYLSIGQRQMVEIAKALARNA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488289759 153 KWLLCDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLIGEF 216
Cdd:PRK11288 160 RVIAFDEPTSSLSAREIEQLFRVIRELRAEGR-VILYVSHRMEEIFALCDAITVFKDGRYVATF 222
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-213 |
1.50e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 114.44 E-value: 1.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQtfskkevRQQQQQM 80
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD-------PEDRRRI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 81 GmvfqhYnLLE------NLKIYDNVA--LPLKLLKEKQ-PEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRN 151
Cdd:COG4152 74 G-----Y-LPEerglypKMKVGEQLVylARLKGLSKAEaKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHD 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488289759 152 PKWLLCDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:COG4152 148 PELLILDEPFSGLDPVNVELLKDVIRELAAKGT-TVIFSSHQMELVEELCDRIVIINKGRKV 208
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-215 |
1.81e-30 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 114.52 E-value: 1.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTfskkEVRQQQQQMG 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS----RARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 82 MVFQHYNL------LENLKIYDN-VALPLKLLKEKQPEkierLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKW 154
Cdd:PRK13537 84 VVPQFDNLdpdftvRENLLVFGRyFGLSAAAARALVPP----LLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 155 LLCDEATSSLDEENT----ESVVRLLHKTHqefrpTIFFVSHELETVKRLCNRILVMEKGQLIGE 215
Cdd:PRK13537 160 LVLDEPTTGLDPQARhlmwERLRSLLARGK-----TILLTTHFMEEAERLCDRLCVIEEGRKIAE 219
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-165 |
2.32e-30 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 111.80 E-value: 2.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLL--NLMEQPS-EGEIRIDGRNVQTfskkeVRQQQ 77
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIagTLSPAFSaSGEVLLNGRRLTA-----LPAEQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 78 QQMGMVFQ------HYNLLENLKIydnvALPLKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRN 151
Cdd:COG4136 76 RRIGILFQddllfpHLSVGENLAF----ALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAE 151
|
170
....*....|....
gi 488289759 152 PKWLLCDEATSSLD 165
Cdd:COG4136 152 PRALLLDEPFSKLD 165
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
17-213 |
2.81e-30 |
|
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: 111.10 E-value: 2.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLN--LMEQPSEGEIRIDGRNVqtfSKKEVRQQqqqMGMVFQHYNLLENLK 94
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPL---DKRSFRKI---IGYVPQDDILHPTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 95 IYDNVALPLKLlkekqpekierlltfvdmahkaeaypAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTESVVR 174
Cdd:cd03213 99 VRETLMFAAKL--------------------------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMS 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488289759 175 LLHKTHQEFRpTIFFVSHEL-ETVKRLCNRILVMEKGQLI 213
Cdd:cd03213 153 LLRRLADTGR-TIICSIHQPsSEIFELFDKLLLLSQGRVI 191
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-225 |
3.05e-30 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 117.09 E-value: 3.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIdGRNVQT--FSkkevrQQQQ 78
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVKIgyFD-----QHQE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 79 QmgmvfqhynLLENLKIYDNVAlplKLLKEKQPEKI----ERLLTFVDMAHKaeaYPAQLSGGEKQRVSIARALSRNPKW 154
Cdd:COG0488 389 E---------LDPDKTVLDELR---DGAPGGTEQEVrgylGRFLFSGDDAFK---PVGVLSGGEKARLALAKLLLSPPNV 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488289759 155 LLCDEATSSLDEENTESVVRLLhkthQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIgEFLNNPQQYEE 225
Cdd:COG0488 454 LLLDEPTNHLDIETLEALEEAL----DDFPGTVLLVSHDRYFLDRVATRILEFEDGGVR-EYPGGYDDYLE 519
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-215 |
3.13e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 113.26 E-value: 3.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVY------QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGrnVQTFSKKEVR 74
Cdd:PRK13633 4 MIKCKNVSYKYesneesTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 75 QQQQQMGMVFQHY-NLLENLKIYDNVAL-P--LKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSR 150
Cdd:PRK13633 82 DIRNKAGMVFQNPdNQIVATIVEEDVAFgPenLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 151 NPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRlCNRILVMEKGQLIGE 215
Cdd:PRK13633 162 RPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVME 225
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
6-226 |
3.29e-30 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 112.56 E-value: 3.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 6 NVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLM-----EQPSEGEIRIDGRNVQTfSKKEVRQQQQQM 80
Cdd:PRK14239 10 DLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYS-PRTDTVDLRKEI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 81 GMVFQHYNLLEnLKIYDNVALPLKL--LKEKQ--PEKIERLL----TFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNP 152
Cdd:PRK14239 89 GMVFQQPNPFP-MSIYENVVYGLRLkgIKDKQvlDEAVEKSLkgasIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 153 KWLLCDEATSSLDEENTESVVRLLHKTHQEFrpTIFFVSHELETVKRLCNRILVMEKGQLIgEFLN------NPQQYEEE 226
Cdd:PRK14239 168 KIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLI-EYNDtkqmfmNPKHKETE 244
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-215 |
3.45e-30 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 114.54 E-value: 3.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVqtfsKKEVRQQQQQMG 81
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV----PARARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 82 MVFQHYNL------LENLKIYDNValpLKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWL 155
Cdd:PRK13536 118 VVPQFDNLdleftvRENLLVFGRY---FGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLL 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488289759 156 LCDEATSSLDEENT----ESVVRLLHKTHqefrpTIFFVSHELETVKRLCNRILVMEKGQLIGE 215
Cdd:PRK13536 195 ILDEPTTGLDPHARhliwERLRSLLARGK-----TILLTTHFMEEAERLCDRLCVLEAGRKIAE 253
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-213 |
4.37e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 112.97 E-value: 4.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETH--ALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLN---LMEQPSEGEIRIDGRNVQTFSKKEVRQQ 76
Cdd:PRK13640 6 VEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINgllLPDDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 77 qqqMGMVFQHY-NLLENLKIYDNVALPLKLLKEKQPEKIE---RLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNP 152
Cdd:PRK13640 86 ---VGIVFQNPdNQFVGATVGDDVAFGLENRAVPRPEMIKivrDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488289759 153 KWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKrLCNRILVMEKGQLI 213
Cdd:PRK13640 163 KIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLL 222
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2-214 |
5.35e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 113.19 E-value: 5.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQ-----ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSK-KEVRQ 75
Cdd:PRK13634 3 ITFQKVEHRYQyktpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKnKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 76 QQQQMGMVFQ--HYNLLENLKIYD------NVALPlkllKEKQPEKIERLLTFVDMAHKA-EAYPAQLSGGEKQRVSIAR 146
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDicfgpmNFGVS----EEDAKQKAREMIELVGLPEELlARSPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488289759 147 ALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIG 214
Cdd:PRK13634 159 VLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFL 226
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-213 |
5.81e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 113.26 E-value: 5.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQ-----ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSK------ 70
Cdd:PRK13651 3 IKVKNIVKIFNkklptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKtkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 71 ---------------KEVRQQQQQMGMVFQ--HYNLLENLKIYDNVALPLKLLKEKQpEKIERLLTFVDMAHKAEAY--- 130
Cdd:PRK13651 83 vleklviqktrfkkiKKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKE-EAKKRAAKYIELVGLDESYlqr 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 131 -PAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEK 209
Cdd:PRK13651 162 sPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVLEWTKRTIFFKD 240
|
....
gi 488289759 210 GQLI 213
Cdd:PRK13651 241 GKII 244
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-211 |
5.92e-30 |
|
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: 108.69 E-value: 5.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDgrnvqtfskkevrqqqqqmg 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 82 mvfqhynllENLKIydnvalplkllkekqpekierlltfvdmahkaeAYPAQLSGGEKQRVSIARALSRNPKWLLCDEAT 161
Cdd:cd03221 61 ---------STVKI---------------------------------GYFEQLSGGEKMRLALAKLLLENPNLLLLDEPT 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488289759 162 SSLDEENTESVVRLLhkthQEFRPTIFFVSHELETVKRLCNRILVMEKGQ 211
Cdd:cd03221 99 NHLDLESIEALEEAL----KEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-215 |
9.30e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 112.11 E-value: 9.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQ---ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGrnvQTFSKKEVRQQQ 77
Cdd:PRK13642 4 ILEVENLVFKYEkesDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDG---ELLTAENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 78 QQMGMVFQHY-NLLENLKIYDNVALPLK---LLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPK 153
Cdd:PRK13642 81 RKIGMVFQNPdNQFVGATVEDDVAFGMEnqgIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488289759 154 WLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRlCNRILVMEKGQLIGE 215
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKE 221
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
16-211 |
1.36e-29 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 112.90 E-value: 1.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 16 ALKNIHFSVQLGEIVGIVGKSGSGKS-TLLRLLNLMEQPS--EGEIRIDGRNVQTFSKKEV-RQQQQQMGMVFQH--YNL 89
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANGriGGSATFNGREILNLPEKELnKLRAEQISMIFQDpmTSL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 90 LENLKIYDNVALPLKLLK-----EKQPEKIeRLLTFVDM--AHK-AEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEAT 161
Cdd:PRK09473 111 NPYMRVGEQLMEVLMLHKgmskaEAFEESV-RMLDAVKMpeARKrMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPT 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488289759 162 SSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQ 211
Cdd:PRK09473 190 TALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 239
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
8-213 |
1.39e-29 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 116.11 E-value: 1.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 8 SKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQQQQMGMVFQ-- 85
Cdd:PRK10261 331 NRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQdp 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 86 HYNLLENLKIYDNVALPLK----LLKEKQPEKIERLLTFVDM-AHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEA 160
Cdd:PRK10261 411 YASLDPRQTVGDSIMEPLRvhglLPGKAAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEA 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488289759 161 TSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:PRK10261 491 VSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-193 |
3.38e-29 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 109.42 E-value: 3.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQqqqM 80
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQ---V 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 81 GMVFQHYNLLENlKIYDNVALPLKLLKEK-QPEKIERLLTFVDMA-HKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCD 158
Cdd:PRK10247 84 SYCAQTPTLFGD-TVYDNLIFPWQIRNQQpDPAIFLDDLERFALPdTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLD 162
|
170 180 190
....*....|....*....|....*....|....*
gi 488289759 159 EATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHE 193
Cdd:PRK10247 163 EITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
20-213 |
5.33e-29 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 111.50 E-value: 5.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 20 IHFSVQLGE-------------IVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRN-VQTFSKKEVRQQQQQMGMVFQ 85
Cdd:PRK11144 4 LNFKQQLGDlcltvnltlpaqgITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVlFDAEKGICLPPEKRRIGYVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 86 ------HYNLLENLKiYDnvalplklLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDE 159
Cdd:PRK11144 84 darlfpHYKVRGNLR-YG--------MAKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488289759 160 ATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:PRK11144 155 PLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVK 208
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-213 |
6.04e-29 |
|
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: 108.39 E-value: 6.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVY----------------------QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIR 59
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 60 IDGRNVQTFSkkevrqqqqqMGMVFQhynllENLKIYDNVALPLKLLKEKQPEKIERLLTFVDMAHKAEAYPAQL---SG 136
Cdd:cd03220 81 VRGRVSSLLG----------LGGGFN-----PELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVktySS 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488289759 137 GEKQRVSIARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:cd03220 146 GMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGK-TVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-230 |
7.83e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 109.44 E-value: 7.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQE-THALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRqqqQQM 80
Cdd:PRK13647 5 IEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVR---SKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 81 GMVFQHY-NLLENLKIYDNVA---LPLKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLL 156
Cdd:PRK13647 82 GLVFQDPdDQVFSSTVWDDVAfgpVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488289759 157 CDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLIGE----FLNNPQQYEEEPLSY 230
Cdd:PRK13647 162 LDEPMAYLDPRGQETLMEILDRLHNQGK-TVIVATHDVDLAAEWADQVIVLKEGRVLAEgdksLLTDEDIVEQAGLRL 238
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-236 |
1.08e-28 |
|
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: 112.97 E-value: 1.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQ--PSEGEI----------------RIDGR 63
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyhvalcekcgyverpSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 64 NVQT--------------FSKKEVRQQQQQMGMVFQH-YNLLENLKIYDNVALPLKLLKEKQPEKIER---LLTFVDMAH 125
Cdd:TIGR03269 81 PCPVcggtlepeevdfwnLSDKLRRRIRKRIAIMLQRtFALYGDDTVLDNVLEALEEIGYEGKEAVGRavdLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 126 KAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRIL 205
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240
|
250 260 270
....*....|....*....|....*....|.
gi 488289759 206 VMEKGQLIGEflNNPQQYEEEPLSYLEKVER 236
Cdd:TIGR03269 241 WLENGEIKEE--GTPDEVVAVFMEGVSEVEK 269
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
16-215 |
1.15e-28 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 110.22 E-value: 1.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 16 ALKNIHFSVQLGEIVGIVGKSGSGKS-TLLRLLNLMEQP---SEGEIRIDGRNVQTFSKKEVRQ-QQQQMGMVFQH---- 86
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPgrvMAEKLEFNGQDLQRISEKERRNlVGAEVAMIFQDpmts 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 87 --------YNLLENLKIYDNVALplkllKEKQPEKIErLLTFV---DMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWL 155
Cdd:PRK11022 102 lnpcytvgFQIMEAIKVHQGGNK-----KTRRQRAID-LLNQVgipDPASRLDVYPHQLSGGMSQRVMIAMAIACRPKLL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 156 LCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIGE 215
Cdd:PRK11022 176 IADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVET 235
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-212 |
1.23e-28 |
|
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: 112.92 E-value: 1.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVY--QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKkevRQQQQQ 79
Cdd:COG4618 331 LSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDR---EELGRH 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 80 MGMVFQHYNLLENlKIYDNVALplklLKEKQPEKIerlltfVDMAHKAEA----------Y-------PAQLSGGEKQRV 142
Cdd:COG4618 408 IGYLPQDVELFDG-TIAENIAR----FGDADPEKV------VAAAKLAGVhemilrlpdgYdtrigegGARLSGGQRQRI 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488289759 143 SIARALSRNPKWLLCDEATSSLDEENTESVVRLLhkthQEFRP---TIFFVSHELeTVKRLCNRILVMEKGQL 212
Cdd:COG4618 477 GLARALYGDPRLVVLDEPNSNLDDEGEAALAAAI----RALKArgaTVVVITHRP-SLLAAVDKLLVLRDGRV 544
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
11-213 |
2.37e-28 |
|
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: 107.42 E-value: 2.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 11 YQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRqqqqQMGMVF-QHYNL 89
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLR----RIGVVFgQKTQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 90 LENLKIYDNVALpLK----LLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLD 165
Cdd:cd03267 107 WWDLPVIDSFYL-LAaiydLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488289759 166 EENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:cd03267 186 VVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-220 |
2.47e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 108.20 E-value: 2.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQpSEGEIRIDGRnVQTFSKK------EVRQ 75
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGR-VEFFNQNiyerrvNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 76 QQQQMGMVFQHYNLLEnLKIYDNVALPLKLL----KEKQPEKIERLLTFVDM----AHKAEAYPAQLSGGEKQRVSIARA 147
Cdd:PRK14258 86 LRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVgwrpKLEIDDIVESALKDADLwdeiKHKIHKSALDLSGGQQQRLCIARA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 148 LSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLC----------NRILVMEKGQLIGEFL 217
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSdftaffkgneNRIGQLVEFGLTKKIF 244
|
...
