|
Name |
Accession |
Description |
Interval |
E-value |
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-255 |
1.08e-131 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 372.85 E-value: 1.08e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 4 AIHVQGLNKTF-SHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDRsngGQVQVLGREVQSSGRlnGQVR 82
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTS---GEILVDGQDVTALRG--RALR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 83 RLRADIGYIFQQFNLVNRLSVLDNVLLGCLGRMPRWRGSLALFNREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVA 162
Cdd:COG3638 77 RLRRRIGMIFQQFNLVPRLSVLTNVLAGRLGRTSTWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 163 IARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGLAQDLSK 242
Cdd:COG3638 157 IARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAELTD 236
|
250
....*....|...
gi 492088662 243 QFLNDLYGADADA 255
Cdd:COG3638 237 AVLREIYGGEAEE 249
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-249 |
1.66e-111 |
|
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: 321.44 E-value: 1.66e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSH-KSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQSSGRLNgqVRR 83
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLV---EPTSGSVLIDGTDINKLKGKA--LRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 84 LRADIGYIFQQFNLVNRLSVLDNVLLGCLGRMPRWRGSLALFNREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAI 163
Cdd:cd03256 76 LRRQIGMIFQQFNLIERLSVLENVLSGRLGRRSTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 164 ARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGLAQDLSKQ 243
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDE 235
|
....*.
gi 492088662 244 FLNDLY 249
Cdd:cd03256 236 VLDEIY 241
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-249 |
2.24e-110 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 319.65 E-value: 2.24e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 1 MNDAIHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDRSNGGQVQVLGREVQSSGRLNGQ 80
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIELLGRTVQREGRLARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 81 VRRLRADIGYIFQQFNLVNRLSVLDNVLLGCLGRMPRWRGSLALFNREEKQRAMAALDRVGLADLATQRASTLSGGQQQR 160
Cdd:PRK09984 81 IRKSRANTGYIFQQFNLVNRLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 161 VAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGLAQDL 240
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF 240
|
....*....
gi 492088662 241 SKQFLNDLY 249
Cdd:PRK09984 241 DNERFDHLY 249
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
5-250 |
3.59e-105 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 305.38 E-value: 3.59e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSH-KSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVqssGRLNGQ-VR 82
Cdd:TIGR02315 2 LEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLV---EPSSGSILLEGTDI---TKLRGKkLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 83 RLRADIGYIFQQFNLVNRLSVLDNVLLGCLGRMPRWRGSLALFNREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVA 162
Cdd:TIGR02315 76 KLRRRIGMIFQHYNLIERLTVLENVLHGRLGYKPTWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 163 IARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGLAQDLSK 242
Cdd:TIGR02315 156 IARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDD 235
|
....*...
gi 492088662 243 QFLNDLYG 250
Cdd:TIGR02315 236 EVLRHIYG 243
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-231 |
3.83e-81 |
|
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: 243.55 E-value: 3.83e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKS----ALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGREVQSSGrlNGQ 80
Cdd:cd03255 1 IELKNLSKTYGGGGekvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGL---DRPTSGEVRVDGTDISKLS--EKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 81 VRRLRAD-IGYIFQQFNLVNRLSVLDNVLLGCLGRmprwrgslALFNREEKQRAMAALDRVGLADLATQRASTLSGGQQQ 159
Cdd:cd03255 76 LAAFRRRhIGFVFQSFNLLPDLTALENVELPLLLA--------GVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492088662 160 RVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAvRYCPRAVALKGGRI 231
Cdd:cd03255 148 RVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-232 |
2.67e-80 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 241.49 E-value: 2.67e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 1 MNDAIHVQGLNKTFSHKS----ALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGREVQSSGR 76
Cdd:COG1136 1 MSPLLELRNLTKSYGTGEgevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGL---DRPTSGEVLIDGQDISSLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 77 lnGQVRRLRAD-IGYIFQQFNLVNRLSVLDNVLLGC-LGRMPRwrgslalfnREEKQRAMAALDRVGLADLATQRASTLS 154
Cdd:COG1136 78 --RELARLRRRhIGFVFQFFNLLPELTALENVALPLlLAGVSR---------KERRERARELLERVGLGDRLDHRPSQLS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492088662 155 GGQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAvRYCPRAVALKGGRIH 232
Cdd:COG1136 147 GGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELA-ARADRVIRLRDGRIV 223
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-254 |
8.98e-71 |
|
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: 218.37 E-value: 8.98e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 4 AIHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQSSGRlngqvRR 83
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLL---KPSSGEVLLDGRDLASLSR-----RE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 84 LRADIGYIFQQFNLVNRLSVLDNVLLGclgRMPrWRGSLALFNREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAI 163
Cdd:COG1120 73 LARRIAYVPQEPPAPFGLTVRELVALG---RYP-HLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 164 ARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGLAQD-LSK 242
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEvLTP 228
|
250
....*....|..
gi 492088662 243 QFLNDLYGADAD 254
Cdd:COG1120 229 ELLEEVYGVEAR 240
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-252 |
1.80e-68 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 212.26 E-value: 1.80e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 1 MNDAIHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVqssgrlngq 80
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLL---PPTSGTVRLFGKPP--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 81 vRRLRADIGYIFQQFNlVNR---LSVLDNVLLGCLGRMPRWRGslalFNREEKQRAMAALDRVGLADLATQRASTLSGGQ 157
Cdd:COG1121 71 -RRARRRIGYVPQRAE-VDWdfpITVRDVVLMGRYGRRGLFRR----PSRADREAVDEALERVGLEDLADRPIGELSGGQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 158 QQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRsDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGLA 237
Cdd:COG1121 145 QQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRR-EGKTILVVTHDLGAVREYFDRVLLLNRGLVAHGPPE 223
|
250
....*....|....*
gi 492088662 238 QDLSKQFLNDLYGAD 252
Cdd:COG1121 224 EVLTPENLSRAYGGP 238
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-246 |
3.27e-68 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 211.39 E-value: 3.27e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGREVQSSGRlngQVRRL 84
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLL---EEPDSGTITVDGEDLTDSKK---DINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 85 RADIGYIFQQFNLVNRLSVLDNVLLGclgrmPRW-RGslalFNREE-KQRAMAALDRVGLADLATQRASTLSGGQQQRVA 162
Cdd:COG1126 76 RRKVGMVFQQFNLFPHLTVLENVTLA-----PIKvKK----MSKAEaEERAMELLERVGLADKADAYPAQLSGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 163 IARALTQRAEVILADEPIASLDPESAR---RVMEILADinrsDGKT-VVVTlHQVDYAvrycpRAVA-----LKGGRIHF 233
Cdd:COG1126 147 IARALAMEPKVMLFDEPTSALDPELVGevlDVMRDLAK----EGMTmVVVT-HEMGFA-----REVAdrvvfMDGGRIVE 216
|
250 260
....*....|....*....|.
gi 492088662 234 DGLAQDL--------SKQFLN 246
Cdd:COG1126 217 EGPPEEFfenpqherTRAFLS 237
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-265 |
4.67e-67 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 208.38 E-value: 4.67e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQSsgrlngQVRRL 84
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLL---RPTSGEVRVLGEDVAR------DPAEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 85 RADIGYIFQQFNLVNRLSVLDNV-LLGCLGRMPRwrgslalfnREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAI 163
Cdd:COG1131 72 RRRIGYVPQEPALYPDLTVRENLrFFARLYGLPR---------KEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 164 ARALTQRAEVILADEPIASLDPESARRVMEILADINRsDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGLAQDLSKQ 243
Cdd:COG1131 143 ALALLHDPELLILDEPTSGLDPEARRELWELLRELAA-EGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
250 260
....*....|....*....|..
gi 492088662 244 FLNDLYgadadasLMITERSRR 265
Cdd:COG1131 222 LLEDVF-------LELTGEEAR 236
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-235 |
1.14e-65 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 204.13 E-value: 1.14e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSH-KSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGREVqssGRL-NGQVR 82
Cdd:COG2884 2 IRFENVSKRYPGgREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGE---ERPTSGQVLVNGQDL---SRLkRREIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 83 RLRADIGYIFQQFNLVNRLSVLDNVLLG--CLGrMPRwrgslalfnREEKQRAMAALDRVGLADLATQRASTLSGGQQQR 160
Cdd:COG2884 76 YLRRRIGVVFQDFRLLPDRTVYENVALPlrVTG-KSR---------KEIRRRVREVLDLVGLSDKAKALPHELSGGEQQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492088662 161 VAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSdGKTVVVTLHqvDYA-VRYCP-RAVALKGGRIHFDG 235
Cdd:COG2884 146 VAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATH--DLElVDRMPkRVLELEDGRLVRDE 219
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-231 |
4.43e-63 |
|
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: 197.37 E-value: 4.43e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGREVQSSGRlngQVRRL 84
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLL---EEPDSGTIIIDGLKLTDDKK---NINEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 85 RADIGYIFQQFNLVNRLSVLDNVLLGclgrmPRWRgsLALFNREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAIA 164
Cdd:cd03262 75 RQKVGMVFQQFNLFPHLTVLENITLA-----PIKV--KGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492088662 165 RALTQRAEVILADEPIASLDPESARRVMEILADINRSdGKTVVVTLHQVDYAVRYCPRAVALKGGRI 231
Cdd:cd03262 148 RALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-240 |
3.10e-61 |
|
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: 193.32 E-value: 3.10e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLnkTFSH---KSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDRsngGQVQVLGREVQSSgrlngQV 81
Cdd:COG1122 1 IELENL--SFSYpggTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTS---GEVLVDGKDITKK-----NL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 82 RRLRADIGYIFQ----QfnLVNRlSVLDNVLLGclgrmPRWRGslalFNREE-KQRAMAALDRVGLADLATQRASTLSGG 156
Cdd:COG1122 71 RELRRKVGLVFQnpddQ--LFAP-TVEEDVAFG-----PENLG----LPREEiRERVEEALELVGLEHLADRPPHELSGG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 157 QQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSdGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGL 236
Cdd:COG1122 139 QKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGT 217
|
....
gi 492088662 237 AQDL 240
Cdd:COG1122 218 PREV 221
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
4-232 |
5.30e-60 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 191.07 E-value: 5.30e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 4 AIHVQGLNKTFSHKS----ALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGREVqssgrlng 79
Cdd:COG1116 7 ALELRGVSKRFPTGGggvtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGL---EKPTSGEVLVDGKPV-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 80 qvRRLRADIGYIFQQFNLVNRLSVLDNVLLGC-LGRMPRwrgslalfnREEKQRAMAALDRVGLADLATQRASTLSGGQQ 158
Cdd:COG1116 76 --TGPGPDRGVVFQEPALLPWLTVLDNVALGLeLRGVPK---------AERRERARELLELVGLAGFEDAYPHQLSGGMR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492088662 159 QRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVV-VTlHQVDYAVRYCPRAVALKG--GRIH 232
Cdd:COG1116 145 QRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLfVT-HDVDEAVFLADRVVVLSArpGRIV 220
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-230 |
3.68e-59 |
|
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: 186.24 E-value: 3.68e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGREVQssgRLNGQVRRL 84
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGL---EEPDSGSILIDGEDLT---DLEDELPPL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 85 RADIGYIFQQFNLVNRLSVLDNVLLGclgrmprwrgslalfnreekqramaaldrvgladlatqrastLSGGQQQRVAIA 164
Cdd:cd03229 75 RRRIGMVFQDFALFPHLTVLENIALG------------------------------------------LSGGQQQRVALA 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492088662 165 RALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGR 230
Cdd:cd03229 113 RALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-231 |
1.26e-57 |
|
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: 183.94 E-value: 1.26e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKS----ALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGREVQssgRLNG- 79
Cdd:cd03258 2 IELKNVSKVFGDTGgkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGL---ERPTSGSVLVDGTDLT---LLSGk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 80 QVRRLRADIGYIFQQFNLVNRLSVLDNVLLGC-LGRMPRwrgslalfnREEKQRAMAALDRVGLADLATQRASTLSGGQQ 158
Cdd:cd03258 76 ELRKARRRIGMIFQHFNLLSSRTVFENVALPLeIAGVPK---------AEIEERVLELLELVGLEDKADAYPAQLSGGQK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492088662 159 QRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRI 231
Cdd:cd03258 147 QRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-231 |
1.28e-57 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 187.59 E-value: 1.28e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKS----ALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGREVqssGRLNG- 79
Cdd:COG1135 2 IELENLSKTFPTKGgpvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLL---ERPTSGSVLVDGVDL---TALSEr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 80 QVRRLRADIGYIFQQFNLVNRLSVLDNVL--LGCLGrMPRwrgslalfnREEKQRAMAALDRVGLADLATQRASTLSGGQ 157
Cdd:COG1135 76 ELRAARRKIGMIFQHFNLLSSRTVAENVAlpLEIAG-VPK---------AEIRKRVAELLELVGLSDKADAYPSQLSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492088662 158 QQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRI 231
Cdd:COG1135 146 KQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-235 |
9.27e-57 |
|
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: 181.19 E-value: 9.27e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 6 HVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDRsngGQVQVLGREVqssgrlngqvRRLR 85
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTS---GSIRVFGKPL----------EKER 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 86 ADIGYIFQQFNlVNR---LSVLDNVLLGCLGRMPRWRGslalFNREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVA 162
Cdd:cd03235 68 KRIGYVPQRRS-IDRdfpISVRDVVLMGLYGHKGLFRR----LSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492088662 163 IARALTQRAEVILADEPIASLDPESARRVMEILADINRsDGKTVVVTLHQVDYAVRYCPRAVALKgGRIHFDG 235
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRR-EGMTILVVTHDLGLVLEYFDRVLLLN-RTVVASG 213
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-245 |
1.92e-56 |
|
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: 181.33 E-value: 1.92e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 1 MNDAIHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGREVQSSGRlnGQ 80
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGL---LRPDSGEILVDGQDITGLSE--KE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 81 VRRLRADIGYIFQQFNLVNRLSVLDNVLLGcL---GRMPRwrgslalfnREEKQRAMAALDRVGLADLATQRASTLSGGQ 157
Cdd:COG1127 77 LYELRRRIGMLFQGGALFDSLTVFENVAFP-LrehTDLSE---------AEIRELVLEKLELVGLPGAADKMPSELSGGM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 158 QQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGLA 237
Cdd:COG1127 147 RKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTP 226
|
250
....*....|....*
gi 492088662 238 QDLS-------KQFL 245
Cdd:COG1127 227 EELLasddpwvRQFL 241
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-238 |
1.02e-55 |
|
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: 179.17 E-value: 1.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 4 AIHVQGLNKTFSHKSALV----DLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGREVqssGRLNG 79
Cdd:COG4181 8 IIELRGLTKTVGTGAGELtilkGISLEVEAGESVAIVGASGSGKSTLLGLLAGL---DRPTSGTVRLAGQDL---FALDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 80 QVR-RLRAD-IGYIFQQFNLVNRLSVLDNVLLgclgrmPrwrgsLALFNREE-KQRAMAALDRVGLADLATQRASTLSGG 156
Cdd:COG4181 82 DARaRLRARhVGFVFQSFQLLPTLTALENVML------P-----LELAGRRDaRARARALLERVGLGHRLDHYPAQLSGG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 157 QQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRyCPRAVALKGGRIHFDGL 236
Cdd:COG4181 151 EQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTA 229
|
..
gi 492088662 237 AQ 238
Cdd:COG4181 230 AT 231
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
11-230 |
2.95e-55 |
|
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: 177.27 E-value: 2.95e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 11 NKTFSH----KSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGREVQSSgrlngQVRRLRA 86
Cdd:cd03225 4 NLSFSYpdgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGL---LGPTSGEVLVDGKDLTKL-----SLKELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 87 DIGYIFQQFN--LVNrLSVLDNVLLGCLGR-MPRwrgslalfnREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAI 163
Cdd:cd03225 76 KVGLVFQNPDdqFFG-PTVEEEVAFGLENLgLPE---------EEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492088662 164 ARALTQRAEVILADEPIASLDPESARRVMEILADINRsDGKTVVVTLHQVDYAVRYCPRAVALKGGR 230
Cdd:cd03225 146 AGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKA-EGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-231 |
3.33e-55 |
|
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: 177.28 E-value: 3.33e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKS----ALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGREVQSSGRlngq 80
Cdd:cd03293 1 LEVRNVSKTYGGGGgavtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGL---ERPTSGEVLVDGEPVTGPGP---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 81 vrrlraDIGYIFQQFNLVNRLSVLDNVLLGC-LGRMPRwrgslalfnREEKQRAMAALDRVGLADLATQRASTLSGGQQQ 159
Cdd:cd03293 74 ------DRGYVFQQDALLPWLTVLDNVALGLeLQGVPK---------AEARERAEELLELVGLSGFENAYPHQLSGGMRQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492088662 160 RVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVV-VTlHQVDYAVRYCPRAVALKG--GRI 231
Cdd:cd03293 139 RVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLlVT-HDIDEAVFLADRVVVLSArpGRI 212
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-231 |
1.54e-54 |
|
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: 175.40 E-value: 1.54e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGREVQSsgrlngqVRRL 84
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGL---ERPDSGEILIDGRDVTG-------VPPE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 85 RADIGYIFQQFNLVNRLSVLDNVLLGC-LGRMPRwrgslalfnREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAI 163
Cdd:cd03259 71 RRNIGMVFQDYALFPHLTVAENIAFGLkLRGVPK---------AEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492088662 164 ARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRI 231
Cdd:cd03259 142 ARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-240 |
1.24e-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: 181.64 E-value: 1.24e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKS-----ALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGREVqsSGRLNG 79
Cdd:COG1123 261 LEVRNLSKRYPVRGkggvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGL---LRPTSGSILFDGKDL--TKLSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 80 QVRRLRADIGYIFQ----QFNlvNRLSVLDNVLLGC--LGRMPRwrgslalfnREEKQRAMAALDRVGL-ADLATQRAST 152
Cdd:COG1123 336 SLRELRRRVQMVFQdpysSLN--PRMTVGDIIAEPLrlHGLLSR---------AERRERVAELLERVGLpPDLADRYPHE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 153 LSGGQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIH 232
Cdd:COG1123 405 LSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIV 484
|
....*...
gi 492088662 233 FDGLAQDL 240
Cdd:COG1123 485 EDGPTEEV 492
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
5-240 |
2.92e-52 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 170.66 E-value: 2.92e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDrsnGGQVQVLGREVQSSgrlNGQVRRL 84
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEIT---SGDLIVDGLKVNDP---KVDERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 85 RADIGYIFQQFNLVNRLSVLDNVLLGCLgrmpRWRGSlalfNREE-KQRAMAALDRVGLADLATQRASTLSGGQQQRVAI 163
Cdd:PRK09493 76 RQEAGMVFQQFYLFPHLTALENVMFGPL----RVRGA----SKEEaEKQARELLAKVGLAERAHHYPSELSGGQQQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 164 ARALTQRAEVILADEPIASLDPE---SARRVMEILADinrsDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGLAQDL 240
Cdd:PRK09493 148 ARALAVKPKLMLFDEPTSALDPElrhEVLKVMQDLAE----EGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVL 223
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-240 |
4.78e-52 |
|
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: 169.99 E-value: 4.78e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGREVQSSGRlnGQVRRL 84
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGL---LRPDSGEVLIDGEDISGLSE--AELYRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 85 RADIGYIFQQFNLVNRLSVLDNVLLgclgrmpRWRGSLALFNREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAIA 164
Cdd:cd03261 76 RRRMGMLFQSGALFDSLTVFENVAF-------PLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492088662 165 RALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGLAQDL 240
Cdd:cd03261 149 RALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-247 |
6.94e-52 |
|
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: 169.65 E-value: 6.94e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDRsngGQVQVLGREVQSsgrlngQVRRL 84
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDS---GSILIDGEDVRK------EPREA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 85 RADIGYIFQQFNLVNRLSVLDNV-LLGCLGRMPRwrgslalfnREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAI 163
Cdd:COG4555 73 RRQIGVLPDERGLYDRLTVRENIrYFAELYGLFD---------EELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVAL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 164 ARALTQRAEVILADEPIASLDPESARRVMEILADInRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGLAQDLSKQ 243
Cdd:COG4555 144 ARALVHDPKVLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
|
....
gi 492088662 244 FLND 247
Cdd:COG4555 223 IGEE 226
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
7-211 |
1.70e-51 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 167.41 E-value: 1.70e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 7 VQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGrevQSSGRLNGQVRR--L 84
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLL---EKFDSGQVYLNG---QETPPLNSKKASkfR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 85 RADIGYIFQQFNLVNRLSVLDNVLLGCLGRMprwrgslalFNREEKQRAM-AALDRVGLADLATQRASTLSGGQQQRVAI 163
Cdd:TIGR03608 75 REKLGYLFQNFALIENETVEENLDLGLKYKK---------LSKKEKREKKkEALEKVGLNLKLKQKIYELSGGEQQRVAL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 492088662 164 ARALTQRAEVILADEPIASLDPESARRVMEILADINRSdGKTVVVTLH 211
Cdd:TIGR03608 146 ARAILKPPPLILADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTH 192
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-235 |
2.84e-50 |
|
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: 163.38 E-value: 2.84e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 7 VQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQSSGRlngqvRRLRA 86
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLL---KPSSGEILLDGKDLASLSP-----KELAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 87 DIGYIFQqfnlvnrlsvldnvllgclgrmprwrgslalfnreekqramaALDRVGLADLATQRASTLSGGQQQRVAIARA 166
Cdd:cd03214 74 KIAYVPQ------------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARA 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492088662 167 LTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDG 235
Cdd:cd03214 112 LAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
7-239 |
4.53e-50 |
|
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: 164.92 E-value: 4.53e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 7 VQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDrsnGGQVQVLGREVqsSGRlnGQVRRLRA 86
Cdd:cd03219 3 VRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPT---SGSVLFDGEDI--TGL--PPHEIARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 87 DIGYIFQQFNLVNRLSVLDNVLLGCLGRMPRWRGSLALFNREEK--QRAMAALDRVGLADLATQRASTLSGGQQQRVAIA 164
Cdd:cd03219 76 GIGRTFQIPRLFPELTVLENVMVAAQARTGSGLLLARARREEREarERAEELLERVGLADLADRPAGELSYGQQRRLEIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492088662 165 RALTQRAEVILADEPIASLDPESARRVMEILADINRsDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGLAQD 239
Cdd:cd03219 156 RALATDPKLLLLDEPAAGLNPEETEELAELIRELRE-RGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDE 229
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-231 |
1.85e-49 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 166.51 E-value: 1.85e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKS----ALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGREVQSSGrlNGQ 80
Cdd:PRK11153 2 IELKNISKVFPQGGrtihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLL---ERPTSGRVLVDGQDLTALS--EKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 81 VRRLRADIGYIFQQFNLVNRLSVLDNVLLGC-LGRMPRwrgslalfnREEKQRAMAALDRVGLADLATQRASTLSGGQQQ 159
Cdd:PRK11153 77 LRKARRQIGMIFQHFNLLSSRTVFDNVALPLeLAGTPK---------AEIKARVTELLELVGLSDKADRYPAQLSGGQKQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492088662 160 RVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRI 231
Cdd:PRK11153 148 RVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-235 |
3.92e-48 |
|
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: 160.59 E-value: 3.92e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 1 MNDAIHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGREVqsSGRlnGQ 80
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGF---YRPTSGRILFDGRDI--TGL--PP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 81 VRRLRADIGYIFQQFNLVNRLSVLDNVLLGCLGRMPR--WRGSLALFN-----REEKQRAMAALDRVGLADLATQRASTL 153
Cdd:COG0411 74 HRIARLGIARTFQNPRLFPELTVLENVLVAAHARLGRglLAALLRLPRarreeREARERAEELLERVGLADRADEPAGNL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 154 SGGQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHF 233
Cdd:COG0411 154 SYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIA 233
|
..
gi 492088662 234 DG 235
Cdd:COG0411 234 EG 235
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-235 |
1.42e-47 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 159.54 E-value: 1.42e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 6 HVQGLNKTFSHKsALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQSSGRLNgqVRRLR 85
Cdd:TIGR04521 8 YIYQPGTPFEKK-ALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLL---KPTSGTVTIDGRDITAKKKKK--LKDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 86 ADIGYIFQQ-----FnlvnRLSVLDNVLLGclgrmPRWRGslalFNREE-KQRAMAALDRVGL-ADLATQRASTLSGGQQ 158
Cdd:TIGR04521 82 KKVGLVFQFpehqlF----EETVYKDIAFG-----PKNLG----LSEEEaEERVKEALELVGLdEEYLERSPFELSGGQM 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492088662 159 QRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDG 235
Cdd:TIGR04521 149 RRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDG 225
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
4-251 |
3.58e-47 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 157.99 E-value: 3.58e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 4 AIHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGREVQSSGRLNGQ--- 80
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLL---EQPEAGTIRVGDITIDTARSLSQQkgl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 81 VRRLRADIGYIFQQFNLVNRLSVLDNVLLG--CLGRMPRwrgslalfnREEKQRAMAALDRVGLADLATQRASTLSGGQQ 158
Cdd:PRK11264 80 IRQLRQHVGFVFQNFNLFPHRTVLENIIEGpvIVKGEPK---------EEATARARELLAKVGLAGKETSYPRRLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 159 QRVAIARALTQRAEVILADEPIASLDPEsarRVMEILADINR--SDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGL 236
Cdd:PRK11264 151 QRVAIARALAMRPEVILFDEPTSALDPE---LVGEVLNTIRQlaQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGP 227
|
250 260
....*....|....*....|...
gi 492088662 237 AQDL--------SKQFLNDLYGA 251
Cdd:PRK11264 228 AKALfadpqqprTRQFLEKFLLQ 250
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
5-231 |
4.01e-47 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 160.31 E-value: 4.01e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGREVQSsgrlNGQVRRL 84
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGL---ETPDSGRIVLNGRDLFT----NLPPRER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 85 RadIGYIFQQFNLVNRLSVLDNVLLGcLGRMPRwrgslalFNREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAIA 164
Cdd:COG1118 76 R--VGFVFQHYALFPHMTVAENIAFG-LRVRPP-------SKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492088662 165 RALTQRAEVILADEPIASLDPESA---RRVM-EILADINRSdgkTVVVTlHQVDYAVRYCPRAVALKGGRI 231
Cdd:COG1118 146 RALAVEPEVLLLDEPFGALDAKVRkelRRWLrRLHDELGGT---TVFVT-HDQEEALELADRVVVMNQGRI 212
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-245 |
4.77e-47 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 157.65 E-value: 4.77e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 4 AIHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGREVQSSGRLNG---- 79
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLL---ETPDSGEIRVGGEEIRLKPDRDGelvp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 80 ----QVRRLRADIGYIFQQFNLVNRLSVLDNVLLG---CLGRmPRwrgslalfnREEKQRAMAALDRVGLADLATQRAST 152
Cdd:COG4598 85 adrrQLQRIRTRLGMVFQSFNLWSHMTVLENVIEApvhVLGR-PK---------AEAIERAEALLAKVGLADKRDAYPAH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 153 LSGGQQQRVAIARALTQRAEVILADEPIASLDPESAR---RVMEILADinrsDGKTVVVTLHQVDYAVRYCPRAVALKGG 229
Cdd:COG4598 155 LSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGevlKVMRDLAE----EGRTMLVVTHEMGFARDVSSHVVFLHQG 230
|
250 260
....*....|....*....|....
gi 492088662 230 RIHFDGLAQDL--------SKQFL 245
Cdd:COG4598 231 RIEEQGPPAEVfgnpkserLRQFL 254
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-231 |
1.25e-46 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 156.33 E-value: 1.25e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 4 AIHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGREVQSSGRLN-GQVR 82
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLL---EMPRSGTLNIAGNHFDFSKTPSdKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 83 RLRADIGYIFQQFNLVNRLSVLDNvllgcLGRMP-RWRGslaLFNREEKQRAMAALDRVGLADLATQRASTLSGGQQQRV 161
Cdd:PRK11124 79 ELRRNVGMVFQQYNLWPHLTVQQN-----LIEAPcRVLG---LSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 162 AIARALTQRAEVILADEPIASLDPESARRVMEILADINRSdGKTVVVTLHQVDYAVRYCPRAVALKGGRI 231
Cdd:PRK11124 151 AIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
5-231 |
1.37e-46 |
|
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: 155.26 E-value: 1.37e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHK-SALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVqsSGRLNGQVRR 83
Cdd:cd03292 1 IEFINVTKTYPNGtAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEE---LPTSGTIRVNGQDV--SDLRGRAIPY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 84 LRADIGYIFQQFNLVNRLSVLDNVL--LGCLGRMPRwrgslalfnrEEKQRAMAALDRVGLADLATQRASTLSGGQQQRV 161
Cdd:cd03292 76 LRRKIGVVFQDFRLLPDRNVYENVAfaLEVTGVPPR----------EIRKRVPAALELVGLSHKHRALPAELSGGEQQRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 162 AIARALTQRAEVILADEPIASLDPESARRVMEILADINRSdGKTVVVTLHQVDYAVRYCPRAVALKGGRI 231
Cdd:cd03292 146 AIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-240 |
1.70e-46 |
|
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: 162.77 E-value: 1.70e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 1 MNDAIHVQGLNKTFSH--KSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDRSNGGQVQVLGREVQSSGrln 78
Cdd:COG1123 1 MTPLLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRISGEVLLDGRDLLELS--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 79 gqVRRLRADIGYIFQQF-NLVNRLSVLDNVLLGC-LGRMPRwrgslalfnREEKQRAMAALDRVGLADLATQRASTLSGG 156
Cdd:COG1123 78 --EALRGRRIGMVFQDPmTQLNPVTVGDQIAEALeNLGLSR---------AEARARVLELLEAVGLERRLDRYPHQLSGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 157 QQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGL 236
Cdd:COG1123 147 QRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGP 226
|
....
gi 492088662 237 AQDL 240
Cdd:COG1123 227 PEEI 230
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
4-231 |
3.54e-46 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 155.17 E-value: 3.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 4 AIHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGREVQSSGRLN-GQVR 82
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLL---ETPDSGQLNIAGHQFDFSQKPSeKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 83 RLRADIGYIFQQFNLVNRLSVLDNvllgcLGRMPRWrgSLALFNREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVA 162
Cdd:COG4161 79 LLRQKVGMVFQQYNLWPHLTVMEN-----LIEAPCK--VLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492088662 163 IARALTQRAEVILADEPIASLDPESARRVMEILADINRSdGKTVVVTLHQVDYAVRYCPRAVALKGGRI 231
Cdd:COG4161 152 IARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQT-GITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-253 |
5.42e-46 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 154.93 E-value: 5.42e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 4 AIHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAG-LaycdRSNGGQVQVLGREVQS-SGRlngQV 81
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGeL----SPDSGEVRLNGRPLADwSPA---EL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 82 RRLRAdigYIFQQFNLVNRLSVLDNVLlgcLGRMPrwrgsLALFNREEKQRAMAALDRVGLADLATQRASTLSGGQQQRV 161
Cdd:PRK13548 75 ARRRA---VLPQHSSLSFPFTVEEVVA---MGRAP-----HGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 162 AIARALTQRAE------VILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDG 235
Cdd:PRK13548 144 QLARVLAQLWEpdgpprWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADG 223
|
250
....*....|....*....
gi 492088662 236 LAQD-LSKQFLNDLYGADA 253
Cdd:PRK13548 224 TPAEvLTPETLRRVYGADV 242
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-231 |
5.86e-46 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 157.57 E-value: 5.86e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 1 MNDA-IHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycdrsnggqvqvlgrEVQSSGR--L 77
Cdd:COG3842 1 MAMPaLELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGF----------------ETPDSGRilL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 78 NGQV-------RRlraDIGYIFQQFNLVNRLSVLDNVLLGclgrmPRWRGslalFNREE-KQRAMAALDRVGLADLATQR 149
Cdd:COG3842 65 DGRDvtglppeKR---NVGMVFQDYALFPHLTVAENVAFG-----LRMRG----VPKAEiRARVAELLELVGLEGLADRY 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 150 ASTLSGGQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVV-VTlHQVDYAVRYCPRAVALKG 228
Cdd:COG3842 133 PHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIyVT-HDQEEALALADRIAVMND 211
|
...