gi 488289759 218 NNP 220
Cdd:PRK14258 245 NSP 247
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-213 |
2.55e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 108.38 E-value: 2.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQ-----ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNV--QTfSKKEVR 74
Cdd:PRK13641 3 IKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpET-GNKNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 75 QQQQQMGMVFQ--HYNLLENLKIYDNVALPLKL------LKEKQPEKIERLLTFVDMAHKAeayPAQLSGGEKQRVSIAR 146
Cdd:PRK13641 82 KLRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFgfsedeAKEKALKWLKKVGLSEDLISKS---PFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488289759 147 ALSRNPKWLLCDEATSSLDEENTESVVRLLhKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:PRK13641 159 VMAYEPEILCLDEPAAGLDPEGRKEMMQLF-KDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLI 224
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-159 |
2.93e-28 |
|
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: 106.86 E-value: 2.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVqtfSKKEVrQQQQQMG 81
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI---TKLPM-HKRARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 82 MVF--QHYNLLENLKIYDNVALPL---KLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLL 156
Cdd:cd03218 77 IGYlpQEASIFRKLTVEENILAVLeirGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
...
gi 488289759 157 CDE 159
Cdd:cd03218 157 LDE 159
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-213 |
3.30e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 107.91 E-value: 3.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQ-----ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSK-KEVRQ 75
Cdd:PRK13649 3 INLQNVSYTYQagtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 76 QQQQMGMVFQ--HYNLLENLKIYDNVALPLKL-LKEKQPEKIER-LLTFVDMAHKA-EAYPAQLSGGEKQRVSIARALSR 150
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNFgVSQEEAEALAReKLALVGISESLfEKNPFELSGGQMRRVAIAGILAM 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488289759 151 NPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:PRK13649 163 EPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGM-TIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-215 |
4.09e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 107.58 E-value: 4.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQ-ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVqtfSKKEVRQQQQQ 79
Cdd:PRK13652 3 LIETRDLCYSYSgSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPI---TKENIREVRKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 80 MGMVFQHYN-LLENLKIYDNVA---LPLKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWL 155
Cdd:PRK13652 80 VGLVFQNPDdQIFSPTVEQDIAfgpINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 156 LCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIGE 215
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAY 219
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-215 |
4.85e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 107.94 E-value: 4.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQ-----ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSK-KEVRQ 75
Cdd:PRK13646 3 IRFDNVSYTYQkgtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 76 QQQQMGMVFQhynLLENLKIYDNVALPL-------KLLKEKQPEKIERLLTFVDMAHKA-EAYPAQLSGGEKQRVSIARA 147
Cdd:PRK13646 83 VRKRIGMVFQ---FPESQLFEDTVEREIifgpknfKMNLDEVKNYAHRLLMDLGFSRDVmSQSPFQMSGGQMRKIAIVSI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488289759 148 LSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIGE 215
Cdd:PRK13646 160 LAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQ 227
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-227 |
5.15e-28 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 107.16 E-value: 5.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQQQQM 80
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 81 GMVFQHYNLLENLKIYDNVALPLK--------LLKEKQPEKIERlltfVDMAHKAEAYPAQLSGGEKQRVSIARALSRNP 152
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVAYPLRehtqlpapLLHSTVMMKLEA----VGLRGAAKLMPSELSGGMARRAALARAIALEP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 153 KWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIGEflNNPQQYEEEP 227
Cdd:PRK11831 163 DLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAH--GSAQALQANP 235
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-213 |
5.29e-28 |
|
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: 111.05 E-value: 5.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQET-----HALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRID-GRNVQTFSKKEVR 74
Cdd:TIGR03269 279 IIKVRNVSKRYISVdrgvvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 75 QQ---QQQMGMVFQHYNLLENLKIYDNV--ALPLKLLKEKQPEKIERLLTFVDMAHKA-----EAYPAQLSGGEKQRVSI 144
Cdd:TIGR03269 359 GRgraKRYIGILHQEYDLYPHRTVLDNLteAIGLELPDELARMKAVITLKMVGFDEEKaeeilDKYPDELSEGERHRVAL 438
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488289759 145 ARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:TIGR03269 439 AQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIV 507
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-226 |
7.14e-28 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 111.35 E-value: 7.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVY---QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQqq 78
Cdd:TIGR00958 479 IEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQ-- 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 79 qMGMVFQHyNLLENLKIYDNVALPLKLLKEKQPEKIERLLTFVDMAHKAE--------AYPAQLSGGEKQRVSIARALSR 150
Cdd:TIGR00958 557 -VALVGQE-PVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPngydtevgEKGSQLSGGQKQRIAIARALVR 634
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488289759 151 NPKWLLCDEATSSLDEEntesVVRLLHKTHQEFRPTIFFVSHELETVKRlCNRILVMEKGQLiGEFLNNPQQYEEE 226
Cdd:TIGR00958 635 KPRVLILDEATSALDAE----CEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSV-VEMGTHKQLMEDQ 704
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-215 |
1.82e-27 |
|
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: 103.55 E-value: 1.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVY--QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFsKKEVRqqqQQ 79
Cdd:cd03247 1 LSINNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL-EKALS---SL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 80 MGMVFQHYNLLeNLKIYDNVAlplkllkekqpekierlltfvdmahkaeaypAQLSGGEKQRVSIARALSRNPKWLLCDE 159
Cdd:cd03247 77 ISVLNQRPYLF-DTTLRNNLG-------------------------------RRFSGGERQRLALARILLQDAPIVLLDE 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488289759 160 ATSSLDEENTESVVRLLHKTHQEfrPTIFFVSHELETVKRLcNRILVMEKGQLIGE 215
Cdd:cd03247 125 PTVGLDPITERQLLSLIFEVLKD--KTLIWITHHLTGIEHM-DKILFLENGKIIMQ 177
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-213 |
2.13e-27 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 105.17 E-value: 2.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLL----RLLNlmeqPSEGEIRIDGRNVQTFSKKEVrqq 76
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLsmisRLLP----PDSGEVLVDGLDVATTPSREL--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 77 QQQMGMVFQHYNLLENLKIYDNVAL---PL---KLLKEKQpEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSR 150
Cdd:COG4604 74 AKRLAILRQENHINSRLTVRELVAFgrfPYskgRLTAEDR-EIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQ 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488289759 151 NPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:COG4604 153 DTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVV 215
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-213 |
4.58e-27 |
|
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: 103.26 E-value: 4.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQE--THALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQqqq 79
Cdd:cd03369 7 IEVENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSS--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 80 MGMVFQHYNLLE-----NLKIYDnvalplkllkEKQPEKIERLLtfvdmahKAEAYPAQLSGGEKQRVSIARALSRNPKW 154
Cdd:cd03369 84 LTIIPQDPTLFSgtirsNLDPFD----------EYSDEEIYGAL-------RVSEGGLNLSQGQRQLLCLARALLKRPRV 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488289759 155 LLCDEATSSLDEENTESVVRLLHKTHQEfrPTIFFVSHELETVKRlCNRILVMEKGQLI 213
Cdd:cd03369 147 LVLDEATASIDYATDALIQKTIREEFTN--STILTIAHRLRTIID-YDKILVMDAGEVK 202
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-213 |
6.00e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 104.40 E-value: 6.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQ-----ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVqTFSKKEVRq 75
Cdd:COG1101 1 MLELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV-TKLPEYKR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 76 qQQQMGMVFQhyNLL----ENLKIYDNVALPLK----------LLKEKQPEKIERLLTF-VDMAHKAEAYPAQLSGGEKQ 140
Cdd:COG1101 79 -AKYIGRVFQ--DPMmgtaPSMTIEENLALAYRrgkrrglrrgLTKKRRELFRELLATLgLGLENRLDTKVGLLSGGQRQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488289759 141 RVSIARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:COG1101 156 ALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-213 |
6.32e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 105.55 E-value: 6.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQ---------------------ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIR 59
Cdd:COG4586 1 IIEVENLSKTYRvyekepglkgalkglfrreyrEVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 60 IDGRNVQtfskKEVRQQQQQMGMVF-QHYNLLENLKIYDNvalpLKLLKE--KQPEKI--ERLLTFVDMAHKAEAY--PA 132
Cdd:COG4586 81 VLGYVPF----KRRKEFARRIGVVFgQRSQLWWDLPAIDS----FRLLKAiyRIPDAEykKRLDELVELLDLGELLdtPV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 133 -QLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQ 211
Cdd:COG4586 153 rQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGR 232
|
..
gi 488289759 212 LI 213
Cdd:COG4586 233 II 234
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-210 |
7.66e-27 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 107.83 E-value: 7.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKkevrQQQQQM 80
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTP----AKAHQL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 81 G--MVFQHYNLLENLKIYDNVALPLKlLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCD 158
Cdd:PRK15439 87 GiyLVPQEPLLFPNLSVKENILFGLP-KRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488289759 159 EATSSLDEENTESVVR----LLHKTHqefrpTIFFVSHELETVKRLCNRILVMEKG 210
Cdd:PRK15439 166 EPTASLTPAETERLFSrireLLAQGV-----GIVFISHKLPEIRQLADRISVMRDG 216
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-214 |
2.37e-26 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 106.41 E-value: 2.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEvrQQQQQM 80
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKL--AAQLGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 81 GMVFQHYNLLENLKIYDNVALPLKLLKE----------KQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSR 150
Cdd:PRK09700 83 GIIYQELSVIDELTVLENLYIGRHLTKKvcgvniidwrEMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488289759 151 NPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLIG 214
Cdd:PRK09700 163 DAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGT-AIVYISHKLAEIRRICDRYTVMKDGSSVC 225
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-221 |
3.21e-26 |
|
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: 101.60 E-value: 3.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLR-LLNLMeQPSEGEIRIDGRNVQTFSKKEVRQqqqq 79
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKaISGLL-PPRSGSIRFDGEDITGLPPHRIAR---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 80 MGMVF--QHYNLLENLKIYDNVALPLKLLKEKQPEK--IERLLT-FVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKW 154
Cdd:COG0410 78 LGIGYvpEGRRIFPSLTVEENLLLGAYARRDRAEVRadLERVYElFPRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488289759 155 LLCDEATSSL-----DEenTESVVRLLHKTHQefrpTIFFVSHELETVKRLCNRILVMEKGQLI-----GEFLNNPQ 221
Cdd:COG0410 158 LLLDEPSLGLaplivEE--IFEIIRRLNREGV----TILLVEQNARFALEIADRAYVLERGRIVlegtaAELLADPE 228
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-159 |
3.50e-26 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 101.64 E-value: 3.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKkevrQQQQQM 80
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPM----HKRARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 81 GMVF--QHYNLLENLKIYDNVALPLKLL---KEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWL 155
Cdd:COG1137 79 GIGYlpQEASIFRKLTVEDNILAVLELRklsKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFI 158
|
....
gi 488289759 156 LCDE 159
Cdd:COG1137 159 LLDE 162
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-211 |
3.53e-26 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 105.94 E-value: 3.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 12 QETHALKNIHFSVQLGEIVGIVGKSGSGKS-TLLRLLNLMEQPS----EGEIRIDGRNVQTFSKKEVRQ-QQQQMGMVFQ 85
Cdd:PRK15134 20 TVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQTLRGvRGNKIAMIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 86 H----YNLLENL--KIYDNVALPLKLLKEKQPEKIERLLTFVDMAHKAE---AYPAQLSGGEKQRVSIARALSRNPKWLL 156
Cdd:PRK15134 100 EpmvsLNPLHTLekQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKrltDYPHQLSGGERQRVMIAMALLTRPELLI 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 157 CDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQ 211
Cdd:PRK15134 180 ADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
12-213 |
3.72e-26 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 106.09 E-value: 3.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 12 QETHALKNIHFSVQLGEIVGIVGKSGSGKS-TLLRLLNLMEQpSEGEIRIDG-----RNVQTFSKKEVRQQQQQ------ 79
Cdd:PRK10261 27 QKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-AGGLVQCDKmllrrRSRQVIELSEQSAAQMRhvrgad 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 80 MGMVFQHYNLLENL------KIYDNVALPLKLLKEKQPEKIERLLTFVDMAHKAEA---YPAQLSGGEKQRVSIARALSR 150
Cdd:PRK10261 106 MAMIFQEPMTSLNPvftvgeQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTIlsrYPHQLSGGMRQRVMIAMALSC 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488289759 151 NPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:PRK10261 186 RPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-213 |
4.32e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 102.78 E-value: 4.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQ-----ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKK--EVR 74
Cdd:PRK13645 7 IILDNVSYTYAkktpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKikEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 75 QQQQQMGMVFQ--HYNLLENlKIYDNVAL-PLKLLKEKQP--EKIERLLTFVDMAHK-AEAYPAQLSGGEKQRVSIARAL 148
Cdd:PRK13645 87 RLRKEIGLVFQfpEYQLFQE-TIEKDIAFgPVNLGENKQEayKKVPELLKLVQLPEDyVKRSPFELSGGQKRRVALAGII 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 149 SRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:PRK13645 166 AMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVI 230
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-210 |
6.47e-26 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 104.15 E-value: 6.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVrqqQQQM 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAA---SRRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 81 GMVFQHYNLLENLKIYDNVAL---P----LKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPK 153
Cdd:PRK09536 80 ASVPQDTSLSFEFDVRQVVEMgrtPhrsrFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 154 WLLCDEATSSLD---EENTESVVRLLHKTHQefrpTIFFVSHELETVKRLCNRILVMEKG 210
Cdd:PRK09536 160 VLLLDEPTASLDinhQVRTLELVRRLVDDGK----TAVAAIHDLDLAARYCDELVLLADG 215
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-213 |
8.86e-26 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 101.40 E-value: 8.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVY---------QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVqTFSKK 71
Cdd:PRK15112 4 LLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFGDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 72 EVRQQQqqMGMVFQ--HYNLLENLKIYDNVALPLKLLKEKQPE----KIERLLTFVDM-AHKAEAYPAQLSGGEKQRVSI 144
Cdd:PRK15112 83 SYRSQR--IRMIFQdpSTSLNPRQRISQILDFPLRLNTDLEPEqrekQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488289759 145 ARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:PRK15112 161 ARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVV 229
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
17-213 |
2.85e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 103.39 E-value: 2.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLnLMEQPSEGEIRIDGrnvQTFSKKEVRQQQQQMGMVFQHYNLLENlKIY 96
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSLLNAL-LGFLPYQGSLKING---IELRELDPESWRKHLSWVGQNPQLPHG-TLR 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 97 DNVALPLKLLKEkqpEKIERLLT------FVDMAHKAEAYP-----AQLSGGEKQRVSIARALSRNPKWLLCDEATSSLD 165
Cdd:PRK11174 441 DNVLLGNPDASD---EQLQQALEnawvseFLPLLPQGLDTPigdqaAGLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488289759 166 EENTESVVRLLHKTHQefRPTIFFVSHELETVKRlCNRILVMEKGQLI 213
Cdd:PRK11174 518 AHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQ-WDQIWVMQDGQIV 562
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-213 |
3.59e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 100.19 E-value: 3.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQ-----ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSK-KEVR 74
Cdd:PRK13643 1 MIKFEKVNYTYQpnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKqKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 75 QQQQQMGMVFQ--HYNLLENLKIYDNVALPLKL-LKEKQPEKI-ERLLTFVDMAHKA-EAYPAQLSGGEKQRVSIARALS 149
Cdd:PRK13643 81 PVRKKVGVVFQfpESQLFEETVLKDVAFGPQNFgIPKEKAEKIaAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488289759 150 RNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:PRK13643 161 MEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQ-TVVLVTHLMDDVADYADYVYLLEKGHII 223
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
16-216 |
9.90e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 101.64 E-value: 9.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 16 ALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRqqqqQMGMVF-----QHYNLL 90
Cdd:COG3845 273 ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERR----RLGVAYipedrLGRGLV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 91 ENLKIYDNVAL------PL--------KLLKEKQPEKIERLltfvDMAHKAEAYPA-QLSGGEKQRVSIARALSRNPKWL 155
Cdd:COG3845 349 PDMSVAENLILgryrrpPFsrggfldrKAIRAFAEELIEEF----DVRTPGPDTPArSLSGGNQQKVILARELSRDPKLL 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488289759 156 LCDEATSSLDEENTESVvrllhktHQEFRP------TIFFVSHELETVKRLCNRILVMEKGQLIGEF 216
Cdd:COG3845 425 IAAQPTRGLDVGAIEFI-------HQRLLElrdagaAVLLISEDLDEILALSDRIAVMYEGRIVGEV 484
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
16-213 |
2.01e-24 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 101.35 E-value: 2.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 16 ALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQQQ---QMGMVFQHyNLLEN 92
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINylpQEPYIFSG-SILEN 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 93 LKIYDNVALplkllkekQPEKIERLLTFVDMAHKAEAYP-----------AQLSGGEKQRVSIARALSRNPKWLLCDEAT 161
Cdd:TIGR01193 568 LLLGAKENV--------SQDEIWAACEIAEIKDDIENMPlgyqtelseegSSISGGQKQRIALARALLTDSKVLILDEST 639
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488289759 162 SSLDEENTESVV-RLLHKTHQefrpTIFFVSHELETVKRlCNRILVMEKGQLI 213
Cdd:TIGR01193 640 SNLDTITEKKIVnNLLNLQDK----TIIFVAHRLSVAKQ-SDKIIVLDHGKII 687
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-226 |
2.84e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 100.52 E-value: 2.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 6 NVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIridgrnvqtfskkeVRQQQQQMGMVFQ 85
Cdd:COG0488 3 NLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV--------------SIPKGLRIGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 86 HYNLLENLKIYDNVALPLKLLKE--KQPEKIERLLTFV--DMAHKAE-----------AYPAQ----------------- 133
Cdd:COG0488 69 EPPLDDDLTVLDTVLDGDAELRAleAELEELEAKLAEPdeDLERLAElqeefealggwEAEARaeeilsglgfpeedldr 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 134 ----LSGGEKQRVSIARALSRNPKWLLCDEATSSLDeenTESVVRL---LhkthQEFRPTIFFVSHE---LETVkrlCNR 203
Cdd:COG0488 149 pvseLSGGWRRRVALARALLSEPDLLLLDEPTNHLD---LESIEWLeefL----KNYPGTVLVVSHDryfLDRV---ATR 218
|
250 260
....*....|....*....|...
gi 488289759 204 ILVMEKGQLIgEFLNNPQQYEEE 226
Cdd:COG0488 219 ILELDRGKLT-LYPGNYSAYLEQ 240
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
14-215 |
3.96e-24 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 96.78 E-value: 3.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 14 THALKNIHFSVQ-------------LGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKK----EVRQQ 76
Cdd:PRK10575 11 TFALRNVSFRVPgrtllhplsltfpAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKafarKVAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 77 QQQMGMVfqhynllENLKIYDNVAL-------PLKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALS 149
Cdd:PRK10575 91 PQQLPAA-------EGMTVRELVAIgrypwhgALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488289759 150 RNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIGE 215
Cdd:PRK10575 164 QDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQ 229
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-226 |
5.50e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 96.39 E-value: 5.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQ--PS---EGEIRIDGRNV--QTFSKKEVR 74
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNLyaPDVDPVEVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 75 QQqqqMGMVFQHYNLLENlKIYDNVALPLKLL--KEKQPEKIERLLT----FVDMAHKAEAYPAQLSGGEKQRVSIARAL 148
Cdd:PRK14243 91 RR---IGMVFQKPNPFPK-SIYDNIAYGARINgyKGDMDELVERSLRqaalWDEVKDKLKQSGLSLSGGQQQRLCIARAI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 149 SRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFrpTIFFVSHELETVKRLCN-----RILVMEKGQLIGEFL------ 217
Cdd:PRK14243 167 AVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDmtaffNVELTEGGGRYGYLVefdrte 244
|
250
....*....|..
gi 488289759 218 ---NNPQQYEEE 226
Cdd:PRK14243 245 kifNSPQQQATR 256
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-215 |
9.10e-24 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 98.92 E-value: 9.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEvrQQQQQM 80
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKS--SQEAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 81 GMVFQHYNLLENLKIYDNVALPL-------KLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPK 153
Cdd:PRK10762 82 GIIHQELNLIPQLTIAENIFLGRefvnrfgRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESK 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488289759 154 WLLCDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLIGE 215
Cdd:PRK10762 162 VIIMDEPTDALTDTETESLFRVIRELKSQGR-GIVYISHRLKEIFEICDDVTVFRDGQFIAE 222
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
15-213 |
9.20e-24 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 97.28 E-value: 9.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 15 HALKNIHFSVQLGEIVGIVGKSGSGKSTLLR-LLNLME---QPSEGEIRIDGRNVQTFSKKEVRQ-QQQQMGMVFQHYN- 88
Cdd:COG4170 21 KAVDRVSLTLNEGEIRGLVGESGSGKSLIAKaICGITKdnwHVTADRFRWNGIDLLKLSPRERRKiIGREIAMIFQEPSs 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 89 -LLENLKIYDNV--ALPLKLLKEK-------QPEKIERLLTFVDMA-HKA--EAYPAQLSGGEKQRVSIARALSRNPKWL 155
Cdd:COG4170 101 cLDPSAKIGDQLieAIPSWTFKGKwwqrfkwRKKRAIELLHRVGIKdHKDimNSYPHELTEGECQKVMIAMAIANQPRLL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488289759 156 LCDEATSSLdEENTES-VVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:COG4170 181 IADEPTNAM-ESTTQAqIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTV 238
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-213 |
1.15e-23 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 99.02 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETH-ALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQqqqM 80
Cdd:PRK10790 341 IDIDNVSFAYRDDNlVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQG---V 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 81 GMVFQHYNLLENlKIYDNVALPlkllKEKQPEKIERLLTFVDMAHKAEAYPA-----------QLSGGEKQRVSIARALS 149
Cdd:PRK10790 418 AMVQQDPVVLAD-TFLANVTLG----RDISEEQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALARVLV 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488289759 150 RNPKWLLCDEATSSLDEENTESVVRLLHKTHQefRPTIFFVSHELETVKRlCNRILVMEKGQLI 213
Cdd:PRK10790 493 QTPQILILDEATANIDSGTEQAIQQALAAVRE--HTTLVVIAHRLSTIVE-ADTILVLHRGQAV 553
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-214 |
1.86e-23 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 98.08 E-value: 1.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMeQPS---EGEIRIDGRNVQTFSKKEVrqQQ 77
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEELQASNIRDT--ER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 78 QQMGMVFQHYNLLENLKIYDNVALPLKLLK------EKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRN 151
Cdd:PRK13549 82 AGIAIIHQELALVKELSVLENIFLGNEITPggimdyDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 152 PKWLLCDEATSSLDEENTESVVRLLH--KTHQefrPTIFFVSHELETVKRLCNRILVMEKGQLIG 214
Cdd:PRK13549 162 ARLLILDEPTASLTESETAVLLDIIRdlKAHG---IACIYISHKLNEVKAISDTICVIRDGRHIG 223
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
6-221 |
2.11e-23 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 94.58 E-value: 2.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 6 NVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEvrQQQQQMGMVFQ 85
Cdd:PRK10895 8 NLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA--RARRGIGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 86 HYNLLENLKIYDNVALPLK----LLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEAT 161
Cdd:PRK10895 86 EASIFRRLSVYDNLMAVLQirddLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488289759 162 SSLDEENTESVVRLLhkthQEFRPT---IFFVSHELETVKRLCNRILVMEKGQLIG-----EFLNNPQ 221
Cdd:PRK10895 166 AGVDPISVIDIKRII----EHLRDSglgVLITDHNVRETLAVCERAYIVSQGHLIAhgtptEILQDEH 229
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
6-213 |
6.96e-23 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 93.45 E-value: 6.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 6 NVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGR-----NVQTFSKKEVRQ-QQQQ 79
Cdd:PRK11701 11 GLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAERRRlLRTE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 80 MGMVFQH------------YNLLENL-----KIYDNV-ALPLKLLK--EKQPEKIERLltfvdmahkaeayPAQLSGGEK 139
Cdd:PRK11701 91 WGFVHQHprdglrmqvsagGNIGERLmavgaRHYGDIrATAGDWLErvEIDAARIDDL-------------PTTFSGGMQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488289759 140 QRVSIARALSRNPKWLLCDEATSSLDeentESV-VRLLHKTHQ---EFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:PRK11701 158 QRLQIARNLVTHPRLVFMDEPTGGLD----VSVqARLLDLLRGlvrELGLAVVIVTHDLAVARLLAHRLLVMKQGRVV 231
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
17-211 |
9.96e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 96.03 E-value: 9.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRidgrnvqtfskkevRQQQQQMGMVFQH-YNLLENLKi 95
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA--------------RPAGARVLFLPQRpYLPLGTLR- 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 96 yDNVALPlKLLKEKQPEKIERLLTFVDMAHKAE------AYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENT 169
Cdd:COG4178 444 -EALLYP-ATAEAFSDAELREALEAVGLGHLAErldeeaDWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENE 521
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488289759 170 ESVVRLLHKTHQEfrPTIFFVSHElETVKRLCNRILVMEKGQ 211
Cdd:COG4178 522 AALYQLLREELPG--TTVISVGHR-STLAAFHDRVLELTGDG 560
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
15-216 |
1.20e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 95.47 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 15 HALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQqqqmGMVF-----QHYNL 89
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRA----GIAYvpedrKGEGL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 90 LENLKIYDNVALP-------LKLLKEKQPEKI-ERLLTFVDM-AHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEA 160
Cdd:COG1129 342 VLDLSIRENITLAsldrlsrGGLLDRRRERALaEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEP 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 161 TSSLD----EEntesVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLIGEF 216
Cdd:COG1129 422 TRGIDvgakAE----IYRLIRELAAEGK-AVIVISSELPELLGLSDRILVMREGRIVGEL 476
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
8-213 |
1.20e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 94.15 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 8 SKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRI----------DGRNVQTFSKKEVR--- 74
Cdd:PRK13631 33 EKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknNHELITNPYSKKIKnfk 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 75 QQQQQMGMVFQ--HYNLLENLKIYDNVALPLKLlKEKQPEKIERLLTFVDMAHKAEAY----PAQLSGGEKQRVSIARAL 148
Cdd:PRK13631 113 ELRRRVSMVFQfpEYQLFKDTIEKDIMFGPVAL-GVKKSEAKKLAKFYLNKMGLDDSYlersPFGLSGGQKRRVAIAGIL 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 149 SRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:PRK13631 192 AIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNK-TVFVITHTMEHVLEVADEVIVMDKGKIL 255
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
17-213 |
1.77e-22 |
|
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: 91.56 E-value: 1.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSE---GEIRIDGRNVqtfSKKEVrqqQQQMGMVFQHYNLLENL 93
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPR---KPDQF---QKCVAYVRQDDILLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 94 KIYD------NVALPlKLLKEKQPEKIERLLTFVDMAHK--AEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLD 165
Cdd:cd03234 97 TVREtltytaILRLP-RKSSDAIRKKRVEDVLLRDLALTriGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488289759 166 EENTESVVRLLHKT-----------HQEfRPTIFfvsheletvkRLCNRILVMEKGQLI 213
Cdd:cd03234 176 SFTALNLVSTLSQLarrnriviltiHQP-RSDLF----------RLFDRILLLSSGEIV 223
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-214 |
1.15e-21 |
|
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: 92.97 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPS--EGEIRIDGRNVQTFSKKEVrqQQQ 78
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASNIRDT--ERA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 79 QMGMVFQHYNLLENLKIYDNVAL----PLKLLKEKQPEKIER---LLTFVDMAHKAEAYP-AQLSGGEKQRVSIARALSR 150
Cdd:TIGR02633 79 GIVIIHQELTLVPELSVAENIFLgneiTLPGGRMAYNAMYLRaknLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488289759 151 NPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIfFVSHELETVKRLCNRILVMEKGQLIG 214
Cdd:TIGR02633 159 QARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACV-YISHKLNEVKAVCDTICVIRDGQHVA 221
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-215 |
1.24e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 90.07 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVrqqQQQM 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQL---ARRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 81 GMVFQHYNLLENLKIYDNVA------LPL-KLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPK 153
Cdd:PRK11231 79 ALLPQHHLTPEGITVRELVAygrspwLSLwGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488289759 154 WLLCDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLIGE 215
Cdd:PRK11231 159 VVLLDEPTTYLDINHQVELMRLMRELNTQGK-TVVTVLHDLNQASRYCDHLVVLANGHVMAQ 219
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
15-222 |
3.42e-21 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 91.65 E-value: 3.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 15 HALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLL------NLMEQPSegeIRIDGRNVQtfsKKEVRQQQ---QQMGMVFQ 85
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALafrspkGVKGSGS---VLLNGMPID---AKEMRAISayvQQDDLFIP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 86 HYNLLENLKIYDNVALPLKLLKEKQPEKIERLLT---FVDMAHKAEAYPAQ---LSGGEKQRVSIARALSRNPKWLLCDE 159
Cdd:TIGR00955 113 TLTVREHLMFQAHLRMPRRVTKKEKRERVDEVLQalgLRKCANTRIGVPGRvkgLSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488289759 160 ATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIgeFLNNPQQ 222
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVA--YLGSPDQ 253
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4-213 |
3.90e-21 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 91.33 E-value: 3.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 4 LVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVrqQQQQMGMV 83
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEA--LENGISMV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 84 FQHYNLLENLKIYDNVAL---PLKLL---KEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLC 157
Cdd:PRK10982 79 HQELNLVLQRSVMDNMWLgryPTKGMfvdQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488289759 158 DEATSSLDEENTESVVRLLHKThQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:PRK10982 159 DEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
2-167 |
4.62e-21 |
|
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: 87.03 E-value: 4.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQtfskkEVRQQQQQMG 81
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLA-----EQRDEPHENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 82 MVFQHYN-------LLENLKIYDNVALPLKLlkekqpeKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARA-LSRNPK 153
Cdd:TIGR01189 76 LYLGHLPglkpelsALENLHFWAAIHGGAQR-------TIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLwLSRRPL 148
|
170
....*....|....