gi 492088662 229 GRI 231
Cdd:COG3842 212 GRI 214
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
25-240 |
9.15e-46 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 153.76 E-value: 9.15e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 25 LSIQPGEMVALIGASGSGKSTLLRHLAGLaycdrsnggqvqvlgrEVQSSGRL--NGQ-VRRLRAD---IGYIFQQFNLV 98
Cdd:COG3840 20 LTIAAGERVAILGPSGAGKSTLLNLIAGF----------------LPPDSGRIlwNGQdLTALPPAerpVSMLFQENNLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 99 NRLSVLDNVllgCLGRMPRWRgslalFNREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAIARALTQRAEVILADE 178
Cdd:COG3840 84 PHLTVAQNI---GLGLRPGLK-----LTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492088662 179 PIASLDPeSARRVM-EILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGLAQDL 240
Cdd:COG3840 156 PFSALDP-ALRQEMlDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAAL 217
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-231 |
1.85e-45 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 151.89 E-value: 1.85e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGREVQSSgrlngQVRRL 84
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADL---DPPTSGEIYLDGKPLSAM-----PPPEW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 85 RADIGYIFQQFNLVnRLSVLDNVLLGclgrmprWRGSLALFNREekqRAMAALDRVGL-ADLATQRASTLSGGQQQRVAI 163
Cdd:COG4619 73 RRQVAYVPQEPALW-GGTVRDNLPFP-------FQLRERKFDRE---RALELLERLGLpPDILDKPVERLSGGERQRLAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492088662 164 ARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRI 231
Cdd:COG4619 142 IRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-231 |
2.18e-45 |
|
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: 150.63 E-value: 2.18e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQSSGRlngqvrRL 84
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLL---KPDSGEIKVLGKDIKKEPE------EV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 85 RADIGYIFQQFNLVNRLSVLDNVllgclgrmprwrgslalfnreekqramaaldrvgladlatqrasTLSGGQQQRVAIA 164
Cdd:cd03230 72 KRRIGYLPEEPSLYENLTVRENL--------------------------------------------KLSGGMKQRLALA 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492088662 165 RALTQRAEVILADEPIASLDPESARRVMEILADINRsDGKTVVVTLHQVDYAVRYCPRAVALKGGRI 231
Cdd:cd03230 108 QALLHDPELLILDEPTSGLDPESRREFWELLRELKK-EGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-235 |
1.72e-44 |
|
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: 149.65 E-value: 1.72e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKSALVDLALSIQPGeMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQSsgrlngQVRRL 84
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLT---PPSSGTIRIDGQDVLK------QPQKL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 85 RADIGYIFQQFNLVNRLSVLDNV-LLGCLGRMPrwrgslalfNREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAI 163
Cdd:cd03264 71 RRRIGYLPQEFGVYPNFTVREFLdYIAWLKGIP---------SKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGI 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492088662 164 ARALTQRAEVILADEPIASLDPESARRVMEILADInrSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDG 235
Cdd:cd03264 142 AQALVGDPSILIVDEPTAGLDPEERIRFRNLLSEL--GEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-211 |
9.32e-44 |
|
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: 148.10 E-value: 9.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGL--AYCDRSNGGQVQVLGREVQSsgrLNGQVR 82
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndLIPGAPDEGEVLLDGKDIYD---LDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 83 RLRADIGYIFQQFNLVnRLSVLDNVLLGclgrmPRWRGSLAlfNREEKQRAMAALDRVGLADLATQR--ASTLSGGQQQR 160
Cdd:cd03260 78 ELRRRVGMVFQKPNPF-PGSIYDNVAYG-----LRLHGIKL--KEELDERVEEALRKAALWDEVKDRlhALGLSGGQQQR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 492088662 161 VAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSdgKTVVVTLH 211
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTH 198
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-247 |
4.12e-43 |
|
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: 147.26 E-value: 4.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 4 AIHVQGLNKTFSHKS----ALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDRsngGQVQVLGREVQSSGRlng 79
Cdd:COG1124 1 MLEVRNLSVSYGQGGrrvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWS---GEVTFDGRPVTRRRR--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 80 qvRRLRADIGYIFQQ-FNLVN-RLSVLDnVLLGCLgrmprwrgsLALFNREEKQRAMAALDRVGL-ADLATQRASTLSGG 156
Cdd:COG1124 75 --KAFRRRVQMVFQDpYASLHpRHTVDR-ILAEPL---------RIHGLPDREERIAELLEQVGLpPSFLDRYPHQLSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 157 QQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGL 236
Cdd:COG1124 143 QRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELT 222
|
250
....*....|.
gi 492088662 237 AQDLSKQFLND 247
Cdd:COG1124 223 VADLLAGPKHP 233
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
5-231 |
1.08e-42 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 145.25 E-value: 1.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKS----ALVDLALSIQPGEMVALIGASGSGKSTLLrHLAGLAycDRSNGGQVQVLGREVQSSGrlNGQ 80
Cdd:NF038007 2 LNMQNAEKCYITKTiktkVLNHLNFSVEKGDFVSIMGPSGSGKSTLL-NIIGMF--DSLDSGSLTLAGKEVTNLS--YSQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 81 VRRLRAD-IGYIFQQFNLVNRLSVLDNVLLgclgrmP-RWRGslaLFNREEKQRAMAALDRVGLADLATQRASTLSGGQQ 158
Cdd:NF038007 77 KIILRRElIGYIFQSFNLIPHLSIFDNVAL------PlKYRG---VAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492088662 159 QRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSdGKTVVVTLHQVDyAVRYCPRAVALKGGRI 231
Cdd:NF038007 148 QRVAIARAMVSNPALLLADEPTGNLDSKNARAVLQQLKYINQK-GTTIIMVTHSDE-ASTYGNRIINMKDGKL 218
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-254 |
1.96e-42 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 145.61 E-value: 1.96e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQS--SGRLNGQVR 82
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLL---PPDSGEVLVDGLDVATtpSRELAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 83 RLRadigyifQQFNLVNRLSVLDnvLLGcLGRMPRWRGSLalfNREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVA 162
Cdd:COG4604 79 ILR-------QENHINSRLTVRE--LVA-FGRFPYSKGRL---TAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 163 IARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGLAQD-LS 241
Cdd:COG4604 146 IAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEiIT 225
|
250
....*....|...
gi 492088662 242 KQFLNDLYGADAD 254
Cdd:COG4604 226 PEVLSDIYDTDIE 238
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
19-230 |
3.10e-42 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 143.93 E-value: 3.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 19 ALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDRsngGQVQVLGREVQssgRLNG-QVRRLRADIGYIFQQFNL 97
Cdd:TIGR02673 17 ALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSR---GQVRIAGEDVN---RLRGrQLPLLRRRIGVVFQDFRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 98 VNRLSVLDNVLLGClgrmpRWRGSLAlfnREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAIARALTQRAEVILAD 177
Cdd:TIGR02673 91 LPDRTVYENVALPL-----EVRGKKE---REIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLAD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 492088662 178 EPIASLDPESARRVMEILADINRSdGKTVVVTLHQVDYAVRYCPRAVALKGGR 230
Cdd:TIGR02673 163 EPTGNLDPDLSERILDLLKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
22-181 |
1.04e-41 |
|
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: 140.48 E-value: 1.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 22 DLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDRsngGQVQVLGREVQSSGRlngqvRRLRADIGYIFQQFNLVNRL 101
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTE---GTILLDGQDLTDDER-----KSLRKEIGYVFQDPQLFPRL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 102 SVLDNVLLGCLGRmprwrgslALFNREEKQRAMAALDRVGLADLATQRA----STLSGGQQQRVAIARALTQRAEVILAD 177
Cdd:pfam00005 75 TVRENLRLGLLLK--------GLSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLD 146
|
....
gi 492088662 178 EPIA 181
Cdd:pfam00005 147 EPTA 150
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-243 |
1.59e-41 |
|
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: 143.72 E-value: 1.59e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTF--SHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDRsngGQVQVLGREVQSSGRLNgQVR 82
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTS---GKVTVDGLDTLDEENLW-EIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 83 RLradIGYIFQ----QFnlVNRLsVLDNVLLGC--LGrmprwrgslalFNREE-KQRAMAALDRVGLADLATQRASTLSG 155
Cdd:TIGR04520 77 KK---VGMVFQnpdnQF--VGAT-VEDDVAFGLenLG-----------VPREEmRKRVDEALKLVGMEDFRDREPHLLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 156 GQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRyCPRAVALKGGRIHFDG 235
Cdd:TIGR04520 140 GQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEG 218
|
....*...
gi 492088662 236 LAQDLSKQ 243
Cdd:TIGR04520 219 TPREIFSQ 226
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-231 |
2.94e-41 |
|
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: 141.87 E-value: 2.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKS----ALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVqsSGRLNGQ 80
Cdd:cd03257 2 LEVKNLSVSFPTGGgsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLL---KPTSGSIIFDGKDL--LKLSRRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 81 VRRLRADIGYIFQQ-FNLVN-RLSVLDNVL--LGCLGRMPRwrgslalfNREEKQRAMAALDRVGL-ADLATQRASTLSG 155
Cdd:cd03257 77 RKIRRKEIQMVFQDpMSSLNpRMTIGEQIAepLRIHGKLSK--------KEARKEAVLLLLVGVGLpEEVLNRYPHELSG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492088662 156 GQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRI 231
Cdd:cd03257 149 GQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
19-231 |
3.88e-41 |
|
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: 142.78 E-value: 3.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 19 ALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQSSGRlnGQVRRLRA-DIGYIFQQFNL 97
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLI---EPTSGKVLIDGQDIAAMSR--KELRELRRkKISMVFQSFAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 98 VNRLSVLDNVLLGC-LGRMPRwrgslalfnREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAIARALTQRAEVILA 176
Cdd:cd03294 114 LPHRTVLENVAFGLeVQGVPR---------AEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLM 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 492088662 177 DEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRI 231
Cdd:cd03294 185 DEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-252 |
7.42e-41 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 141.79 E-value: 7.42e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDRsngGQVQVLGREVqssGRLNGQVR-R 83
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSS---GEVRLNGRPL---AAWSPWELaR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 84 LRAdigyIFQQFNLVN-RLSVLDNVLLGclgRMPrWRGSlalfNREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVA 162
Cdd:COG4559 76 RRA----VLPQHSSLAfPFTVEEVVALG---RAP-HGSS----AAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 163 IARALTQ-------RAEVILADEPIASLDPESARRVMEILADINRSDGkTVVVTLHQVDYAVRYCPRAVALKGGRIHFDG 235
Cdd:COG4559 144 LARVLAQlwepvdgGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGG-GVVAVLHDLNLAAQYADRILLLHQGRLVAQG 222
|
250
....*....|....*...
gi 492088662 236 LAQD-LSKQFLNDLYGAD 252
Cdd:COG4559 223 TPEEvLTDELLERVYGAD 240
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-212 |
7.60e-41 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 139.92 E-value: 7.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQSsgrlngQVRRL 84
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLL---PPSAGEVLWNGEPIRD------AREDY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 85 RADIGYIFQQFNLVNRLSVLDNVLLgclgrmprWRGSLALFNREEkqRAMAALDRVGLADLATQRASTLSGGQQQRVAIA 164
Cdd:COG4133 74 RRRLAYLGHADGLKPELTVRENLRF--------WAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALA 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 492088662 165 RALTQRAEVILADEPIASLDPESARRVMEILADiNRSDGKTVVVTLHQ 212
Cdd:COG4133 144 RLLLSPAPLWLLDEPFTALDAAGVALLAELIAA-HLARGGAVLLTTHQ 190
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
4-231 |
6.74e-40 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 141.75 E-value: 6.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 4 AIHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGREVqssgrlNGQVRR 83
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGL---EDPTSGEILIGGRDV------TDLPPK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 84 LRaDIGYIFQQFNLVNRLSVLDNVLLGC-LGRMPRwrgslalfnREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVA 162
Cdd:COG3839 74 DR-NIAMVFQSYALYPHMTVYENIAFPLkLRKVPK---------AEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492088662 163 IARALTQRAEVILADEPIASLDPESaRRVMEI-LADINRSDGKTVV-VTLHQVDyAVRYCPRAVALKGGRI 231
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLDAKL-RVEMRAeIKRLHRRLGTTTIyVTHDQVE-AMTLADRIAVMNDGRI 212
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-240 |
2.19e-39 |
|
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: 137.47 E-value: 2.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 4 AIHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGREVqssGRLNGQVRr 83
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGL---ERPDSGTILFGGEDA---TDVPVQER- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 84 lraDIGYIFQQFNLVNRLSVLDNVLLGCLGRMPRWRGSLAlfnrEEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAI 163
Cdd:cd03296 75 ---NVGFVFQHYALFRHMTVFDNVAFGLRVKPRSERPPEA----EIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492088662 164 ARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGLAQDL 240
Cdd:cd03296 148 ARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
19-240 |
2.26e-39 |
|
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: 136.80 E-value: 2.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 19 ALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVqssGRLNGQvRRLRADIGYIFQQFNLV 98
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLL---PPRSGSIRFDGRDI---TGLPPH-ERARAGIGYVPEGRRIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 99 NRLSVLDNVLLGCLGRmprwrgslalfnreEKQRAMAALDRV-----GLADLATQRASTLSGGQQQRVAIARALTQRAEV 173
Cdd:cd03224 88 PELTVEENLLLGAYAR--------------RRAKRKARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492088662 174 ILADEPIASLDPESARRVMEILADINRSdGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGLAQDL 240
Cdd:cd03224 154 LLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-240 |
9.35e-39 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 138.68 E-value: 9.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 4 AIHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycdrsnggqvqvlgrEVQSSGRL--NGQ- 80
Cdd:PRK10851 2 SIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGL----------------EHQTSGHIrfHGTd 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 81 VRRLRA---DIGYIFQQFNLVNRLSVLDNVLLGcLGRMPRW-RGSLALFnreeKQRAMAALDRVGLADLATQRASTLSGG 156
Cdd:PRK10851 66 VSRLHArdrKVGFVFQHYALFRHMTVFDNIAFG-LTVLPRReRPNAAAI----KAKVTQLLEMVQLAHLADRYPAQLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 157 QQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGL 236
Cdd:PRK10851 141 QKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGT 220
|
....
gi 492088662 237 AQDL 240
Cdd:PRK10851 221 PDQV 224
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
4-218 |
1.00e-38 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 135.89 E-value: 1.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 4 AIHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLaglaycDRSN--------GGQVQVLGREVQSSG 75
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSL------NRMNdlvpgvriEGKVLFDGQDIYDKK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 76 RlngQVRRLRADIGYIFQQFNLVNrLSVLDNVLLGclgrmPRWRGslaLFNREE-KQRAMAALDRVGLADLATQRAST-- 152
Cdd:TIGR00972 75 I---DVVELRRRVGMVFQKPNPFP-MSIYDNIAYG-----PRLHG---IKDKKElDEIVEESLKKAALWDEVKDRLHDsa 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492088662 153 --LSGGQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADInrSDGKTVVVTLHQVDYAVR 218
Cdd:TIGR00972 143 lgLSGGQQQRLCIARALAVEPEVLLLDEPTSALDPIATGKIEELIQEL--KKKYTIVIVTHNMQQAAR 208
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-230 |
3.21e-38 |
|
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: 131.60 E-value: 3.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 6 HVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQSSGRlngqvRRLR 85
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLL---KPTSGEILIDGKDIAKLPL-----EELR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 86 ADIGYIFQqfnlvnrlsvldnvllgclgrmprwrgslalfnreekqramaaldrvgladlatqrastLSGGQQQRVAIAR 165
Cdd:cd00267 73 RRIGYVPQ-----------------------------------------------------------LSGGQRQRVALAR 93
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492088662 166 ALTQRAEVILADEPIASLDPESARRVMEILADINRsDGKTVVVTLHQVDYAVRYCPRAVALKGGR 230
Cdd:cd00267 94 ALLLNPDLLLLDEPTSGLDPASRERLLELLRELAE-EGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-243 |
4.58e-38 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 139.77 E-value: 4.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 1 MNDAIHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGlAYcdRSNGGQVQVLGREVQSSGRLNGQ 80
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSG-VY--QPDSGEILLDGEPVRFRSPRDAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 81 vrrlRADIGYIFQQFNLVNRLSVLDNVllgCLGRMPRWRGslaLFN-REEKQRAMAALDRVGLADLATQRASTLSGGQQQ 159
Cdd:COG1129 78 ----AAGIAIIHQELNLVPNLSVAENI---FLGREPRRGG---LIDwRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 160 RVAIARALTQRAEVILADEPIASLDPESARRVMEILADInRSDGKTVV-VT--LHQVdYAVryCPRAVALKGGRIHFDGL 236
Cdd:COG1129 148 LVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIyIShrLDEV-FEI--ADRVTVLRDGRLVGTGP 223
|
....*..
gi 492088662 237 AQDLSKQ 243
Cdd:COG1129 224 VAELTED 230
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
18-231 |
6.74e-38 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 133.37 E-value: 6.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 18 SALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGrevQSSGRLNGQVR-RLRA-DIGYIFQQF 95
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGL---DDGSSGEVSLVG---QPLHQMDEEARaKLRAkHVGFVFQSF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 96 NLVNRLSVLDNVLLGCLGRMPRwrgslalfNREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAIARALTQRAEVIL 175
Cdd:PRK10584 98 MLIPTLNALENVELPALLRGES--------SRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLF 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 492088662 176 ADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRyCPRAVALKGGRI 231
Cdd:PRK10584 170 ADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQL 224
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
20-231 |
9.78e-38 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 140.63 E-value: 9.78e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 20 LVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGREVQSSGrlNGQVRRLRAD-IGYIFQQFNLV 98
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCL---DKPTSGTYRVAGQDVATLD--ADALAQLRREhFGFIFQRYHLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 99 NRLSVLDNVllgclgRMPRWRGSLAlfNREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAIARALTQRAEVILADE 178
Cdd:PRK10535 99 SHLTAAQNV------EVPAVYAGLE--RKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 492088662 179 PIASLDPESARRVMEILADInRSDGKTVVVTLHQVDYAVRyCPRAVALKGGRI 231
Cdd:PRK10535 171 PTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEI 221
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-231 |
1.05e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 134.09 E-value: 1.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 1 MNDAIHVQGLnkTFSHKS---ALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDRsngGQVQVLGREVQSSgrl 77
Cdd:PRK13647 1 MDNIIEVEDL--HFRYKDgtkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQR---GRVKVMGREVNAE--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 78 ngQVRRLRADIGYIFQQ-FNLVNRLSVLDNVLLGclgrmPRwrgSLALFNREEKQRAMAALDRVGLADLATQRASTLSGG 156
Cdd:PRK13647 73 --NEKWVRSKVGLVFQDpDDQVFSSTVWDDVAFG-----PV---NMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492088662 157 QQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSdGKTVVVTLHQVDYAVRYCPRAVALKGGRI 231
Cdd:PRK13647 143 QKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRV 216
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-231 |
1.80e-37 |
|
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: 131.63 E-value: 1.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDRsngGQVQVLGREVQSSGrlngqvrrl 84
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDS---GEVLFDGKPLDIAA--------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 85 RADIGYIFQQFNLVNRLSVLDNVL-LGCLGRMPRwrgslalfnREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAI 163
Cdd:cd03269 69 RNRIGYLPEERGLYPKMKVIDQLVyLAQLKGLKK---------EEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQF 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492088662 164 ARALTQRAEVILADEPIASLDPESARRVMEILADInRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRI 231
Cdd:cd03269 140 IAAVIHDPELLILDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-231 |
2.05e-37 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 135.16 E-value: 2.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 1 MNDAIHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGREVQssgRLNGQ 80
Cdd:TIGR03265 1 SSPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGL---ERQTAGTIYQGGRDIT---RLPPQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 81 VRrlraDIGYIFQQFNLVNRLSVLDNVLLGCLGR-MPRwrgslalfnREEKQRAMAALDRVGLADLATQRASTLSGGQQQ 159
Cdd:TIGR03265 75 KR----DYGIVFQSYALFPNLTVADNIAYGLKNRgMGR---------AEVAERVAELLDLVGLPGSERKYPGQLSGGQQQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492088662 160 RVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRI 231
Cdd:TIGR03265 142 RVALARALATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVI 213
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
19-255 |
2.80e-37 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 132.68 E-value: 2.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 19 ALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDrsnGGQVQVLGREVQSSGrlngqvrrlrADIGYIFQQFNLV 98
Cdd:COG4525 22 ALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPS---SGEITLDGVPVTGPG----------ADRGVVFQKDALL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 99 NRLSVLDNVLLGC-LGRMPRwrgslalfnREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAIARALTQRAEVILAD 177
Cdd:COG4525 89 PWLNVLDNVAFGLrLRGVPK---------AERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 178 EPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKG--GRIhFDGLAQDLSKQFLNdlyGADADA 255
Cdd:COG4525 160 EPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPgpGRI-VERLELDFSRRFLA---GEDARA 235
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-231 |
2.89e-37 |
|
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: 132.04 E-value: 2.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKSALV-DLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQSSGRLngqvrR 83
Cdd:cd03295 1 IEFENVTKRYGGGKKAVnNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLI---EPTSGEIFIDGEDIREQDPV-----E 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 84 LRADIGYIFQQFNLVNRLSVLDNVLLgclgrMPrwrgSLALFNREE-KQRAMAALDRVGL--ADLATQRASTLSGGQQQR 160
Cdd:cd03295 73 LRRKIGYVIQQIGLFPHMTVEENIAL-----VP----KLLKWPKEKiRERADELLALVGLdpAEFADRYPHELSGGQQQR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492088662 161 VAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRI 231
Cdd:cd03295 144 VGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEI 214
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-231 |
2.97e-37 |
|
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: 131.59 E-value: 2.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGREVQssgrlngQVRRL 84
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGF---ETPTSGEILLDGKDIT-------NLPPH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 85 RADIGYIFQQFNLVNRLSVLDNVLLGC-LGRMPRwrgslalfnREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAI 163
Cdd:cd03300 71 KRPVNTVFQNYALFPHLTVFENIAFGLrLKKLPK---------AEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAI 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492088662 164 ARALTQRAEVILADEPIASLDPEsARRVMEI-LADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRI 231
Cdd:cd03300 142 ARALVNEPKVLLLDEPLGALDLK-LRKDMQLeLKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-240 |
3.78e-37 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 132.01 E-value: 3.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 2 NDAIHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRhlaGLAYCDRSNGGQVQVLGREVQ----SSGRL 77
Cdd:PRK10619 3 ENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLR---CINFLEKPSEGSIVVNGQTINlvrdKDGQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 78 N----GQVRRLRADIGYIFQQFNLVNRLSVLDNVllgclgrMPRWRGSLALFNREEKQRAMAALDRVGLADLATQR-AST 152
Cdd:PRK10619 80 KvadkNQLRLLRTRLTMVFQHFNLWSHMTVLENV-------MEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKyPVH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 153 LSGGQQQRVAIARALTQRAEVILADEPIASLDPE---SARRVMEILADinrsDGKTVVVTLHQVDYAVRYCPRAVALKGG 229
Cdd:PRK10619 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPElvgEVLRIMQQLAE----EGKTMVVVTHEMGFARHVSSHVIFLHQG 228
|
250
....*....|.
gi 492088662 230 RIHFDGLAQDL 240
Cdd:PRK10619 229 KIEEEGAPEQL 239
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
17-240 |
6.97e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 132.45 E-value: 6.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 17 KSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQvLGREVQSSGRLNGQVRRLRADIGYIFQ--Q 94
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLL---QPTSGTVT-IGERVITAGKKNKKLKPLRKKVGIVFQfpE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 95 FNLVNRlSVLDNVllgCLGRMprwrgSLALFNREEKQRAMAALDRVGL-ADLATQRASTLSGGQQQRVAIARALTQRAEV 173
Cdd:PRK13634 96 HQLFEE-TVEKDI---CFGPM-----NFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEV 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492088662 174 ILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGLAQDL 240
Cdd:PRK13634 167 LVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-231 |
2.30e-36 |
|
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: 128.78 E-value: 2.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKS--ALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQSsgrlngQVR 82
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGEL---RPTSGTAYINGYSIRT------DRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 83 RLRADIGYIFQQFNLVNRLSVLDNVLLGClgrmpRWRGslaLFNREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVA 162
Cdd:cd03263 72 AARQSLGYCPQFDALFDELTVREHLRFYA-----RLKG---LPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLS 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492088662 163 IARALTQRAEVILADEPIASLDPESARRVMEILADINRsdGKTVVVTLHQVDYAVRYCPRAVALKGGRI 231
Cdd:cd03263 144 LAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKL 210
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
10-235 |
2.79e-36 |
|
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: 128.38 E-value: 2.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 10 LNKT-FSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGREVQSSgrlngqvRRLRADI 88
Cdd:cd03298 3 LDKIrFSYGEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGF---ETPQSGRVLINGVDVTAA-------PPADRPV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 89 GYIFQQFNLVNRLSVLDNVllgCLGRMPRWRgslalFNREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAIARALT 168
Cdd:cd03298 73 SMLFQENNLFAHLTVEQNV---GLGLSPGLK-----LTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLV 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492088662 169 QRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDG 235
Cdd:cd03298 145 RDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
22-252 |
4.23e-36 |
|
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: 129.05 E-value: 4.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 22 DLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCdrSNGGQVQVLGREVqssGRLNgqVRRLRADIGYI--FQQFNLVN 99
Cdd:COG1119 21 DISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPP--TYGNDVRLFGERR---GGED--VWELRKRIGLVspALQLRFPR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 100 RLSVLDNVLLGCLGRMPRWRGslalFNREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAIARALTQRAEVILADEP 179
Cdd:COG1119 94 DETVLDVVLSGFFDSIGLYRE----PTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEP 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492088662 180 IASLDPESARRVMEILADINRSDGKTVV-VTlHQVDYAVRYCPRAVALKGGRIHFDGLAQD-LSKQFLNDLYGAD 252
Cdd:COG1119 170 TAGLDLGARELLLALLDKLAAEGAPTLVlVT-HHVEEIPPGITHVLLLKDGRVVAAGPKEEvLTSENLSEAFGLP 243
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-240 |
6.67e-36 |
|
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: 127.87 E-value: 6.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQSsgrlngQVRRL 84
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLL---KPTSGRATVAGHDVVR------EPREV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 85 RADIGYIFQQFNLVNRLSVLDNVLlgclgrmprWRGSLA-LFNREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAI 163
Cdd:cd03265 72 RRRIGIVFQDLSVDDELTGWENLY---------IHARLYgVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEI 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492088662 164 ARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGLAQDL 240
Cdd:cd03265 143 ARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
7-242 |
1.34e-35 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 127.87 E-value: 1.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 7 VQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQvlgrevqsSGrlNGQVRRLRA 86
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGL---ETPSAGELL--------AG--TAPLAEARE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 87 DIGYIFQQFNLVNRLSVLDNVLLGCLGRmprWRgslalfnreekQRAMAALDRVGLADLATQRASTLSGGQQQRVAIARA 166
Cdd:PRK11247 82 DTRLMFQDARLLPWKKVIDNVGLGLKGQ---WR-----------DAALQALAAVGLADRANEWPAALSGGQKQRVALARA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492088662 167 LTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDgLAQDLSK 242
Cdd:PRK11247 148 LIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLD-LTVDLPR 222
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-243 |
1.74e-35 |
|
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: 134.19 E-value: 1.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 4 AIHVQGLNKTFSHKSALV--DLALSIQPGEMVALIGASGSGKSTLLRHLAGLaYcdRSNGGQVqvlgrevqssgRLNGQ- 80
Cdd:COG2274 473 DIELENVSFRYPGDSPPVldNISLTIKPGERVAIVGRSGSGKSTLLKLLLGL-Y--EPTSGRI-----------LIDGId 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 81 -----VRRLRADIGYIFQQFNLVNRlSVLDNVLLGCLGRmprwrgslalfnreEKQRAMAALDRVGLAD--------LAT 147
Cdd:COG2274 539 lrqidPASLRRQIGVVLQDVFLFSG-TIRENITLGDPDA--------------TDEEIIEAARLAGLHDfiealpmgYDT 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 148 Q---RASTLSGGQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRsdGKTVVVTLHQVDyAVRYCPRAV 224
Cdd:COG2274 604 VvgeGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLS-TIRLADRII 680
|
250
....*....|....*....
gi 492088662 225 ALKGGRIHFDGLAQDLSKQ 243
Cdd:COG2274 681 VLDKGRIVEDGTHEELLAR 699
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
5-235 |
2.00e-35 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 130.45 E-value: 2.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDRsngGQVQVLGREVQssgrlngQVRRL 84
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDS---GRIMLDGQDIT-------HVPAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 85 RADIGYIFQQFNLVNRLSVLDNVLLGClgRMPRwrgslaLFNREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAIA 164
Cdd:PRK09452 85 NRHVNTVFQSYALFPHMTVFENVAFGL--RMQK------TPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492088662 165 RALTQRAEVILADEPIASLDPEsARRVMEI-LADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDG 235
Cdd:PRK09452 157 RAVVNKPKVLLLDESLSALDYK-LRKQMQNeLKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDG 227
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
29-235 |
2.13e-35 |
|
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: 126.26 E-value: 2.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 29 PGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGREVQSSGR---LNGQVRRlradIGYIFQQFNLVNRLSVLD 105
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGL---EKPDGGTIVLNGTVLFDSRKkinLPPQQRK----IGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 106 NVLLGclgrMPRWRgslalfNREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAIARALTQRAEVILADEPIASLDP 185
Cdd:cd03297 95 NLAFG----LKRKR------NREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 492088662 186 ESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDG 235
Cdd:cd03297 165 ALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-243 |
2.62e-35 |
|
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: 132.96 E-value: 2.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 4 AIHVQGLnkTFSH---KSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQSSGRlngq 80
Cdd:COG4988 336 SIELEDV--SFSYpggRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFL---PPYSGSILINGVDLSDLDP---- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 81 vRRLRADIGYIFQQFNLVNrLSVLDNVLLGclgrmprwrgslalfnREE--KQRAMAALDRVGLAD--------LATQ-- 148
Cdd:COG4988 407 -ASWRRQIAWVPQNPYLFA-GTIRENLRLG----------------RPDasDEELEAALEAAGLDEfvaalpdgLDTPlg 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 149 -RASTLSGGQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADInrSDGKTVVVTLHQVDyAVRYCPRAVALK 227
Cdd:COG4988 469 eGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL--AKGRTVILITHRLA-LLAQADRILVLD 545
|
250
....*....|....*.
gi 492088662 228 GGRIHFDGLAQDLSKQ 243
Cdd:COG4988 546 DGRIVEQGTHEELLAK 561
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-256 |
1.24e-34 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 126.38 E-value: 1.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 4 AIHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDrsnGGQVQVLGREVQssgrlngqvRR 83
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPD---SGEVLWDGEPLD---------PE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 84 LRADIGY------IFQqfnlvnRLSVLDNVLLgcLGR---MPRwrgslalfnREEKQRAMAALDRVGLADLATQRASTLS 154
Cdd:COG4152 69 DRRRIGYlpeergLYP------KMKVGEQLVY--LARlkgLSK---------AEAKRRADEWLERLGLGDRANKKVEELS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 155 GGQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSdGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFD 234
Cdd:COG4152 132 KGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLS 210
|
250 260
....*....|....*....|....
gi 492088662 235 GLAQDLSKQFLNDLY--GADADAS 256
Cdd:COG4152 211 GSVDEIRRQFGRNTLrlEADGDAG 234
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
19-231 |
1.54e-34 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 128.30 E-value: 1.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 19 ALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVqssGRLNG-QVRRLRA-DIGYIFQQFN 96
Cdd:COG4175 42 GVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLI---EPTAGEVLIDGEDI---TKLSKkELRELRRkKMSMVFQHFA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 97 LVNRLSVLDNVLLGC-LGRMPRwrgslalfnREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAIARALTQRAEVIL 175
Cdd:COG4175 116 LLPHRTVLENVAFGLeIQGVPK---------AERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILL 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 492088662 176 ADEPIASLDPeSARRVM-EILADINRSDGKTVV-VTlHQVDYAVRYCPRAVALKGGRI 231
Cdd:COG4175 187 MDEAFSALDP-LIRREMqDELLELQAKLKKTIVfIT-HDLDEALRLGDRIAIMKDGRI 242
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-235 |
1.96e-34 |
|
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: 123.48 E-value: 1.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGREVQssgRLNGQVRRl 84
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGL---IKPDSGEITFDGKSYQ---KNIEALRR- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 85 radIGYIFQQFNLVNRLSVLDNVLLGCLGRMPRwrgslalfnreeKQRAMAALDRVGLADLATQRASTLSGGQQQRVAIA 164
Cdd:cd03268 74 ---IGALIEAPGFYPNLTARENLRLLARLLGIR------------KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIA 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492088662 165 RALTQRAEVILADEPIASLDPESARRVMEILADINRSdGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDG 235
Cdd:cd03268 139 LALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-230 |
3.09e-34 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 121.72 E-value: 3.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLnkTFSHKS----ALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGREVQSSGRlngq 80
Cdd:cd03228 1 IEFKNV--SFSYPGrpkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRL---YDPTSGEILIDGVDLRDLDL---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 81 vRRLRADIGYIFQQFNLVNRlSVLDNVLlgclgrmprwrgslalfnreekqramaaldrvgladlatqrastlSGGQQQR 160
Cdd:cd03228 72 -ESLRKNIAYVPQDPFLFSG-TIRENIL---------------------------------------------SGGQRQR 104
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 161 VAIARALTQRAEVILADEPIASLDPESARRVMEILAdiNRSDGKTVVVTLHQVDyAVRYCPRAVALKGGR 230
Cdd:cd03228 105 IAIARALLRDPPILILDEATSALDPETEALILEALR--ALAKGKTVIVIAHRLS-TIRDADRIIVLDDGR 171
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
19-240 |
3.76e-34 |
|
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: 123.55 E-value: 3.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 19 ALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVqssGRLNGQvRRLRADIGY------IF 92
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLL---PPRSGSIRFDGEDI---TGLPPH-RIARLGIGYvpegrrIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 93 QQfnlvnrLSVLDNVLLGclgrmprwrgslaLFNREEKQRAMAALDRVG-----LADLATQRASTLSGGQQQRVAIARAL 167
Cdd:COG0410 91 PS------LTVEENLLLG-------------AYARRDRAEVRADLERVYelfprLKERRRQRAGTLSGGEQQMLAIGRAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492088662 168 TQRAEVILADEPIASLDPESARRVMEILADINRsDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGLAQDL 240
Cdd:COG0410 152 MSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNR-EGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
19-211 |
4.34e-34 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 121.96 E-value: 4.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 19 ALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycdrsnggqvqvlgrEVQSSGRLngqVRRLRADIGYIFQQFNLV 98
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGV----------------LRPTSGTV---RRAGGARVAYVPQRSEVP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 99 NRL--SVLDNVLLGclgrmpRW--RGSLALFNREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAIARALTQRAEVI 174
Cdd:NF040873 68 DSLplTVRDLVAMG------RWarRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLL 141
|
170 180 190
....*....|....*....|....*....|....*..
gi 492088662 175 LADEPIASLDPESARRVMEILADInRSDGKTVVVTLH 211
Cdd:NF040873 142 LLDEPTTGLDAESRERIIALLAEE-HARGATVVVVTH 177
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-235 |
8.76e-34 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 123.97 E-value: 8.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 1 MNDAIHVQGLNKTFSHKS--ALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDRsngGQVQVLGREVQSSgrln 78
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEA---GTITVGGMVLSEE---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 79 gQVRRLRADIGYIFQqfNLVNRL---SVLDNVLLGCLGR-MPRwrgslalfnREEKQRAMAALDRVGLADLATQRASTLS 154
Cdd:PRK13635 75 -TVWDVRRQVGMVFQ--NPDNQFvgaTVQDDVAFGLENIgVPR---------EEMVERVDQALRQVGMEDFLNREPHRLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 155 GGQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRyCPRAVALKGGRIHFD 234
Cdd:PRK13635 143 GGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEE 221
|
.
gi 492088662 235 G 235
Cdd:PRK13635 222 G 222
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-277 |
1.49e-33 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 127.45 E-value: 1.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 1 MNDAIHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaYcdRSNGGQVQVLGREVqssgRLNGQ 80
Cdd:COG3845 2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGL-Y--QPDSGEILIDGKPV----RIRSP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 81 VRRLRADIGYIFQQFNLVNRLSVLDNVLLGclgRMPRWRGSLALfnREEKQRAMAALDRVGLA-DLaTQRASTLSGGQQQ 159
Cdd:COG3845 75 RDAIALGIGMVHQHFMLVPNLTVAENIVLG---LEPTKGGRLDR--KAARARIRELSERYGLDvDP-DAKVEDLSVGEQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 160 RVAIARALTQRAEVILADEPIASLDPESARRVMEILADInRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGLAQD 239
Cdd:COG3845 149 RVEILKALYRGARILILDEPTAVLTPQEADELFEILRRL-AAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAE 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 492088662 240 LSKQFLndlygadadASLMI-------TERSRRVRQKPRLELAKV 277
Cdd:COG3845 228 TSEEEL---------AELMVgrevllrVEKAPAEPGEVVLEVENL 263
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
16-231 |
2.13e-33 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 121.46 E-value: 2.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 16 HKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGREVQS-SGRLNGQVRRLRadIGYIFQQ 94
Cdd:PRK11629 21 QTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGL---DTPTSGDVIFNGQPMSKlSSAAKAELRNQK--LGFIYQF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 95 FNLVNRLSVLDNVLLGCL-GRMPRwrgslalfnREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAIARALTQRAEV 173
Cdd:PRK11629 96 HHLLPDFTALENVAMPLLiGKKKP---------AEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 492088662 174 ILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYcPRAVALKGGRI 231
Cdd:PRK11629 167 VLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRL 223
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-197 |
4.26e-33 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 121.30 E-value: 4.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 1 MNDAIHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLayCDRSNG----GQVQVLGREVQSSGR 76
Cdd:COG1117 8 LEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRM--NDLIPGarveGEILLDGEDIYDPDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 77 lngQVRRLRADIGYIFQQFNLVNrLSVLDNVLLGclgrmPRWRGSLalfNREE-KQRAMAALDRVGLAD-----LaTQRA 150
Cdd:COG1117 86 ---DVVELRRRVGMVFQKPNPFP-KSIYDNVAYG-----LRLHGIK---SKSElDEIVEESLRKAALWDevkdrL-KKSA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 492088662 151 STLSGGQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILAD 197
Cdd:COG1117 153 LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILE 199
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-253 |
7.85e-33 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 124.18 E-value: 7.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDrsnGGQVQVLGREVQSSgrlngQVRRL 84
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPT---AGTVLVAGDDVEAL-----SARAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 85 RADIGYIFQQFNLVNRLSVLDNVLLGclgRMPRwRGSLALFNREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAIA 164
Cdd:PRK09536 76 SRRVASVPQDTSLSFEFDVRQVVEMG---RTPH-RSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 165 RALTQRAEVILADEPIASLDPESARRVMEILADInRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGLAQD-LSKQ 243
Cdd:PRK09536 152 RALAQATPVLLLDEPTASLDINHQVRTLELVRRL-VDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADvLTAD 230
|
250
....*....|
gi 492088662 244 FLNDLYGADA 253
Cdd:PRK09536 231 TLRAAFDART 240
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-240 |
1.08e-32 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 119.69 E-value: 1.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 25 LSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDRsngGQVqvlgrevqssgRLNGQVRRL----RADIGYIFQQFNLVNR 100
Cdd:PRK10771 20 LTVERGERVAILGPSGAGKSTLLNLIAGFLTPAS---GSL-----------TLNGQDHTTtppsRRPVSMLFQENNLFSH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 101 LSVLDNVLLGClgrmprwRGSLALfNREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAIARALTQRAEVILADEPI 180
Cdd:PRK10771 86 LTVAQNIGLGL-------NPGLKL-NAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 181 ASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGLAQDL 240
Cdd:PRK10771 158 SALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
5-253 |
1.23e-32 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 120.12 E-value: 1.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQSSGRlngqvRRL 84
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLL---TPQSGTVFLGDKPISMLSS-----RQL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 85 RADIGYIFQQFNLVNRLSVLDNVllgCLGRMPrWrgsLALFNR---EEKQRAMAALDRVGLADLATQRASTLSGGQQQRV 161
Cdd:PRK11231 75 ARRLALLPQHHLTPEGITVRELV---AYGRSP-W---LSLWGRlsaEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 162 AIARALTQRAEVILADEPIASLDPESARRVMEILADINrSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGLAQD-L 240
Cdd:PRK11231 148 FLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELN-TQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEvM 226
|
250
....*....|...
gi 492088662 241 SKQFLNDLYGADA 253
Cdd:PRK11231 227 TPGLLRTVFDVEA 239
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
17-231 |
1.96e-32 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes 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 transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 122.27 E-value: 1.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 17 KSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREV--QSSGRLNGQVRRlraDIGYIFQQ 94
Cdd:TIGR01186 6 KKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLI---EPTAGQIFIDGENImkQSPVELREVRRK---KIGMVFQQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 95 FNLVNRLSVLDNVLLGClgrmprwrgSLALFNREE-KQRAMAALDRVGLADLATQRASTLSGGQQQRVAIARALTQRAEV 173
Cdd:TIGR01186 80 FALFPHMTILQNTSLGP---------ELLGWPEQErKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDI 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 492088662 174 ILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRI 231
Cdd:TIGR01186 151 LLMDEAFSALDPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEI 208
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-243 |
1.99e-32 |
|
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: 124.88 E-value: 1.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 4 AIHVQGLnkTFSH----KSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQssgRLNG 79
Cdd:COG4987 333 SLELEDV--SFRYpgagRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFL---DPQSGSITLGGVDLR---DLDE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 80 QvrRLRADIGYIFQQFNLVNRlSVLDNVLLGclgrmprwrgslalfnREE--KQRAMAALDRVGLADLATQ--------- 148
Cdd:COG4987 405 D--DLRRRIAVVPQRPHLFDT-TLRENLRLA----------------RPDatDEELWAALERVGLGDWLAAlpdgldtwl 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 149 --RASTLSGGQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADinRSDGKTVVVTLHQVDyAVRYCPRAVAL 226
Cdd:COG4987 466 geGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLE--ALAGRTVLLITHRLA-GLERMDRILVL 542
|
250
....*....|....*..
gi 492088662 227 KGGRIHFDGLAQDLSKQ 243
Cdd:COG4987 543 EDGRIVEQGTHEELLAQ 559
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
5-231 |
2.05e-32 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 120.97 E-value: 2.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKSALVD-LALSIQPGEMVALIGASGSGKSTLLRHLaglaycdrsN------GGQVQVLGREVQSSgrl 77
Cdd:COG1125 2 IEFENVTKRYPDGTVAVDdLSLTIPAGEFTVLVGPSGCGKTTTLRMI---------NrlieptSGRILIDGEDIRDL--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 78 ngQVRRLRADIGYIFQQFNLVNRLSVLDNV-----LLGclgrmprWrgslalfNREE-KQRAMAALDRVGL--ADLATQR 149
Cdd:COG1125 70 --DPVELRRRIGYVIQQIGLFPHMTVAENIatvprLLG-------W-------DKERiRARVDELLELVGLdpEEYRDRY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 150 ASTLSGGQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVV-VTlHQVDYAVRYCPRAVALKG 228
Cdd:COG1125 134 PHELSGGQQQRVGVARALAADPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVfVT-HDIDEALKLGDRIAVMRE 212
|
...
gi 492088662 229 GRI 231
Cdd:COG1125 213 GRI 215
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-235 |
2.21e-32 |
|
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: 118.62 E-value: 2.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKS----ALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQSSGRlngQ 80
Cdd:cd03266 2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLL---EPDAGFATVDGFDVVKEPA---E 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 81 VRRlraDIGYIFQQFNLVNRLSVLDNVllgclgrmpRWRGSLALFNREE-KQRAMAALDRVGLADLATQRASTLSGGQQQ 159
Cdd:cd03266 76 ARR---RLGFVSDSTGLYDRLTARENL---------EYFAGLYGLKGDElTARLEELADRLGMEELLDRRVGGFSTGMRQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492088662 160 RVAIARALTQRAEVILADEPIASLDPESARRVMEILADInRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDG 235
Cdd:cd03266 144 KVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-207 |
3.22e-32 |
|
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: 120.54 E-value: 3.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKSALV----DLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDRSNGGQVQVLGREVQS-SGRlng 79
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVkavdGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGITSGEILFDGEDLLKlSEK--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 80 QVRRLR-ADIGYIFQqfnlvNRLSVLDnvllgclgrmPRWR-GS-----LALFN----REEKQRAMAALDRVGLADlATQ 148
Cdd:COG0444 79 ELRKIRgREIQMIFQ-----DPMTSLN----------PVMTvGDqiaepLRIHGglskAEARERAIELLERVGLPD-PER 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492088662 149 RAS----TLSGGQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVV 207
Cdd:COG0444 143 RLDryphELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAIL 205
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
18-231 |
5.81e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 119.03 E-value: 5.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 18 SALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQSSgrlNGQVRRLRADIGYIFQqfNL 97
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGIL---KPTSGEVLIKGEPIKYD---KKSLLEVRKTVGIVFQ--NP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 98 VNRL---SVLDNVLLGCLgrmprwrgSLALFNREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAIARALTQRAEVI 174
Cdd:PRK13639 88 DDQLfapTVEEDVAFGPL--------NLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEII 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 492088662 175 LADEPIASLDPESARRVMEILADINRsDGKTVVVTLHQVDYAVRYCPRAVALKGGRI 231
Cdd:PRK13639 160 VLDEPTSGLDPMGASQIMKLLYDLNK-EGITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
17-232 |
9.00e-32 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 116.90 E-value: 9.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 17 KSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGREVQssgRL-NGQVRRLRADIGYIFQQF 95
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGI---ERPSAGKIWFSGHDIT---RLkNREVPFLRRQIGMIFQDH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 96 NLVNRLSVLDNVLLGCLgrmprwrgsLALFNREE-KQRAMAALDRVGLADLATQRASTLSGGQQQRVAIARALTQRAEVI 174
Cdd:PRK10908 89 HLLMDRTVYDNVAIPLI---------IAGASGDDiRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 492088662 175 LADEPIASLDPESARRVMEILADINRSdGKTVVVTLHQVDYAVRYCPRAVALKGGRIH 232
Cdd:PRK10908 160 LADEPTGNLDDALSEGILRLFEEFNRV-GVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
22-240 |
1.23e-31 |
|
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: 119.82 E-value: 1.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 22 DLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDRsngGQVQVLGREVQSSGR-LNGQVRRLRadIGYIFQQFNLVNR 100
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDS---GRIRLGGEVLQDSARgIFLPPHRRR--IGYVFQEARLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 101 LSVLDNVLLGclgrmpRWRGSlalfnreeKQRAMAALDRV----GLADLATQRASTLSGGQQQRVAIARALTQRAEVILA 176
Cdd:COG4148 92 LSVRGNLLYG------RKRAP--------RAERRISFDEVvellGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492088662 177 DEPIASLDPESARRVMEILADINRSDGKTVV-VTlHQVDYAVRYCPRAVALKGGRIHFDGLAQDL 240
Cdd:COG4148 158 DEPLAALDLARKAEILPYLERLRDELDIPILyVS-HSLDEVARLADHVVLLEQGRVVASGPLAEV 221
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-229 |
2.02e-31 |
|
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: 116.41 E-value: 2.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 20 LVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQSSGrlngqvrrlrADIGYIFQQFNLVN 99
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLA---QPTSGGVILEGKQITEPG----------PDRMVVFQNYSLLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 100 RLSVLDNVLLGCLGRMPRwrgslalFNREEKQRAMAA-LDRVGLADLATQRASTLSGGQQQRVAIARALTQRAEVILADE 178
Cdd:TIGR01184 68 WLTVRENIALAVDRVLPD-------LSKSERRAIVEEhIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDE 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 492088662 179 PIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGG 229
Cdd:TIGR01184 141 PFGALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
12-240 |
3.28e-31 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 117.49 E-value: 3.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 12 KTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQSsgrlngQVRRLRADIGYI 91
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLL---RPTSGTARVAGYDVVR------EPRKVRRSIGIV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 92 FQQFNLVNRLSVLDNVLL-GCLGRMPRWrgslalfnrEEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAIARALTQR 170
Cdd:TIGR01188 72 PQYASVDEDLTGRENLEMmGRLYGLPKD---------EAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 171 AEVILADEPIASLDPESARRVMEILADINrSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGLAQDL 240
Cdd:TIGR01188 143 PDVLFLDEPTTGLDPRTRRAIWDYIRALK-EEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
19-216 |
3.63e-31 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 114.44 E-value: 3.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 19 ALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQSSGRlngQVRRLRADIGYIFQqfNLV 98
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLL---RPQSGAVLIDGEPLDYSRK---GLLERRQRVGLVFQ--DPD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 99 NRL---SVLDNVLLGclgrmPRwrgSLALFNREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAIARALTQRAEVIL 175
Cdd:TIGR01166 79 DQLfaaDVDQDVAFG-----PL---NLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 492088662 176 ADEPIASLDPESARRVMEILADInRSDGKTVVVTLHQVDYA 216
Cdd:TIGR01166 151 LDEPTAGLDPAGREQMLAILRRL-RAEGMTVVISTHDVDLA 190
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
5-235 |
6.71e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 116.72 E-value: 6.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKS-----ALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGL-------------AYCDRSNGGQVQV 66
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALllpdtgtiewifkDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 67 LGREV---QSSGRLNGQVRRLRADIGYIFQ--QFNLVNRlSVLDNVLLGclgrmPRwrgSLALFNREEKQRAMAALDRVG 141
Cdd:PRK13651 83 VLEKLviqKTRFKKIKKIKEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFG-----PV---SMGVSKEEAKKRAAKYIELVG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 142 LADLATQRAS-TLSGGQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSdGKTVVVTLHQVDYAVRYC 220
Cdd:PRK13651 154 LDESYLQRSPfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWT 232
|
250
....*....|....*
gi 492088662 221 PRAVALKGGRIHFDG 235
Cdd:PRK13651 233 KRTIFFKDGKIIKDG 247
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
22-186 |
1.74e-30 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 113.35 E-value: 1.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 22 DLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDRSNGGQVQVLGREVQssgRLNGQVRRlradIGYIFQQFNLVNRL 101
Cdd:COG4136 19 PLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFSASGEVLLNGRRLT---ALPAEQRR----IGILFQDDLLFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 102 SVLDNVLLGCLGRMPRwrgslalfnREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAIARALTQRAEVILADEPIA 181
Cdd:COG4136 92 SVGENLAFALPPTIGR---------AQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFS 162
|
....*
gi 492088662 182 SLDPE 186
Cdd:COG4136 163 KLDAA 167
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-243 |
2.24e-30 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 116.36 E-value: 2.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 2 NDAIHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGREVQSSGRlngQV 81
Cdd:PRK11432 4 KNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGL---EKPTEGQIFIDGEDVTHRSI---QQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 82 RrlraDIGYIFQQFNLVNRLSVLDNVLLGClgRMprwrgsLALFNREEKQRAMAALDRVGLADLATQRASTLSGGQQQRV 161
Cdd:PRK11432 78 R----DICMVFQSYALFPHMSLGENVGYGL--KM------LGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 162 AIARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGLAQDLS 241
Cdd:PRK11432 146 ALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELY 225
|
..
gi 492088662 242 KQ 243
Cdd:PRK11432 226 RQ 227
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-231 |
4.42e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 113.47 E-value: 4.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLA--YCDRSNGGQVQVLGREVqssgrLNGQVR 82
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelYPEARVSGEVYLDGQDI-----FKMDVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 83 RLRADIGYIFQQFNLVNRLSVLDNVLLGC-LGRMPRWRgslalfnREEKQRAMAALDRVGLADLATQR----ASTLSGGQ 157
Cdd:PRK14247 79 ELRRRVQMVFQIPNPIPNLSIFENVALGLkLNRLVKSK-------KELQERVRWALEKAQLWDEVKDRldapAGKLSGGQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492088662 158 QQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSdgKTVVVTLHQVDYAVRYCPRAVALKGGRI 231
Cdd:PRK14247 152 QQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
23-250 |
5.70e-30 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 113.34 E-value: 5.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 23 LALSIQPGEMVALIGASGSGKSTLLRhlaglaycdrsnggqvqVLGR-EVQSSGR--LNGQV------RRLRADIGYIFQ 93
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLK-----------------MLGRhQPPSEGEilLDAQPleswssKAFARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 94 QFNLVNRLSVLDNVllgCLGRMPrWRGSLALFNREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAIARALTQRAEV 173
Cdd:PRK10575 93 QLPAAEGMTVRELV---AIGRYP-WHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRC 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492088662 174 ILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGLAQDLSK-QFLNDLYG 250
Cdd:PRK10575 169 LLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRgETLEQIYG 246
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
14-250 |
2.44e-29 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 112.00 E-value: 2.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 14 FSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQSSGrlNGQVRRlraDIGYIFQ 93
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLM---TPAHGHVWLDGEHIQHYA--SKEVAR---RIGLLAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 94 QFNLVNRLSVLDNVLLGCLGRMP---RWRgslalfnREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAIARALTQR 170
Cdd:PRK10253 89 NATTPGDITVQELVARGRYPHQPlftRWR-------KEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 171 AEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGLAQDL-SKQFLNDLY 249
Cdd:PRK10253 162 TAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIvTAELIERIY 241
|
.
gi 492088662 250 G 250
Cdd:PRK10253 242 G 242
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
13-231 |
2.47e-29 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 116.42 E-value: 2.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 13 TFSH---KSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaYcdRSNGGQVQVLGREVQssgrlngQVRR--LRAD 87
Cdd:COG1132 346 SFSYpgdRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRF-Y--DPTSGRILIDGVDIR-------DLTLesLRRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 88 IGYIFQQFNLVNRlSVLDNVLLGCLGrmprwrgslalFNREEKQRA--MAALDRV------GLADLATQRASTLSGGQQQ 159
Cdd:COG1132 416 IGVVPQDTFLFSG-TIRENIRYGRPD-----------ATDEEVEEAakAAQAHEFiealpdGYDTVVGERGVNLSGGQRQ 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492088662 160 RVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRsdGKTVVVTLHQVDyAVRYCPRAVALKGGRI 231
Cdd:COG1132 484 RIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLS-TIRNADRILVLDDGRI 552
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
19-235 |
2.78e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 112.25 E-value: 2.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 19 ALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQSSGRlngQVRRLRADIGYIFQQFNlv 98
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGIL---KPSSGRILFDGKPIDYSRK---GLMKLRESVGMVFQDPD-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 99 NRL---SVLDNVLLGCLgrmprwrgSLALFNREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAIARALTQRAEVIL 175
Cdd:PRK13636 93 NQLfsaSVYQDVSFGAV--------NLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 176 ADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDG 235
Cdd:PRK13636 165 LDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQG 224
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
17-231 |
2.90e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 112.23 E-value: 2.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 17 KSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQSSGRlNGQVRRLRADIGYIFQ--Q 94
Cdd:PRK13641 20 KKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALL---KPSSGTITIAGYHITPETG-NKNLKKLRKKVSLVFQfpE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 95 FNLVNRlSVLDNVLLGclgrmPRwrgSLALFNREEKQRAMAALDRVGLA-DLATQRASTLSGGQQQRVAIARALTQRAEV 173
Cdd:PRK13641 96 AQLFEN-TVLKDVEFG-----PK---NFGFSEDEAKEKALKWLKKVGLSeDLISKSPFELSGGQMRRVAIAGVMAYEPEI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 492088662 174 ILADEPIASLDPESARRVMEILADINRSdGKTVVVTLHQVDYAVRYCPRAVALKGGRI 231
Cdd:PRK13641 167 LCLDEPAAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
13-232 |
3.03e-29 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 110.04 E-value: 3.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 13 TFSHK---SALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQSSgrlngqvRRLRAdIG 89
Cdd:cd03226 6 SFSYKkgtEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLI---KESSGSILLNGKPIKAK-------ERRKS-IG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 90 YIFQ--QFNLVnRLSVLDNVLLGcLGRMPrwrgslalfnrEEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAIARAL 167
Cdd:cd03226 75 YVMQdvDYQLF-TDSVREELLLG-LKELD-----------AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492088662 168 TQRAEVILADEPIASLDPESARRVMEILADInRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIH 232
Cdd:cd03226 142 LSGKDLLIFDEPTSGLDYKNMERVGELIREL-AAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-266 |
4.63e-29 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 112.62 E-value: 4.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 4 AIHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDRsngGQVQVLGREVQSsgrlngQVRR 83
Cdd:PRK13536 41 AIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDA---GKITVLGVPVPA------RARL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 84 LRADIGYIFQQFNLVNRLSVLDNVLLgcLGRMPRwrgslaLFNREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAI 163
Cdd:PRK13536 112 ARARIGVVPQFDNLDLEFTVRENLLV--FGRYFG------MSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 164 ARALTQRAEVILADEPIASLDPESARRVMEILADInRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGLAQDLSKQ 243
Cdd:PRK13536 184 ARALINDPQLLILDEPTTGLDPHARHLIWERLRSL-LARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDE 262
|
250 260
....*....|....*....|....*...
gi 492088662 244 FLN----DLYGADADA-SLMITERSRRV 266
Cdd:PRK13536 263 HIGcqviEIYGGDPHElSSLVKPYARRI 290
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-231 |
4.93e-29 |
|
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: 109.65 E-value: 4.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGREVQssgrlngQVRRL 84
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGL---EEPTSGRIYIGGRDVT-------DLPPK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 85 RADIGYIFQQFNLVNRLSVLDNVLLGC-LGRMPRwrgslalfnREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAI 163
Cdd:cd03301 71 DRDIAMVFQNYALYPHMTVYDNIAFGLkLRKVPK---------DEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492088662 164 ARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRI 231
Cdd:cd03301 142 GRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
19-240 |
9.98e-29 |
|
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: 109.50 E-value: 9.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 19 ALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDRsngGQVQVLGREVQSSGRlngqvRRLRADIGYIFQQFNLV 98
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPEN---GRVLVDGHDLALADP-----AWLRRQVGVVLQENVLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 99 NRlSVLDNVLLGCLGrMPRWRgslalfnREEKQRAMAALD-----RVGLADLATQRASTLSGGQQQRVAIARALTQRAEV 173
Cdd:cd03252 89 NR-SIRDNIALADPG-MSMER-------VIEAAKLAGAHDfiselPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492088662 174 ILADEPIASLDPESARRVMEILADInrSDGKTVVVTLHQVDyAVRYCPRAVALKGGRIHFDGLAQDL 240
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDI--CAGRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
35-235 |
1.32e-28 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 111.05 E-value: 1.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 35 LIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGREVQssgrlngQVRRLRADIGYIFQQFNLVNRLSVLDNVLLGClgr 114
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGF---EQPDSGSIMLDGEDVT-------NVPPHLRHINMVFQSYALFPHMTVEENVAFGL--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 115 mpRWRGslaLFNREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEI 194
Cdd:TIGR01187 68 --KMRK---VPRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLE 142
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 492088662 195 LADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDG 235
Cdd:TIGR01187 143 LKTIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIG 183
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
7-240 |
1.81e-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: 108.40 E-value: 1.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 7 VQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVqvlgrevqssgRLNGQ------ 80
Cdd:cd03218 3 AENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLV---KPDSGKI-----------LLDGQditklp 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 81 -VRRLRADIGYIFQQFNLVNRLSVLDNvLLGCLGRMPrwrgslaLFNREEKQRAMAALDRVGLADLATQRASTLSGGQQQ 159
Cdd:cd03218 69 mHKRARLGIGYLPQEASIFRKLTVEEN-ILAVLEIRG-------LSKKEREEKLEELLEEFHITHLRKSKASSLSGGERR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 160 RVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSdGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGLAQD 239
Cdd:cd03218 141 RVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDR-GIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEE 219
|
.
gi 492088662 240 L 240
Cdd:cd03218 220 I 220
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
11-230 |
2.16e-28 |
|
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: 107.56 E-value: 2.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 11 NKTFSHKSA-------LVDLALSIQPGEMVALIGASGSGKSTLLRHLAGlaycdrsnggQVQVLGREVQSSGRlngqvrr 83
Cdd:cd03250 5 DASFTWDSGeqetsftLKDINLEVPKGELVAIVGPVGSGKSSLLSALLG----------ELEKLSGSVSVPGS------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 84 lradIGYIFQQFNLVNRlSVLDNVLLGclgrMPrwrgslalFNREEKQRAM--AALDRvglaDLAT----------QRAS 151
Cdd:cd03250 68 ----IAYVSQEPWIQNG-TIRENILFG----KP--------FDEERYEKVIkaCALEP----DLEIlpdgdlteigEKGI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 152 TLSGGQQQRVAIARALTQRAEVILADEPIASLDPESARRVME--ILADInrSDGKTVVVTLHQVDYaVRYCPRAVALKGG 229
Cdd:cd03250 127 NLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLL--LNNKTRILVTHQLQL-LPHADQIVVLDNG 203
|
.
gi 492088662 230 R 230
Cdd:cd03250 204 R 204
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
4-247 |
2.20e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 109.31 E-value: 2.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 4 AIHVQGLnkTFS----HKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQSSgrlng 79
Cdd:PRK13632 7 MIKVENV--SFSypnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLL---KPQSGEIKIDGITISKE----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 80 QVRRLRADIGYIFQqfNLVNR---LSVLDNVLLGCLGRMprwrgslalFNREEKQRAMAAL-DRVGLADLATQRASTLSG 155
Cdd:PRK13632 77 NLKEIRKKIGIIFQ--NPDNQfigATVEDDIAFGLENKK---------VPPKKMKDIIDDLaKKVGMEDYLDKEPQNLSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 156 GQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRyCPRAVALKGGRIhfdg 235
Cdd:PRK13632 146 GQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKL---- 220
|
250
....*....|..
gi 492088662 236 LAQDLSKQFLND 247
Cdd:PRK13632 221 IAQGKPKEILNN 232
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-246 |
3.91e-28 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 108.32 E-value: 3.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 1 MNDAI-HVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLaglaycDRSNGgqvqvLGREVQSSGRL-- 77
Cdd:PRK14239 1 MTEPIlQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSI------NRMND-----LNPEVTITGSIvy 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 78 NGQ--------VRRLRADIGYIFQQFNLVNrLSVLDNVLLGclgrmprwrgsLALFNREEKQRAMAALDR--VGLA---- 143
Cdd:PRK14239 70 NGHniysprtdTVDLRKEIGMVFQQPNPFP-MSIYENVVYG-----------LRLKGIKDKQVLDEAVEKslKGASiwde 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 144 --DLATQRASTLSGGQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILadINRSDGKTVVVTLHQVDYAVRYCP 221
Cdd:PRK14239 138 vkDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETL--LGLKDDYTMLLVTRSMQQASRISD 215
|
250 260
....*....|....*....|....*.