gi 488289759 154 WLLcDEATSSLDEE 167
Cdd:TIGR01189 149 WIL-DEPTTALDKA 161
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
11-213 |
5.93e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 88.53 E-value: 5.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 11 YQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQtFSKKEVRQQQQQMGMVFQHYN-L 89
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD-YSKRGLLALRQQVATVFQDPEqQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 90 LENLKIYDNVALPLKLLKEKQPE---KIERLLTFVDmAHKAEAYPAQ-LSGGEKQRVSIARALSRNPKWLLCDEATSSLD 165
Cdd:PRK13638 90 IFYTDIDSDIAFSLRNLGVPEAEitrRVDEALTLVD-AQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488289759 166 EENTESVVRLLHKTHQEFRPTIfFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:PRK13638 169 PAGRTQMIAIIRRIVAQGNHVI-ISSHDIDLIYEISDAVYVLRQGQIL 215
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
2-200 |
1.01e-20 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 86.94 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLL--NLMEQPSEGEIRIDgrnVQTFSKKEVrqqqqq 79
Cdd:COG2401 31 LEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLagALKGTPVAGCVDVP---DNQFGREAS------ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 80 mgmvfqhynLLENLKIYDNVALPLKLLkekqpekierlltfvDMAHKAEAY-----PAQLSGGEKQRVSIARALSRNPKW 154
Cdd:COG2401 102 ---------LIDAIGRKGDFKDAVELL---------------NAVGLSDAVlwlrrFKELSTGQKFRFRLALLLAERPKL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488289759 155 LLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRL 200
Cdd:COG2401 158 LVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVIDDL 203
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
18-225 |
1.06e-20 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 90.47 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 18 KNIHFSVQLGEIVGIVGKSGSGKST----LLRLLNL--------------------MEQPSE------------------ 55
Cdd:PTZ00265 1185 KDLTFSCDSKKTTAIVGETGSGKSTvmslLMRFYDLkndhhivfknehtndmtneqDYQGDEeqnvgmknvnefsltkeg 1264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 56 ------------GEIRIDGRNVQTFSKKEVRQqqqqMGMVFQHYNLLENLKIYDNValplKLLKEKQP-EKIERLLTFVD 122
Cdd:PTZ00265 1265 gsgedstvfknsGKILLDGVDICDYNLKDLRN----LFSIVSQEPMLFNMSIYENI----KFGKEDATrEDVKRACKFAA 1336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 123 MAHKAEAYPAQ-----------LSGGEKQRVSIARALSRNPKWLLCDEATSSLDeENTEsvvRLLHKTHQEFR----PTI 187
Cdd:PTZ00265 1337 IDEFIESLPNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLD-SNSE---KLIEKTIVDIKdkadKTI 1412
|
250 260 270
....*....|....*....|....*....|....*...
gi 488289759 188 FFVSHELETVKRlCNRILVMEKGQLIGEFLNNPQQYEE 225
Cdd:PTZ00265 1413 ITIAHRIASIKR-SDKIVVFNNPDRTGSFVQAHGTHEE 1449
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
16-220 |
1.77e-20 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 86.97 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 16 ALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKkevrQQQQQMGMV--FQHYNL---- 89
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPG----HQIARMGVVrtFQHVRLfrem 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 90 --LENLKI----YDNVALPLKLLK-----EKQPEKIERL---LTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWL 155
Cdd:PRK11300 96 tvIENLLVaqhqQLKTGLFSGLLKtpafrRAESEALDRAatwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEIL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 156 LCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIG-----EFLNNP 220
Cdd:PRK11300 176 MLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLAngtpeEIRNNP 245
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
18-215 |
2.10e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 86.96 E-value: 2.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 18 KNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVrqqQQQMGMVFQHYNLLENLKIYD 97
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEV---ARRIGLLAQNATTPGDITVQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 98 NVA---LPLKLL----KEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTE 170
Cdd:PRK10253 101 LVArgrYPHQPLftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488289759 171 SVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIGE 215
Cdd:PRK10253 181 DLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQ 225
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-215 |
2.95e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 86.69 E-value: 2.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 5 VNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEG-----EIRIDGRNVqtFSKKEVRQQQQQ 79
Cdd:PRK14271 25 VNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSI--FNYRDVLEFRRR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 80 MGMVFQHYNLLEnLKIYDNVA--------LPLKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRN 151
Cdd:PRK14271 103 VGMLFQRPNPFP-MSIMDNVLagvrahklVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVN 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488289759 152 PKWLLCDEATSSLDEENTESVVRLLHKTHQefRPTIFFVSHELETVKRLCNRILVMEKGQLIGE 215
Cdd:PRK14271 182 PEVLLLDEPTSALDPTTTEKIEEFIRSLAD--RLTVIIVTHNLAQAARISDRAALFFDGRLVEE 243
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
16-194 |
9.89e-20 |
|
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: 87.42 E-value: 9.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 16 ALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQQ---QQMGMVFqHYNLLEN 92
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVsvcAQDAHLF-DTTVREN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 93 LKIydnvALPlkllkEKQPEKIERLLTFVDMAHKAEAYP-----------AQLSGGEKQRVSIARALSRNPKWLLCDEAT 161
Cdd:TIGR02868 429 LRL----ARP-----DATDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDEPT 499
|
170 180 190
....*....|....*....|....*....|...
gi 488289759 162 SSLDEENTESVVRLLHKTHQEFrpTIFFVSHEL 194
Cdd:TIGR02868 500 EHLDAETADELLEDLLAALSGR--TVVLITHHL 530
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
17-209 |
1.23e-19 |
|
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: 82.59 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNvqtfskkevrqqqqQMGMVFQH-Ynllenlki 95
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE--------------DLLFLPQRpY-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 96 ydnvaLPLKLLKEkqpekierlltfvdmahkAEAYP--AQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTESVV 173
Cdd:cd03223 75 -----LPLGTLRE------------------QLIYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLY 131
|
170 180 190
....*....|....*....|....*....|....*.
gi 488289759 174 RLLhkthQEFRPTIFFVSHElETVKRLCNRILVMEK 209
Cdd:cd03223 132 QLL----KELGITVISVGHR-PSLWKFHDRVLDLDG 162
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-216 |
1.55e-19 |
|
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: 87.31 E-value: 1.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQE--THALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQQQ- 78
Cdd:TIGR00957 1285 VEFRNYCLRYREdlDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITi 1364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 79 --QMGMVFQHyNLLENLKIYDN-------VALPLKLLK---EKQPEKIErlltfvdmaHKAEAYPAQLSGGEKQRVSIAR 146
Cdd:TIGR00957 1365 ipQDPVLFSG-SLRMNLDPFSQysdeevwWALELAHLKtfvSALPDKLD---------HECAEGGENLSVGQRQLVCLAR 1434
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 147 ALSRNPKWLLCDEATSSLDEEnTESVVRLLHKTHQEfRPTIFFVSHELETVKRLcNRILVMEKGQlIGEF 216
Cdd:TIGR00957 1435 ALLRKTKILVLDEATAAVDLE-TDNLIQSTIRTQFE-DCTVLTIAHRLNTIMDY-TRVIVLDKGE-VAEF 1500
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-215 |
1.67e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 83.77 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFskKEVRQQQQQM 80
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDW--QTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 81 GMVFQHYNLLENLKIYDNVALPLKLLKEKQ-PEKIERLLTFVDMAHKAEAYPA-QLSGGEKQRVSIARALSRNPKWLLCD 158
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMGGFFAERDQfQERIKWVYELFPRLHERRIQRAgTMSGGEQQMLAIGRALMSQPRLLLLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 159 EATSSLdeenTESVVRLLHKTHQEFRP---TIFFVSHELETVKRLCNRILVMEKGQLIGE 215
Cdd:PRK11614 163 EPSLGL----APIIIQQIFDTIEQLREqgmTIFLVEQNANQALKLADRGYVLENGHVVLE 218
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-197 |
3.90e-19 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 83.24 E-value: 3.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRidgrnvqtfskkevRQQQQQM 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK--------------RNGKLRI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 81 GMVFQhynllenlKIYDNVALPL------KLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKW 154
Cdd:PRK09544 70 GYVPQ--------KLYLDTTLPLtvnrflRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488289759 155 LLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETV 197
Cdd:PRK09544 142 LVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLV 184
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
17-182 |
8.58e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 81.46 E-value: 8.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNvQTFSKkeVRQQQQQMGmvfqHYNLL-ENLKI 95
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD-IDDPD--VAEACHYLG----HRNAMkPALTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 96 YDNVALPLKLLKEKQPEkIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARAL-SRNPKWLLcDEATSSLDEENTESVVR 174
Cdd:PRK13539 91 AENLEFWAAFLGGEELD-IAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLvSNRPIWIL-DEPTAALDAAAVALFAE 168
|
....*...
gi 488289759 175 LLhKTHQE 182
Cdd:PRK13539 169 LI-RAHLA 175
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-210 |
8.73e-19 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 85.08 E-value: 8.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVY---QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRI-DGRNVQTFSKKEVRQQq 77
Cdd:PTZ00265 383 IQFKNVRFHYdtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSK- 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 78 qqMGMVFQHYNLLENlKIYDNVALPLKLLKE------------------------------------------------- 108
Cdd:PTZ00265 462 --IGVVSQDPLLFSN-SIKNNIKYSLYSLKDlealsnyynedgndsqenknkrnscrakcagdlndmsnttdsneliemr 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 109 KQPEKIERLlTFVDMAHKA------EAYP-----------AQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTES 171
Cdd:PTZ00265 539 KNYQTIKDS-EVVDVSKKVlihdfvSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYL 617
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 488289759 172 VVRLLHKTH-QEFRPTIfFVSHELETVkRLCNRILVM---EKG 210
Cdd:PTZ00265 618 VQKTINNLKgNENRITI-IIAHRLSTI-RYANTIFVLsnrERG 658
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-238 |
1.82e-18 |
|
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: 83.83 E-value: 1.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 4 LVNVSKVYQET-HALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRI-DGRNV-------QTFSKKEVR 74
Cdd:TIGR03719 7 MNRVSKVVPPKkEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPqPGIKVgylpqepQLDPTKTVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 75 qQQQQMGM-----VFQHYNllenlKIYDNVALPL----KLLKE--KQPEKIE-----RLLTFVDMAHKA------EAYPA 132
Cdd:TIGR03719 87 -ENVEEGVaeikdALDRFN-----EISAKYAEPDadfdKLAAEqaELQEIIDaadawDLDSQLEIAMDAlrcppwDADVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 133 QLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTESVVRLLHkthqEFRPTIFFVSHELETVKRLCNRILVMEKGQL 212
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQ----EYPGTVVAVTHDRYFLDNVAGWILELDRGRG 236
|
250 260
....*....|....*....|....*.
gi 488289759 213 IgeflnnPqqYEEEPLSYLEKVERSL 238
Cdd:TIGR03719 237 I------P--WEGNYSSWLEQKQKRL 254
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
8-211 |
5.99e-18 |
|
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: 79.05 E-value: 5.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 8 SKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLnLME-QPSEGEIRIDGR-----------------NVQtfs 69
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL-LGElEKLSGSVSVPGSiayvsqepwiqngtireNIL--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 70 kkevrqqqqqMGMVFQH--YN-------LLENLKIydnvaLPLKLLKEkqpekI-ERLLTfvdmahkaeaypaqLSGGEK 139
Cdd:cd03250 88 ----------FGKPFDEerYEkvikacaLEPDLEI-----LPDGDLTE-----IgEKGIN--------------LSGGQK 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488289759 140 QRVSIARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRlCNRILVMEKGQ 211
Cdd:cd03250 134 QRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-240 |
6.40e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 82.33 E-value: 6.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQQQ---QMGMVFQ---HYNLl 90
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSiipQSPVLFSgtvRFNI- 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 91 ENLKIYDNVALPLKLLKEKQPEKIERLLTFVDmahkAEAYPA--QLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEEn 168
Cdd:PLN03232 1331 DPFSEHNDADLWEALERAHIKDVIDRNPFGLD----AEVSEGgeNFSVGQRQLLSLARALLRRSKILVLDEATASVDVR- 1405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488289759 169 TESvvrLLHKT-HQEFRP-TIFFVSHELETVKRlCNRILVMEKGQLIgEFlNNPQQYEEEPLSYLEKVERSLRP 240
Cdd:PLN03232 1406 TDS---LIQRTiREEFKScTMLVIAHRLNTIID-CDKILVLSSGQVL-EY-DSPQELLSRDTSAFFRMVHSTGP 1473
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
16-213 |
7.19e-18 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 82.07 E-value: 7.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 16 ALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRqqqQQMGMVFQHYNLLENlKI 95
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWR---SRLAVVSQTPFLFSD-TV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 96 YDNVALPLKLLKEKQPEKIERLLTF-VDMAHKAEAYPAQ-------LSGGEKQRVSIARALSRNPKWLLCDEATSSLDEE 167
Cdd:PRK10789 406 ANNIALGRPDATQQEIEHVARLASVhDDILRLPQGYDTEvgergvmLSGGQKQRISIARALLLNAEILILDDALSAVDGR 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488289759 168 nTESvvRLLHKTHQ--EFRpTIFFVSHELETVKRlCNRILVMEKGQLI 213
Cdd:PRK10789 486 -TEH--QILHNLRQwgEGR-TVIISAHRLSALTE-ASEILVMQHGHIA 528
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
15-212 |
9.85e-18 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 81.48 E-value: 9.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 15 HALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQQQQmgmvfqhynlLENLK 94
Cdd:PRK13545 38 YALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTG----------IENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 95 IYdnvALPLKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTESVVR 174
Cdd:PRK13545 108 LK---GLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLD 184
|
170 180 190
....*....|....*....|....*....|....*...
gi 488289759 175 LLHKtHQEFRPTIFFVSHELETVKRLCNRILVMEKGQL 212
Cdd:PRK13545 185 KMNE-FKEQGKTIFFISHSLSQVKSFCTKALWLHYGQV 221
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
19-182 |
1.06e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 78.31 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 19 NIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQtfskkEVRQQQQQMGMVFQHYN-----L--LE 91
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR-----RQRDEYHQDLLYLGHQPgikteLtaLE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 92 NLKIYdnvalpLKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIAR-ALSRNPKWLLcDEATSSLDEENTE 170
Cdd:PRK13538 94 NLRFY------QRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARlWLTRAPLWIL-DEPFTAIDKQGVA 166
|
170 180
....*....|....*....|...