gi 492088662 222 R-AVALKGGRIHFDglaqDLSKQFLN 246
Cdd:PRK14239 216 RtGFFLDGDLIEYN----DTKQMFMN 237
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-228 |
4.15e-28 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 108.82 E-value: 4.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 1 MNDAIHVQGLNKTFSH-KSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQSSGRLNg 79
Cdd:PRK15056 3 QQAGIVVNDVTVTWRNgHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFV---RLASGKISILGQPTRQALQKN- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 80 qvrrlraDIGYIFQQFNLVNRLSVL--DNVLLGCLGRMprwrGSLALFNREEKQRAMAALDRVGLADLATQRASTLSGGQ 157
Cdd:PRK15056 79 -------LVAYVPQSEEVDWSFPVLveDVVMMGRYGHM----GWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492088662 158 QQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADInRSDGKTVVVTLHQVDYAVRYCPRAVALKG 228
Cdd:PRK15056 148 KKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYTVMVKG 217
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
19-212 |
4.31e-28 |
|
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: 112.38 E-value: 4.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 19 ALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQSsgrlnGQVRRLRADIGYIFQQFNLV 98
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFV---DPTEGSIAVNGVPLAD-----ADADSWRDQIAWVPQHPFLF 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 99 NRlSVLDNVLLGCLGRMPrwrgslalfnrEEKQRAM--AALDRV------GLADLATQRASTLSGGQQQRVAIARALTQR 170
Cdd:TIGR02857 409 AG-TIAENIRLARPDASD-----------AEIREALerAGLDEFvaalpqGLDTPIGEGGAGLSGGQAQRLALARAFLRD 476
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 492088662 171 AEVILADEPIASLDPESARRVMEILADInrSDGKTVVVTLHQ 212
Cdd:TIGR02857 477 APLLLLDEPTAHLDAETEAEVLEALRAL--AQGRTVLLVTHR 516
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-218 |
4.54e-28 |
|
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: 107.52 E-value: 4.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 1 MNDAIHVQGLNKTFS-HK------SALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCD------RSNGGQVQVl 67
Cdd:COG4778 1 MTTLLEVENLSKTFTlHLqggkrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDsgsilvRHDGGWVDL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 68 greVQSSGRlngQVRRLRAD-IGYIFQQFNLVNRLSVLDNV---LLGclgrmprwRGslalFNREE-KQRAMAALDRVG- 141
Cdd:COG4778 80 ---AQASPR---EILALRRRtIGYVSQFLRVIPRVSALDVVaepLLE--------RG----VDREEaRARARELLARLNl 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 142 ---LADLAtqrASTLSGGQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADInRSDGKTVVVTLHqvDYAVR 218
Cdd:COG4778 142 perLWDLP---PATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFH--DEEVR 215
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
22-240 |
4.76e-28 |
|
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: 110.20 E-value: 4.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 22 DLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQSSGR---LNGQVRRlradIGYIFQQFNLV 98
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLT---RPDEGEIVLNGRTLFDSRKgifLPPEKRR----IGYVFQEARLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 99 NRLSVLDNVLLGclgrMPRWRGSLALFNREEkqramaALDRVGLADLATQRASTLSGGQQQRVAIARALTQRAEVILADE 178
Cdd:TIGR02142 88 PHLSVRGNLRYG----MKRARPSERRISFER------VIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492088662 179 PIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGLAQDL 240
Cdd:TIGR02142 158 PLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
19-235 |
5.24e-28 |
|
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: 106.91 E-value: 5.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 19 ALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQssgRLNGQVrrLRADIGYIFQQFNLV 98
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLY---KPTSGSVLLDGTDIR---QLDPAD--LRRNIGYVPQDVTLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 99 NRlSVLDNVLLGCLgrmprwrgslalfnREEKQRAMAALDRVGLADLATQ-----------RASTLSGGQQQRVAIARAL 167
Cdd:cd03245 91 YG-TLRDNITLGAP--------------LADDERILRAAELAGVTDFVNKhpngldlqigeRGRGLSGGQRQAVALARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492088662 168 TQRAEVILADEPIASLDPESARRVMEILADINRsdGKTVVVTLHQVDyAVRYCPRAVALKGGRIHFDG 235
Cdd:cd03245 156 LNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPS-LLDLVDRIIVMDSGRIVADG 220
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-217 |
5.26e-28 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 107.86 E-value: 5.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 4 AIHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDrsnGGQVQVLGREVQSSGrlngqvrr 83
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQ---HGSITLDGKPVEGPG-------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 84 lrADIGYIFQQFNLVNRLSVLDNVLLGC-LGRMPRwrgslalfnREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVA 162
Cdd:PRK11248 70 --AERGVVFQNEGLLPWRNVQDNVAFGLqLAGVEK---------MQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVG 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 492088662 163 IARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAV 217
Cdd:PRK11248 139 IARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAV 193
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-230 |
1.71e-27 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 109.15 E-value: 1.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 1 MNDAI---------------HVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQ 65
Cdd:PRK11607 1 MNDAIprpqaktrkaltpllEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGF---EQPTAGQIM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 66 VLGREVqssgrlnGQVRRLRADIGYIFQQFNLVNRLSVLDNVLLGC-LGRMPRwrgslalfnREEKQRAMAALDRVGLAD 144
Cdd:PRK11607 78 LDGVDL-------SHVPPYQRPINMMFQSYALFPHMTVEQNIAFGLkQDKLPK---------AEIASRVNEMLGLVHMQE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 145 LATQRASTLSGGQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAV 224
Cdd:PRK11607 142 FAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIA 221
|
....*.
gi 492088662 225 ALKGGR 230
Cdd:PRK11607 222 IMNRGK 227
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-231 |
2.10e-27 |
|
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: 103.66 E-value: 2.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 7 VQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQSSGRlngqVRRLRA 86
Cdd:cd03216 3 LRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLY---KPDSGEILVDGKEVSFASP----RDARRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 87 DIGYIFQqfnlvnrlsvldnvllgclgrmprwrgslalfnreekqramaaldrvgladlatqrastLSGGQQQRVAIARA 166
Cdd:cd03216 76 GIAMVYQ-----------------------------------------------------------LSVGERQMVEIARA 96
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492088662 167 LTQRAEVILADEPIASLDPESARRVMEILADInRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRI 231
Cdd:cd03216 97 LARNARLLILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
17-243 |
2.55e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 106.71 E-value: 2.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 17 KSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYcdrSNGGQVQVLGREVQSSGrlngQVRRLRADIGYIFQqfN 96
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLI---PSEGKVYVDGLDTSDEE----NLWDIRNKAGMVFQ--N 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 97 LVNRLS---VLDNVLLGclgrmPRwrgSLALFNREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAIARALTQRAEV 173
Cdd:PRK13633 94 PDNQIVatiVEEDVAFG-----PE---NLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPEC 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 174 ILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRyCPRAVALKGGRIHFDGLAQDLSKQ 243
Cdd:PRK13633 166 IIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
5-231 |
2.57e-27 |
|
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: 105.50 E-value: 2.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKSaLVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDRsngGQVQVLGREVQSsgrLNGQVRrl 84
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDS---GKILLNGKDITN---LPPEKR-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 85 raDIGYIFQQFNLVNRLSVLDNVLLGC-LGRMPRwrgslalFNREEKQRAMAALdrVGLADLATQRASTLSGGQQQRVAI 163
Cdd:cd03299 72 --DISYVPQNYALFPHMTVYKNIAYGLkKRKVDK-------KEIERKVLEIAEM--LGIDHLLNRKPETLSGGEQQRVAI 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492088662 164 ARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRI 231
Cdd:cd03299 141 ARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
9-238 |
5.43e-27 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 109.23 E-value: 5.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 9 GLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGREVqssgRLNGQVRRLRADI 88
Cdd:PRK11288 9 GIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGN---YQPDAGSILIDGQEM----RFASTTAALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 89 GYIFQQFNLVNRLSVLDNVllgCLGRMPRWRGSLalfNREE-KQRAMAALDRVGLADLATQRASTLSGGQQQRVAIARAL 167
Cdd:PRK11288 82 AIIYQELHLVPEMTVAENL---YLGQLPHKGGIV---NRRLlNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492088662 168 TQRAEVILADEPIASLDPESARRVMEILADInRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRI--HFDGLAQ 238
Cdd:PRK11288 156 ARNARVIAFDEPTSSLSAREIEQLFRVIREL-RAEGRVILYVSHRMEEIFALCDAITVFKDGRYvaTFDDMAQ 227
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-243 |
7.67e-27 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 108.72 E-value: 7.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREV-QSSGRLNGQVrr 83
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIH---EPTKGTITINNINYnKLDHKLAAQL-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 84 lraDIGYIFQQFNLVNRLSVLDNVLlgcLGRMP--RWRGSLALFNREEKQRAMAALDRVGLADLATQRASTLSGGQQQRV 161
Cdd:PRK09700 81 ---GIGIIYQELSVIDELTVLENLY---IGRHLtkKVCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQML 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 162 AIARALTQRAEVILADEPIASLDPESARRVMEILADInRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGLAQDLS 241
Cdd:PRK09700 155 EIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQL-RKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVS 233
|
..
gi 492088662 242 KQ 243
Cdd:PRK09700 234 ND 235
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
11-243 |
1.35e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 105.20 E-value: 1.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 11 NKTFSHKsALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVlGREVQSSGRLNGQVRRLRADIGY 90
Cdd:PRK13643 14 NSPFASR-ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLL---QPTEGKVTV-GDIVVSSTSKQKEIKPVRKKVGV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 91 IFQ--QFNLVNRlSVLDNVLLGclgrmPRwrgSLALFNREEKQRAMAALDRVGLADLATQRAS-TLSGGQQQRVAIARAL 167
Cdd:PRK13643 89 VFQfpESQLFEE-TVLKDVAFG-----PQ---NFGIPKEKAEKIAAEKLEMVGLADEFWEKSPfELSGGQMRRVAIAGIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492088662 168 TQRAEVILADEPIASLDPESARRVMEILADINRSdGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGLAQDLSKQ 243
Cdd:PRK13643 160 AMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
5-240 |
1.48e-26 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 103.57 E-value: 1.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVqvlgrevqssgRLNGQV--- 81
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLV---KPDSGRI-----------FLDGEDith 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 82 ----RRLRADIGY------IFQqfnlvnRLSVLDNVLLgclgrmprwrgslAL----FNREE-KQRAMAALDRVGLADLA 146
Cdd:COG1137 70 lpmhKRARLGIGYlpqeasIFR------KLTVEDNILA-------------VLelrkLSKKErEERLEELLEEFGITHLR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 147 TQRASTLSGGQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADInRSDGKTVVVTLHQVDYAVRYCPRAVAL 226
Cdd:COG1137 131 KSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHL-KERGIGVLITDHNVRETLGICDRAYII 209
|
250
....*....|....
gi 492088662 227 KGGRIHFDGLAQDL 240
Cdd:COG1137 210 SEGKVLAEGTPEEI 223
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-234 |
2.70e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 103.63 E-value: 2.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTF-----SHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDRsngGQVQVLGREVQssgRLNg 79
Cdd:COG1101 2 LELKNLSKTFnpgtvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDS---GSILIDGKDVT---KLP- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 80 QVRRLRaDIGYIFQqfnlvN-------RLSVLDNVLLGCL-GRMPRWRGSLALFNREEKQRAMAALDRvGLADLATQRAS 151
Cdd:COG1101 75 EYKRAK-YIGRVFQ-----DpmmgtapSMTIEENLALAYRrGKRRGLRRGLTKKRRELFRELLATLGL-GLENRLDTKVG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 152 TLSGGQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRI 231
Cdd:COG1101 148 LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
...
gi 492088662 232 HFD 234
Cdd:COG1101 228 ILD 230
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
8-231 |
2.84e-26 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 103.61 E-value: 2.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 8 QGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGREVqssGRLNG-QVRRLRA 86
Cdd:PRK10419 16 GGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGL---ESPSQGNVSWRGEPL---AKLNRaQRKAFRR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 87 DIGYIFQQ-FNLVN-RLSVLDNVllgclgRMPrWRGSLALFNREEKQRAMAALDRVGLAD-LATQRASTLSGGQQQRVAI 163
Cdd:PRK10419 90 DIQMVFQDsISAVNpRKTVREII------REP-LRHLLSLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492088662 164 ARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRI 231
Cdd:PRK10419 163 ARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
15-235 |
4.96e-26 |
|
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: 101.09 E-value: 4.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 15 SHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGlaycdrsnggqvQVLGREVQSSGRLNGQ---VRRLRADIGYI 91
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAG------------RRTGLGVSGEVLINGRpldKRSFRKIIGYV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 92 FQQFNLVNRLSVLDNVLlgclgrmprwrgslalfnreekqraMAALDRVgladlatqrastLSGGQQQRVAIARALTQRA 171
Cdd:cd03213 88 PQDDILHPTLTVRETLM-------------------------FAAKLRG------------LSGGERKRVSIALELVSNP 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492088662 172 EVILADEPIASLDPESARRVMEILADInRSDGKTVVVTLHQVDYAV-RYCPRAVALKGGRIHFDG 235
Cdd:cd03213 131 SLLFLDEPTSGLDSSSALQVMSLLRRL-ADTGRTIICSIHQPSSEIfELFDKLLLLSQGRVIYFG 194
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
11-231 |
6.85e-26 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 101.48 E-value: 6.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 11 NKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYcdrsnggqvqvlgrEVQSSGRLNGQ-VRRL---RA 86
Cdd:TIGR01277 5 KVRYEYEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIE--------------PASGSIKVNDQsHTGLapyQR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 87 DIGYIFQQFNLVNRLSVLDNVLLGClgrmprwRGSLALfNREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAIARA 166
Cdd:TIGR01277 71 PVSMLFQENNLFAHLTVRQNIGLGL-------HPGLKL-NAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARC 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492088662 167 LTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRI 231
Cdd:TIGR01277 143 LVRPNPILLLDEPFSALDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
7-231 |
9.87e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 103.39 E-value: 9.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 7 VQGLNKTFSHKS-----ALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQV----LGREVQSSGRL 77
Cdd:PRK13631 24 VKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLI---KSKYGTIQVgdiyIGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 78 NGQV-------RRLRADIGYIFQ--QFNLVnRLSVLDNVLLGCLgrmprwrgSLALFNREEKQRAMAALDRVGLADLATQ 148
Cdd:PRK13631 101 TNPYskkiknfKELRRRVSMVFQfpEYQLF-KDTIEKDIMFGPV--------ALGVKKSEAKKLAKFYLNKMGLDDSYLE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 149 RAS-TLSGGQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADiNRSDGKTVVVTLHQVDYAVRYCPRAVALK 227
Cdd:PRK13631 172 RSPfGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMD 250
|
....
gi 492088662 228 GGRI 231
Cdd:PRK13631 251 KGKI 254
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-217 |
1.00e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 102.57 E-value: 1.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 2 NDAIHVQGLNKTF--SHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDRSNGGQVQVLGREVQSSgrlng 79
Cdd:PRK13640 3 DNIVEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAK----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 80 QVRRLRADIGYIFQqfNLVNRL---SVLDNVLLGCLGR-MPRwrgslalfnrEEKQRAMA-ALDRVGLADLATQRASTLS 154
Cdd:PRK13640 78 TVWDIREKVGIVFQ--NPDNQFvgaTVGDDVAFGLENRaVPR----------PEMIKIVRdVLADVGMLDYIDSEPANLS 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492088662 155 GGQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAV 217
Cdd:PRK13640 146 GGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEAN 208
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
11-235 |
1.08e-25 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 106.10 E-value: 1.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 11 NKTFSH----KSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQssgrlngQVRR--L 84
Cdd:TIGR03375 468 NVSFAYpgqeTPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLY---QPTEGSVLLDGVDIR-------QIDPadL 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 85 RADIGYIFQqfnlvnrlsvlDNVLL-GCLgrmprwRGSLALFNRE-EKQRAMAALDRVGLADLA-----------TQRAS 151
Cdd:TIGR03375 538 RRNIGYVPQ-----------DPRLFyGTL------RDNIALGAPYaDDEEILRAAELAGVTEFVrrhpdgldmqiGERGR 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 152 TLSGGQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADInrSDGKTVVVTLHQ------VDyavrycpRAVA 225
Cdd:TIGR03375 601 SLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRW--LAGKTLVLVTHRtslldlVD-------RIIV 671
|
250
....*....|
gi 492088662 226 LKGGRIHFDG 235
Cdd:TIGR03375 672 MDNGRIVADG 681
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
5-235 |
1.12e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 102.43 E-value: 1.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKS-----ALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQSSgrlNG 79
Cdd:PRK13637 3 IKIENLTHIYMEGTpfekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLL---KPTSGKIIIDGVDITDK---KV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 80 QVRRLRADIGYIFQ--QFNLVNRlSVLDNVLLGclgrmPRwrgSLALFNREEKQRAMAALDRVGLA--DLATQRASTLSG 155
Cdd:PRK13637 77 KLSDIRKKVGLVFQypEYQLFEE-TIEKDIAFG-----PI---NLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 156 GQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDG 235
Cdd:PRK13637 148 GQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQG 227
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
5-218 |
1.20e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 101.78 E-value: 1.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRhlaglayC-DRSNG--------GQVQVLGREVQSSG 75
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILR-------CfNRLNDlipgfrveGKVTFHGKNLYAPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 76 RLNGQVRRlraDIGYIFQQFNLVNRlSVLDNVLLGclGRMPRWRGSL-ALFNREEKQramAAL-DRVglADLATQRASTL 153
Cdd:PRK14243 84 VDPVEVRR---RIGMVFQKPNPFPK-SIYDNIAYG--ARINGYKGDMdELVERSLRQ---AALwDEV--KDKLKQSGLSL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492088662 154 SGGQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSdgKTVVVTLHQVDYAVR 218
Cdd:PRK14243 153 SGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAAR 215
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
4-240 |
1.21e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 102.13 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 4 AIHVQGLNKTFS-----HKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYcdrSNGGQVQVLGREVQSSGRlN 78
Cdd:PRK13649 2 GINLQNVSYTYQagtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHV---PTQGSVRVDDTLITSTSK-N 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 79 GQVRRLRADIGYIFQqF--NLVNRLSVLDNVLLGclgrmPRwrgSLALFNREEKQRAMAALDRVGLA-DLATQRASTLSG 155
Cdd:PRK13649 78 KDIKQIRKKVGLVFQ-FpeSQLFEETVLKDVAFG-----PQ---NFGVSQEEAEALAREKLALVGISeSLFEKNPFELSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 156 GQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSdGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDG 235
Cdd:PRK13649 149 GQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSG 227
|
....*
gi 492088662 236 LAQDL 240
Cdd:PRK13649 228 KPKDI 232
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
14-249 |
1.46e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 102.17 E-value: 1.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 14 FSHKsALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQSSGRlNGQVRRLRADIGYIFQ 93
Cdd:PRK13646 18 YEHQ-AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALL---KPTTGTVTVDDITITHKTK-DKYIRPVRKRIGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 94 --QFNLVNRlSVLDNVLLGclgrmPRWRGslalFNREE-KQRAMAALDRVGLA-DLATQRASTLSGGQQQRVAIARALTQ 169
Cdd:PRK13646 93 fpESQLFED-TVEREIIFG-----PKNFK----MNLDEvKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 170 RAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGLAQDL--SKQFLND 247
Cdd:PRK13646 163 NPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELfkDKKKLAD 242
|
..
gi 492088662 248 LY 249
Cdd:PRK13646 243 WH 244
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
10-200 |
1.79e-25 |
|
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: 105.15 E-value: 1.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 10 LNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdrSNGGQVQVLGREVQSSGRlnGQVRRLRADIG 89
Cdd:COG4172 292 FRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI----PSEGEIRFDGQDLDGLSR--RALRPLRRRMQ 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 90 YIFQQ-FNLVN-RLSVLDNVLLGCLGRMPRWRGslalfnREEKQRAMAALDRVGLADLATQR-ASTLSGGQQQRVAIARA 166
Cdd:COG4172 366 VVFQDpFGSLSpRMTVGQIIAEGLRVHGPGLSA------AERRARVAEALEEVGLDPAARHRyPHEFSGGQRQRIAIARA 439
|
170 180 190
....*....|....*....|....*....|....
gi 492088662 167 LTQRAEVILADEPIASLDPESARRVMEILADINR 200
Cdd:COG4172 440 LILEPKLLVLDEPTSALDVSVQAQILDLLRDLQR 473
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
7-184 |
1.90e-25 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 102.50 E-value: 1.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 7 VQGLNKTF-----------SHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGREVqssG 75
Cdd:COG4608 10 VRDLKKHFpvrgglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRL---EEPTSGEILFDGQDI---T 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 76 RLNG-QVRRLRADIGYIFQqfnlvNRLSVLDnvllgclgrmPRWR-GS-----LALFN----REEKQRAMAALDRVGL-A 143
Cdd:COG4608 84 GLSGrELRPLRRRMQMVFQ-----DPYASLN----------PRMTvGDiiaepLRIHGlaskAERRERVAELLELVGLrP 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 492088662 144 DLATQRASTLSGGQQQRVAIARALTQRAEVILADEPIASLD 184
Cdd:COG4608 149 EHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-218 |
2.19e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 101.07 E-value: 2.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 1 MNDAIHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDRSNG--GQVQVLGREVQSSGRLN 78
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARveGEVRLFGRNIYSPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 79 GQVRRlraDIGYIFQQFNLVNRLSVLDNVLLGC-LGRMPRWRGSLalfnreeKQRAMAALDRVGLADLATQR----ASTL 153
Cdd:PRK14267 81 IEVRR---EVGMVFQYPNPFPHLTIYDNVAIGVkLNGLVKSKKEL-------DERVEWALKKAALWDEVKDRlndyPSNL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492088662 154 SGGQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINrsDGKTVVVTLHQVDYAVR 218
Cdd:PRK14267 151 SGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELK--KEYTIVLVTHSPAQAAR 213
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
20-231 |
2.93e-25 |
|
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: 100.31 E-value: 2.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 20 LVDLALSIQPGEMVALIGASGSGKSTLLRHLagLAYCDrSNGGQVQVLGREVQSsgrLNgqVRRLRADIGYIFQQFNLVN 99
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLL--ERFYD-PTSGEILLDGVDIRD---LN--LRWLRSQIGLVSQEPVLFD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 100 RlSVLDNVLLGclgrmprwrgslaLFNREEKQRAMAALDR------VGLAD----LATQRASTLSGGQQQRVAIARALTQ 169
Cdd:cd03249 91 G-TIAENIRYG-------------KPDATDEEVEEAAKKAnihdfiMSLPDgydtLVGERGSQLSGGQKQRIAIARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492088662 170 RAEVILADEPIASLDPESARRVMEILADINRsdGKTVVVTLHQVDyAVRYCPRAVALKGGRI 231
Cdd:cd03249 157 NPKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLS-TIRNADLIAVLQNGQV 215
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
11-231 |
3.24e-25 |
|
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: 99.99 E-value: 3.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 11 NKTFSH---KSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaYcdRSNGGQVQVLGREVQSSGRlngqvRRLRAD 87
Cdd:cd03254 7 NVNFSYdekKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRF-Y--DPQKGQILIDGIDIRDISR-----KSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 88 IGYIFQQFNLVNRlSVLDNVLLGClgrmprwrgslalfNREEKQRAMAALDRVGLADL-----------ATQRASTLSGG 156
Cdd:cd03254 79 IGVVLQDTFLFSG-TIMENIRLGR--------------PNATDEEVIEAAKEAGAHDFimklpngydtvLGENGGNLSQG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492088662 157 QQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINrsDGKTVVVTLHQVDyAVRYCPRAVALKGGRI 231
Cdd:cd03254 144 ERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLM--KGRTSIIIAHRLS-TIKNADKILVLDDGKI 215
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
19-245 |
7.73e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 100.06 E-value: 7.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 19 ALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQSSGRLNGqVRRLradIGYIFQ--QFN 96
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLL---RPQKGKVLVSGIDTGDFSKLQG-IRKL---VGIVFQnpETQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 97 LVNRlSVLDNVLLGclgrmPRwrgSLALFNREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAIARALTQRAEVILA 176
Cdd:PRK13644 90 FVGR-TVEEDLAFG-----PE---NLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492088662 177 DEPIASLDPESARRVMEILADINRSdGKTVVVTLHQVDyAVRYCPRAVALKGGRIHFDG----LAQDLSKQFL 245
Cdd:PRK13644 161 DEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGepenVLSDVSLQTL 231
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-245 |
8.39e-25 |
|
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: 102.96 E-value: 8.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAG--------------LAYCDRSN--------GG 62
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdqyeptsgriiyhVALCEKCGyverpskvGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 63 QVQVLGREVQSS-----GRLNGQVRRLRADIGYIFQQ-FNLVNRLSVLDNVL--LGCLGrmprWRGSLALfnreekQRAM 134
Cdd:TIGR03269 81 PCPVCGGTLEPEevdfwNLSDKLRRRIRKRIAIMLQRtFALYGDDTVLDNVLeaLEEIG----YEGKEAV------GRAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 135 AALDRVGLADLATQRASTLSGGQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVD 214
Cdd:TIGR03269 151 DLIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPE 230
|
250 260 270
....*....|....*....|....*....|.
gi 492088662 215 YAVRYCPRAVALKGGRIHFDGLAQDLSKQFL 245
Cdd:TIGR03269 231 VIEDLSDKAIWLENGEIKEEGTPDEVVAVFM 261
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
11-231 |
9.39e-25 |
|
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: 98.84 E-value: 9.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 11 NKTFS---HKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLagLAYCDrSNGGQVQVLGREVQssgrlNGQVRRLRAD 87
Cdd:cd03253 5 NVTFAydpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLL--FRFYD-VSSGSILIDGQDIR-----EVTLDSLRRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 88 IGYIFQQFNLVNRlSVLDNVLLGCLGRmprwrgslalfNREEKQRA--MAALDRV------GLADLATQRASTLSGGQQQ 159
Cdd:cd03253 77 IGVVPQDTVLFND-TIGYNIRYGRPDA-----------TDEEVIEAakAAQIHDKimrfpdGYDTIVGERGLKLSGGEKQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492088662 160 RVAIARALTQRAEVILADEPIASLDPESARRVMEILADInrSDGKTVVVTLHQVDYAVRyCPRAVALKGGRI 231
Cdd:cd03253 145 RVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDV--SKGRTTIVIAHRLSTIVN-ADKIIVLKDGRI 213
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
11-212 |
1.10e-24 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 98.50 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 11 NKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDRSNGGQVQVLGREVQSsgrlnGQVRRlraDIGY 90
Cdd:cd03234 14 KNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSGQILFNGQPRKP-----DQFQK---CVAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 91 IFQQFNLVNRLSVLDNVLLGCLGRMPRwrgslaLFNREEKQR--AMAALDRVGLADLATQRASTLSGGQQQRVAIARALT 168
Cdd:cd03234 86 VRQDDILLPGLTVRETLTYTAILRLPR------KSSDAIRKKrvEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 492088662 169 QRAEVILADEPIASLDPESARRVMEILADINRSdGKTVVVTLHQ 212
Cdd:cd03234 160 WDPKVLILDEPTSGLDSFTALNLVSTLSQLARR-NRIVILTIHQ 202
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-244 |
1.22e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 100.55 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 4 AIHVQGLNKTF-----------SHKS----------ALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDrsnGG 62
Cdd:COG4586 1 IIEVENLSKTYrvyekepglkgALKGlfrreyreveAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPT---SG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 63 QVQVLGREVQSsgrlngQVRRLRADIGYIFQQfnlvnR------LSVLDN-VLLGCLGRMPrwrgslalfnREEKQRAMA 135
Cdd:COG4586 78 EVRVLGYVPFK------RRKEFARRIGVVFGQ-----RsqlwwdLPAIDSfRLLKAIYRIP----------DAEYKKRLD 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 136 AL-DRVGLADLATQRASTLSGGQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVD 214
Cdd:COG4586 137 ELvELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMD 216
|
250 260 270
....*....|....*....|....*....|
gi 492088662 215 YAVRYCPRAVALKGGRIHFDGLAQDLSKQF 244
Cdd:COG4586 217 DIEALCDRVIVIDHGRIIYDGSLEELKERF 246
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
22-231 |
1.84e-24 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 100.87 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 22 DLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycDRSNGgqvqvlgrEVQSSGRLNGQVRRLRADIGYIFQQFNLVNRL 101
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLE--DITSG--------DLFIGEKRMNDVPPAERGVGMVFQSYALYPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 102 SVLDNVLLGClgrmprwrgSLALFNREE-KQRAMAALDRVGLADLATQRASTLSGGQQQRVAIARALTQRAEVILADEPI 180
Cdd:PRK11000 91 SVAENMSFGL---------KLAGAKKEEiNQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 492088662 181 ASLDpeSARRV-MEI-LADINRSDGKTVV-VTLHQVDyAVRYCPRAVALKGGRI 231
Cdd:PRK11000 162 SNLD--AALRVqMRIeISRLHKRLGRTMIyVTHDQVE-AMTLADKIVVLDAGRV 212
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
7-211 |
1.91e-24 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 98.52 E-value: 1.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 7 VQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaYcdRSNGGQVQVLGREVQssGRLNGQVRRLra 86
Cdd:PRK11300 8 VSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGF-Y--KPTGGTILLRGQHIE--GLPGHQIARM-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 87 diGYI--FQQFNLVNRLSVLDNVL-----------LGCLGRMPRWRGSlalfNREEKQRAMAALDRVGLADLATQRASTL 153
Cdd:PRK11300 81 --GVVrtFQHVRLFREMTVIENLLvaqhqqlktglFSGLLKTPAFRRA----ESEALDRAATWLERVGLLEHANRQAGNL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 492088662 154 SGGQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLH 211
Cdd:PRK11300 155 AYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEH 212
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-214 |
2.51e-24 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 97.34 E-value: 2.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 16 HKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCdRSNGGQVQVlgrevqssgrlngqvrrlradigyifQQF 95
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKG-TPVAGCVDV--------------------------PDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 96 NLVNRLSVLDNVLLgclgrmprwRGSLALfnreekqrAMAALDRVGLADLATQRA--STLSGGQQQRVAIARALTQRAEV 173
Cdd:COG2401 95 QFGREASLIDAIGR---------KGDFKD--------AVELLNAVGLSDAVLWLRrfKELSTGQKFRFRLALLLAERPKL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 492088662 174 ILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVD 214
Cdd:COG2401 158 LVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYD 198
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
19-212 |
2.88e-24 |
|
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: 101.67 E-value: 2.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 19 ALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDrsnGGQVQVLGREVQSSgrlngQVRRLRADIGYIFQQFNLV 98
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPL---QGEVTLDGVPVSSL-----DQDEVRRRVSVCAQDAHLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 99 NRlSVLDNVLLGCLGRMPrwrgslalfnreekQRAMAALDRVGLADLA-----------TQRASTLSGGQQQRVAIARAL 167
Cdd:TIGR02868 422 DT-TVRENLRLARPDATD--------------EELWAALERVGLADWLralpdgldtvlGEGGARLSGGERQRLALARAL 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 492088662 168 TQRAEVILADEPIASLDPESARRVMEILADInrSDGKTVVVTLHQ 212
Cdd:TIGR02868 487 LADAPILLLDEPTEHLDAETADELLEDLLAA--LSGRTVVLITHH 529
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-185 |
6.32e-24 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 97.22 E-value: 6.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 1 MNDAIHVQGLNKTFSHKS---------ALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGREV 71
Cdd:COG4167 1 MSALLEVRNLSKTFKYRTglfrrqqfeAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGI---IEPTSGEILINGHKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 72 QSSgrlNGQVRRLRadIGYIFQQFN--LVNRLSV---LDNVLlgclgrmprwRGSLALFNREEKQRAMAALDRVGL-ADL 145
Cdd:COG4167 78 EYG---DYKYRCKH--IRMIFQDPNtsLNPRLNIgqiLEEPL----------RLNTDLTAEEREERIFATLRLVGLlPEH 142
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 492088662 146 ATQRASTLSGGQQQRVAIARALTQRAEVILADEPIASLDP 185
Cdd:COG4167 143 ANFYPHMLSSGQKQRVALARALILQPKIIIADEALAALDM 182
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
17-235 |
8.33e-24 |
|
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: 96.25 E-value: 8.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 17 KSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGrEVQSSGRlngqvRRLRADIGYIFQQFN 96
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLL---QPTSGEVRVAG-LVPWKRR-----KKFLRRIGVVFGQKT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 97 -LVNRLSVLDNVLLgclgrmprwrgsLALFNREEKQRAMAALDRVG----LADLATQRASTLSGGQQQRVAIARALTQRA 171
Cdd:cd03267 105 qLWWDLPVIDSFYL------------LAAIYDLPPARFKKRLDELSelldLEELLDTPVRQLSLGQRMRAEIAAALLHEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492088662 172 EVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDG 235
Cdd:cd03267 173 EILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
7-242 |
1.35e-23 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 95.67 E-value: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 7 VQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQssgRLNGQvRRLRA 86
Cdd:TIGR03410 3 VSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLL---PVKSGSIRLDGEDIT---KLPPH-ERARA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 87 DIGYIFQQFNLVNRLSVLDNVLLGclgrmprwrgsLALFNREEKQRAMAALDRVG-LADLATQRASTLSGGQQQRVAIAR 165
Cdd:TIGR03410 76 GIAYVPQGREIFPRLTVEENLLTG-----------LAALPRRSRKIPDEIYELFPvLKEMLGRRGGDLSGGQQQQLAIAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492088662 166 ALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGLAQDLSK 242
Cdd:TIGR03410 145 ALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDE 221
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
27-244 |
1.37e-23 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 99.74 E-value: 1.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 27 IQPGEMVALIGASGSGKSTLLRHLAGlaycdRSNGGQvqvlgrEVQSSGRLNGQV---RRLRADIGYIFQQFNLVNRLSV 103
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALAF-----RSPKGV------KGSGSVLLNGMPidaKEMRAISAYVQQDDLFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 104 LDNVLLGCLGRMPRwrgslALFNREEKQRAMAALDRVGLADLA------TQRASTLSGGQQQRVAIARALTQRAEVILAD 177
Cdd:TIGR00955 117 REHLMFQAHLRMPR-----RVTKKEKRERVDEVLQALGLRKCAntrigvPGRVKGLSGGERKRLAFASELLTDPPLLFCD 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492088662 178 EPIASLDPESARRVMEILADINRSdGKTVVVTLHQVDYAVrYC--PRAVALKGGRIHFDGLAQDLSKQF 244
Cdd:TIGR00955 192 EPTSGLDSFMAYSVVQVLKGLAQK-GKTIICTIHQPSSEL-FElfDKIILMAEGRVAYLGSPDQAVPFF 258
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
23-212 |
1.46e-23 |
|
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: 94.73 E-value: 1.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 23 LALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVqssgrlnGQVRRLRAD-IGYIFQQFNLVNRL 101
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLL---RPDSGEVRWNGTPL-------AEQRDEPHEnILYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 102 SVLDNVllgclgrmpRWrgsLALFNREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAIARALTQRAEVILADEPIA 181
Cdd:TIGR01189 89 SALENL---------HF---WAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180 190
....*....|....*....|....*....|..
gi 492088662 182 SLDPESARRVMEILAD-INRsdGKTVVVTLHQ 212
Cdd:TIGR01189 157 ALDKAGVALLAGLLRAhLAR--GGIVLLTTHQ 186
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
16-240 |
1.69e-23 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 96.43 E-value: 1.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 16 HKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAG-LAYCDRSNG----GQVQVLGREVQSSGRLngQVRRLRAdigY 90
Cdd:PRK13547 13 HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGAPRGarvtGDVTLNGEPLAAIDAP--RLARLRA---V 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 91 IFQQFNLVNRLSVLDNVLlgcLGRMPRWRGSLALfNREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAIARALTQ- 169
Cdd:PRK13547 88 LPQAAQPAFAFSAREIVL---LGRYPHARRAGAL-THRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQl 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492088662 170 --------RAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGLAQDL 240
Cdd:PRK13547 164 wpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-231 |
2.04e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 96.34 E-value: 2.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 1 MNDAIHVQglNKTFSHKS-----ALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDrsnGGQVQVLGREVQSSg 75
Cdd:PRK13650 1 MSNIIEVK--NLTFKYKEdqekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAE---SGQIIIDGDLLTEE- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 76 rlngQVRRLRADIGYIFQqfNLVNRL---SVLDNVLLGCLGR-MPRwrgslalfnREEKQRAMAALDRVGLADLATQRAS 151
Cdd:PRK13650 75 ----NVWDIRHKIGMVFQ--NPDNQFvgaTVEDDVAFGLENKgIPH---------EEMKERVNEALELVGMQDFKEREPA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 152 TLSGGQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDyAVRYCPRAVALKGGRI 231
Cdd:PRK13650 140 RLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLD-EVALSDRVLVMKNGQV 218
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-255 |
2.16e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 96.80 E-value: 2.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 4 AIHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDrsnGGQVQVLGREVQssgrlnGQVRR 83
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPD---AGSISLCGEPVP------SRARH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 84 LRADIGYIFQQFNLVNRLSVLDNVLLgcLGRMprwrgsLALFNREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAI 163
Cdd:PRK13537 78 ARQRVGVVPQFDNLDPDFTVRENLLV--FGRY------FGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 164 ARALTQRAEVILADEPIASLDPESARRVMEILADInRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGLAQDLSKQ 243
Cdd:PRK13537 150 ARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSL-LARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
250
....*....|....*.
gi 492088662 244 FLN----DLYGADADA 255
Cdd:PRK13537 229 EIGcdviEIYGPDPVA 244
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-252 |
2.34e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 95.15 E-value: 2.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 1 MNDAIHVQGLNKTF----------------------SHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDR 58
Cdd:COG1134 1 MSSMIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGI---LE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 59 SNGGQVQVlgrevqssgrlNGQVRRLrADIGYIFQqfnlvNRLSVLDNVLLGC--LGrmprwrgslalFNREEKQRAMaa 136
Cdd:COG1134 78 PTSGRVEV-----------NGRVSAL-LELGAGFH-----PELTGRENIYLNGrlLG-----------LSRKEIDEKF-- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 137 lDRV----GLADLATQRASTLSGGQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADInRSDGKTVVVTLHQ 212
Cdd:COG1134 128 -DEIvefaELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIREL-RESGRTVIFVSHS 205
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 492088662 213 VDYAVRYCPRAVALKGGRIHFDGLAQDLSKQFLNDLYGAD 252
Cdd:COG1134 206 MGAVRRLCDRAIWLEKGRLVMDGDPEEVIAAYEALLAGRE 245
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
20-212 |
2.44e-23 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 94.17 E-value: 2.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 20 LVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQSSgrlngqvrRLRADIGYIFQQFNLVN 99
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLL---PPAAGTIKLDGGDIDDP--------DVAEACHYLGHRNAMKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 100 RLSVLDNVLLgclgrmprWRGslalFNREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAIARALTQRAEVILADEP 179
Cdd:PRK13539 87 ALTVAENLEF--------WAA----FLGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEP 154
|
170 180 190
....*....|....*....|....*....|...
gi 492088662 180 IASLDPESARRVMEILADiNRSDGKTVVVTLHQ 212
Cdd:PRK13539 155 TAALDAAAVALFAELIRA-HLAQGGIVIAATHI 186
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
22-212 |
2.89e-23 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 94.10 E-value: 2.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 22 DLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDrsnGGQVqvlgrevqssgRLNGQ-VRRLR----ADIGYIFQQFN 96
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPD---AGEV-----------LWQGEpIRRQRdeyhQDLLYLGHQPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 97 LVNRLSVLDNVllgclgrmpRWrgSLALFNREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAIAR-ALTQRAEVIL 175
Cdd:PRK13538 85 IKTELTALENL---------RF--YQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARlWLTRAPLWIL 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 492088662 176 aDEPIASLDPESARRVMEILADiNRSDGKTVVVTLHQ 212
Cdd:PRK13538 154 -DEPFTAIDKQGVARLEALLAQ-HAEQGGMVILTTHQ 188
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
8-214 |
4.63e-23 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 98.08 E-value: 4.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 8 QGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaYCDRSNGGQVQVLGREVQSSGrlngqVRRL-RA 86
Cdd:PRK13549 9 KNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHGTYEGEIIFEGEELQASN-----IRDTeRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 87 DIGYIFQQFNLVNRLSVLDNVLLGC----LGRMPrwrgslalFNrEEKQRAMAALDRVGLADLATQRASTLSGGQQQRVA 162
Cdd:PRK13549 83 GIAIIHQELALVKELSVLENIFLGNeitpGGIMD--------YD-AMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVE 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 492088662 163 IARALTQRAEVILADEPIASLDPESARRVMEILADInRSDGKTVVVTLHQVD 214
Cdd:PRK13549 154 IAKALNKQARLLILDEPTASLTESETAVLLDIIRDL-KAHGIACIYISHKLN 204
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
20-231 |
8.00e-23 |
|
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: 91.89 E-value: 8.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 20 LVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQSSGRLNgqvrrLRADIGYIFQQFNLVN 99
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLL---RPTSGRVRLDGADISQWDPNE-----LGDHVGYLPQDDELFS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 100 RlSVLDNVllgclgrmprwrgslalfnreekqramaaldrvgladlatqrastLSGGQQQRVAIARALTQRAEVILADEP 179
Cdd:cd03246 90 G-SIAENI---------------------------------------------LSGGQRQRLGLARALYGNPRILVLDEP 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 492088662 180 IASLDPESARRVMEILADInRSDGKTVVVTLHQVDyAVRYCPRAVALKGGRI 231
Cdd:cd03246 124 NSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPE-TLASADRILVLEDGRV 173
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-188 |
8.15e-23 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 97.38 E-value: 8.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 1 MNDAIHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDrsnGGQVQVLGREVQSSGRLNGQ 80
Cdd:PRK10762 1 MQALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRD---AGSILYLGKEVTFNGPKSSQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 81 vrrlRADIGYIFQQFNLVNRLSVLDNVLLG-----CLGRMpRWrgslalfnREEKQRAMAALDRVGLADLATQRASTLSG 155
Cdd:PRK10762 78 ----EAGIGIIHQELNLIPQLTIAENIFLGrefvnRFGRI-DW--------KKMYAEADKLLARLNLRFSSDKLVGELSI 144
|
170 180 190
....*....|....*....|....*....|....
gi 492088662 156 GQQQRVAIARALTQRAEVILADEPIASL-DPESA 188
Cdd:PRK10762 145 GEQQMVEIAKVLSFESKVIIMDEPTDALtDTETE 178
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-240 |
1.02e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 94.39 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 4 AIHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycDRSNG----GQVQVLGREVQSSGrlng 79
Cdd:PRK14271 21 AMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMN--DKVSGyrysGDVLLGGRSIFNYR---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 80 QVRRLRADIGYIFQQFNLVNrLSVLDNVLLGClgrmprwRGSLALFNREEKQRAMAALDRVGLADLATQRAST----LSG 155
Cdd:PRK14271 95 DVLEFRRRVGMLFQRPNPFP-MSIMDNVLAGV-------RAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDspfrLSG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 156 GQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADInrSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDG 235
Cdd:PRK14271 167 GQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSL--ADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEG 244
|
....*
gi 492088662 236 LAQDL 240
Cdd:PRK14271 245 PTEQL 249
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-230 |
1.61e-22 |
|
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: 96.43 E-value: 1.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaYCDRSNGGQVQVLGREVQSSGRLNGQvrrl 84
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHGTWDGEIYWSGSPLKASNIRDTE---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 85 RADIGYIFQQFNLVNRLSVLDNVLLGCLGRMPRWRGSLALFNReekqRAMAALDRVGL-ADLATQRASTLSGGQQQRVAI 163
Cdd:TIGR02633 77 RAGIVIIHQELTLVPELSVAENIFLGNEITLPGGRMAYNAMYL----RAKNLLRELQLdADNVTRPVGDYGGGQQQLVEI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492088662 164 ARALTQRAEVILADEPIASLDPESARRVMEILADINRSdGKTVVVTLHQVDYAVRYCPRAVALKGGR 230
Cdd:TIGR02633 153 AKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
23-243 |
1.69e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 96.45 E-value: 1.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 23 LALSIQPGEMVALIGASGSGKSTLLRHLAG-LAYcdrsnggqvqvlgrevQSSGRLNGQ-VRRL-----RADIGYIFQQF 95
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGfLPY----------------QGSLKINGIeLRELdpeswRKHLSWVGQNP 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 96 NLVNRlSVLDNVLLGclgrmprwRGSLAlfnreeKQRAMAALDRVGLAD--------LATQ---RASTLSGGQQQRVAIA 164
Cdd:PRK11174 433 QLPHG-TLRDNVLLG--------NPDAS------DEQLQQALENAWVSEflpllpqgLDTPigdQAAGLSVGQAQRLALA 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492088662 165 RALTQRAEVILADEPIASLDPESARRVMEILADInrSDGKTVVVTLHQVDyAVRYCPRAVALKGGRIHFDGLAQDLSKQ 243
Cdd:PRK11174 498 RALLQPCQLLLLDEPTASLDAHSEQLVMQALNAA--SRRQTTLMVTHQLE-DLAQWDQIWVMQDGQIVQQGDYAELSQA 573
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
22-247 |
2.74e-22 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 95.10 E-value: 2.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 22 DLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDRsngGQVQVLGREVQSSGrlNGQVRRLR-ADIGYIFQQFNLVNR 100
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTR---GQVLIDGVDIAKIS--DAELREVRrKKIAMVFQSFALMPH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 101 LSVLDNVLLGClgrmprwrgSLALFNREEKQ-RAMAALDRVGLADLATQRASTLSGGQQQRVAIARALTQRAEVILADEP 179
Cdd:PRK10070 121 MTVLDNTAFGM---------ELAGINAEERReKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEA 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492088662 180 IASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGLAQDLSKQFLND 247
Cdd:PRK10070 192 FSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAND 259
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-213 |
3.29e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 92.79 E-value: 3.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 4 AIHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDrsngGQVQVLGReVQSSG------RL 77
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE----SEVRVEGR-VEFFNqniyerRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 78 NgqVRRLRADIGYIFQQFNLVNrLSVLDNVLLGClgRMPRWRGSLALFNREEkqramAALDRVGLADLATQR----ASTL 153
Cdd:PRK14258 82 N--LNRLRRQVSMVHPKPNLFP-MSVYDNVAYGV--KIVGWRPKLEIDDIVE-----SALKDADLWDEIKHKihksALDL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492088662 154 SGGQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADIN-RSDGKTVVVT--LHQV 213
Cdd:PRK14258 152 SGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVShnLHQV 214
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
11-235 |
6.27e-22 |
|
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: 89.68 E-value: 6.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 11 NKTFSH----KSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGlAYcdRSNGGQVQVLGREVQSsgrLNGQVRRLra 86
Cdd:cd03247 5 NVSFSYpeqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTG-DL--KPQQGEITLDGVPVSD---LEKALSSL-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 87 dIGYIFQQFNLVNRlSVLDNvllgcLGRmprwrgslalfnreekqramaaldrvgladlatqrasTLSGGQQQRVAIARA 166
Cdd:cd03247 77 -ISVLNQRPYLFDT-TLRNN-----LGR-------------------------------------RFSGGERQRLALARI 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492088662 167 LTQRAEVILADEPIASLDPESARRVMEILADINRsdGKTVVVTLHQVDyAVRYCPRAVALKGGRIHFDG 235
Cdd:cd03247 113 LLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLT-GIEHMDKILFLENGKIIMQG 178
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
8-240 |
1.97e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 89.95 E-value: 1.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 8 QGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDrsnGGQVqVLGREVQSSGRLNGQVRRlraD 87
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRD---AGNI-IIDDEDISLLPLHARARR---G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 88 IGYIFQQFNLVNRLSVLDNvLLGCLgrmpRWRGSLALFNREEkqRAMAALDRVGLADLATQRASTLSGGQQQRVAIARAL 167
Cdd:PRK10895 80 IGYLPQEASIFRRLSVYDN-LMAVL----QIRDDLSAEQRED--RANELMEEFHIEHLRDSMGQSLSGGERRRVEIARAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492088662 168 TQRAEVILADEPIASLDPESARRVMEILADInRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGLAQDL 240
Cdd:PRK10895 153 AANPKFILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-197 |
2.10e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 93.33 E-value: 2.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 2 NDAIHVQGLNKTFSHKSALV-DLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycdrsnggqvqvlgrevQSSGRlnGQ 80
Cdd:COG4178 360 DGALALEDLTLRTPDGRPLLeDLSLSLKPGERLLITGPSGSGKSTLLRAIAGL------------------WPYGS--GR 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 81 VRRLRadigyifqqfnlvnrlsvLDNVL---------LGCLgrmprwRGSLALFNREEK---QRAMAALDRVGLADLATQ 148
Cdd:COG4178 420 IARPA------------------GARVLflpqrpylpLGTL------REALLYPATAEAfsdAELREALEAVGLGHLAER 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 492088662 149 ------RASTLSGGQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILAD 197
Cdd:COG4178 476 ldeeadWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE 530
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
6-265 |
4.32e-21 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 92.33 E-value: 4.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 6 HVQGLNKTFSH---KSALVDLALSIQPGEMVALIGASGSGKSTLLrHLAGLAYCDRSngGQVQVLGREVQSSGRlngqvR 82
Cdd:PRK13657 334 AVEFDDVSFSYdnsRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLI-NLLQRVFDPQS--GRILIDGTDIRTVTR-----A 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 83 RLRADIGYIFQQFNLVNRlSVLDNVLLGCLGRMPrwrgslalfnrEEKQRAM---AALDRV-----GLADLATQRASTLS 154
Cdd:PRK13657 406 SLRRNIAVVFQDAGLFNR-SIEDNIRVGRPDATD-----------EEMRAAAeraQAHDFIerkpdGYDTVVGERGRQLS 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 155 GGQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRsdGKTVVVTLHQVDyAVRYCPRAVALKGGRI--- 231
Cdd:PRK13657 474 GGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLS-TVRNADRILVFDNGRVves 550
|
250 260 270
....*....|....*....|....*....|....*
gi 492088662 232 -HFDGLAQdlskqfLNDLYGADADASLMITERSRR 265
Cdd:PRK13657 551 gSFDELVA------RGGRFAALLRAQGMLQEDERR 579
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-231 |
5.23e-21 |
|
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: 87.49 E-value: 5.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 7 VQGLnktfSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGREVqssgRLNGQVRRLRA 86
Cdd:cd03215 7 VRGL----SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGL---RPPASGEITLDGKPV----TRRSPRDAIRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 87 DIGYI---FQQFNLVNRLSVLDNVLLGCLgrmprwrgslalfnreekqramaaldrvgladlatqrastLSGGQQQRVAI 163
Cdd:cd03215 76 GIAYVpedRKREGLVLDLSVAENIALSSL----------------------------------------LSGGNQQKVVL 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492088662 164 ARALTQRAEVILADEPIASLDPESARRVMEILADInRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRI 231
Cdd:cd03215 116 ARWLARDPRVLILDEPTRGVDVGAKAEIYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-179 |
5.85e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.05 E-value: 5.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 7 VQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVlgrevqssgrlNGQVRrlra 86
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGE---LEPDSGEVSI-----------PKGLR---- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 87 dIGYIFQQFNLVNRLSVLDNVLLGCLGR---MPRWRGSLALFNREEK---------------------QRAMAALDRVGL 142
Cdd:COG0488 63 -IGYLPQEPPLDDDLTVLDTVLDGDAELralEAELEELEAKLAEPDEdlerlaelqeefealggweaeARAEEILSGLGF 141
|
170 180 190
....*....|....*....|....*....|....*...
gi 492088662 143 -ADLATQRASTLSGGQQQRVAIARALTQRAEVILADEP 179
Cdd:COG0488 142 pEEDLDRPVSELSGGWRRRVALARALLSEPDLLLLDEP 179
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
19-239 |
9.33e-21 |
|
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: 91.70 E-value: 9.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 19 ALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDrsnGGQVQVLGREVQSSgrlngQVRRLRADIGYIFQQFNLV 98
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPD---SGQILLDGHDLADY-----TLASLRRQVALVSQDVVLF 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 99 NRlSVLDNVLLGCLGRMPRWRGSLALfnreEKQRAMAALDRV--GLADLATQRASTLSGGQQQRVAIARALTQRAEVILA 176
Cdd:TIGR02203 419 ND-TIANNIAYGRTEQADRAEIERAL----AAAYAQDFVDKLplGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILIL 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492088662 177 DEPIASLDPESARRVMEILADINRsdGKTVVVTLHQVDyAVRYCPRAVALKGGRI-----HFDGLAQD 239
Cdd:TIGR02203 494 DEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLS-TIEKADRIVVMDDGRIvergtHNELLARN 558
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
20-252 |
1.93e-20 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 87.59 E-value: 1.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 20 LVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdrSNGGQVQVLGREVQS-SGRlngQVRRLRAdigYIFQQFNlv 98
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL----PGQGEILLNGRPLSDwSAA---ELARHRA---YLSQQQS-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 99 nrlsvldnvllgCLGRMPRWRgSLALF-----NREEKQRAMAAL-DRVGLADLATQRASTLSGGQQQRVAIARALTQ--- 169
Cdd:COG4138 80 ------------PPFAMPVFQ-YLALHqpagaSSEAVEQLLAQLaEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwp 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 170 ----RAEVILADEPIASLD--PESA--RRVMEILAdinrsDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGLAQD-L 240
Cdd:COG4138 147 tinpEGQLLLLDEPMNSLDvaQQAAldRLLRELCQ-----QGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEvM 221
|
250
....*....|..
gi 492088662 241 SKQFLNDLYGAD 252
Cdd:COG4138 222 TPENLSEVFGVK 233
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
7-231 |
2.31e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 90.08 E-value: 2.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 7 VQGLnktfSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGREVqssgRLNGQVRRLRA 86
Cdd:COG1129 259 VEGL----SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGA---DPADSGEIRLDGKPV----RIRSPRDAIRA 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 87 DIGYI---FQQFNLVNRLSVLDNVLLGCLGRMPRWRgslALFNREEKQRAMAALDRVGL-ADLATQRASTLSGGQQQRVA 162
Cdd:COG1129 328 GIAYVpedRKGEGLVLDLSIRENITLASLDRLSRGG---LLDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVV 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492088662 163 IARALTQRAEVILADEPIASLDPeSARRvmEILADINR--SDGKTVVVT---LHQVdyaVRYCPRAVALKGGRI 231
Cdd:COG1129 405 LAKWLATDPKVLILDEPTRGIDV-GAKA--EIYRLIRElaAEGKAVIVIsseLPEL---LGLSDRILVMREGRI 472
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
16-235 |
2.81e-20 |
|
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: 86.43 E-value: 2.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 16 HKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGRevqSSGRLngqvrrlraDIGYIFQqf 95
Cdd:cd03220 34 EFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGI---YPPDSGTVTVRGR---VSSLL---------GLGGGFN-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 96 nlvNRLSVLDNVLLGClgrmpRWRGslalFNREEKQRAMAA-LDRVGLADLATQRASTLSGGQQQRVAIARALTQRAEVI 174
Cdd:cd03220 97 ---PELTGRENIYLNG-----RLLG----LSRKEIDEKIDEiIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492088662 175 LADEPIASLDPESARRVMEILADInRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDG 235
Cdd:cd03220 165 LIDEVLAVGDAAFQEKCQRRLREL-LKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-231 |
3.11e-20 |
|
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: 89.74 E-value: 3.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 19 ALVDLALSIQPGEMVALIGASGSGKS----TLLRhLagLAYCDRSNGGQVQVLGREVQSSGRlnGQVRRLR-ADIGYIFQ 93
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSvtalSILR-L--LPDPAAHPSGSILFDGQDLLGLSE--RELRRIRgNRIAMIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 94 --------------QFNLVNRLSvldnvllgclGRMPRwrgslalfnREEKQRAMAALDRVGLADlATQRAST----LSG 155
Cdd:COG4172 100 epmtslnplhtigkQIAEVLRLH----------RGLSG---------AAARARALELLERVGIPD-PERRLDAyphqLSG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492088662 156 GQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHqvDYAV--RYCPRAVALKGGRI 231
Cdd:COG4172 160 GQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITH--DLGVvrRFADRVAVMRQGEI 235
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
17-239 |
4.20e-20 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 86.52 E-value: 4.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 17 KSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAglAYCDRSNGgQVQVLGREVQSSgrlngQVRRLRADIGYIFQQFN 96
Cdd:cd03251 15 PPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIP--RFYDVDSG-RILIDGHDVRDY-----TLASLRRQIGLVSQDVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 97 LVNRlSVLDNVLLGCLGRmprwrgslalfNREEKQRA--MAALDRV------GLADLATQRASTLSGGQQQRVAIARALT 168
Cdd:cd03251 87 LFND-TVAENIAYGRPGA-----------TREEVEEAarAANAHEFimelpeGYDTVIGERGVKLSGGQRQRIAIARALL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492088662 169 QRAEVILADEPIASLDPESARRVMEILADInrSDGKTVVVTLHQVDyAVRYCPRAVALKGGRI-----HFDGLAQD 239
Cdd:cd03251 155 KDPPILILDEATSALDTESERLVQAALERL--MKNRTTFVIAHRLS-TIENADRIVVLEDGKIvergtHEELLAQG 227
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
33-243 |
6.19e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 86.78 E-value: 6.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 33 VALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQSSgrlngQVRRLRADIGYIFQQFN-LVNRLSVLDNVLLGC 111
Cdd:PRK13652 33 IAVIGPNGAGKSTLFRHFNGIL---KPTSGSVLIRGEPITKE-----NIREVRKFVGLVFQNPDdQIFSPTVEQDIAFGP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 112 LgrmprwrgSLALFNREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAIARALTQRAEVILADEPIASLDPESARRV 191
Cdd:PRK13652 105 I--------NLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKEL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 492088662 192 MEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGLAQDLSKQ 243
Cdd:PRK13652 177 IDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-231 |
8.39e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 86.30 E-value: 8.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 1 MNDAIHVQGLNKTFSHKSALVDL---ALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQSSGRL 77
Cdd:PRK13642 1 MNKILEVENLVFKYEKESDVNQLngvSFSITKGEWVSIIGQNGSGKSTTARLIDGLF---EEFEGKVKIDGELLTAENVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 78 NgqvrrLRADIGYIFQqfNLVNRL---SVLDNVLLGCLGR-MPRwrgslalfnREEKQRAMAALDRVGLADLATQRASTL 153
Cdd:PRK13642 78 N-----LRRKIGMVFQ--NPDNQFvgaTVEDDVAFGMENQgIPR---------EEMIKRVDEALLAVNMLDFKTREPARL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492088662 154 SGGQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRyCPRAVALKGGRI 231
Cdd:PRK13642 142 SGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEI 218
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
15-239 |
1.99e-19 |
|
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: 87.50 E-value: 1.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 15 SHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQSSGRlngqvRRLRADIGYIFQQ 94
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVW---PPTAGSVRLDGADLSQWDR-----EELGRHIGYLPQD 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 95 FNLVNRlSVLDNVllgclgrmprwrgslALFNREEKQRAMAALDRVGLADL--------ATQ---RASTLSGGQQQRVAI 163
Cdd:COG4618 415 VELFDG-TIAENI---------------ARFGDADPEKVVAAAKLAGVHEMilrlpdgyDTRigeGGARLSGGQRQRIGL 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492088662 164 ARALTQRAEVILADEPIASLDPESARRVMEILADInRSDGKTVVVTLHQVDyAVRYCPRAVALKGGRIHFDGLAQD 239
Cdd:COG4618 479 ARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDE 552
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-231 |
2.38e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 84.71 E-value: 2.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 3 DAIHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDRSN---GGQVQVLGREVqssgrLNG 79
Cdd:PRK14246 9 DVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKikvDGKVLYFGKDI-----FQI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 80 QVRRLRADIGYIFQQFNLVNRLSVLDNVLLGCLGRMPRWRgslalfnREEKQRAMAALDRVGL----ADLATQRASTLSG 155
Cdd:PRK14246 84 DAIKLRKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEK-------REIKKIVEECLRKVGLwkevYDRLNSPASQLSG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492088662 156 GQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSdgKTVVVTLHQVDYAVRYCPRAVALKGGRI 231
Cdd:PRK14246 157 GQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
15-211 |
4.27e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 86.80 E-value: 4.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 15 SHKSALVDLALSIQPGEMVALIGASGSGKSTLLrhlaglaycdrsnggqvQVLGREVQ-SSG--RLNGQV------RRLR 85
Cdd:PRK11160 351 QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLL-----------------QLLTRAWDpQQGeiLLNGQPiadyseAALR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 86 ADIGYIFQQFNLVNRlSVLDNVLLGClgrmprwrgslalfNREEKQRAMAALDRVGLADLATQRAS----------TLSG 155
Cdd:PRK11160 414 QAISVVSQRVHLFSA-TLRDNLLLAA--------------PNASDEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSG 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 492088662 156 GQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADInrSDGKTVVVTLH 211
Cdd:PRK11160 479 GEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEH--AQNKTVLMITH 532
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
13-231 |
4.94e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 84.67 E-value: 4.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 13 TFSHKS-----ALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYcdrSNGGQVQVLGREVQSSGRLNGQVRRLRAD 87
Cdd:PRK13645 15 TYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLII---SETGQTIVGDYAIPANLKKIKEVKRLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 88 IGYIFQ--QFNLVNRlSVLDNVLLGclgrmPRWRGSlalfNREEKQRAMAAL-DRVGLA-DLATQRASTLSGGQQQRVAI 163
Cdd:PRK13645 92 IGLVFQfpEYQLFQE-TIEKDIAFG-----PVNLGE----NKQEAYKKVPELlKLVQLPeDYVKRSPFELSGGQKRRVAL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492088662 164 ARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRI 231
Cdd:PRK13645 162 AGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKV 229
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
10-184 |
1.04e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 85.53 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 10 LNKTFSHKSALVDLALSIQPGEMVALIGASGSGKST----LLRHLAglaycdrsNGGQVQVLGREVQSSGRlnGQVRRLR 85
Cdd:PRK15134 292 LKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN--------SQGEIWFDGQPLHNLNR--RQLLPVR 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 86 ADIGYIFQQFN--LVNRLSVLDNVLLGCLGRMPrwrgslALFNREEKQRAMAALDRVGLADLATQR-ASTLSGGQQQRVA 162
Cdd:PRK15134 362 HRIQVVFQDPNssLNPRLNVLQIIEEGLRVHQP------TLSAAQREQQVIAVMEEVGLDPETRHRyPAEFSGGQRQRIA 435
|
170 180
....*....|....*....|..