gi 488289759 171 SVVRLL--H---------KTHQE 182
Cdd:PRK13538 167 RLEALLaqHaeqggmvilTTHQD 189
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
16-199 |
1.23e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 78.04 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 16 ALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFskkeVRQQQQ-------------QMGm 82
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAY----VPQRSEvpdslpltvrdlvAMG- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 83 VFQHYNLLENLKIYDNVAlplkllkekqpekIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATS 162
Cdd:NF040873 82 RWARRGLWRRLTRDDRAA-------------VDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 488289759 163 SLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKR 199
Cdd:NF040873 149 GLDAESRERIIALLAEEHARGA-TVVVVTHDLELVRR 184
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
2-213 |
1.30e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 79.11 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSkvyqETHALKNIHFSVQLGEIVGIVGKSGSGKSTLL-RLLNLMeqPSEGEIRIDGRNVQTFSKKEVRQQ---- 76
Cdd:COG4138 1 LQLNDVA----VAGRLGPISAQVNAGELIHLIGPNGAGKSTLLaRMAGLL--PGQGEILLNGRPLSDWSAAELARHrayl 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 77 -QQQM---GM-VFQHYNLlenlkiydnvALPLKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARAL--- 148
Cdd:COG4138 75 sQQQSppfAMpVFQYLAL----------HQPAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqv 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488289759 149 --SRNP--KWLLCDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:COG4138 145 wpTINPegQLLLLDEPMNSLDVAQQAALDRLLRELCQQGI-TVVMSSHDLNHTLRHADRVWLLKQGKLV 212
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-208 |
1.93e-17 |
|
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: 78.60 E-value: 1.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 27 GEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNV----QTFS-KKEVRQQQQQMGMVFQHYNLlenlKIYDN-VA 100
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVsykpQYIKaDYEGTVRDLLSSITKDFYTH----PYFKTeIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 101 LPLKLlkekqpEKI-ERLLTfvdmahkaeaypaQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTESVVRLLHKT 179
Cdd:cd03237 101 KPLQI------EQIlDREVP-------------ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRF 161
|
170 180
....*....|....*....|....*....
gi 488289759 180 HQEFRPTIFFVSHELETVKRLCNRILVME 208
Cdd:cd03237 162 AENNEKTAFVVEHDIIMIDYLADRLIVFE 190
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-212 |
3.28e-17 |
|
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: 80.44 E-value: 3.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 6 NVSKVYQETH--ALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTfSKKEVRQQqqqMGMV 83
Cdd:TIGR01257 933 NLVKIFEPSGrpAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQS---LGMC 1008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 84 FQHYNLLENLKIYDNVALPLKLLKEKQPE---KIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEA 160
Cdd:TIGR01257 1009 PQHNILFHHLTVAEHILFYAQLKGRSWEEaqlEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488289759 161 TSSLDEENTESVVRLLHKtHQEFRpTIFFVSHELETVKRLCNRILVMEKGQL 212
Cdd:TIGR01257 1089 TSGVDPYSRRSIWDLLLK-YRSGR-TIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-210 |
3.45e-17 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 80.21 E-value: 3.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRqqqQQMGMVFQHYNLLENlkiy 96
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELR---RQFSMIPQDPVLFDG---- 1398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 97 dNVALPLKLLKEKQPEKIERLLTFVDM----AHKAEAYPAQL-------SGGEKQRVSIARA-LSRNPKWLLCDEATSSL 164
Cdd:PTZ00243 1399 -TVRQNVDPFLEASSAEVWAALELVGLrervASESEGIDSRVleggsnySVGQRQLMCMARAlLKKGSGFILMDEATANI 1477
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488289759 165 D---EENTESVVRLLHKTHqefrpTIFFVSHELETVKRlCNRILVMEKG 210
Cdd:PTZ00243 1478 DpalDRQIQATVMSAFSAY-----TVITIAHRLHTVAQ-YDKIIVMDHG 1520
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-212 |
7.42e-17 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 78.86 E-value: 7.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETH-ALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRqqqQQM 80
Cdd:PRK10522 323 LELRNVTFAYQDNGfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYR---KLF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 81 GMVFQHYNLLENLKIYDNvalplkllKEKQPEKIERLLTFVDMAHKAE-----AYPAQLSGGEKQRVSIARALSRNPKWL 155
Cdd:PRK10522 400 SAVFTDFHLFDQLLGPEG--------KPANPALVEKWLERLKMAHKLEledgrISNLKLSKGQKKRLALLLALAEERDIL 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488289759 156 LCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHElETVKRLCNRILVMEKGQL 212
Cdd:PRK10522 472 LLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-213 |
9.68e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 77.23 E-value: 9.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETH-ALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQ---QQ 77
Cdd:PRK15056 7 IVVNDVTVTWRNGHtALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAyvpQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 78 QQMGMVFQhyNLLENLKI---YDNVALpLKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKW 154
Cdd:PRK15056 87 EEVDWSFP--VLVEDVVMmgrYGHMGW-LRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQV 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488289759 155 LLCDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRIlVMEKGQLI 213
Cdd:PRK15056 164 ILLDEPFTGVDVKTEARIISLLRELRDEGK-TMLVSTHNLGSVTEFCDYT-VMVKGTVL 220
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
22-213 |
1.29e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 76.12 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 22 FSVQLGEIVGIVGKSGSGKSTLL-RLLNLMeqPSEGEIRIDGRNVQTFSKKEVRQQ-----QQQM---GM-VFQHYNLle 91
Cdd:PRK03695 17 AEVRAGEILHLVGPNGAGKSTLLaRMAGLL--PGSGSIQFAGQPLEAWSAAELARHraylsQQQTppfAMpVFQYLTL-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 92 nlkiydnvALPLKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARAL-----SRNP--KWLLCDEATSSL 164
Cdd:PRK03695 93 --------HQPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPagQLLLLDEPMNSL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488289759 165 DEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:PRK03695 165 DVAQQAALDRLLSELCQQGI-AVVMSSHDLNHTLRHADRVWLLKQGKLL 212
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
22-165 |
2.07e-16 |
|
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: 74.84 E-value: 2.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 22 FSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQtfskkEVRQQQQQMGMVFQHYN-------LLENLK 94
Cdd:cd03231 21 FTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLD-----FQRDSIARGLLYLGHAPgikttlsVLENLR 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488289759 95 IYDNVAlplkllkekQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARA-LSRNPKWLLcDEATSSLD 165
Cdd:cd03231 96 FWHADH---------SDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLlLSGRPLWIL-DEPTTALD 157
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
18-215 |
2.11e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 77.78 E-value: 2.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 18 KNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGrnvQTFSKKEVRQQQQQmGMVF-----QHYNLLEN 92
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNG---KEINALSTAQRLAR-GLVYlpedrQSSGLYLD 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 93 LKIYDNVA------LPLKLLKEKQPEKIERLLTFVDMAHKAEAYPAQ-LSGGEKQRVSIARALSRNPKWLLCDEATSSLD 165
Cdd:PRK15439 356 APLAWNVCalthnrRGFWIKPARENAVLERYRRALNIKFNHAEQAARtLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488289759 166 EENTESVVRLLHKTHQEfRPTIFFVSHELETVKRLCNRILVMEKGQLIGE 215
Cdd:PRK15439 436 VSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEISGA 484
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-225 |
2.47e-16 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 77.67 E-value: 2.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIdGRNVqtfskkevrqqqqQMG 81
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV-------------KLA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 82 MVFQHYNLLENLK-IYDNVALPLKLLKekqpekierlLTFVDMAHKA------------EAYPAQLSGGEKQRVSIARAL 148
Cdd:TIGR03719 389 YVDQSRDALDPNKtVWEEISGGLDIIK----------LGKREIPSRAyvgrfnfkgsdqQKKVGQLSGGERNRVHLAKTL 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488289759 149 SRNPKWLLCDEATSSLDEENtesvVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIGEFLNNPQQYEE 225
Cdd:TIGR03719 459 KSGGNVLLLDEPTNDLDVET----LRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEGDSHVEWFEGNFSEYEE 531
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
17-213 |
2.55e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 77.86 E-value: 2.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQqqqMGMVFQ---------HY 87
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKV---LGIIPQapvlfsgtvRF 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 88 NLlENLKIYDNVALPLKLLKEKQPEKIERLLTFVDmAHKAEAyPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDee 167
Cdd:PLN03130 1332 NL-DPFNEHNDADLWESLERAHLKDVIRRNSLGLD-AEVSEA-GENFSVGQRQLLSLARALLRRSKILVLDEATAAVD-- 1406
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488289759 168 ntesvVR---LLHKT-HQEFRP-TIFFVSHELETVKRlCNRILVMEKGQLI 213
Cdd:PLN03130 1407 -----VRtdaLIQKTiREEFKScTMLIIAHRLNTIID-CDRILVLDAGRVV 1451
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-192 |
2.57e-16 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 77.47 E-value: 2.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 4 LVNVSKVY-QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRI-DGRNV-------QTFSKKEVR 74
Cdd:PRK11819 9 MNRVSKVVpPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPaPGIKVgylpqepQLDPEKTVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 75 QQ-QQQMGMVFQHYNLLEnlKIYDNVALPL----KLLKE--KQPEKIER-----LLTFVDMAHKA------EAYPAQLSG 136
Cdd:PRK11819 89 ENvEEGVAEVKAALDRFN--EIYAAYAEPDadfdALAAEqgELQEIIDAadawdLDSQLEIAMDAlrcppwDAKVTKLSG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488289759 137 GEKQRVSIARALSRNPKWLLCDEATSSLDeenTESVVRLLHktH-QEFRPTIFFVSH 192
Cdd:PRK11819 167 GERRRVALCRLLLEKPDMLLLDEPTNHLD---AESVAWLEQ--FlHDYPGTVVAVTH 218
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-229 |
5.34e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 76.49 E-value: 5.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 20 IHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKE-VRQ-------QQQQMGMVfQHYNLLE 91
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDaIRAgimlcpeDRKAEGII-PVHSVAD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 92 NLKIY------------------DNVALPLKLLKEKQPEkIERLLTFvdmahkaeaypaqLSGGEKQRVSIARALSRNPK 153
Cdd:PRK11288 351 NINISarrhhlragclinnrweaENADRFIRSLNIKTPS-REQLIMN-------------LSGGNQQKAILGRWLSEDMK 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488289759 154 WLLCDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLIGEfLNNPQQYEEEPLS 229
Cdd:PRK11288 417 VILLDEPTRGIDVGAKHEIYNVIYELAAQGV-AVLFVSSDLPEVLGVADRIVVMREGRIAGE-LAREQATERQALS 490
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
20-176 |
7.02e-16 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 73.73 E-value: 7.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 20 IHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQQQQMGMVFQHYNLLENLKIydnv 99
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLPGLKADLSTLENLHF---- 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488289759 100 alpLKLLKEKQPEKIE-RLLTFVDMAHKAEAYPAQLSGGEKQRVSIARA-LSRNPKWLLcDEATSSLDEENTESVVRLL 176
Cdd:PRK13543 106 ---LCGLHGRRAKQMPgSALAIVGLAGYEDTLVRQLSAGQKKRLALARLwLSPAPLWLL-DEPYANLDLEGITLVNRMI 180
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-216 |
7.45e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 76.20 E-value: 7.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKkevrQQQQQMGMVF-----QHYNLLE 91
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSP----QDGLANGIVYisedrKRDGLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 92 NLKIYDNVALP-LKLLKE-----KQPEKIERLLTFVDMAH----KAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEAT 161
Cdd:PRK10762 344 GMSVKENMSLTaLRYFSRaggslKHADEQQAVSDFIRLFNiktpSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPT 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 162 SSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLIGEF 216
Cdd:PRK10762 424 RGVDVGAKKEIYQLINQFKAEGL-SIILVSSEMPEVLGMSDRILVMHEGRISGEF 477
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-126 |
8.50e-16 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 75.99 E-value: 8.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETH-----ALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVqtfSKKEVRQQ 76
Cdd:COG4615 328 LELRGVTYRYPGEDgdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV---TADNREAY 404
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 488289759 77 QQQMGMVFQHYNLLENLkiydnvalpLKLLKEKQPEKIERLLTFVDMAHK 126
Cdd:COG4615 405 RQLFSAVFSDFHLFDRL---------LGLDGEADPARARELLERLELDHK 445
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
16-213 |
8.61e-16 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 75.22 E-value: 8.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 16 ALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQP----SEGEIRIDGRNVQTFSKKEVRQQ-QQQMGMVFQH---- 86
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRLSPRERRKLvGHNVSMIFQEpqsc 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 87 --------YNLLENLKIYDNVALPLKLLKEKQPEKIERLLTFVDMAHKA--EAYPAQLSGGEKQRVSIARALSRNPKWLL 156
Cdd:PRK15093 102 ldpservgRQLMQNIPGWTYKGRWWQRFGWRKRRAIELLHRVGIKDHKDamRSFPYELTEGECQKVMIAIALANQPRLLI 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488289759 157 CDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:PRK15093 182 ADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
18-221 |
1.23e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 73.58 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 18 KNIHFSVQLGEIVGIVGKSGSGKS-TLLRLLNLME---QPSEGEIRIDGRNV--QTFSKKEVRQQQQQMGMVFQ-----H 86
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILPagvRQTAGRVLLDGKPVapCALRGRKIATIMQNPRSAFNplhtmH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 87 YNLLENLK---IYDNVALPLKLLKEKQPEKIERLLtfvdmahkaEAYPAQLSGGEKQRVSIARAL-SRNPkWLLCDEATS 162
Cdd:PRK10418 100 THARETCLalgKPADDATLTAALEAVGLENAARVL---------KLYPFEMSGGMLQRMMIALALlCEAP-FIIADEPTT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488289759 163 SLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI-----GEFLNNPQ 221
Cdd:PRK10418 170 DLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVeqgdvETLFNAPK 233
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
18-230 |
1.53e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.21 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 18 KNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKE--------VRQQQQQMGMvFQHYNL 89
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDavkkgmayITESRRDNGF-FPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 90 LENLKIYDNVAL-----PLKLLKEKQPEKI---ERLLTFVDmAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEAT 161
Cdd:PRK09700 359 AQNMAISRSLKDggykgAMGLFHEVDEQRTaenQRELLALK-CHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPT 437
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488289759 162 SSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLIGEFLNNPQQYEEEPLSY 230
Cdd:PRK09700 438 RGIDVGAKAEIYKVMRQLADDGK-VILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMSEEEIMAW 505
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-212 |
1.55e-15 |
|
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: 73.74 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQE--THALKNIHFSVQLGEIVGIVGKSGSGKSTL----LRLLNlmeqpSEGEIRIDGRNVQTFSKKEVRq 75
Cdd:cd03289 3 MTVKDLTAKYTEggNAVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGDIQIDGVSWNSVPLQKWR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 76 qqQQMGMVFQ-----------------HYNLLENLKIYDNVAlpLKLLKEKQPEKIErlLTFVDMAHkaeaypaQLSGGE 138
Cdd:cd03289 77 --KAFGVIPQkvfifsgtfrknldpygKWSDEEIWKVAEEVG--LKSVIEQFPGQLD--FVLVDGGC-------VLSHGH 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488289759 139 KQRVSIARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFrpTIFFVSHELETVKRlCNRILVMEKGQL 212
Cdd:cd03289 144 KQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADC--TVILSEHRIEAMLE-CQRFLVIEENKV 214
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-239 |
2.12e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 74.99 E-value: 2.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTfskkevRQQQ--- 77
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVA------RLQQdpp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 78 -QQMGMVF-------QHynLLENLKIYDNValpLKLLKEKQPEK----IERLLTFVDMAH-----------------KAE 128
Cdd:PRK11147 77 rNVEGTVYdfvaegiEE--QAEYLKRYHDI---SHLVETDPSEKnlneLAKLQEQLDHHNlwqlenrinevlaqlglDPD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 129 AYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTESVVRLLhkthQEFRPTIFFVSHELETVKRLCNRILVME 208
Cdd:PRK11147 152 AALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL----KTFQGSIIFISHDRSFIRNMATRIVDLD 227
|
250 260 270
....*....|....*....|....*....|.