gi 492088662 163 IARALTQRAEVILADEPIASLD 184
Cdd:PRK15134 436 IARALILKPSLIILDEPTSSLD 457
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-217 |
1.16e-18 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 83.99 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 19 ALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQssGRLNGQVRRLRADIGYIFQQ--FN 96
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLV---KATDGEVAWLGKDLL--GMKDDEWRAVRSDIQMIFQDplAS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 97 LVNRLSVLDNV---LLGCLGRMPRwrgslalfnREEKQRAMAALDRVGL-ADLATQRASTLSGGQQQRVAIARALTQRAE 172
Cdd:PRK15079 111 LNPRMTIGEIIaepLRTYHPKLSR---------QEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 492088662 173 VILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHqvDYAV 217
Cdd:PRK15079 182 LIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAH--DLAV 224
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
11-211 |
1.31e-18 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 85.07 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 11 NKTFSH----KSALVDLALSIQPGEMVALIGASGSGKSTLLrHLAGLAYcdRSNGGQVQVLGREVQSSgrlngQVRRLRA 86
Cdd:PRK11176 346 NVTFTYpgkeVPALRNINFKIPAGKTVALVGRSGSGKSTIA-NLLTRFY--DIDEGEILLDGHDLRDY-----TLASLRN 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 87 DIGYIFQQFNLVNRlSVLDNVLLGCLGRmprwrgslalFNREEKQRA--MA-ALDRV-----GLADLATQRASTLSGGQQ 158
Cdd:PRK11176 418 QVALVSQNVHLFND-TIANNIAYARTEQ----------YSREQIEEAarMAyAMDFInkmdnGLDTVIGENGVLLSGGQR 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 492088662 159 QRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSdgKTVVVTLH 211
Cdd:PRK11176 487 QRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKN--RTSLVIAH 537
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
19-231 |
1.33e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 85.24 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 19 ALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQV-LGRE-VQSSGRlnGQVRRLRAD--IGYIFQQ 94
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVL---EPTSGEVNVrVGDEwVDMTKP--GPDGRGRAKryIGILHQE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 95 FNLVNRLSVLDNVLLGClgrmprwrgSLALFNREEKQRAMAALDRVGLAD-----LATQRASTLSGGQQQRVAIARALTQ 169
Cdd:TIGR03269 374 YDLYPHRTVLDNLTEAI---------GLELPDELARMKAVITLKMVGFDEekaeeILDKYPDELSEGERHRVALAQVLIK 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492088662 170 RAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRI 231
Cdd:TIGR03269 445 EPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
19-231 |
1.33e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 82.23 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 19 ALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREV---QSSgrlngqvRRLRADIGYIFQQF 95
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDP---RATSGRIVFDGKDItdwQTA-------KIMREAVAIVPEGR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 96 NLVNRLSVLDNVLLGclgrmprwrGSLAlfnreEKQRAMAALDRV-----GLADLATQRASTLSGGQQQRVAIARALTQR 170
Cdd:PRK11614 90 RVFSRMTVEENLAMG---------GFFA-----ERDQFQERIKWVyelfpRLHERRIQRAGTMSGGEQQMLAIGRALMSQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492088662 171 AEVILADEPIASLDPESARRVMEILADInRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRI 231
Cdd:PRK11614 156 PRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
6-231 |
1.48e-18 |
|
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: 82.13 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 6 HVQGLNKTFS-----HKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQSSgrlngQ 80
Cdd:cd03248 11 IVKFQNVTFAyptrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFY---QPQGGQVLLDGKPISQY-----E 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 81 VRRLRADIGYIFQQFNLVNRlSVLDNVLLGcLGRMPRWRgslalfNREEKQRAMAALDRVGLAD----LATQRASTLSGG 156
Cdd:cd03248 83 HKYLHSKVSLVGQEPVLFAR-SLQDNIAYG-LQSCSFEC------VKEAAQKAHAHSFISELASgydtEVGEKGSQLSGG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492088662 157 QQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSdgKTVVVTLHQVDyAVRYCPRAVALKGGRI 231
Cdd:cd03248 155 QKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPER--RTVLVIAHRLS-TVERADQILVLDGGRI 226
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
5-246 |
1.98e-18 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 82.51 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDRsngGQVQVLGREVQSSGRlnGQVRRL 84
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDH---GEILFDGENIPAMSR--SRLYTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 85 RADIGYIFQQFNLVNRLSVLDNVllgclgrmprwrgslALFNREEKQ--------RAMAALDRVGLADLATQRASTLSGG 156
Cdd:PRK11831 83 RKRMSMLFQSGALFTDMNVFDNV---------------AYPLREHTQlpapllhsTVMMKLEAVGLRGAAKLMPSELSGG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 157 QQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGL 236
Cdd:PRK11831 148 MARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGS 227
|
250
....*....|....*..
gi 492088662 237 AQDLS-------KQFLN 246
Cdd:PRK11831 228 AQALQanpdprvRQFLD 244
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
19-208 |
2.41e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 84.31 E-value: 2.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 19 ALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGREVQSSGRLngqvRRLRADIGYI---FQQF 95
Cdd:COG3845 273 ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGL---RPPASGSIRLDGEDITGLSPR----ERRRLGVAYIpedRLGR 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 96 NLVNRLSVLDNVLLGCLGRMPRWRGSLALFNREEK--QRAMAALD-RVGLADlatQRASTLSGGQQQRVAIARALTQRAE 172
Cdd:COG3845 346 GLVPDMSVAENLILGRYRRPPFSRGGFLDRKAIRAfaEELIEEFDvRTPGPD---TPARSLSGGNQQKVILARELSRDPK 422
|
170 180 190
....*....|....*....|....*....|....*.
gi 492088662 173 VILADEPIASLDPESARRVMEILADInRSDGKTVVV 208
Cdd:COG3845 423 LLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLL 457
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
13-209 |
2.68e-18 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 81.05 E-value: 2.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 13 TFSHKSALV--DLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQSSGRLNgqvrrlraDIGY 90
Cdd:PRK13543 18 AFSRNEEPVfgPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLL---HVESGQIQIDGKTATRGDRSR--------FMAY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 91 IFQQFNLVNRLSVLDNVLLGClgrmprwrgslALFNREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAIARALTQR 170
Cdd:PRK13543 87 LGHLPGLKADLSTLENLHFLC-----------GLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSP 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 492088662 171 AEVILADEPIASLDPESARRVMEILADINRSDGKTVVVT 209
Cdd:PRK13543 156 APLWLLDEPYANLDLEGITLVNRMISAHLRGGGAALVTT 194
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
23-212 |
4.57e-18 |
|
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: 80.23 E-value: 4.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 23 LALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdrsnggqvQVLGREVQSSGRLNGQVR-RLRADIGYIFQQFNLVNRL 101
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLS----------PPLAGRVLLNGGPLDFQRdSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 102 SVLDNVllgclgrmpRWrgsLALFNREEKqrAMAALDRVGLADLATQRASTLSGGQQQRVAIARALTQRAEVILADEPIA 181
Cdd:cd03231 89 SVLENL---------RF---WHADHSDEQ--VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170 180 190
....*....|....*....|....*....|.
gi 492088662 182 SLDPESARRVMEILADiNRSDGKTVVVTLHQ 212
Cdd:cd03231 155 ALDKAGVARFAEAMAG-HCARGGMVVLTTHQ 184
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
7-249 |
6.43e-18 |
|
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: 83.52 E-value: 6.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 7 VQGLNKTF--SHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQSSgrlngqVRRL 84
Cdd:TIGR01257 931 VKNLVKIFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLL---PPTSGTVLVGGKDIETN------LDAV 1001
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 85 RADIGYIFQQFNLVNRLSVLDNVLLGCLGRMPRWrgslalfnrEEKQRAMAA-LDRVGLADLATQRASTLSGGQQQRVAI 163
Cdd:TIGR01257 1002 RQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSW---------EEAQLEMEAmLEDTGLHHKRNEEAQDLSGGMQRKLSV 1072
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 164 ARALTQRAEVILADEPIASLDPESARRVMEILadINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGLAQDLSKQ 243
Cdd:TIGR01257 1073 AIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNC 1150
|
....*.
gi 492088662 244 FLNDLY 249
Cdd:TIGR01257 1151 FGTGFY 1156
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-262 |
7.53e-18 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 83.29 E-value: 7.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 17 KSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGlaycdrsnggqvqvlGREVQSsgrlnGQVRRLRAdIGYIFQQFN 96
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLS---------------QFEISE-----GRVWAERS-IAYVPQQAW 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 97 LVNRlSVLDNVLlgclgrmprwrgslalFNREEKQRAMAALDRVGL--ADLAT----------QRASTLSGGQQQRVAIA 164
Cdd:PTZ00243 732 IMNA-TVRGNIL----------------FFDEEDAARLADAVRVSQleADLAQlgggleteigEKGVNLSGGQKARVSLA 794
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 165 RALTQRAEVILADEPIASLDPESARRVMEILAdINRSDGKTVVVTLHQvdyaVRYCPRA---VALKGGRIHFDGLAQDLS 241
Cdd:PTZ00243 795 RAVYANRDVYLLDDPLSALDAHVGERVVEECF-LGALAGKTRVLATHQ----VHVVPRAdyvVALGDGRVEFSGSSADFM 869
|
250 260 270
....*....|....*....|....*....|..
gi 492088662 242 KQFL-----------NDLYGADADASLMITER 262
Cdd:PTZ00243 870 RTSLyatlaaelkenKDSKEGDADAEVAEVDA 901
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-235 |
8.98e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 82.81 E-value: 8.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 2 NDAIHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVqVLGREVQssgrlngqv 81
Cdd:COG0488 313 KKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGE---LEPDSGTV-KLGETVK--------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 82 rrlradIGYIFQ-QFNLVNRLSVLDNV-----------LLGCLGRMprwrgslaLFNREEkqramaaldrvgladlATQR 149
Cdd:COG0488 380 ------IGYFDQhQEELDPDKTVLDELrdgapggteqeVRGYLGRF--------LFSGDD----------------AFKP 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 150 ASTLSGGQQQRVAIARALTQRAEVILADEPIASLDPESarrvMEILAD-INRSDGkTVVVTLHqvDyavRY-----CPRA 223
Cdd:COG0488 430 VGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIET----LEALEEaLDDFPG-TVLLVSH--D---RYfldrvATRI 499
|
250
....*....|...
gi 492088662 224 VALKGGRI-HFDG 235
Cdd:COG0488 500 LEFEDGGVrEYPG 512
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
7-211 |
1.82e-17 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 78.98 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 7 VQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQssgrlngqvRRLRA 86
Cdd:TIGR03740 3 TKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGIL---RPTSGEIIFDGHPWT---------RKDLH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 87 DIGYIFQQFNLVNRLSVLDNVLLGCLgrmprwrgSLALfnreEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAIARA 166
Cdd:TIGR03740 71 KIGSLIESPPLYENLTARENLKVHTT--------LLGL----PDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIA 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 492088662 167 LTQRAEVILADEPIASLDPESARRVMEILADInRSDGKTVVVTLH 211
Cdd:TIGR03740 139 LLNHPKLLILDEPTNGLDPIGIQELRELIRSF-PEQGITVILSSH 182
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
19-195 |
2.60e-17 |
|
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: 78.30 E-value: 2.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 19 ALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDrsnGGQVQVLGREVQSSGRlngqvRRLRADIGYIFQqfnlv 98
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELS---SGSILIDGVDISKIGL-----HDLRSRISIIPQ----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 99 nrlsvlDNVLL-GCLgrmprwRGSLALFNREEKQRAMAALDRVGLADLATQRA-----------STLSGGQQQRVAIARA 166
Cdd:cd03244 86 ------DPVLFsGTI------RSNLDPFGEYSDEELWQALERVGLKEFVESLPggldtvveeggENLSVGQRQLLCLARA 153
|
170 180
....*....|....*....|....*....
gi 492088662 167 LTQRAEVILADEPIASLDPESARRVMEIL 195
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDALIQKTI 182
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
20-244 |
4.87e-17 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 80.47 E-value: 4.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 20 LVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDRsngGQVQVLGREVQSSGRlngqvRRLRADIGYIFQQFNLVN 99
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTS---GSVRLDGADLKQWDR-----ETFGKHIGYLPQDVELFP 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 100 RlSVLDNVllgclgrmprwrgslALFNRE-EKQRAMAALDRVGLADLATQ-----------RASTLSGGQQQRVAIARAL 167
Cdd:TIGR01842 406 G-TVAENI---------------ARFGENaDPEKIIEAAKLAGVHELILRlpdgydtvigpGGATLSGGQRQRIALARAL 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 168 TQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVT-----LHQVDYavrycprAVALKGGRIHFDGLAQDLSK 242
Cdd:TIGR01842 470 YGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVIThrpslLGCVDK-------ILVLQDGRIARFGERDEVLA 542
|
..
gi 492088662 243 QF 244
Cdd:TIGR01842 543 KL 544
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
20-243 |
5.73e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 80.54 E-value: 5.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 20 LVDLALSIQPGEMVALIGASGSGKST---LLRHLaglaYcdRSNGGQVQVLGREVQSSGRlngqvRRLRADIGYIFQQFN 96
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTvaaLLQNL----Y--QPTGGQVLLDGVPLVQYDH-----HYLHRQVALVGQEPV 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 97 LVNRlSVLDNVLLGClgrmprwrgslalfNREEKQRAMAALDRVGLADLAT-----------QRASTLSGGQQQRVAIAR 165
Cdd:TIGR00958 566 LFSG-SVRENIAYGL--------------TDTPDEEIMAAAKAANAHDFIMefpngydtevgEKGSQLSGGQKQRIAIAR 630
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492088662 166 ALTQRAEVILADEPIASLDPESARrvmeILADINRSDGKTVVVTLHQVDyAVRYCPRAVALKGGRIHFDGLAQDLSKQ 243
Cdd:TIGR00958 631 ALVRKPRVLILDEATSALDAECEQ----LLQESRSRASRTVLLIAHRLS-TVERADQILVLKKGSVVEMGTHKQLMED 703
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-244 |
6.08e-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: 80.83 E-value: 6.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 3 DAIHVQGLNKTFSHKS--ALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGlaycDRS-NGGQVQVLGREVQSSgrlng 79
Cdd:TIGR01257 1936 DILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTG----DTTvTSGDATVAGKSILTN----- 2006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 80 qVRRLRADIGYIFQqfnlvnrLSVLDNVLLG--CLGRMPRWRGSLAlfnREEKQRAMAALDRVGLADLATQRASTLSGGQ 157
Cdd:TIGR01257 2007 -ISDVHQNMGYCPQ-------FDAIDDLLTGreHLYLYARLRGVPA---EEIEKVANWSIQSLGLSLYADRLAGTYSGGN 2075
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 158 QQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRsDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGLA 237
Cdd:TIGR01257 2076 KRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIR-EGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTI 2154
|
....*..
gi 492088662 238 QDLSKQF 244
Cdd:TIGR01257 2155 QHLKSKF 2161
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
8-195 |
1.14e-16 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 79.45 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 8 QGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaYCDRSNGGQVqvlgrevqssgRLNGQVRRLR-- 85
Cdd:NF040905 5 RGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHGSYEGEI-----------LFDGEVCRFKdi 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 86 -----ADIGYIFQQFNLVNRLSVLDNVLLGclgrmpRWRGSLALFNREE-KQRAMAALDRVGLADLATQRASTLSGGQQQ 159
Cdd:NF040905 73 rdseaLGIVIIHQELALIPYLSIAENIFLG------NERAKRGVIDWNEtNRRARELLAKVGLDESPDTLVTDIGVGKQQ 146
|
170 180 190
....*....|....*....|....*....|....*.
gi 492088662 160 RVAIARALTQRAEVILADEPIASLDPESARRVMEIL 195
Cdd:NF040905 147 LVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLL 182
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
10-231 |
1.18e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 79.51 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 10 LNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQSSGrlNGQVRRLRADIG 89
Cdd:PRK10261 330 LNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLV---ESQGGEIIFNGQRIDTLS--PGKLQALRRDIQ 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 90 YIFQQ--FNLVNRLSVLDNVllgclgrMPRWRGSLALFNREEKQRAMAALDRVGL-ADLATQRASTLSGGQQQRVAIARA 166
Cdd:PRK10261 405 FIFQDpyASLDPRQTVGDSI-------MEPLRVHGLLPGKAAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARA 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492088662 167 LTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRI 231
Cdd:PRK10261 478 LALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
9-230 |
1.48e-16 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 79.00 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 9 GLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQssgrLNGQVRRLRADI 88
Cdd:PRK10982 3 NISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIY---QKDSGSILFQGKEID----FKSSKEALENGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 89 GYIFQQFNLVNRLSVLDNVLlgcLGRMPRwRGslaLFNREEK--QRAMAALDRVGLADLATQRASTLSGGQQQRVAIARA 166
Cdd:PRK10982 76 SMVHQELNLVLQRSVMDNMW---LGRYPT-KG---MFVDQDKmyRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492088662 167 LTQRAEVILADEPIASLDPESARRVMEILADInRSDGKTVVVTLHQVDYAVRYCPRAVALKGGR 230
Cdd:PRK10982 149 FSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
7-247 |
1.52e-16 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 77.18 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 7 VQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDRSNGGQVQVLGREVQSSGRLNGQVRRL-R 85
Cdd:TIGR02323 6 VSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLSEAERRRLmR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 86 ADIGYIFQQF--NLVNRLSVLDNVLLGCLGRMPRWRGSLalfnreeKQRAMAALDRVGL-ADLATQRASTLSGGQQQRVA 162
Cdd:TIGR02323 86 TEWGFVHQNPrdGLRMRVSAGANIGERLMAIGARHYGNI-------RATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRLQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 163 IARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIhfdgLAQDLSK 242
Cdd:TIGR02323 159 IARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRV----VESGLTD 234
|
....*
gi 492088662 243 QFLND 247
Cdd:TIGR02323 235 QVLDD 239
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
12-212 |
2.74e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 78.38 E-value: 2.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 12 KTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGlaycdRSNGGQVQvlGREVQSSGRLNGQVRRlraDIGYI 91
Cdd:PLN03211 76 RQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAG-----RIQGNNFT--GTILANNRKPTKQILK---RTGFV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 92 FQQFNLVNRLSVLDNVLLGCLGRMPRwrgSLAlfnREEKQR-AMAALDRVGLAD-----LATQRASTLSGGQQQRVAIAR 165
Cdd:PLN03211 146 TQDDILYPHLTVRETLVFCSLLRLPK---SLT---KQEKILvAESVISELGLTKcentiIGNSFIRGISGGERKRVSIAH 219
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 492088662 166 ALTQRAEVILADEPIASLDPESARRVMEILADINRSdGKTVVVTLHQ 212
Cdd:PLN03211 220 EMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQK-GKTIVTSMHQ 265
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-184 |
4.70e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 75.98 E-value: 4.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 1 MNDAIHVQGLNKTF---------SHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREV 71
Cdd:PRK15112 1 VETLLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMI---EPTSGELLIDDHPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 72 qSSGRLNGQVRRLRAdigyIFQ----QFNLVNRLSVLDNVLLgclgrmprwRGSLALFNREEKQRAMAALDRVGL-ADLA 146
Cdd:PRK15112 78 -HFGDYSYRSQRIRM----IFQdpstSLNPRQRISQILDFPL---------RLNTDLEPEQREKQIIETLRQVGLlPDHA 143
|
170 180 190
....*....|....*....|....*....|....*...
gi 492088662 147 TQRASTLSGGQQQRVAIARALTQRAEVILADEPIASLD 184
Cdd:PRK15112 144 SYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLD 181
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
19-200 |
6.65e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 76.16 E-value: 6.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 19 ALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGREVQSSGRlnGQVRRLRADIGYIFQqfnlv 98
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMI---ETPTGGELYYQGQDLLKADP--EAQKLLRQKIQIVFQ----- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 99 NRLSVLDnvllgclgrmPRWR------------GSLALFNREEKQRAMAAldRVGLADLATQR-ASTLSGGQQQRVAIAR 165
Cdd:PRK11308 100 NPYGSLN----------PRKKvgqileepllinTSLSAAERREKALAMMA--KVGLRPEHYDRyPHMFSGGQRQRIAIAR 167
|
170 180 190
....*....|....*....|....*....|....*
gi 492088662 166 ALTQRAEVILADEPIASLDPESARRVMEILADINR 200
Cdd:PRK11308 168 ALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQ 202
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
19-242 |
1.03e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 74.79 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 19 ALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVqvlgreVQSSGRLNGQ-VRRLRADIGYIFQqfNL 97
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGI---EKVKSGEI------FYNNQAITDDnFEKLRKHIGIVFQ--NP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 98 VNRLsvldnvllgcLGRMPRWRGSLALFNR----EEKQRAMA-ALDRVGLADLATQRASTLSGGQQQRVAIARALTQRAE 172
Cdd:PRK13648 93 DNQF----------VGSIVKYDVAFGLENHavpyDEMHRRVSeALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPS 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 173 VILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRyCPRAVALKGGRIHFDGLAQDLSK 242
Cdd:PRK13648 163 VIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
20-195 |
1.17e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 75.68 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 20 LVDLALSIQ---PGEMV-ALIGASGSGKSTLLRHLAGLAYCDRsngGQVQVLGRE-VQSSGRLNGQVRRLRadIGYIFQQ 94
Cdd:PRK11144 10 LGDLCLTVNltlPAQGItAIFGRSGAGKTSLINAISGLTRPQK---GRIVLNGRVlFDAEKGICLPPEKRR--IGYVFQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 95 FNLVNRLSVLDNVLLGCLGRMPrwrgslALFNReekqraMAALdrVGLADLATQRASTLSGGQQQRVAIARALTQRAEVI 174
Cdd:PRK11144 85 ARLFPHYKVRGNLRYGMAKSMV------AQFDK------IVAL--LGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELL 150
|
170 180
....*....|....*....|.
gi 492088662 175 LADEPIASLDPESARRVMEIL 195
Cdd:PRK11144 151 LMDEPLASLDLPRKRELLPYL 171
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
4-231 |
1.29e-15 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 75.65 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 4 AIHVQGLNKTFSHK-SALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGREVqssgrlNGQVR 82
Cdd:PRK11650 3 GLKLQAVRKSYDGKtQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGL---ERITSGEIWIGGRVV------NELEP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 83 RLRaDIGYIFQQFNLVNRLSVLDNVLLGCLGR-MPRwrgslalfnREEKQRAMAALDRVGLADLATQRASTLSGGQQQRV 161
Cdd:PRK11650 74 ADR-DIAMVFQNYALYPHMSVRENMAYGLKIRgMPK---------AEIEERVAEAARILELEPLLDRKPRELSGGQRQRV 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492088662 162 AIARALTQRAEVILADEPIASLDpesAR-RV-MEI-LADINRSDGKT-VVVTLHQVDyAVRYCPRAVALKGGRI 231
Cdd:PRK11650 144 AMGRAIVREPAVFLFDEPLSNLD---AKlRVqMRLeIQRLHRRLKTTsLYVTHDQVE-AMTLADRVVVMNGGVA 213
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
14-214 |
1.49e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 74.66 E-value: 1.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 14 FSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQSSGRlngQVRRLRADIGYIFQ 93
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLL---RPQKGAVLWQGKPLDYSKR---GLLALRQQVATVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 94 QFNLVNRLSVLDNVLLGCLGrmprwrgSLALFNREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAIARALTQRAEV 173
Cdd:PRK13638 85 DPEQQIFYTDIDSDIAFSLR-------NLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARY 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 492088662 174 ILADEPIASLDPESARRVMEILADInRSDGKTVVVTLHQVD 214
Cdd:PRK13638 158 LLLDEPTAGLDPAGRTQMIAIIRRI-VAQGNHVIISSHDID 197
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-260 |
2.39e-15 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 74.76 E-value: 2.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 1 MNDAIHVQGLNKTFSHKSALV----DLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDRSNGGQVQVLGREVqssgr 76
Cdd:PRK09473 9 ADALLDVKDLRVTFSTPDGDVtavnDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIGGSATFNGREI----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 77 LN---GQVRRLRAD-IGYIFQ----QFNLVNRLS-VLDNVLLgclgrmprwrgslaLFNREEKQRAMAA----LDRVGLA 143
Cdd:PRK09473 84 LNlpeKELNKLRAEqISMIFQdpmtSLNPYMRVGeQLMEVLM--------------LHKGMSKAEAFEEsvrmLDAVKMP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 144 DlATQRAST----LSGGQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRY 219
Cdd:PRK09473 150 E-ARKRMKMypheFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGI 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 492088662 220 CPRAVALKGGRIHFDGLAQDL--------SKQFLNDLYGADADASLMIT 260
Cdd:PRK09473 229 CDKVLVMYAGRTMEYGNARDVfyqpshpySIGLLNAVPRLDAEGESLLT 277
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
18-229 |
2.85e-15 |
|
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: 72.75 E-value: 2.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 18 SALVDLALSIQPGEMVALIGASGSGKSTLLrhLAGLaycdrsngGQVQVLGREVQSSGRLNGQV------RRLRADIGYI 91
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLL--LAIL--------GEMQTLEGKVHWSNKNESEPsfeatrSRNRYSVAYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 92 FQQFNLVNRlSVLDNVLLGclgrmprwrgslALFNreeKQRAMAALDRVGLA---DLAT--------QRASTLSGGQQQR 160
Cdd:cd03290 85 AQKPWLLNA-TVEENITFG------------SPFN---KQRYKAVTDACSLQpdiDLLPfgdqteigERGINLSGGQRQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492088662 161 VAIARALTQRAEVILADEPIASLDPESARRVM-EILADINRSDGKTVVVTLHQvdyaVRYCPRA---VALKGG 229
Cdd:cd03290 149 ICVARALYQNTNIVFLDDPFSALDIHLSDHLMqEGILKFLQDDKRTLVLVTHK----LQYLPHAdwiIAMKDG 217
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-240 |
5.48e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 74.78 E-value: 5.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 4 AIHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQSSG-RlngqvR 82
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGAR---KIQQGRVEVLGGDMADARhR-----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 83 RLRADIGYIFQQF--NLVNRLSVLDNVLLgcLGRmprwrgslaLF--NREEKQRAMAAL-DRVGLADLATQRASTLSGGQ 157
Cdd:NF033858 73 AVCPRIAYMPQGLgkNLYPTLSVFENLDF--FGR---------LFgqDAAERRRRIDELlRATGLAPFADRPAGKLSGGM 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 158 QQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADI-NRSDGKTVVVTLHQVDYAVRYcPRAVALKGGRIHFDGL 236
Cdd:NF033858 142 KQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIrAERPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGT 220
|
....
gi 492088662 237 AQDL 240
Cdd:NF033858 221 PAEL 224
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
22-231 |
8.85e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 73.67 E-value: 8.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 22 DLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGREVQSSGRLN------GQVRRLRADIGYiFQQF 95
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGV---DKRAGGEIRLNGKDISPRSPLDavkkgmAYITESRRDNGF-FPNF 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 96 NLVNRLSVLDNVLLGclgrmpRWRGSLALFN-REEKQRAMAALDRVGL-ADLATQRASTLSGGQQQRVAIARALTQRAEV 173
Cdd:PRK09700 357 SIAQNMAISRSLKDG------GYKGAMGLFHeVDEQRTAENQRELLALkCHSVNQNITELSGGNQQKVLISKWLCCCPEV 430
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492088662 174 ILADEPIASLDPESAR---RVMEILADinrsDGKTVVVTLHQVDYAVRYCPRAVALKGGRI 231
Cdd:PRK09700 431 IIFDEPTRGIDVGAKAeiyKVMRQLAD----DGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
20-211 |
9.60e-15 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 73.70 E-value: 9.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 20 LVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaYcDrSNGGQVQVLG---REV-QSSgrlngqvrrLRADIGYIFQQF 95
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRF-Y-D-VTSGRILIDGqdiRDVtQAS---------LRAAIGIVPQDT 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 96 NLVNRlSVLDNVLLGclgrmpRWRGSlalfnREEKQRA--MAALDR--VGLAD-LATQ---RASTLSGGQQQRVAIARAL 167
Cdd:COG5265 442 VLFND-TIAYNIAYG------RPDAS-----EEEVEAAarAAQIHDfiESLPDgYDTRvgeRGLKLSGGEKQRVAIARTL 509
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 492088662 168 TQRAEVILADEPIASLDPESARRVMEILADINRsdGKTVVVTLH 211
Cdd:COG5265 510 LKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAH 551
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-184 |
1.11e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 71.68 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 1 MNDAIHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRhlaglaycdrsnggqvQVLGREVQSSGRLNGQ 80
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVR----------------VVLGLVAPDEGVIKRN 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 81 vRRLRadIGYIFQQFNLvnrlsvlDNVLLGCLGRMPRWRGSLalfnreEKQRAMAALDRVGLADLATQRASTLSGGQQQR 160
Cdd:PRK09544 65 -GKLR--IGYVPQKLYL-------DTTLPLTVNRFLRLRPGT------KKEDILPALKRVQAGHLIDAPMQKLSGGETQR 128
|
170 180
....*....|....*....|....
gi 492088662 161 VAIARALTQRAEVILADEPIASLD 184
Cdd:PRK09544 129 VLLARALLNRPQLLVLDEPTQGVD 152
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
20-214 |
1.24e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 71.28 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 20 LVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDRsngGQVQVLGREVQSsgrLNGQvrRLRADIGYIFQQFNLVN 99
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTS---GTLLFEGEDIST---LKPE--IYRQQVSYCAQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 100 RlSVLDNVLLGCLGRMprwrgslalfNREEKQRAMAALDRVGLAD-LATQRASTLSGGQQQRVAIARALTQRAEVILADE 178
Cdd:PRK10247 95 D-TVYDNLIFPWQIRN----------QQPDPAIFLDDLERFALPDtILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 492088662 179 PIASLDPESARRVMEILADINRSDGKTVVVTLHQVD 214
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKD 199
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-211 |
2.59e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 72.85 E-value: 2.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 4 AIHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGL--AycdrsNGGQVQVLGREVQSSgrlNGQV 81
Cdd:NF033858 266 AIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLlpA-----SEGEAWLFGQPVDAG---DIAT 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 82 RRlRadIGYIFQQFNLVNRLSVLDNVLL-GCLGRMPRwrgslalfnREEKQRAMAALDRVGLADLATQRASTLSGGQQQR 160
Cdd:NF033858 338 RR-R--VGYMSQAFSLYGELTVRQNLELhARLFHLPA---------AEIAARVAEMLERFDLADVADALPDSLPLGIRQR 405
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 492088662 161 VAIARALTQRAEVILADEPIASLDPeSAR-RVMEILADINRSDGKTVVVTLH 211
Cdd:NF033858 406 LSLAVAVIHKPELLILDEPTSGVDP-VARdMFWRLLIELSREDGVTIFISTH 456
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
7-247 |
2.70e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 70.73 E-value: 2.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 7 VQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDRsngGQVQVLGR--EVQSSGRLNGQVRR- 83
Cdd:PRK11701 9 VRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDA---GEVHYRMRdgQLRDLYALSEAERRr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 84 -LRADIGYIFQQ------------FNLVNRLSVLDNvllgclgrmpRWRGSLalfnreeKQRAMAALDRVGL-ADLATQR 149
Cdd:PRK11701 86 lLRTEWGFVHQHprdglrmqvsagGNIGERLMAVGA----------RHYGDI-------RATAGDWLERVEIdAARIDDL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 150 ASTLSGGQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGG 229
Cdd:PRK11701 149 PTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQG 228
|
250
....*....|....*...
gi 492088662 230 RIhfdgLAQDLSKQFLND 247
Cdd:PRK11701 229 RV----VESGLTDQVLDD 242
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-240 |
3.11e-14 |
|
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: 72.67 E-value: 3.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 23 LALSIQPGEMVALIGASGSGKSTLLRHLagLAYCDRsnggqvqvlgrevqssgrLNGQVRrLRADIGYIFQQFNLVNRlS 102
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSAL--LAEMDK------------------VEGHVH-MKGSVAYVPQQAWIQND-S 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 103 VLDNVLLGCLGRMPRWRGSL---ALFNREEkqrAMAALDRVGLAdlatQRASTLSGGQQQRVAIARALTQRAEVILADEP 179
Cdd:TIGR00957 715 LRENILFGKALNEKYYQQVLeacALLPDLE---ILPSGDRTEIG----EKGVNLSGGQKQRVSLARAVYSNADIYLFDDP 787
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492088662 180 IASLDPESARRVME-ILADINRSDGKTVVVTLHqvdyAVRYCPRA---VALKGGRIHFDGLAQDL 240
Cdd:TIGR00957 788 LSAVDAHVGKHIFEhVIGPEGVLKNKTRILVTH----GISYLPQVdviIVMSGGKISEMGSYQEL 848
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-187 |
3.62e-14 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 71.89 E-value: 3.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 6 HVQGLNKTF-SHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVqvlgrevqssgrlngqVRRL 84
Cdd:TIGR03719 6 TMNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV---DKDFNGEA----------------RPQP 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 85 RADIGYIFQQFNLVNRLSVLDNVLLGClgrmPRWRGSLALFNR----------------EEKQRAMAALDRVGLADLATQ 148
Cdd:TIGR03719 67 GIKVGYLPQEPQLDPTKTVRENVEEGV----AEIKDALDRFNEisakyaepdadfdklaAEQAELQEIIDAADAWDLDSQ 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 492088662 149 ---------------RASTLSGGQQQRVAIARALTQRAEVILADEPIASLDPES 187
Cdd:TIGR03719 143 leiamdalrcppwdaDVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-190 |
4.43e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 71.62 E-value: 4.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVLGREVQssgRLN-GQVRR 83
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGI---VPPDSGTLEIGGNPCA---RLTpAKAHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 84 LraDIGYIFQQFNLVNRLSVLDNVLLGclgrMPRwrgslalfnREEKQRAMAALdrvgLADLATQ-----RASTLSGGQQ 158
Cdd:PRK15439 86 L--GIYLVPQEPLLFPNLSVKENILFG----LPK---------RQASMQKMKQL----LAALGCQldldsSAGSLEVADR 146
|
170 180 190
....*....|....*....|....*....|..
gi 492088662 159 QRVAIARALTQRAEVILADEPIASLDPESARR 190
Cdd:PRK15439 147 QIVEILRGLMRDSRILILDEPTASLTPAETER 178
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-211 |
1.52e-13 |
|
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: 66.32 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAglaycdrsnggqvqvlGREVQSSGRLNgqvRRL 84
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIA----------------GELEPDEGIVT---WGS 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 85 RADIGYiFQQfnlvnrlsvldnvllgclgrmprwrgslalfnreekqramaaldrvgladlatqrastLSGGQQQRVAIA 164
Cdd:cd03221 62 TVKIGY-FEQ----------------------------------------------------------LSGGEKMRLALA 82
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 492088662 165 RALTQRAEVILADEPIASLDPESARRVMEILADINRsdgkTVVVTLH 211
Cdd:cd03221 83 KLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPG----TVILVSH 125
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
15-212 |
2.71e-13 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 66.88 E-value: 2.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 15 SHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGlaycdRSNGGqvqVLGREVQSSGRLNGQvrRLRADIGYIFQQ 94
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG-----RKTAG---VITGEILINGRPLDK--NFQRSTGYVEQQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 95 fnlvnrlsvldNVLLGCLgrmprwrgslalfNREEKQRAMAALdrvgladlatqRAstLSGGQQQRVAIARALTQRAEVI 174
Cdd:cd03232 88 -----------DVHSPNL-------------TVREALRFSALL-----------RG--LSVEQRKRLTIGVELAAKPSIL 130
|
170 180 190
....*....|....*....|....*....|....*...
gi 492088662 175 LADEPIASLDPESARRVMEILADINRSdGKTVVVTLHQ 212
Cdd:cd03232 131 FLDEPTSGLDSQAAYNIVRFLKKLADS-GQAILCTIHQ 167
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1-231 |
3.15e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 67.80 E-value: 3.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 1 MNDAIHVQGLnkTFSHKSALV-DLALSIQPGEMVALIGASGSGKS-TLLRHLAGLAYCDRSNGGQVQVLGREVQSSGrLN 78
Cdd:PRK10418 1 MPQQIELRNI--ALQAAQPLVhGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILPAGVRQTAGRVLLDGKPVAPCA-LR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 79 GQVrrlradIGYIFQQ----FNLVNRLSVLDNVLLGCLGRMPRwrgslalfnreeKQRAMAALDRVGLAD---LATQRAS 151
Cdd:PRK10418 78 GRK------IATIMQNprsaFNPLHTMHTHARETCLALGKPAD------------DATLTAALEAVGLENaarVLKLYPF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 152 TLSGGQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRI 231
Cdd:PRK10418 140 EMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
11-242 |
4.38e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 69.00 E-value: 4.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 11 NKTFS-----HKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGlAYCDRSNGGQVqvlgrevqssgrlngqvrrLR 85
Cdd:PLN03130 619 NGYFSwdskaERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLG-ELPPRSDASVV-------------------IR 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 86 ADIGYIFQQFNLVNRlSVLDNVLLGclgrmprwrgslALFNREEKQRAM--AALDRvglaDLAT----------QRASTL 153
Cdd:PLN03130 679 GTVAYVPQVSWIFNA-TVRDNILFG------------SPFDPERYERAIdvTALQH----DLDLlpggdlteigERGVNI 741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 154 SGGQQQRVAIARALTQRAEVILADEPIASLDPESARRVME-ILADINRsdGKT-VVVT--LH---QVDyavrycpRAVAL 226
Cdd:PLN03130 742 SGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDkCIKDELR--GKTrVLVTnqLHflsQVD-------RIILV 812
|
250
....*....|....*.
gi 492088662 227 KGGRIHFDGLAQDLSK 242
Cdd:PLN03130 813 HEGMIKEEGTYEELSN 828
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
11-212 |
4.41e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 68.98 E-value: 4.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 11 NKTFSH---KSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDRsngGQVQVLGREVQSsgrLNGQVrrLRAD 87
Cdd:PRK10790 345 NVSFAYrddNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTE---GEIRLDGRPLSS---LSHSV--LRQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 88 IGYIfQQFNLVNRLSVLDNVLLGclgrmprwrgslalfnRE-EKQRAMAALDRVGLADLAT-----------QRASTLSG 155
Cdd:PRK10790 417 VAMV-QQDPVVLADTFLANVTLG----------------RDiSEEQVWQALETVQLAELARslpdglytplgEQGNNLSV 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 492088662 156 GQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSdgKTVVVTLHQ 212
Cdd:PRK10790 480 GQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAHR 534
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-184 |
4.84e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 68.73 E-value: 4.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 2 NDAIHVQGLNKTFSHKS----ALVDLALSIQPGEMVALIGASGSGKST-------LLRHLAGLAYCD----RSNGGQVQV 66
Cdd:PRK10261 10 RDVLAVENLNIAFMQEQqkiaAVRNLSFSLQRGETLAIVGESGSGKSVtalalmrLLEQAGGLVQCDkmllRRRSRQVIE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 67 LGREVQSsgrlngQVRRLR-ADIGYIFQQfnlvnRLSVLDNVLlgCLGRmpRWRGSLALFNREEKQRAMAA----LDRVG 141
Cdd:PRK10261 90 LSEQSAA------QMRHVRgADMAMIFQE-----PMTSLNPVF--TVGE--QIAESIRLHQGASREEAMVEakrmLDQVR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 492088662 142 LAD---LATQRASTLSGGQQQRVAIARALTQRAEVILADEPIASLD 184
Cdd:PRK10261 155 IPEaqtILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALD 200
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
20-252 |
5.58e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 66.88 E-value: 5.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 20 LVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdrSNGGQVQVLGREVqSSGRLNGQVRRlRAdigYIFQQ----F 95
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL----PGSGSIQFAGQPL-EAWSAAELARH-RA---YLSQQqtppF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 96 NlvnrlsvldnvllgclgrMPRWRgSLALF-----NREEKQRAMAAL-DRVGLADLATQRASTLSGGQQQRVAIARALTQ 169
Cdd:PRK03695 83 A------------------MPVFQ-YLTLHqpdktRTEAVASALNEVaEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 170 -------RAEVILADEPIASLDPESARRVMEILADINRSdGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGLAQD-LS 241
Cdd:PRK03695 144 vwpdinpAGQLLLLDEPMNSLDVAQQAALDRLLSELCQQ-GIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEvLT 222
|
250
....*....|.
gi 492088662 242 KQFLNDLYGAD 252
Cdd:PRK03695 223 PENLAQVFGVN 233
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
22-230 |
8.36e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 67.81 E-value: 8.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 22 DLALSIQPGEMVALIGASGSGKS----TLLRHLAG--LAYcdrsNGGQVQVLGREVqssgrLNGQVRRLRA----DIGYI 91
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSvtalSILRLLPSppVVY----PSGDIRFHGESL-----LHASEQTLRGvrgnKIAMI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 92 FQQ-FNLVNRLSVLDNVLLGCLgrmprwrgSLALFNREEKQRA--MAALDRVG-------LADLATQrastLSGGQQQRV 161
Cdd:PRK15134 98 FQEpMVSLNPLHTLEKQLYEVL--------SLHRGMRREAARGeiLNCLDRVGirqaakrLTDYPHQ----LSGGERQRV 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492088662 162 AIARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGR 230
Cdd:PRK15134 166 MIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
25-211 |
9.03e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 67.24 E-value: 9.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 25 LSIQPGEMVALIGASGSGKSTLLRHLAGLA------YCDRSNGGQVQVLgrevqssgRLNGQVRR--LRADIGYIFQqfn 96
Cdd:COG4170 28 LTLNEGEIRGLVGESGSGKSLIAKAICGITkdnwhvTADRFRWNGIDLL--------KLSPRERRkiIGREIAMIFQ--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 97 lvNRLSVLD-NVLLG--CLGRMPRWRGSLALFNR--EEKQRAMAALDRVGLADLATQRAS---TLSGGQQQRVAIARALT 168
Cdd:COG4170 97 --EPSSCLDpSAKIGdqLIEAIPSWTFKGKWWQRfkWRKKRAIELLHRVGIKDHKDIMNSyphELTEGECQKVMIAMAIA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 492088662 169 QRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLH 211
Cdd:COG4170 175 NQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISH 217
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-242 |
1.28e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 67.69 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 17 KSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGlaycDRSNGGQVQVLgrevqssgrlngqvrrLRADIGYIfQQFN 96
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG----ELSHAETSSVV----------------IRGSVAYV-PQVS 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 97 LVNRLSVLDNVLLGCLGRMPRWRGSLALFNREEKQRAMAALDRVGLAdlatQRASTLSGGQQQRVAIARALTQRAEVILA 176
Cdd:PLN03232 689 WIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIG----ERGVNISGGQKQRVSMARAVYSNSDIYIF 764
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492088662 177 DEPIASLDPESARRVMEILADiNRSDGKTVVVTLHQVDYaVRYCPRAVALKGGRIHFDGLAQDLSK 242
Cdd:PLN03232 765 DDPLSALDAHVAHQVFDSCMK-DELKGKTRVLVTNQLHF-LPLMDRIILVSEGMIKEEGTFAELSK 828
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
22-212 |
1.47e-12 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 64.10 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 22 DLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCdrsnggqvqvlgrevqSSGRLngqVRRLRADIGYIFQQfnlvnrl 101
Cdd:cd03223 19 DLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPW----------------GSGRI---GMPEGEDLLFLPQR------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 102 svldnvllgclGRMPRwrGSLalfnREekqramaAL----DRVgladlatqrastLSGGQQQRVAIARALTQRAEVILAD 177
Cdd:cd03223 73 -----------PYLPL--GTL----RE-------QLiypwDDV------------LSGGEQQRLAFARLLLHKPKFVFLD 116
|
170 180 190
....*....|....*....|....*....|....*
gi 492088662 178 EPIASLDPESARRVMEILadinRSDGKTVVVTLHQ 212
Cdd:cd03223 117 EATSALDEESEDRLYQLL----KELGITVISVGHR 147
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-213 |
2.81e-12 |
|
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: 64.74 E-value: 2.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 26 SIQPGEMVALIGASGSGKSTLLRHLAGLAYCDrsnggqvqvlgrevqssgrlNGQVRRLRADIGYIFQQFNLVNRLSVlD 105
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPD--------------------EGDIEIELDTVSYKPQYIKADYEGTV-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 106 NVLLGCLGRMprwrGSLALFNREekqramaALDRVGLADLATQRASTLSGGQQQRVAIARALTQRAEVILADEPIASLDP 185
Cdd:cd03237 80 DLLSSITKDF----YTHPYFKTE-------IAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
170 180
....*....|....*....|....*...
gi 492088662 186 ESARRVMEILADINRSDGKTVVVTLHQV 213
Cdd:cd03237 149 EQRLMASKVIRRFAENNEKTAFVVEHDI 176
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
7-275 |
5.34e-12 |
|
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: 66.09 E-value: 5.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 7 VQGLNKTFSH--KSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdrSNGGQVQVLGREVQSSgrlngQVRRL 84
Cdd:TIGR01271 1220 VQGLTAKYTEagRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL----STEGEIQIDGVSWNSV-----TLQTW 1290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 85 RADIGYIFQQFnlvnrlsvldNVLLGClgrmprWRGSLALFNREEKQRAMAALDRVGLADLATQ-----------RASTL 153
Cdd:TIGR01271 1291 RKAFGVIPQKV----------FIFSGT------FRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQfpdkldfvlvdGGYVL 1354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 154 SGGQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADiNRSDGkTVVVTLHQVDyAVRYCPRAVALKGGRI-H 232
Cdd:TIGR01271 1355 SNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQ-SFSNC-TVILSEHRVE-ALLECQQFLVIEGSSVkQ 1431
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 492088662 233 FDGLAQDLSKQ-FLNDLYGADADASLMITERSRRVRQKPRLELA 275
Cdd:TIGR01271 1432 YDSIQKLLNETsLFKQAMSAADRLKLFPLHRRNSSKRKPQPKIT 1475
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
3-243 |
1.41e-11 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 63.99 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 3 DAIHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSG--KSTLLRHLAGlaycdrsnggqvQVLGREVQSSGRLNGQ 80
Cdd:NF000106 12 NAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G------------PDAGRRPWRF*TWCAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 81 VRRLRADIGYiFQQFNLVNRLSVLDNVLLGCLGRMprwrgsLALFNREEKQRAMAALDRVGLADLATQRASTLSGGQQQR 160
Cdd:NF000106 80 RRALRRTIG*-HRPVR*GRRESFSGRENLYMIGR*------LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 161 VAIARALTQRAEVILADEPIASLDPESARRVMEILADINRsDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGLAQDL 240
Cdd:NF000106 153 LDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVR-DGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
...
gi 492088662 241 SKQ 243
Cdd:NF000106 232 KTK 234
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
26-242 |
1.52e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 63.61 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 26 SIQPGEMVALIGASGSGKSTLLRHLAGLA-YCDRSNGGQVQVLGREVQssgRLNGQVRR--LRADIGYIFQQ-------- 94
Cdd:PRK11022 29 SVKQGEVVGIVGESGSGKSVSSLAIMGLIdYPGRVMAEKLEFNGQDLQ---RISEKERRnlVGAEVAMIFQDpmtslnpc 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 95 ----FNLVNRLSVLDnvllgclGRMPRWRgslalfnreeKQRAMAALDRVGLADLATQ---RASTLSGGQQQRVAIARAL 167
Cdd:PRK11022 106 ytvgFQIMEAIKVHQ-------GGNKKTR----------RQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAI 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492088662 168 TQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGLAQDLSK 242
Cdd:PRK11022 169 ACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFR 243
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
25-211 |
1.65e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 64.22 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 25 LSIQPGEMVALIGASGSGKSTLLRHLAGLaYCDRSngGQVQVLGREVQSSGRlngqvRRLRADIGYIFQQFNLVNRlsvl 104
Cdd:PRK10522 344 LTIKRGELLFLIGGNGSGKSTLAMLLTGL-YQPQS--GEILLDGKPVTAEQP-----EDYRKLFSAVFTDFHLFDQ---- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 105 dnvLLGCLGRMPrwrgslalfnreEKQRAMAALDRVGLAD---LATQRAST--LSGGQQQRVAIARALTQRAEVILADEP 179
Cdd:PRK10522 412 ---LLGPEGKPA------------NPALVEKWLERLKMAHkleLEDGRISNlkLSKGQKKRLALLLALAEERDILLLDEW 476
|
170 180 190
....*....|....*....|....*....|..
gi 492088662 180 IASLDPESARRVMEILADINRSDGKTVVVTLH 211
Cdd:PRK10522 477 AADQDPHFRREFYQVLLPLLQEMGKTIFAISH 508
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
11-266 |
1.98e-11 |
|
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: 62.95 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 11 NKTFSHKSALV-----DLALSIQPGEMVALIGASGSGKSTLLrhlaglaycdrsnggqVQVLGREVQSSGRLNGQVRrlr 85
Cdd:cd03291 39 NLFFSNLCLVGapvlkNINLKIEKGEMLAITGSTGSGKTSLL----------------MLILGELEPSEGKIKHSGR--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 86 adIGYIfQQFNLVNRLSVLDNVLLGCLGRMPRWRGSLALFNREEKQRAMAALDRVGLAdlatQRASTLSGGQQQRVAIAR 165
Cdd:cd03291 100 --ISFS-SQFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLG----EGGITLSGGQRARISLAR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 166 ALTQRAEVILADEPIASLDPESARRVME-----ILADinrsdgKTVVVTLHQVDYaVRYCPRAVALKGGRIHFDGL---A 237
Cdd:cd03291 173 AVYKDADLYLLDSPFGYLDVFTEKEIFEscvckLMAN------KTRILVTSKMEH-LKKADKILILHEGSSYFYGTfseL 245
|
250 260 270
....*....|....*....|....*....|....*.
gi 492088662 238 QDLSKQFLNDLYGADADASL-------MITERSRRV 266
Cdd:cd03291 246 QSLRPDFSSKLMGYDTFDQFsaerrnsILTETLRRF 281
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-193 |
2.35e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 64.16 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 20 LVDLALSIQPGEMVALIGASGSGKSTLLrhlaglaycdrsnggqVQVLGREVQSSGRLNGQVRrlradIGYIfQQFNLVN 99
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLL----------------MMIMGELEPSEGKIKHSGR-----ISFS-PQTSWIM 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 100 RLSVLDNVLLGCLGRMPRWRGSLALFNREEKQRAMAALDRVGLADLATqrasTLSGGQQQRVAIARALTQRAEVILADEP 179
Cdd:TIGR01271 500 PGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGI----TLSGGQRARISLARAVYKDADLYLLDSP 575
|
170
....*....|....
gi 492088662 180 IASLDPESARRVME 193
Cdd:TIGR01271 576 FTHLDVVTEKEIFE 589
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
12-212 |
3.19e-11 |
|
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: 61.12 E-value: 3.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 12 KTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycdrsnggqvqvlgreVQSSGRLNGQVR--------- 82
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR-----------------TEGNVSVEGDIHyngipykef 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 83 --RLRADIGYIFQQFNLVNRLSV---LDNVLLGCLGRMPRwrgslalfnreekqramaaldrvgladlatqrasTLSGGQ 157
Cdd:cd03233 78 aeKYPGEIIYVSEEDVHFPTLTVretLDFALRCKGNEFVR----------------------------------GISGGE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 492088662 158 QQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQ 212
Cdd:cd03233 124 RKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQ 178
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-197 |
3.36e-11 |
|
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: 63.03 E-value: 3.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDrsnGGQVQVlGREVQssgrlngqvrrl 84
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPD---SGTIEI-GETVK------------ 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 85 radIGYIFQQF-NLVNRLSV-------LDNVLLGclgrmprwrgslalfNREEKQRAMAALDRVGLADlATQRASTLSGG 156
Cdd:TIGR03719 387 ---LAYVDQSRdALDPNKTVweeisggLDIIKLG---------------KREIPSRAYVGRFNFKGSD-QQKKVGQLSGG 447
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 492088662 157 QQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILAD 197
Cdd:TIGR03719 448 ERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLN 488
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-187 |
3.64e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.21 E-value: 3.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 6 HVQGLNKTF-SHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVQVlgrevqSSGrlngqvrrl 84
Cdd:PRK11819 8 TMNRVSKVVpPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV---DKEFEGEARP------APG--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 85 rADIGYIFQQFNLVNRLSVLDNVLLGclgrMPRWRGSLALFNR----------------EEKQRAMAALDRVGLADLATQ 148
Cdd:PRK11819 70 -IKVGYLPQEPQLDPEKTVRENVEEG----VAEVKAALDRFNEiyaayaepdadfdalaAEQGELQEIIDAADAWDLDSQ 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 492088662 149 --RA-------------STLSGGQQQRVAIARALTQRAEVILADEPIASLDPES 187
Cdd:PRK11819 145 leIAmdalrcppwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-187 |
3.66e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 62.99 E-value: 3.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 4 AIHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAglaycdrsngGQVQVLGREVQSSGrlngqvrr 83
Cdd:PRK15064 319 ALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLV----------GELEPDSGTVKWSE-------- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 84 lRADIGYIFQ----QFNlvNRLSVLD------------NVLLGCLGRMprwrgslaLFNreekqramaaldrvglADLAT 147
Cdd:PRK15064 381 -NANIGYYAQdhayDFE--NDLTLFDwmsqwrqegddeQAVRGTLGRL--------LFS----------------QDDIK 433
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 492088662 148 QRASTLSGGQQQRVAIARALTQRAEVILADEPIASLDPES 187
Cdd:PRK15064 434 KSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMES 473
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
18-187 |
4.15e-11 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 60.89 E-value: 4.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 18 SALVDLALSIQPGEMVALIGASGSGKSTLLrhLAGLAYCDRSNGgQVQVLGREVQSSGrlngqVRRLRADIGYIFQqfnl 97
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLI--LALFRFLEAEEG-KIEIDGIDISTIP-----LEDLRSSLTIIPQ---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 98 vnrlsvlDNVLLgclgrMPRWRGSLALFNREEKQRAMAALdRVgladlaTQRASTLSGGQQQRVAIARALTQRAEVILAD 177
Cdd:cd03369 90 -------DPTLF-----SGTIRSNLDPFDEYSDEEIYGAL-RV------SEGGLNLSQGQRQLLCLARALLKRPRVLVLD 150
|
170
....*....|
gi 492088662 178 EPIASLDPES 187
Cdd:cd03369 151 EATASIDYAT 160
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
20-212 |
5.45e-11 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 62.94 E-value: 5.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 20 LVDLALSIQPGEMVALIGASGSGKSTLLRHLAGlaycdRSNGGQVQvlgREVQSSGRLNGQVRRLRADiGYIFQQFNLVN 99
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG-----RKTGGYIE---GDIRISGFPKKQETFARIS-GYCEQNDIHSP 966
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 100 RLSVLDNVLLGCLGRMPRWRGslalfnREEKQR------AMAALDRVGLADLATQRASTLSGGQQQRVAIARALTQRAEV 173
Cdd:PLN03140 967 QVTVRESLIYSAFLRLPKEVS------KEEKMMfvdevmELVELDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVANPSI 1040
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 492088662 174 ILADEPIASLDPESARRVMEILAdiNRSD-GKTVVVTLHQ 212
Cdd:PLN03140 1041 IFMDEPTSGLDARAAAIVMRTVR--NTVDtGRTVVCTIHQ 1078
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
22-184 |
6.04e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.33 E-value: 6.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 22 DLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQSSGRLNGqvrrLRADIGYIFQQFN---LV 98
Cdd:PRK10762 270 DVSFTLRKGEILGVSGLMGAGRTELMKVLYGAL---PRTSGYVTLDGHEVVTRSPQDG----LANGIVYISEDRKrdgLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 99 NRLSVLDNVLLGCLGRMPRWRGSLalfNREEKQraMAALDRVGLADLAT----QRASTLSGGQQQRVAIARALTQRAEVI 174
Cdd:PRK10762 343 LGMSVKENMSLTALRYFSRAGGSL---KHADEQ--QAVSDFIRLFNIKTpsmeQAIGLLSGGNQQKVAIARGLMTRPKVL 417
|
170
....*....|
gi 492088662 175 LADEPIASLD 184
Cdd:PRK10762 418 ILDEPTRGVD 427
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
21-222 |
6.49e-11 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 61.74 E-value: 6.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 21 VD-LALSIQPGEMVALIGASGSGKSTLLRHLAGLA------YCDRSNGGQVQVLgrevqssgRLNGQVRR--LRADIGYI 91
Cdd:PRK15093 23 VDrVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTkdnwrvTADRMRFDDIDLL--------RLSPRERRklVGHNVSMI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 92 FQQFNlvnrlSVLD---NVLLGCLGRMPRW--RGSLALFNREEKQRAMAALDRVGLADLATQRAS---TLSGGQQQRVAI 163
Cdd:PRK15093 95 FQEPQ-----SCLDpseRVGRQLMQNIPGWtyKGRWWQRFGWRKRRAIELLHRVGIKDHKDAMRSfpyELTEGECQKVMI 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 492088662 164 ARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDYAVRYCPR 222
Cdd:PRK15093 170 AIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADK 228
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
25-211 |
8.44e-11 |
|
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: 61.74 E-value: 8.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 25 LSIQPGEMVALIGASGSGKSTLLRHLAGLaYcdRSNGGQVQVLGREVQSSGRlngqvRRLRADIGYIFQQFNLVNRLsvl 104
Cdd:COG4615 353 LTIRRGELVFIVGGNGSGKSTLAKLLTGL-Y--RPESGEILLDGQPVTADNR-----EAYRQLFSAVFSDFHLFDRL--- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 105 dnvllgclgrmprwrgsLALFNREEKQRAMAALDRVGLAD---LATQRAST--LSGGQQQRVAIARALTQRAEVILADEP 179
Cdd:COG4615 422 -----------------LGLDGEADPARARELLERLELDHkvsVEDGRFSTtdLSQGQRKRLALLVALLEDRPILVFDEW 484
|
170 180 190
....*....|....*....|....*....|....
gi 492088662 180 IASLDPEsARRV--MEILADInRSDGKTVVVTLH 211
Cdd:COG4615 485 AADQDPE-FRRVfyTELLPEL-KARGKTVIAISH 516
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
27-252 |
1.06e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.05 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 27 IQPGEMVALIGASGSGKSTLLRHLAGlaycdRSNGGQVQ-----VLGREVQSSGRlngqvRRlradIGYIFQQFNLVNRL 101
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLNVLAE-----RVTTGVITggdrlVNGRPLDSSFQ-----RS----IGYVQQQDLHLPTS 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 102 SVLDNVLLGCLGRMPrwrgslALFNREEKQRAM-AALDRVGLADLATQRAST----LSGGQQQRVAIARALTQRAEVIL- 175
Cdd:TIGR00956 852 TVRESLRFSAYLRQP------KSVSKSEKMEYVeEVIKLLEMESYADAVVGVpgegLNVEQRKRLTIGVELVAKPKLLLf 925
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 176 ADEPIASLDPESARRVMEI---LADinrsDGKTVVVTLHQvdyavrycPRAVAL----------KGGR-IHFDGLAQDlS 241
Cdd:TIGR00956 926 LDEPTSGLDSQTAWSICKLmrkLAD----HGQAILCTIHQ--------PSAILFeefdrllllqKGGQtVYFGDLGEN-S 992
|
250
....*....|...
gi 492088662 242 KQFLN--DLYGAD 252
Cdd:TIGR00956 993 HTIINyfEKHGAP 1005
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
20-214 |
1.51e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 61.18 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 20 LVDLALSIQPGEMVALIGASGSGKSTLLRHLAGlaycDRSNG--GQVQVLGREvQSSGRLNGQVRRlraDIGYIFQQFNL 97
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG----DHPQGysNDLTLFGRR-RGSGETIWDIKK---HIGYVSSSLHL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 98 VNRLS--VLDNVLLGclgrmprWRGSLALFNR-EEKQR--AMAALDRVGLAD-LATQRASTLSGGQQQRVAIARALTQRA 171
Cdd:PRK10938 348 DYRVStsVRNVILSG-------FFDSIGIYQAvSDRQQklAQQWLDILGIDKrTADAPFHSLSWGQQRLALIVRALVKHP 420
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 492088662 172 EVILADEPIASLDP---ESARRVMEILadINRSDGKTVVVTLHQVD 214
Cdd:PRK10938 421 TLLILDEPLQGLDPlnrQLVRRFVDVL--ISEGETQLLFVSHHAED 464
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
152-213 |
5.29e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 60.04 E-value: 5.29e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492088662 152 TLSGGQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQV 213
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI 1419
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-211 |
5.43e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 59.41 E-value: 5.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 26 SIQPGEMVALIGASGSGKSTLLRHLAGlaycdrsnggqvqvlgREVQSSGRLNGQVR------RLRADIGYIFQQFnlvn 99
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAG----------------VLKPDEGEVDEDLKisykpqYISPDYDGTVEEF---- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 100 rlsvLDNVLlgclgrMPRWRGSLalFNREekqramaALDRVGLADLATQRASTLSGGQQQRVAIARALTQRAEVILADEP 179
Cdd:COG1245 422 ----LRSAN------TDDFGSSY--YKTE-------IIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEP 482
|
170 180 190
....*....|....*....|....*....|..
gi 492088662 180 IASLDPESARRVMEILADINRSDGKTVVVTLH 211
Cdd:COG1245 483 SAHLDVEQRLAVAKAIRRFAENRGKTAMVVDH 514
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
18-235 |
8.07e-10 |
|
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: 56.56 E-value: 8.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 18 SALVDLALSIQPGEMVALIGASGSGKSTLLrhLAGLAycdrsnggqvqvlgreVQSSGRLNGQVRRLrADIGYIFqqfnl 97
Cdd:cd03238 9 HNLQNLDVSIPLNVLVVVTGVSGSGKSTLV--NEGLY----------------ASGKARLISFLPKF-SRNKLIF----- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 98 VNRLSVLDNVLLGCLgrmprwrgslalfnreekqramaaldRVGladlatQRASTLSGGQQQRVAIARALTQRAE--VIL 175
Cdd:cd03238 65 IDQLQFLIDVGLGYL--------------------------TLG------QKLSTLSGGELQRVKLASELFSEPPgtLFI 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492088662 176 ADEPIASLDPESARRVMEILADInRSDGKTVVVTLHQV------DYAVRYCPRAvALKGGRIHFDG 235
Cdd:cd03238 113 LDEPSTGLHQQDINQLLEVIKGL-IDLGNTVILIEHNLdvlssaDWIIDFGPGS-GKSGGKVVFSG 176
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
15-243 |
9.90e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 58.57 E-value: 9.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 15 SHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLagLAYCDRSNGgQVQVLGREVqSSGRLNGQVRRLRadigyIFQQ 94
Cdd:PRK10789 326 TDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLI--QRHFDVSEG-DIRFHDIPL-TKLQLDSWRSRLA-----VVSQ 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 95 FNLVNRLSVLDNVLLGCLGRMPrwrgslalfnrEEKQRAmAALDRV---------GLADLATQRASTLSGGQQQRVAIAR 165
Cdd:PRK10789 397 TPFLFSDTVANNIALGRPDATQ-----------QEIEHV-ARLASVhddilrlpqGYDTEVGERGVMLSGGQKQRISIAR 464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492088662 166 ALTQRAEVILADEPIASLDpesARRVMEILADINR-SDGKTVVVTLHQVDyAVRYCPRAVALKGGRIHFDGLAQDLSKQ 243
Cdd:PRK10789 465 ALLLNAEILILDDALSAVD---GRTEHQILHNLRQwGEGRTVIISAHRLS-ALTEASEILVMQHGHIAQRGNHDQLAQQ 539
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-189 |
4.61e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.60 E-value: 4.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 21 VDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQSSGRLNgqvrRLRADIGYI---FQQFNL 97
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLR---PARGGRIMLNGKEINALSTAQ----RLARGLVYLpedRQSSGL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 98 VNRLSVLDNVLLGCLGRMPRWRgslalfnREEKQRAMaaLDR------VGLADlATQRASTLSGGQQQRVAIARALTQRA 171
Cdd:PRK15439 353 YLDAPLAWNVCALTHNRRGFWI-------KPARENAV--LERyrralnIKFNH-AEQAARTLSGGNQQKVLIAKCLEASP 422
|
170
....*....|....*...
gi 492088662 172 EVILADEPIASLDPeSAR 189
Cdd:PRK15439 423 QLLIVDEPTRGVDV-SAR 439
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
145-242 |
5.07e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 56.96 E-value: 5.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 145 LATQRASTLSGGQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQVDyAVRYCPRAV 224
Cdd:PTZ00265 572 LVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLS-TIRYANTIF 650
|
90 100
....*....|....*....|..
gi 492088662 225 AL----KGGRIHFDGLAQDLSK 242
Cdd:PTZ00265 651 VLsnreRGSTVDVDIIGEDPTK 672
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-215 |
5.20e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.74 E-value: 5.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 27 IQPGEMVALIGASGSGKSTLLRHLAGlaycdrsnggqvqvlgREVQSSGRLNGQVR------RLRADIGYIFQQFnlvnr 100
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAG----------------VLKPDEGEVDPELKisykpqYIKPDYDGTVEDL----- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 101 lsvLDNVllgclgrMPRWRGSLalFNREekqramaALDRVGLADLATQRASTLSGGQQQRVAIARALTQRAEVILADEPI 180
Cdd:PRK13409 421 ---LRSI-------TDDLGSSY--YKSE-------IIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPS 481
|
170 180 190
....*....|....*....|....*....|....*...