gi 488289759 209 KGQLIgeflNNPQQYEEeplsYLEKVERSLR 239
Cdd:PRK11147 228 RGKLV----SYPGNYDQ----YLLEKEEALR 250
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-193 |
2.34e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 71.90 E-value: 2.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVqtfsKKEVRQQQQQM 80
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTYQKQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 81 GMVFQHYNLLENLKIYDNVALPLKLlkEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEA 160
Cdd:PRK13540 77 CFVGHRSGINPYLTLRENCLYDIHF--SPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEP 154
|
170 180 190
....*....|....*....|....*....|...
gi 488289759 161 TSSLDEENTESVVRLLhKTHQEFRPTIFFVSHE 193
Cdd:PRK13540 155 LVALDELSLLTIITKI-QEHRAKGGAVLLTSHQ 186
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-219 |
7.12e-15 |
|
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: 73.32 E-value: 7.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 19 NIHFSVQLGEIVGIVGKSGSGKSTLLR-LLNLMEQPSEGEIRIDGRNVQTFSKKE--------VRQQQQQMGMVFQ---H 86
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPVDIRNPAQairagiamVPEDRKRHGIVPIlgvG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 87 YNLleNLKIYDNVALPLKLLKEKQPEKIERLLTFVDMAHKAEAYP-AQLSGGEKQRVSIARALSRNPKWLLCDEATSSLD 165
Cdd:TIGR02633 358 KNI--TLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488289759 166 EENTESVVRLLHKTHQEfRPTIFFVSHELETVKRLCNRILVMEKGQLIGEFLNN 219
Cdd:TIGR02633 436 VGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDFVNH 488
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
19-219 |
1.20e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 72.65 E-value: 1.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 19 NIHFSVQLGEIVGIVGKSGSGKSTLLR-LLNLMEQPSEGEIRIDGRNVQTFSKKEVrqQQQQMGMVFQ---HYNLLENLK 94
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQcLFGAYPGRWEGEIFIDGKPVKIRNPQQA--IAQGIAMVPEdrkRDGIVPVMG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 95 IYDNVALPL-----------KLLKEKQPEK-IERLLtfVDMAHkAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATS 162
Cdd:PRK13549 358 VGKNITLAAldrftggsridDAAELKTILEsIQRLK--VKTAS-PELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTR 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488289759 163 SLDEENTESVVRLLHKTHQEfRPTIFFVSHELETVKRLCNRILVMEKGQLIGEFLNN 219
Cdd:PRK13549 435 GIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKLKGDLINH 490
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-208 |
2.09e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 71.76 E-value: 2.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 27 GEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDgrnvQTFSKKEVRQQQQQMGMVFQhynLLENLK-------IYDNV 99
Cdd:PRK13409 365 GEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE----LKISYKPQYIKPDYDGTVED---LLRSITddlgssyYKSEI 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 100 ALPLKLlkekqpekiERLLtfvdmahkaEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTESVVRLLHKT 179
Cdd:PRK13409 438 IKPLQL---------ERLL---------DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRI 499
|
170 180
....*....|....*....|....*....
gi 488289759 180 HQEFRPTIFFVSHELETVKRLCNRILVME 208
Cdd:PRK13409 500 AEEREATALVVDHDIYMIDYISDRLMVFE 528
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
23-208 |
4.61e-14 |
|
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: 70.97 E-value: 4.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 23 SVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIR---------------IDGRnVQTFSKKEVRQQqqqmgmvfqhy 87
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDedlkisykpqyispdYDGT-VEEFLRSANTDD----------- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 88 nlLENLKIYDNVALPLKLlkekqpekiERLLtfvdmahkaEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEE 167
Cdd:COG1245 430 --FGSSYYKTEIIKPLGL---------EKLL---------DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 489
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488289759 168 NTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVME 208
Cdd:COG1245 490 QRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMVFE 530
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1-213 |
9.97e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 69.82 E-value: 9.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLnlmeqpS--------EGEIRIDGrNVQTFskKE 72
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVL------SgvyphgsyEGEILFDG-EVCRF--KD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 73 VRQQQQQmGMVFQHYNL--LENLKIYDNVALPLKLLK------EKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSI 144
Cdd:NF040905 72 IRDSEAL-GIVIIHQELalIPYLSIAENIFLGNERAKrgvidwNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488289759 145 ARALSRNPKWLLCDEATSSLDEENTESVVRLLHkthqEFRP---TIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:NF040905 151 AKALSKDVKLLILDEPTAALNEEDSAALLDLLL----ELKAqgiTSIIISHKLNEIRRVADSITVLRDGRTI 218
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-225 |
1.05e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 69.92 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRidgrnvqtFSKKevrqqqQQMG 81
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK--------WSEN------ANIG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 82 MVFQ-HYNLLEN-LKIYDNVAlplkllKEKQPEKIE--------RLLTFVDMAHKAeayPAQLSGGEKQRVSIARALSRN 151
Cdd:PRK15064 386 YYAQdHAYDFENdLTLFDWMS------QWRQEGDDEqavrgtlgRLLFSQDDIKKS---VKVLSGGEKGRMLFGKLMMQK 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488289759 152 PKWLLCDEATSSLDEENTESVVRLLHKthqeFRPTIFFVSHELETVKRLCNRILVMEKGQLIgEFLNNpqqYEE 225
Cdd:PRK15064 457 PNVLVMDEPTNHMDMESIESLNMALEK----YEGTLIFVSHDREFVSSLATRIIEITPDGVV-DFSGT---YEE 522
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-210 |
1.58e-13 |
|
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: 69.66 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQETH--ALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTfskkEVRQQQQ 78
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT----NISDVHQ 2012
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 79 QMGMVFQHYNLLENLKIYDNVALPLKlLKEKQPEKIERLLTF----VDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKW 154
Cdd:TIGR01257 2013 NMGYCPQFDAIDDLLTGREHLYLYAR-LRGVPAEEIEKVANWsiqsLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPL 2091
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488289759 155 LLCDEATSSLDEENTESVVRLLHKTHQEFRPTIfFVSHELETVKRLCNRILVMEKG 210
Cdd:TIGR01257 2092 VLLDEPTTGMDPQARRMLWNTIVSIIREGRAVV-LTSHSMEECEALCTRLAIMVKG 2146
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
17-208 |
3.36e-13 |
|
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: 68.78 E-value: 3.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 17 LKNIHFSVQLGEIVGIVGKSGSGKSTL----LRLLNlmeqpSEGEIRIDGRNVQTFSkkeVRQQQQQMGMV--------- 83
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLlsalLRLLS-----TEGEIQIDGVSWNSVT---LQTWRKAFGVIpqkvfifsg 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 84 --------FQHYNLLENLKIYDNVAlpLKLLKEKQPEKIERLLtfVDMAHkaeaypaQLSGGEKQRVSIARALSRNPKWL 155
Cdd:TIGR01271 1307 tfrknldpYEQWSDEEIWKVAEEVG--LKSVIEQFPDKLDFVL--VDGGY-------VLSNGHKQLMCLARSILSKAKIL 1375
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488289759 156 LCDEATSSLDEENTESVVRLLHKTHQEFrpTIFFVSHELETVKRlCNRILVME 208
Cdd:TIGR01271 1376 LLDEPSAHLDPVTLQIIRKTLKQSFSNC--TVILSEHRVEALLE-CQQFLVIE 1425
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
15-225 |
4.01e-13 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 66.76 E-value: 4.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 15 HALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGrnvqtfskkevrqqqqQMGMVFQHYNLLENLK 94
Cdd:PRK13546 38 FALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG----------------EVSVIAISAGLSGQLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 95 IYDNVALPL-------KLLKEKQPEKIErlltFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEE 167
Cdd:PRK13546 102 GIENIEFKMlcmgfkrKEIKAMTPKIIE----FSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQT 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 168 NTESVVRLLHKtHQEFRPTIFFVSHELETVKRLCNRILVMEKGQL--IGEFLNNPQQYEE 225
Cdd:PRK13546 178 FAQKCLDKIYE-FKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLkdYGELDDVLPKYEA 236
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
17-213 |
4.07e-13 |
|
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: 65.75 E-value: 4.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPS---EGEIRIDGRNvqtfSKKEVRQQQQQMGMVFQHynllenl 93
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIP----YKEFAEKYPGEIIYVSEE------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 94 kiyDNvalplkllkeKQPE-KIERLLTFVDMAhKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENT-ES 171
Cdd:cd03233 92 ---DV----------HFPTlTVRETLDFALRC-KGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTAlEI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488289759 172 VVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:cd03233 158 LKCIRTMADVLKTTTFVSLYQASDEIYDLFDKVLVLYEGRQI 199
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
27-208 |
1.39e-12 |
|
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: 63.75 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 27 GEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTfskkevrqqqqqmgmvfqhynllenlkiydnvalplkll 106
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVY--------------------------------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 107 kekQPEKIErlltfvdmahkaeaypaqLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPT 186
Cdd:cd03222 66 ---KPQYID------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKT 124
|
170 180
....*....|....*....|..
gi 488289759 187 IFFVSHELETVKRLCNRILVME 208
Cdd:cd03222 125 ALVVEHDLAVLDYLSDRIHVFE 146
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
17-210 |
1.41e-12 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 64.19 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPS--EGEIRIDGR-NVQTFskkevrqqQQQMGMVFQHYNLLENL 93
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRpLDKNF--------QRSTGYVEQQDVHSPNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 94 KIYDNvalplkllkekqpekierlLTFvdmahkaEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTESVV 173
Cdd:cd03232 95 TVREA-------------------LRF-------SALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIV 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 488289759 174 RLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKG 210
Cdd:cd03232 149 RFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRG 185
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-225 |
2.55e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 65.53 E-value: 2.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIdGRNVqtfskkevrqqqqQMG 81
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV-------------KLA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 82 MVFQHYNLLENLK-IYDNVALPLKLLKEKQPEKIERlltfvdmahkaeAYPA--------------QLSGGEKQRVSIAR 146
Cdd:PRK11819 391 YVDQSRDALDPNKtVWEEISGGLDIIKVGNREIPSR------------AYVGrfnfkggdqqkkvgVLSGGERNRLHLAK 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 147 ALSRNPKWLLCDEATSSLDEENtesvVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEkgqliGE-----FLNNPQ 221
Cdd:PRK11819 459 TLKQGGNVLLLDEPTNDLDVET----LRALEEALLEFPGCAVVISHDRWFLDRIATHILAFE-----GDsqvewFEGNFQ 529
|
....
gi 488289759 222 QYEE 225
Cdd:PRK11819 530 EYEE 533
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
17-178 |
3.17e-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: 63.31 E-value: 3.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLlnLMEQPS----EGEIRIDGRNvqtfskkevrqqqqqmgmvfqhynlLEN 92
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKT--IMGHPKyevtEGEILFKGED-------------------------ITD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 93 LKIYDNVALPLKLLKEKQPE----KIERLLTFVDMAhkaeaypaqLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEEN 168
Cdd:cd03217 69 LPPEERARLGIFLAFQYPPEipgvKNADFLRYVNEG---------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDA 139
|
170
....*....|
gi 488289759 169 TESVVRLLHK 178
Cdd:cd03217 140 LRLVAEVINK 149
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
16-211 |
5.02e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 65.15 E-value: 5.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 16 ALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIR-----IDGRNVQTfsKKEVrqqqqqmGMVFQHYNLL 90
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWlfgqpVDAGDIAT--RRRV-------GYMSQAFSLY 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 91 ENLKIYDNVALPLKLL---KEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEE 167
Cdd:NF033858 352 GELTVRQNLELHARLFhlpAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPV 431
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488289759 168 NTESVVRLLHKTHQEFRPTIFFVSH---ELEtvkRlCNRILVMEKGQ 211
Cdd:NF033858 432 ARDMFWRLLIELSREDGVTIFISTHfmnEAE---R-CDRISLMHAGR 474
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
12-211 |
6.25e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.52 E-value: 6.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 12 QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPS--EGEIRIDGRnvqtfskKEVRQQQQQMGMVFQ---- 85
Cdd:PLN03211 79 QERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNR-------KPTKQILKRTGFVTQddil 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 86 --HYNLLENLKIYDNVALPLKLLKEKQPEKIERLLTFVDMAhKAE------AYPAQLSGGEKQRVSIARALSRNPKWLLC 157
Cdd:PLN03211 152 ypHLTVRETLVFCSLLRLPKSLTKQEKILVAESVISELGLT-KCEntiignSFIRGISGGERKRVSIAHEMLINPSLLIL 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488289759 158 DEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQ 211
Cdd:PLN03211 231 DEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGR 284
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-204 |
2.78e-11 |
|
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: 59.69 E-value: 2.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 27 GEIVGIVGKSGSGKSTLLRLL-NLMEQPSEGEIRIDGrnvqtfskkevrqqqqqmgmvfqhynllenlkiydnvalplkl 105
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALaRELGPPGGGVIYIDG------------------------------------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 106 lkekqpEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENT-----ESVVRLLHKTH 180
Cdd:smart00382 39 ------EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEallllLEELRLLLLLK 112
|
170 180
....*....|....*....|....
gi 488289759 181 QEFRPTIFFVSHELETVKRLCNRI 204
Cdd:smart00382 113 SEKNLTVILTTNDEKDLGPALLRR 136
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
23-207 |
1.47e-10 |
|
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: 59.30 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 23 SVQLGEIVGIVGKSGSGKSTLLRLL------NLMEQPSEGEIR--ID---GRNVQTFSKKeVRQQQQQMGMVFQHYNLLE 91
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILagklkpNLGKFDDPPDWDeiLDefrGSELQNYFTK-LLEGDVKVIVKPQYVDLIP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 92 NlKIYDNVALPLKLLKEKqpEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTES 171
Cdd:cd03236 101 K-AVKGKVGELLKKKDER--GKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLN 177
|
170 180 190
....*....|....*....|....*....|....*.
gi 488289759 172 VVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVM 207
Cdd:cd03236 178 AARLIRELAEDDN-YVLVVEHDLAVLDYLSDYIHCL 212
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
17-210 |
2.41e-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: 58.50 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLrLLNLME-QPSEGEIRIDGRNVQTFSKKEVRQQQQQMGMVFQHYNLLENLKI 95
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLL-LAILGEmQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLLNATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 96 YDNVALPLKLLKEKQPEKIER--------LLTFVDMAHKAEAyPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEE 167
Cdd:cd03290 96 EENITFGSPFNKQRYKAVTDAcslqpdidLLPFGDQTEIGER-GINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488289759 168 NT-----ESVVRLLhkthQEFRPTIFFVSHELETVKRlCNRILVMEKG 210
Cdd:cd03290 175 LSdhlmqEGILKFL----QDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
13-165 |
2.78e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 60.14 E-value: 2.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 13 ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLnLMEQP--SEGEIRIDGRNVQTfskkevrqqqQQMGMVFqhynll 90
Cdd:PLN03130 629 ERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAM-LGELPprSDASVVIRGTVAYV----------PQVSWIF------ 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 91 eNLKIYDNVALPLKLlkekQPEKIERLLTFVDMAHKAEAYPA-----------QLSGGEKQRVSIARALSRNPKWLLCDE 159
Cdd:PLN03130 692 -NATVRDNILFGSPF----DPERYERAIDVTALQHDLDLLPGgdlteigergvNISGGQKQRVSMARAVYSNSDVYIFDD 766
|
....*.
gi 488289759 160 ATSSLD 165
Cdd:PLN03130 767 PLSALD 772
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1-214 |
3.41e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 59.36 E-value: 3.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQEThaLKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKE-------- 72
Cdd:PRK10982 250 ILEVRNLTSLRQPS--IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEainhgfal 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 73 VRQQQQQMGMVFQ---HYN-LLENLKIYDNvalPLKLLKEKqpeKIERLLTFV--DMAHKAEAYPAQ---LSGGEKQRVS 143
Cdd:PRK10982 328 VTEERRSTGIYAYldiGFNsLISNIRNYKN---KVGLLDNS---RMKSDTQWVidSMRVKTPGHRTQigsLSGGNQQKVI 401
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488289759 144 IARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLIG 214
Cdd:PRK10982 402 IGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDK-GIIIISSEMPELLGITDRILVMSNGLVAG 471
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
17-211 |
2.91e-09 |
|
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: 56.02 E-value: 2.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRnvQTFSKK------EVRQQQQQMGMVFQHYNLL 90
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--ISFSSQfswimpGTIKENIIFGVSYDEYRYK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 91 ENLKiydnvALPLKLLKEKQPEKIERLLtfvdmahkAEAyPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLD----E 166
Cdd:cd03291 131 SVVK-----ACQLEEDITKFPEKDNTVL--------GEG-GITLSGGQRARISLARAVYKDADLYLLDSPFGYLDvfteK 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488289759 167 ENTESVVRLLHKTHqefrpTIFFVSHELETVKRlCNRILVMEKGQ 211
Cdd:cd03291 197 EIFESCVCKLMANK-----TRILVTSKMEHLKK-ADKILILHEGS 235
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
17-213 |
4.29e-09 |
|
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: 55.30 E-value: 4.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVqtfSKKEVRQQQQQMGMVFQ---------HY 87
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDI---SKLPLHTLRSRLSIILQdpilfsgsiRF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 88 NLLENLKIYDNV---ALP---LKLLKEKQPEKIERLLTfvdmaHKAEAYpaqlSGGEKQRVSIARALSRNPKWLLCDEAT 161
Cdd:cd03288 114 NLDPECKCTDDRlweALEiaqLKNMVKSLPGGLDAVVT-----EGGENF----SVGQRQLFCLARAFVRKSSILIMDEAT 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488289759 162 SSLDEEnTESVVRLLHKTHQEFRpTIFFVSHELETVKRlCNRILVMEKGQLI 213
Cdd:cd03288 185 ASIDMA-TENILQKVVMTAFADR-TVVTIAHRVSTILD-ADLVLVLSRGILV 233
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-194 |
5.86e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 55.56 E-value: 5.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 27 GEIVGIVGKSGSGKSTLLRLL---------NLMEQPSEGEI--RIDGRNVQTF----SKKEVR-----QQQQQMGMVFQH 86
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILsgelkpnlgDYDEEPSWDEVlkRFRGTELQDYfkklANGEIKvahkpQYVDLIPKVFKG 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 87 yNLLENLKIYDNvalplkllKEKQPEKIERLltfvDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDE 166
Cdd:COG1245 179 -TVRELLEKVDE--------RGKLDELAEKL----GLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI 245
|
170 180
....*....|....*....|....*...
gi 488289759 167 ENTESVVRLLHKTHQEFRPtIFFVSHEL 194
Cdd:COG1245 246 YQRLNVARLIRELAEEGKY-VLVVEHDL 272
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
18-193 |
6.12e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 55.64 E-value: 6.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 18 KNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIridgrnvqtFSKKEVRqqqqqMGMVFQHYnlLENLKIYD 97
Cdd:PLN03073 526 KNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV---------FRSAKVR-----MAVFSQHH--VDGLDLSS 589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 98 NVALPLKLLKEKQPEKIER--LLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTESVVRL 175
Cdd:PLN03073 590 NPLLYMMRCFPGVPEQKLRahLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQG 669
|
170
....*....|....*...
gi 488289759 176 LhkthQEFRPTIFFVSHE 193
Cdd:PLN03073 670 L----VLFQGGVLMVSHD 683
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
14-210 |
6.75e-09 |
|
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: 55.69 E-value: 6.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 14 THALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRnvQTFSKKE------VRQQQQQMGMVFQHY 87
Cdd:TIGR01271 439 TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR--ISFSPQTswimpgTIKDNIIFGLSYDEY 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 88 NLLENLKiydnvALPLKLLKEKQPEKIERLLTFVDMAhkaeaypaqLSGGEKQRVSIARALSRNPKWLLCDEATSSLD-- 165
Cdd:TIGR01271 517 RYTSVIK-----ACQLEEDIALFPEKDKTVLGEGGIT---------LSGGQRARISLARAVYKDADLYLLDSPFTHLDvv 582
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488289759 166 --EENTESVVRLLHKTHqefrpTIFFVSHELETVKRlCNRILVMEKG 210
Cdd:TIGR01271 583 teKEIFESCLCKLMSNK-----TRILVTSKLEHLKK-ADKILLLHEG 623
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
17-179 |
9.01e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.50 E-value: 9.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLN---LMEQPSEGEIRIDGRNVQ-TFSKKEVRQQQQQMGMvfQHYNLLEN 92
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLAervTTGVITGGDRLVNGRPLDsSFQRSIGYVQQQDLHL--PTSTVRES 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 93 LKIYDNVALPLKLLKEKQPEKIERLLTFVDMAHKAEAY---PAQ-LSGGEKQRVSIARALSRNPKWLL-CDEATSSLDEE 167
Cdd:TIGR00956 857 LRFSAYLRQPKSVSKSEKMEYVEEVIKLLEMESYADAVvgvPGEgLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQ 936
|
170
....*....|..
gi 488289759 168 NTESVVRLLHKT 179
Cdd:TIGR00956 937 TAWSICKLMRKL 948
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-200 |
9.25e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 55.37 E-value: 9.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLnLMEQPSEGEIRIDGRNVQTFSKkevrqqqqQMGMVFqhynlleNLKIY 96
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAM-LGELSHAETSSVVIRGSVAYVP--------QVSWIF-------NATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 97 DNVALPLKLlkekQPEKIERLLTFVDMAHKAEAYPAQ-----------LSGGEKQRVSIARALSRNPKWLLCDEATSSLD 165
Cdd:PLN03232 697 ENILFGSDF----ESERYWRAIDVTALQHDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
170 180 190
....*....|....*....|....*....|....*
gi 488289759 166 EentesvvrllHKTHQEFRPTIffvSHELETVKRL 200
Cdd:PLN03232 773 A----------HVAHQVFDSCM---KDELKGKTRV 794
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
17-215 |
1.07e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 54.45 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLL--NLMEQPS------EGEIRIDGRNV------QTFSKKEVRQQQQQMGM 82
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALagDLTGGGAprgarvTGDVTLNGEPLaaidapRLARLRAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 83 VFQHYNLLeNLKIYDNvALPLKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALS---------RNPK 153
Cdd:PRK13547 97 AFSAREIV-LLGRYPH-ARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAqlwpphdaaQPPR 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488289759 154 WLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIGE 215
Cdd:PRK13547 175 YLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAH 236
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-165 |
1.75e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 54.36 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVqtfSKKEVRQQQ---- 77
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDM---ADARHRRAVcpri 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 78 ----QQMGMvfqhyNLLENLKIYDNVALPLKLLKEKQPE---KIERLLTFVDMAHKAEAyPA-QLSGGEKQRVSIARALS 149
Cdd:NF033858 79 aympQGLGK-----NLYPTLSVFENLDFFGRLFGQDAAErrrRIDELLRATGLAPFADR-PAgKLSGGMKQKLGLCCALI 152
|
170
....*....|....*.
gi 488289759 150 RNPKWLLCDEATSSLD 165
Cdd:NF033858 153 HDPDLLILDEPTTGVD 168
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-165 |
1.96e-08 |
|
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: 54.57 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLR-LLNLMEQpSEGEIRIDGrnvqtfSKKEVRQQQqqmgmvfqhynLLENLKI 95
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDK-VEGHVHMKG------SVAYVPQQA-----------WIQNDSL 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 96 YDNVALPLKLLKEKQPEKIERLLTFVDMahkaEAYPA-----------QLSGGEKQRVSIARALSRNPKWLLCDEATSSL 164
Cdd:TIGR00957 716 RENILFGKALNEKYYQQVLEACALLPDL----EILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAV 791
|
.
gi 488289759 165 D 165
Cdd:TIGR00957 792 D 792
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
29-176 |
2.37e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 52.57 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 29 IVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQQQQMGMVFQhYNLLENLK----IYDNValplk 104
Cdd:PRK13541 28 ITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIGHNLGLKLE-MTVFENLKfwseIYNSA----- 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488289759 105 llkekqpEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTESVVRLL 176
Cdd:PRK13541 102 -------ETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLI 166
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-165 |
5.40e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.89 E-value: 5.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 27 GEIVGIVGKSGSGKSTLLRLL---------NLMEQPSEGEI--RIDGRNVQTF----SKKEVR-----QQQQQMGMVFQH 86
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILsgelipnlgDYEEEPSWDEVlkRFRGTELQNYfkklYNGEIKvvhkpQYVDLIPKVFKG 178
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488289759 87 yNLLENLKIYDNvalplkllKEKQPEKIERLltfvDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLD 165
Cdd:PRK13409 179 -KVRELLKKVDE--------RGKLDEVVERL----GLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
7-193 |
1.06e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.09 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 7 VSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIdgrnvqtfsKKEVRqqqqqMGMVFQH 86
Cdd:PRK10636 318 VSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL---------AKGIK-----LGYFAQH 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 87 YnlLENLKIYDNvalPLKLLKEKQPEKIERLLT-----FVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEAT 161
Cdd:PRK10636 384 Q--LEFLRADES---PLQHLARLAPQELEQKLRdylggFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPT 458
|
170 180 190
....*....|....*....|....*....|..
gi 488289759 162 SSLDEENTESVVRLLhkthQEFRPTIFFVSHE 193
Cdd:PRK10636 459 NHLDLDMRQALTEAL----IDFEGALVVVSHD 486
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-213 |
1.40e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 50.80 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLlnLMEQPS----EGEIRIDGRNVQTFSKKEvrqq 76
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKV--IAGHPAykilEGDILFKGESILDLEPEE---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 77 QQQMG--MVFQH------YNLLENLKIYDNVALPLKLLKEKQP----EKIERLLTFVDMAHK------AEAYpaqlSGGE 138
Cdd:CHL00131 81 RAHLGifLAFQYpieipgVSNADFLRLAYNSKRKFQGLPELDPleflEIINEKLKLVGMDPSflsrnvNEGF----SGGE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 139 KQRVSIARALSRNPKWLLCDEATSSLD----EENTESVVRLLHKTHqefrpTIFFVSHeletVKRLCNRIL-----VMEK 209
Cdd:CHL00131 157 KKRNEILQMALLDSELAILDETDSGLDidalKIIAEGINKLMTSEN-----SIILITH----YQRLLDYIKpdyvhVMQN 227
|
....
gi 488289759 210 GQLI 213
Cdd:CHL00131 228 GKII 231
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-180 |
2.78e-07 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 49.62 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVsKVYQETHalkNIHFSvqlGEIVGIVGKSGSGKSTLLRLLNL---MEQPSEGEIRIDGRNVQ--------TFSK 70
Cdd:COG0419 5 LRLENF-RSYRDTE---TIDFD---DGLNLIVGPNGAGKSTILEAIRYalyGKARSRSKLRSDLINVGseeasvelEFEH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 71 KE-----VRQQQQQMGMVFQHYNLLE-------NLKIYDNVALPLKLLKEKQPEKIERLLTFVDMAHKAEAY------PA 132
Cdd:COG0419 78 GGkryriERRQGEFAEFLEAKPSERKealkrllGLEIYEELKERLKELEEALESALEELAELQKLKQEILAQlsgldpIE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488289759 133 QLSGGEKQRVSIARALSrnpkwLLCDeaTSSLDEENTESVVRLLHK----TH 180
Cdd:COG0419 158 TLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEElaiiTH 202
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
5-211 |
3.42e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 48.86 E-value: 3.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 5 VNVSKVYQetHALKNIHFSVQLGEIVGIVGKSGSGKSTLLrllnLMEQPSEGEIRIDGrNVQTFSKkevrqqqQQMGMVF 84
Cdd:cd03238 1 LTVSGANV--HNLQNLDVSIPLNVLVVVTGVSGSGKSTLV----NEGLYASGKARLIS-FLPKFSR-------NKLIFID 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 85 QHYNLLENLKIYdnvaLPLkllkekqpekiERLLtfvdmahkaeaypAQLSGGEKQRVSIARALSRNPK--WLLCDEATS 162
Cdd:cd03238 67 QLQFLIDVGLGY----LTL-----------GQKL-------------STLSGGELQRVKLASELFSEPPgtLFILDEPST 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488289759 163 SLDEENT----ESVVRLLHKTHqefrpTIFFVSHELETVKRlCNRILVMEKGQ 211
Cdd:cd03238 119 GLHQQDInqllEVIKGLIDLGN-----TVILIEHNLDVLSS-ADWIIDFGPGS 165
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-174 |
3.88e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.55 E-value: 3.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLRllNLMeqpSEGEIRiDGRNVQTFSKKEVRQQQQQMgmvfqhynlleNLKIY 96
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQ--SLL---SQFEIS-EGRVWAERSIAYVPQQAWIM-----------NATVR 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 97 DNVALplkllkeKQPEKIERLLTFVDMAhKAEAYPAQL---------------SGGEKQRVSIARALSRNPKWLLCDEAT 161
Cdd:PTZ00243 739 GNILF-------FDEEDAARLADAVRVS-QLEADLAQLgggleteigekgvnlSGGQKARVSLARAVYANRDVYLLDDPL 810
|
170
....*....|...
gi 488289759 162 SSLDEENTESVVR 174
Cdd:PTZ00243 811 SALDAHVGERVVE 823
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-193 |
6.11e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.56 E-value: 6.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 3 ELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDgrnvqtfSKKEVrqqqqqmgM 82
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG-------TKLEV--------A 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 83 VF-QHYNLLENLK-IYDNVAlplkllKEKQPEKI---ER-----LLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNP 152
Cdd:PRK11147 386 YFdQHRAELDPEKtVMDNLA------EGKQEVMVngrPRhvlgyLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPS 459
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488289759 153 KWLLCDEATSSLDEENTEsvvrLLHKTHQEFRPTIFFVSHE 193
Cdd:PRK11147 460 NLLILDEPTNDLDVETLE----LLEELLDSYQGTVLLVSHD 496
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
134-192 |
5.75e-06 |
|
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: 46.67 E-value: 5.75e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 488289759 134 LSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTESVVRLLhkthQEFRPTIFFVSH 192
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLC----REFGITLFSVSH 637
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
10-216 |
6.13e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 46.71 E-value: 6.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 10 VYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLlrllnLME-------QPSEGEIRIDGRNVQTFSKKE--------VR 74
Cdd:NF040905 269 LHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTEL-----AMSvfgrsygRNISGTVFKDGKEVDVSTVSDaidaglayVT 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 75 QQQQQMGMvfqhyNLLENLKiyDNVALP-LKLLKEKqpekierllTFVDmAHK----AEAYPA--------------QLS 135
Cdd:NF040905 344 EDRKGYGL-----NLIDDIK--RNITLAnLGKVSRR---------GVID-ENEeikvAEEYRKkmniktpsvfqkvgNLS 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 136 GGEKQRVSIARALSRNPKWLLCDEATSSLD-----EENTesVVRLLHKTHQefrpTIFFVSHELETVKRLCNRILVMEKG 210
Cdd:NF040905 407 GGNQQKVVLSKWLFTDPDVLILDEPTRGIDvgakyEIYT--IINELAAEGK----GVIVISSELPELLGMCDRIYVMNEG 480
|
....*.
gi 488289759 211 QLIGEF 216
Cdd:NF040905 481 RITGEL 486
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
17-213 |
6.34e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 46.64 E-value: 6.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNL----MEQPSEGEIRIDGrnvqtFSKKEVRQQQQ-------QMGMVFQ 85
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASntdgFHIGVEGVITYDG-----ITPEEIKKHYRgdvvynaETDVHFP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 86 HYNLLENLkiyDNVALplklLKEKQ--PEKIERLltfVDMAHKAEAYPAQL------------------SGGEKQRVSIA 145
Cdd:TIGR00956 152 HLTVGETL---DFAAR----CKTPQnrPDGVSRE---EYAKHIADVYMATYglshtrntkvgndfvrgvSGGERKRVSIA 221
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 146 RALSRNPKWLLCDEATSSLDEENTESVVRLLhKTHQEFRPTIFFVS--HELETVKRLCNRILVMEKGQLI 213
Cdd:TIGR00956 222 EASLGGAKIQCWDNATRGLDSATALEFIRAL-KTSANILDTTPLVAiyQCSQDAYELFDKVIVLYEGYQI 290
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
14-198 |
1.44e-05 |
|
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: 44.56 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 14 THALKNIHFSVQLGEIVGIVGKSGSGKSTLL---------------------RLLNLMEQPS----EG---EIRIDgrnv 65
Cdd:cd03270 8 EHNLKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKPDvdsiEGlspAIAID---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 66 QTFSKKEVRqqqQQMGMVFQHYNLLENLkiYDNVALplkllkekqpekIERL-------LTFVDMAHKAEAypaqLSGGE 138
Cdd:cd03270 84 QKTTSRNPR---STVGTVTEIYDYLRLL--FARVGI------------RERLgflvdvgLGYLTLSRSAPT----LSGGE 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488289759 139 KQRVSIARALSRNPKWLL--CDEATSSLDEENTESVVRLLHKThQEFRPTIFFVSHELETVK 198
Cdd:cd03270 143 AQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDTIR 203
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
14-217 |
1.72e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.59 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 14 THALKNIHFSVQLGEIVGIVGKSGSGKSTLLR------LLNLMEQPSEGEIRIDG----------RNVQTFSKK------ 71
Cdd:PRK00635 608 KHNLKDLTISLPLGRLTVVTGVSGSGKSSLINdtlvpaVEEFIEQGFCSNLSIQWgaisrlvhitRDLPGRSQRsiplty 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 72 -----EVRQ---QQ---QQMGMVFQHYNL------------LENLKIYDN---VALPLKLLKEKQPEKIE------RLLT 119
Cdd:PRK00635 688 ikafdDLRElfaEQprsKRLGLTKSHFSFntplgacaecqgLGSITTTDNrtsIPCPSCLGKRFLPQVLEvrykgkNIAD 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 120 FVDM-AHKAEAY----P-----------------------AQLSGGEKQRVSIARAL---SRNPKWLLCDEATSSLDEEN 168
Cdd:PRK00635 768 ILEMtAYEAEKFfldePsihekihalcslgldylplgrplSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHD 847
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 488289759 169 TESVVRLLHK-THQEFrpTIFFVSHELETVKrLCNRILVM--EKGQLIGEFL 217
Cdd:PRK00635 848 IKALIYVLQSlTHQGH--TVVIIEHNMHVVK-VADYVLELgpEGGNLGGYLL 896
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
32-200 |
2.10e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 44.14 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 32 IVGKSGSGKSTLLRLLNLM---EQPSEGEIRIDGRNVqtFSKKEVRqqqQQMGMVFQH-----YNLLENLKIYDNVALPl 103
Cdd:cd03240 27 IVGQNGAGKTTIIEALKYAltgELPPNSKGGAHDPKL--IREGEVR---AQVKLAFENangkkYTITRSLAILENVIFC- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 104 kllkeKQpEKIERLLtfVDMahkaeayPAQLSGGEKQ------RVSIARALSRNPKWLLCDEATSSLDEEN-TESVVRLL 176
Cdd:cd03240 101 -----HQ-GESNWPL--LDM-------RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENiEESLAEII 165
|
170 180
....*....|....*....|....
gi 488289759 177 HKTHQEFRPTIFFVSHELETVKRL 200
Cdd:cd03240 166 EERKSQKNFQLIVITHDEELVDAA 189
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
17-179 |
2.79e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.84 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPS--EGEIRIDG--RNVQTFSKkeVRQQQQQMGMVFQHYNLLEN 92
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGfpKKQETFAR--ISGYCEQNDIHSPQVTVRES 973
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 93 LKIYDNVALPLKLLKEKQPEKIERLLTFVDMAHKAEA---YPA--QLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEE 167
Cdd:PLN03140 974 LIYSAFLRLPKEVSKEEKMMFVDEVMELVELDNLKDAivgLPGvtGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDAR 1053
|
170
....*....|..
gi 488289759 168 NTESVVRLLHKT 179
Cdd:PLN03140 1054 AAAIVMRTVRNT 1065
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
27-214 |
3.88e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.47 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 27 GEIVGIVGKSGSGKSTLLRLLNL--------------MEQPSEGE--------IRIDGRNVQTFsKKEVRQQQQQMGMVF 84
Cdd:PLN03073 203 GRHYGLVGRNGTGKTTFLRYMAMhaidgipkncqilhVEQEVVGDdttalqcvLNTDIERTQLL-EEEAQLVAQQRELEF 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 85 QHYNLLENLKIYDNVAlplKLLKEKQPEKIERLLTFVDmAHKAEAYPA------------------QLSGGEKQRVSIAR 146
Cdd:PLN03073 282 ETETGKGKGANKDGVD---KDAVSQRLEEIYKRLELID-AYTAEARAAsilaglsftpemqvkatkTFSGGWRMRIALAR 357
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488289759 147 ALSRNPKWLLCDEATSSLDEEntesVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIG 214
Cdd:PLN03073 358 ALFIEPDLLLLDEPTNHLDLH----AVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKLVT 421
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
32-200 |
4.08e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 42.73 E-value: 4.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 32 IVGKSGSGKSTLLRLLNLMEqpsegeiridgrnvqtfskkevrqqqqqmGMVFQHYNLLENLKIYDNVALplkllkekqp 111
Cdd:cd03227 26 ITGPNGSGKSTILDAIGLAL-----------------------------GGAQSATRRRSGVKAGCIVAA---------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 112 EKIERLLTFVdmahkaeaypaQLSGGEKQRVSIARAL---SRNPKWLLC-DEATSSLDEENTESVVRLLHKTHQEFRpTI 187
Cdd:cd03227 67 VSAELIFTRL-----------QLSGGEKELSALALILalaSLKPRPLYIlDEIDRGLDPRDGQALAEAILEHLVKGA-QV 134
|
170
....*....|...
gi 488289759 188 FFVSHELETVKRL 200
Cdd:cd03227 135 IVITHLPELAELA 147
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-165 |
5.77e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 43.24 E-value: 5.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLME--QPSEGEIRIDGRNVQTFSKKEvrQQQQ 78
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPED--RAGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 79 QMGMVFQHYNLLENL--KIYDNVALPlKLLKEKQPEKIERlLTFVD-MAHKAE--AYPAQL---------SGGEKQRVSI 144
Cdd:PRK09580 79 GIFMAFQYPVEIPGVsnQFFLQTALN-AVRSYRGQEPLDR-FDFQDlMEEKIAllKMPEDLltrsvnvgfSGGEKKRNDI 156
|
170 180
....*....|....*....|.
gi 488289759 145 ARALSRNPKWLLCDEATSSLD 165
Cdd:PRK09580 157 LQMAVLEPELCILDESDSGLD 177
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-195 |
1.42e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.31 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLlnlmeqpsegeirIDGRNVQTFSKKEV---RQQ-- 76
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSL-------------ITGDHPQGYSNDLTlfgRRRgs 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 77 -------QQQMGMVFQHYNL----------------LENLKIYDNVAlplkllkEKQPEKIERLLTFVDM-AHKAEAYPA 132
Cdd:PRK10938 328 getiwdiKKHIGYVSSSLHLdyrvstsvrnvilsgfFDSIGIYQAVS-------DRQQKLAQQWLDILGIdKRTADAPFH 400
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488289759 133 QLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELE 195
Cdd:PRK10938 401 SLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAE 463
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
132-178 |
1.53e-04 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 39.53 E-value: 1.53e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 132 AQLSGGEKQR---VSIARALS--------RNPKWLLC--DEATSSLDEENTESVVRLLHK 178
Cdd:pfam13558 31 GGLSGGEKQLlayLPLAAALAaqygsaegRPPAPRLVflDEAFAKLDEENIRTALELLRA 90
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
15-198 |
2.27e-04 |
|
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: 41.45 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 15 HALKNIHFSVQLGEIVGIVGKSGSGKSTLL---------RLLNL-MEQPSEGE-----------IRID----GR----NV 65
Cdd:cd03271 9 NNLKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlypalaRRLHLkKEQPGNHDrieglehidkvIVIDqspiGRtprsNP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 66 QTFSK--KEVRQqqqqmgmVF------QHYN--LLE----NLKIYDNVALPLK---LLKEKQPEKIERLLTFVD--MAHK 126
Cdd:cd03271 89 ATYTGvfDEIRE-------LFcevckgKRYNreTLEvrykGKSIADVLDMTVEealEFFENIPKIARKLQTLCDvgLGYI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488289759 127 AEAYPA-QLSGGEKQRVSIARALSRNPK----WLLcDEATSSLdeeNTESVVRLLHKTHQ--EFRPTIFFVSHELETVK 198
Cdd:cd03271 162 KLGQPAtTLSGGEAQRIKLAKELSKRSTgktlYIL-DEPTTGL---HFHDVKKLLEVLQRlvDKGNTVVVIEHNLDVIK 236
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
1-44 |
2.42e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.98 E-value: 2.42e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 488289759 1 MIELVNVSKvyqetHALKNIHFSVQLGEIVGIVGKSGSGKSTLL 44
Cdd:PRK00349 614 FLKLKGARE-----NNLKNVDVEIPLGKFTCVTGVSGSGKSTLI 652
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
1-44 |
2.52e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.92 E-value: 2.52e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 488289759 1 MIELVNVSKvyqetHALKNIHFSVQLGEIVGIVGKSGSGKSTLL 44
Cdd:TIGR00630 613 FLTLKGARE-----NNLKNITVSIPLGLFTCITGVSGSGKSTLI 651
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
20-211 |
3.00e-04 |
|
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: 40.72 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 20 IHFS-VQLGEIVGIVGKSGSGKSTLLrllNLMEQPSEGEIRIDGRNVQTFS-----KKEVR-----QQQQQMGMVFQHYN 88
Cdd:cd03279 20 IDFTgLDNNGLFLICGPTGAGKSTIL---DAITYALYGKTPRYGRQENLRSvfapgEDTAEvsftfQLGGKKYRVERSRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 89 LleNLKIYDNVA-LPlkllkekQPEkIERLLTfvdmahkaEAYpAQLSGGEKQRVSIARALS----------RNPKWLLC 157
Cdd:cd03279 97 L--DYDQFTRIVlLP-------QGE-FDRFLA--------RPV-STLSGGETFLASLSLALAlsevlqnrggARLEALFI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488289759 158 DEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQ 211
Cdd:cd03279 158 DEGFGTLDPEALEAVATALELIRTENR-MVGVISHVEELKERIPQRLEVIKTPG 210
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
17-224 |
3.28e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 41.31 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLnlmeqpsEGEIRIDGRNV---QTFSKKEVRQQQQQMGMVFQHYnLLENL 93
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALL-------KNEISADGGSYtfpGNWQLAWVNQETPALPQPALEY-VIDGD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 94 KIYDNVALPLKLLKEKQP--------------------EKIERLLTFVDMAHKAEAYPAQ-LSGGEKQRVSIARALSRNP 152
Cdd:PRK10636 89 REYRQLEAQLHDANERNDghaiatihgkldaidawtirSRAASLLHGLGFSNEQLERPVSdFSGGWRMRLNLAQALICRS 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488289759 153 KWLLCDEATSSLDEEntesVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKgQLIGEFLNNPQQYE 224
Cdd:PRK10636 169 DLLLLDEPTNHLDLD----AVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQ-QSLFEYTGNYSSFE 235
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
91-215 |
5.36e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 40.49 E-value: 5.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 91 ENLKIydnVALPLKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTE 170
Cdd:NF000106 105 ENLYM---IGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRN 181
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 488289759 171 SVVRLLHKTHQEfRPTIFFVSHELETVKRLCNRILVMEKGQLIGE 215
Cdd:NF000106 182 EVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIAD 225
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
1-43 |
4.73e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.08 E-value: 4.73e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 488289759 1 MIELVNVSKvyqetHALKNIHFSVQLGEIVGIVGKSGSGKSTL 43
Cdd:COG0178 610 FLTIKGARE-----NNLKNVDVEIPLGVLTCVTGVSGSGKSTL 647
|
|
| MobB |
pfam03205 |
Molybdopterin guanine dinucleotide synthesis protein B; This protein contains a P-loop. |
29-47 |
5.23e-03 |
|
Molybdopterin guanine dinucleotide synthesis protein B; This protein contains a P-loop.
Pssm-ID: 427196 [Multi-domain] Cd Length: 133 Bit Score: 35.99 E-value: 5.23e-03
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
14-43 |
5.92e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 37.69 E-value: 5.92e-03
10 20 30
....*....|....*....|....*....|
gi 488289759 14 THALKNIHFSVQLGEIVGIVGKSGSGKSTL 43
Cdd:TIGR00630 9 EHNLKNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
|