gi 492088662 181 ASLDPESARRVMEILADINRSDGKTVVVTLHQV---DY 215
Cdd:PRK13409 482 AHLDVEQRLAVAKAIRRIAEEREATALVVDHDIymiDY 519
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
27-191 |
6.90e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 56.33 E-value: 6.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 27 IQPGEMVALIGASGSGKST-LLRHLAGLAYCdrsnGGQVQVLGREVQSSGrlngqVRRLRadigyifQQFNLVNRLSVLd 105
Cdd:PTZ00243 1333 IAPREKVGIVGRTGSGKSTlLLTFMRMVEVC----GGEIRVNGREIGAYG-----LRELR-------RQFSMIPQDPVL- 1395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 106 nvllgclgrmprWRGSLAL----FNREEKQRAMAALDRVGLAD-LATQR----------ASTLSGGQQQRVAIARALTQR 170
Cdd:PTZ00243 1396 ------------FDGTVRQnvdpFLEASSAEVWAALELVGLRErVASESegidsrvlegGSNYSVGQRQLMCMARALLKK 1463
|
170 180
....*....|....*....|..
gi 492088662 171 AE-VILADEPIASLDPESARRV 191
Cdd:PTZ00243 1464 GSgFILMDEATANIDPALDRQI 1485
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
27-246 |
7.13e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 56.27 E-value: 7.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 27 IQPGEMVALIGASGSGKSTLLRHLAGlaycdRSNGGQVQVLGREVQSSGRLNGQVRRLRADIGYIFQQFNLVNRLSVLDN 106
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIAS-----NTDGFHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVHFPHLTVGET 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 107 VLLGCLGRMPRWRGSLalFNREEKQRAMA--ALDRVGLADLATQRAST-----LSGGQQQRVAIARALTQRAEVILADEP 179
Cdd:TIGR00956 159 LDFAARCKTPQNRPDG--VSREEYAKHIAdvYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKIQCWDNA 236
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492088662 180 IASLDPESAR---RVMEILADINRSdgkTVVVTLHQV-DYAVRYCPRAVALKGGRIHFDGLAQDLSKQFLN 246
Cdd:TIGR00956 237 TRGLDSATALefiRALKTSANILDT---TPLVAIYQCsQDAYELFDKVIVLYEGYQIYFGPADKAKQYFEK 304
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-189 |
1.05e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.51 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDrsnGGQVQVlGREVQssgrlngqvrrl 84
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPD---SGTIKI-GETVK------------ 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 85 radIGYIFQQF-NLVNRLSV-------LDNVLLGclgrmprwrgslalfNREEKQRAMAAldRVGL--ADlATQRASTLS 154
Cdd:PRK11819 389 ---LAYVDQSRdALDPNKTVweeisggLDIIKVG---------------NREIPSRAYVG--RFNFkgGD-QQKKVGVLS 447
|
170 180 190
....*....|....*....|....*....|....*
gi 492088662 155 GGQQQRVAIARALTQRAEVILADEPIASLDPESAR 189
Cdd:PRK11819 448 GGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLR 482
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
20-275 |
2.99e-08 |
|
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: 53.32 E-value: 2.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 20 LVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDrsngGQVQVLGREVQSSgrlngQVRRLRADIGYIFQQFNLVN 99
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE----GDIQIDGVSWNSV-----PLQKWRKAFGVIPQKVFIFS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 100 rlsvldnvllGCLgrmprwRGSLALFNREEKQRAMAALDRVGLADLATQ-----------RASTLSGGQQQRVAIARALT 168
Cdd:cd03289 91 ----------GTF------RKNLDPYGKWSDEEIWKVAEEVGLKSVIEQfpgqldfvlvdGGCVLSHGHKQLMCLARSVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 169 QRAEVILADEPIASLDPESARRVMEILAdiNRSDGKTVVVTLHQVDyAVRYCPRAVALKGGRI-HFDGLAQDLS-KQFLN 246
Cdd:cd03289 155 SKAKILLLDEPSAHLDPITYQVIRKTLK--QAFADCTVILSEHRIE-AMLECQRFLVIEENKVrQYDSIQKLLNeKSHFK 231
|
250 260
....*....|....*....|....*....
gi 492088662 247 DLYGADADASLMITERSRRVRQKPRLELA 275
Cdd:cd03289 232 QAISPSDRLKLFPRRNSSKSKRKPRPQIQ 260
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
15-212 |
3.49e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 52.57 E-value: 3.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 15 SHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVlgrevqssgrLNGQVRRL-RADIGYIFQ 93
Cdd:PRK13541 11 IEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIM---QPSSGNIYY----------KNCNINNIaKPYCTYIGH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 94 QFNLVNRLSVLDNVLLgclgrmprWRgslALFNREEKqrAMAALDRVGLADLATQRASTLSGGQQQRVAIARALTQRAEV 173
Cdd:PRK13541 78 NLGLKLEMTVFENLKF--------WS---EIYNSAET--LYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDL 144
|
170 180 190
....*....|....*....|....*....|....*....
gi 492088662 174 ILADEPIASLDPESaRRVMEILADINRSDGKTVVVTLHQ 212
Cdd:PRK13541 145 WLLDEVETNLSKEN-RDLLNNLIVMKANSGGIVLLSSHL 182
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-257 |
4.63e-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: 53.80 E-value: 4.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 20 LVDLALSIQPGEMVALIGASGSGKSTLLrhlAGLAYCDRSNGGQVQVLGREVQSSGrlngqVRRLRADIGYIFQqfnlvn 99
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLT---LGLFRINESAEGEIIIDGLNIAKIG-----LHDLRFKITIIPQ------ 1367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 100 rlsvlDNVLLGCLGRMprwrgSLALFNREEKQRAMAALDRVGLADLAT-----------QRASTLSGGQQQRVAIARALT 168
Cdd:TIGR00957 1368 -----DPVLFSGSLRM-----NLDPFSQYSDEEVWWALELAHLKTFVSalpdkldhecaEGGENLSVGQRQLVCLARALL 1437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 169 QRAEVILADEPIASLDPESARRVMEILAdiNRSDGKTVVVTLHQVDYAVRYCpRAVALKGGRIHFDGLAQDLSKQfLNDL 248
Cdd:TIGR00957 1438 RKTKILVLDEATAAVDLETDNLIQSTIR--TQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQ-RGIF 1513
|
....*....
gi 492088662 249 YGADADASL 257
Cdd:TIGR00957 1514 YSMAKDAGL 1522
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
124-235 |
1.17e-07 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 51.10 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 124 LFNREEKQRAMAALDRVGLADLATQR-ASTLSGGQQQRVAIARAL-TQRAEVI-LADEPIASLDPESARRVMEILADInR 200
Cdd:cd03270 108 LFARVGIRERLGFLVDVGLGYLTLSRsAPTLSGGEAQRIRLATQIgSGLTGVLyVLDEPSIGLHPRDNDRLIETLKRL-R 186
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 492088662 201 SDGKTVVVTLH------QVDYAVRYCPRAvALKGGRIHFDG 235
Cdd:cd03270 187 DLGNTVLVVEHdedtirAADHVIDIGPGA-GVHGGEIVAQG 226
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
5-212 |
1.31e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 50.72 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQVLGREVQSsgrlngqvrrl 84
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLL---NPEKGEILFERQSIKK----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 85 raDIGYIFQQFNLV-NRLSVLDNVLL--GCLGRMPRWRGSLALfnrEEKQRAMAaldrvgLADLATQRASTLSGGQQQRV 161
Cdd:PRK13540 68 --DLCTYQKQLCFVgHRSGINPYLTLreNCLYDIHFSPGAVGI---TELCRLFS------LEHLIDYPCGLLSSGQKRQV 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 492088662 162 AIARALTQRAEVILADEPIASLDPESARRVMEILADiNRSDGKTVVVTLHQ 212
Cdd:PRK13540 137 ALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQE-HRAKGGAVLLTSHQ 186
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-217 |
1.53e-07 |
|
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: 51.21 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 28 QPGEMVALIGASGSGKSTLLRHLAGL------AYCDRSNGGQV--QVLGREVQS--SGRLNGQVRRLRADigyifQQFNL 97
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKlkpnlgKFDDPPDWDEIldEFRGSELQNyfTKLLEGDVKVIVKP-----QYVDL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 98 VNRlSVLDNVLlgclgrmprwrgslALFNREEKQRAMAAL-DRVGLADLATQRASTLSGGQQQRVAIARALTQRAEVILA 176
Cdd:cd03236 99 IPK-AVKGKVG--------------ELLKKKDERGKLDELvDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFF 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 492088662 177 DEPIASLDPE---SARRVMEILADinrsDGKTVVVTLHqvDYAV 217
Cdd:cd03236 164 DEPSSYLDIKqrlNAARLIRELAE----DDNYVLVVEH--DLAV 201
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
25-231 |
2.74e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 51.07 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 25 LSIQPGEMVALIGASGSGKSTLLRHLAGLaycDRSNGGQVqvlgrevqssgRLNGQVRRLRADIGYIFQQFNL------- 97
Cdd:PRK11288 274 FSVRAGEIVGLFGLVGAGRSELMKLLYGA---TRRTAGQV-----------YLDGKPIDIRSPRDAIRAGIMLcpedrka 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 98 ---VNRLSVLDNVLLGCLGRMPRWRgsLALFNREEKQRA---MAALdRVGLADlATQRASTLSGGQQQRVAIARALTQRA 171
Cdd:PRK11288 340 egiIPVHSVADNINISARRHHLRAG--CLINNRWEAENAdrfIRSL-NIKTPS-REQLIMNLSGGNQQKAILGRWLSEDM 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 172 EVILADEPIASLDPESARRVMEILADINRsDGKTVVVTLHQVDYAVRYCPRAVALKGGRI 231
Cdd:PRK11288 416 KVILLDEPTRGIDVGAKHEIYNVIYELAA-QGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
25-187 |
2.95e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.10 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 25 LSIQPGEMVALIGASGSGKSTLLRhlaglaycdrsnggqvqVLGREVQ-SSGRLNGQ----VRRLRAD------------ 87
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMK-----------------ILNGEVLlDDGRIIYEqdliVARLQQDpprnvegtvydf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 88 ----IGYIFQQFNLVNRLSVLdnvllgcLGRMPRWRgslalfNREEKQRAMAALDRVGLADL--------------ATQR 149
Cdd:PRK11147 87 vaegIEEQAEYLKRYHDISHL-------VETDPSEK------NLNELAKLQEQLDHHNLWQLenrinevlaqlgldPDAA 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 492088662 150 ASTLSGGQQQRVAIARALTQRAEVILADEPIASLDPES 187
Cdd:PRK11147 154 LSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET 191
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
20-212 |
4.49e-07 |
|
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: 49.06 E-value: 4.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 20 LVDLALSIQPGEMVALIGASGSGKSTLLRHLAGL-AYcdRSNGGQVQVLGREVqssgrLNGQV-RRLRADIGYIFQqfnl 97
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpKY--EVTEGEILFKGEDI-----TDLPPeERARLGIFLAFQ---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 98 vnrlsvldnvllgclgRMPRWRG-SLALFNREekqramaaLDrVGladlatqrastLSGGQQQRVAIARALTQRAEVILA 176
Cdd:cd03217 85 ----------------YPPEIPGvKNADFLRY--------VN-EG-----------FSGGEKKRNEILQLLLLEPDLAIL 128
|
170 180 190
....*....|....*....|....*....|....*.
gi 492088662 177 DEPIASLDPESARRVMEILADINRSDGKTVVVTLHQ 212
Cdd:cd03217 129 DEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQ 164
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
130-246 |
4.63e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 50.98 E-value: 4.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 130 KQRaMAALDRVGLADLATQRA-STLSGGQQQRVAIARALTqrAEVI----LADEPIASLDPESARRVMEILADInRSDGK 204
Cdd:PRK00635 454 KSR-LSILIDLGLPYLTPERAlATLSGGEQERTALAKHLG--AELIgityILDEPSIGLHPQDTHKLINVIKKL-RDQGN 529
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 492088662 205 TVVVTLHQ------VDYAVRYCPRAvALKGGRIHFDGLAQDlskqFLN 246
Cdd:PRK00635 530 TVLLVEHDeqmislADRIIDIGPGA-GIFGGEVLFNGSPRE----FLA 572
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
132-214 |
6.13e-07 |
|
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: 49.54 E-value: 6.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 132 RAMAALDRVGLADLAT-QRASTLSGGQQQRVAIARALTQRAE----VILaDEPIASLDPESARRVMEILADInRSDGKTV 206
Cdd:cd03271 148 RKLQTLCDVGLGYIKLgQPATTLSGGEAQRIKLAKELSKRSTgktlYIL-DEPTTGLHFHDVKKLLEVLQRL-VDKGNTV 225
|
....*...
gi 492088662 207 VVTLHQVD 214
Cdd:cd03271 226 VVIEHNLD 233
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-217 |
1.05e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.42 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 27 IQPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQ-------VL----GREVQS--SGRLNGQVRRLRaDIGYIFQ 93
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGEL---IPNLGDYEeepswdeVLkrfrGTELQNyfKKLYNGEIKVVH-KPQYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 94 qfnlvnrlsvLDNVLLGCLGRMprwrgslaLFNREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAIARALTQRAEV 173
Cdd:PRK13409 172 ----------IPKVFKGKVREL--------LKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADF 233
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 492088662 174 ILADEPIASLDPESARRVMEILADInrSDGKTVVVTLHqvDYAV 217
Cdd:PRK13409 234 YFFDEPTSYLDIRQRLNVARLIREL--AEGKYVLVVEH--DLAV 273
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
5-184 |
1.22e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.47 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 5 IHVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDRSNGGQVQVLGREVQSSGR------LN 78
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMHAIDGIPKNCQILHVEQEVVGDDTtalqcvLN 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 79 GQVRRLRadigYIFQQFNLVNRLSVLDNVLLGCLGRMPRWRGS--------LA-LFNREEKQRAMAALDRV-----GL-- 142
Cdd:PLN03073 258 TDIERTQ----LLEEEAQLVAQQRELEFETETGKGKGANKDGVdkdavsqrLEeIYKRLELIDAYTAEARAasilaGLsf 333
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 492088662 143 -ADLATQRASTLSGGQQQRVAIARALTQRAEVILADEPIASLD 184
Cdd:PLN03073 334 tPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1-247 |
1.98e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 47.89 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 1 MNDAIHVQGLNKTFShksALVDLALSIQPGEMVALIGASGSGKSTLlrhlaglaycdrSN--GGQVQVLGREVQSSGrln 78
Cdd:PRK13546 24 MKDALIPKHKNKTFF---ALDDISLKAYEGDVIGLVGINGSGKSTL------------SNiiGGSLSPTVGKVDRNG--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 79 gqvrrlraDIGYIFQQFNLVNRLSVLDNVLLGCLgrmprwrgsLALFNREEKQRAMAALDRVG-LADLATQRASTLSGGQ 157
Cdd:PRK13546 86 --------EVSVIAISAGLSGQLTGIENIEFKML---------CMGFKRKEIKAMTPKIIEFSeLGEFIYQPVKKYSSGM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 158 QQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADInRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGLA 237
Cdd:PRK13546 149 RAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGEL 227
|
250
....*....|...
gi 492088662 238 QDLSK---QFLND 247
Cdd:PRK13546 228 DDVLPkyeAFLND 240
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-217 |
2.46e-06 |
|
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: 48.24 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 28 QPGEMVALIGASGSGKSTLLRHLAGLAycdRSNGGQVQ-------VL----GREVQS--SGRLNGQVRrlradIGYIFQQ 94
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGEL---KPNLGDYDeepswdeVLkrfrGTELQDyfKKLANGEIK-----VAHKPQY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 95 FNLVNRlsvldnVLLGclgrmprwRGSLALFNREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAIARALTQRAEVI 174
Cdd:COG1245 169 VDLIPK------VFKG--------TVRELLEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFY 234
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 492088662 175 LADEPIASLDPESARRVMEILADINRsDGKTVVVTLHqvDYAV 217
Cdd:COG1245 235 FFDEPSSYLDIYQRLNVARLIRELAE-EGKYVLVVEH--DLAI 274
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
33-196 |
3.56e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.93 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 33 VALIGASGSGKSTLLRHLAGlaycdrsnggqvqvlgrEVQSSgrlNGQVRRLRADIGYIFQQFNlVNRLSVLDNVLLgcl 112
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISG-----------------ELQPS---SGTVFRSAKVRMAVFSQHH-VDGLDLSSNPLL--- 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 113 gRMPRwrgslaLFNREEKQRAMAALDRVGLA-DLATQRASTLSGGQQQRVAIARALTQRAEVILADEPIASLDPESARRV 191
Cdd:PLN03073 594 -YMMR------CFPGVPEQKLRAHLGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEAL 666
|
....*
gi 492088662 192 MEILA 196
Cdd:PLN03073 667 IQGLV 671
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-274 |
3.94e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.58 E-value: 3.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 19 ALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYcdrSNGGQVQVLGRE--VQSSGRLNGQvrrlradigyifqqfn 96
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTM---PNKGTVDIKGSAalIAISSGLNGQ---------------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 97 lvnrLSVLDNVLLGclGRMprwrgsLALFNREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAIARALTQRAEVILA 176
Cdd:PRK13545 100 ----LTGIENIELK--GLM------MGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 177 DEPIASLDPESARRVMEILADInRSDGKTVVVTLHQVDYAVRYCPRAVALKGGRIHFDGLAQDLSKQFLNDLYGADAdas 256
Cdd:PRK13545 168 DEALSVGDQTFTKKCLDKMNEF-KEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYDEFLKKYNQ--- 243
|
250
....*....|....*...
gi 492088662 257 lMITERSRRVRQKPRLEL 274
Cdd:PRK13545 244 -MSVEERKDFREEQISQF 260
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
153-213 |
1.00e-05 |
|
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: 44.87 E-value: 1.00e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492088662 153 LSGGQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVTLHQV 213
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDL 132
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
33-198 |
1.58e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 44.62 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 33 VALIGASGSGKSTLLRhlaGLAYCdrsnggqvqvLGREVQSSGRLNGQVRRLRADIGYI-------------------FQ 93
Cdd:COG0419 26 NLIVGPNGAGKSTILE---AIRYA----------LYGKARSRSKLRSDLINVGSEEASVelefehggkryrierrqgeFA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 94 QFNLVN---RLSVLDNVL-LGCLGRMPRWRGSL--ALFNREEKQRAMAALDRVGLADLAT-QRASTLSGGQQQRVAIARA 166
Cdd:COG0419 93 EFLEAKpseRKEALKRLLgLEIYEELKERLKELeeALESALEELAELQKLKQEILAQLSGlDPIETLSGGERLRLALADL 172
|
170 180 190
....*....|....*....|....*....|..
gi 492088662 167 LtqraEVILaDepIASLDPESARRVMEILADI 198
Cdd:COG0419 173 L----SLIL-D--FGSLDEERLERLLDALEEL 197
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
132-214 |
1.62e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 46.16 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 132 RAMAALDRVGLADLAT-QRASTLSGGQQQRVAIARALTQRAE---VILADEPIASLDPESARRVMEILADInRSDGKTVV 207
Cdd:TIGR00630 808 RKLQTLCDVGLGYIRLgQPATTLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLHFDDIKKLLEVLQRL-VDKGNTVV 886
|
....*..
gi 492088662 208 VTLHQVD 214
Cdd:TIGR00630 887 VIEHNLD 893
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-231 |
2.31e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 45.74 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 23 LALSIQPGEMVALIGASGSGKSTLLRHLAGLAYCDRsngGQVQVLGREVQSSGRLNgqVRRLradigyifqqfnlvnrLS 102
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEK---GRIMIDDCDVAKFGLTD--LRRV----------------LS 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 103 VLDNVLLGCLGRMprwRGSLALFNREEKQRAMAALDRVGLADLATQR-----------ASTLSGGQQQRVAIARALTQRA 171
Cdd:PLN03232 1314 IIPQSPVLFSGTV---RFNIDPFSEHNDADLWEALERAHIKDVIDRNpfgldaevsegGENFSVGQRQLLSLARALLRRS 1390
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 172 EVILADEPIASLDPESARRVMEILADINRSdgKTVVVTLHQVDYAVRyCPRAVALKGGRI 231
Cdd:PLN03232 1391 KILVLDEATASVDVRTDSLIQRTIREEFKS--CTMLVIAHRLNTIID-CDKILVLSSGQV 1447
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
102-212 |
2.36e-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: 43.50 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 102 SVLDNVLLGCLGRMPRWRGSLalfnrEEKQRAMAALDRVGLADLATQrastLSGGQQQRVAIARAL----TQRAEVILAD 177
Cdd:cd03227 36 TILDAIGLALGGAQSATRRRS-----GVKAGCIVAAVSAELIFTRLQ----LSGGEKELSALALILalasLKPRPLYILD 106
|
90 100 110
....*....|....*....|....*....|....*
gi 492088662 178 EPIASLDPESARRVMEILADiNRSDGKTVVVTLHQ 212
Cdd:cd03227 107 EIDRGLDPRDGQALAEAILE-HLVKGAQVIVITHL 140
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
6-184 |
2.68e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 45.31 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 6 HVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGlAYCDRSNGgQVQVLGREVqssgRLNGQVRRLR 85
Cdd:PRK13549 264 NLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFG-AYPGRWEG-EIFIDGKPV----KIRNPQQAIA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 86 ADIGYI---FQQFNLVNRLSVLDNVLLGCLGRMPRwrGSLALFNREEK--QRAMAALdRVGLADLAtQRASTLSGGQQQR 160
Cdd:PRK13549 338 QGIAMVpedRKRDGIVPVMGVGKNITLAALDRFTG--GSRIDDAAELKtiLESIQRL-KVKTASPE-LAIARLSGGNQQK 413
|
170 180
....*....|....*....|....
gi 492088662 161 VAIARALTQRAEVILADEPIASLD 184
Cdd:PRK13549 414 AVLAKCLLLNPKILILDEPTRGID 437
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
7-197 |
4.54e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.56 E-value: 4.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 7 VQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAglaycdrsngGQVQvlgrevQSSGRLNgqvRRLRA 86
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLML----------GQLQ------ADSGRIH---CGTKL 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 87 DIGYiFQQF--NLVNRLSVLDNVLLGclgrmprwrgslalfnreeKQRAMA-ALDRVGLADL-----ATQRAST----LS 154
Cdd:PRK11147 383 EVAY-FDQHraELDPEKTVMDNLAEG-------------------KQEVMVnGRPRHVLGYLqdflfHPKRAMTpvkaLS 442
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 492088662 155 GGQQQRVAIARALTQRAEVILADEPIASLDPESARRVMEILAD 197
Cdd:PRK11147 443 GGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDS 485
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
140-235 |
5.09e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 44.62 E-value: 5.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 140 VGLADLATQR-ASTLSGGQQQRVAIAR----ALTQRAEVIlaDEPIASLDPESARRVMEILADInRSDGKTVVV------ 208
Cdd:TIGR00630 475 VGLDYLSLSRaAGTLSGGEAQRIRLATqigsGLTGVLYVL--DEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVvehded 551
|
90 100
....*....|....*....|....*..
gi 492088662 209 TLHQVDYAVRYCPRAvALKGGRIHFDG 235
Cdd:TIGR00630 552 TIRAADYVIDIGPGA-GEHGGEVVASG 577
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
24-214 |
1.02e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.46 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 24 ALSIQPGEMVALIGASGSGKSTLLRHLAGlaycdrsnggQVQVLGREVQSS----GRLN-GQVRRLRADIgyiFQQFNlV 98
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAG----------ELPLLSGERQSQfshiTRLSfEQLQKLVSDE---WQRNN-T 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 99 NRLSVLDNVLlgclGRMPRwrgSLALFNREEKQRAMAALDRVGLADLATQRASTLSGGQQQRVAIARALTQRAEVILADE 178
Cdd:PRK10938 89 DMLSPGEDDT----GRTTA---EIIQDEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDE 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 492088662 179 PIASLDPESARRVMEILADINRSdGKTVVVTLHQVD 214
Cdd:PRK10938 162 PFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFD 196
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-211 |
1.41e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 41.20 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 29 PGEMVALIGASGSGKSTLLRHLAGLAYCDrsnggqvqvlgrevqssgrlNGQVRRLRADigyifqqfnlvnrlsvldnvl 108
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPP--------------------GGGVIYIDGE--------------------- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 109 lgclgrmprwrgslalfnreekqRAMAALDRVGLADLATQRASTLSGGQQQRVAIARALTQRAEVILADEPIASLDPESA 188
Cdd:smart00382 40 -----------------------DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQE 96
|
170 180
....*....|....*....|....*...
gi 492088662 189 RRVMEI-----LADINRSDGKTVVVTLH 211
Cdd:smart00382 97 ALLLLLeelrlLLLLKSEKNLTVILTTN 124
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
27-213 |
1.82e-04 |
|
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: 41.82 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 27 IQPGEMVALIGASGSGKSTLlrHLAGLAYCDRSNGgQVQVLGREVQSSgrlngQVRRLRADIGYIFQ---------QFNL 97
Cdd:cd03288 44 IKPGQKVGICGRTGSGKSSL--SLAFFRMVDIFDG-KIVIDGIDISKL-----PLHTLRSRLSIILQdpilfsgsiRFNL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 98 VNRLSVLDNVLlgclgrmprWRgSLALFNREEKQRAMAAldrvGLADLATQRASTLSGGQQQRVAIARALTQRAEVILAD 177
Cdd:cd03288 116 DPECKCTDDRL---------WE-ALEIAQLKNMVKSLPG----GLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMD 181
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 492088662 178 EPIASLDPES----ARRVMEILADinrsdgKTVVVTLHQV 213
Cdd:cd03288 182 EATASIDMATenilQKVVMTAFAD------RTVVTIAHRV 215
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
34-211 |
2.28e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 41.44 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 34 ALIGASGSGKSTLLRHLAGLAYCDRSNGGQVQVLGREVQSSGRLNGQVR-RLRADIGyifQQFNLVNRLSVLDNVLlgcl 112
Cdd:cd03240 26 LIVGQNGAGKTTIIEALKYALTGELPPNSKGGAHDPKLIREGEVRAQVKlAFENANG---KKYTITRSLAILENVI---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 113 grmprwrgslalFNREEkqramaaldrvGLADLATQRASTLSGGQQQ------RVAIARALTQRAEVILADEPIASLDPE 186
Cdd:cd03240 99 ------------FCHQG-----------ESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEE 155
|
170 180
....*....|....*....|....*.
gi 492088662 187 SARRVM-EILADINRSDGKTVVVTLH 211
Cdd:cd03240 156 NIEESLaEIIEERKSQKNFQLIVITH 181
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
148-214 |
3.12e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.98 E-value: 3.12e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492088662 148 QRASTLSGGQQQRVAIARALTQRAE----VILaDEPIASLDPESARRVMEILADInRSDGKTVVVTLHQVD 214
Cdd:PRK00349 826 QPATTLSGGEAQRVKLAKELSKRSTgktlYIL-DEPTTGLHFEDIRKLLEVLHRL-VDKGNTVVVIEHNLD 894
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
7-215 |
3.38e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 41.32 E-value: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 7 VQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycdrsnggQVQVLGREVQSSGR-LNGQVRRLR 85
Cdd:PRK09580 4 IKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRE--------DYEVTGGTVEFKGKdLLELSPEDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 86 ADIGyIFQQFNLVNRLSVLDNVLLgclgrmprWRGSLalfNREEKQRAMAALDRVGLADLATQRASTL------------ 153
Cdd:PRK09580 76 AGEG-IFMAFQYPVEIPGVSNQFF--------LQTAL---NAVRSYRGQEPLDRFDFQDLMEEKIALLkmpedlltrsvn 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 154 ---SGGQQQRVAIARALTQRAEVILADEPIASLDPESARRVME---ILADINRSdgkTVVVTLHQ--VDY 215
Cdd:PRK09580 144 vgfSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADgvnSLRDGKRS---FIIVTHYQriLDY 210
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
7-52 |
4.66e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 40.78 E-value: 4.66e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 492088662 7 VQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAG 52
Cdd:CHL00131 10 IKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG 55
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
143-211 |
7.57e-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: 39.94 E-value: 7.57e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492088662 143 ADLATQRASTLSGGQQQRVAIARALT----------QRAEVILADEPIASLDPESARRVMEILADInRSDGKTVVVTLH 211
Cdd:cd03279 114 DRFLARPVSTLSGGETFLASLSLALAlsevlqnrggARLEALFIDEGFGTLDPEALEAVATALELI-RTENRMVGVISH 191
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
72-227 |
8.05e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. 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: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.72 E-value: 8.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 72 QSSGRLNGQVRRLRADIGYIFQQFnlVNRLSVLDNVLLGCLgRMPRWRGSLALFNREEKQRAMAALDRVGLADLATQRAS 151
Cdd:TIGR00618 873 QLSDKLNGINQIKIQFDGDALIKF--LHEITLYANVRLANQ-SEGRFHGRYADSHVNARKYQGLALLVADAYTGSVRPSA 949
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 152 TLSGGQQQRVAIARAL----------TQRAEVILADEPIASLDPESARRVMEILADINRSdGKTVVVTLHQVDYAVRYCP 221
Cdd:TIGR00618 950 TLSGGETFLASLSLALaladllstsgGTVLDSLFIDEGFGSLDEDSLDRAIGILDAIREG-SKMIGIISHVPEFRERIPH 1028
|
....*.
gi 492088662 222 RAVALK 227
Cdd:TIGR00618 1029 RILVKK 1034
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
131-208 |
1.12e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.39 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 131 QRAMAALDRVGLADLAT-QRASTLSGGQQQRVAIARALTQRAE---VILADEPIASLDPESARRVMEILadiNR--SDGK 204
Cdd:COG0178 804 ARKLQTLQDVGLGYIKLgQPATTLSGGEAQRVKLASELSKRSTgktLYILDEPTTGLHFHDIRKLLEVL---HRlvDKGN 880
|
....
gi 492088662 205 TVVV 208
Cdd:COG0178 881 TVVV 884
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-184 |
1.29e-03 |
|
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: 39.81 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 6 HVQGLNKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGlAYCDRSNGgQVQVLGREVQssgrLNGQVRRLR 85
Cdd:TIGR02633 262 NLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFG-AYPGKFEG-NVFINGKPVD----IRNPAQAIR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 86 ADIGYI---FQQFNLVNRLSVLDNVLLGCLGRmprWRGSLALFNREEKQRAMAALDRVGL----ADLATQRastLSGGQQ 158
Cdd:TIGR02633 336 AGIAMVpedRKRHGIVPILGVGKNITLSVLKS---FCFKMRIDAAAELQIIGSAIQRLKVktasPFLPIGR---LSGGNQ 409
|
170 180
....*....|....*....|....*.
gi 492088662 159 QRVAIARALTQRAEVILADEPIASLD 184
Cdd:TIGR02633 410 QKAVLAKMLLTNPRVLILDEPTRGVD 435
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
23-76 |
1.46e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 39.53 E-value: 1.46e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 492088662 23 LALSIQPGEMVALIGASGSGKSTLLRHLAglaycdrsnGGQVQVLG--REVQSSGR 76
Cdd:PRK01889 188 LAAWLSGGKTVALLGSSGVGKSTLVNALL---------GEEVQKTGavREDDSKGR 234
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
27-142 |
3.72e-03 |
|
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.
Pssm-ID: 463892 [Multi-domain] Cd Length: 193 Bit Score: 37.75 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 27 IQPGEMVALIGASGSGKSTLLRHLA-GLAYCDRSNGGQVQVLGREV---QSSGRLNGQVRRLRAdigyIFQQFNLVNRLS 102
Cdd:pfam13481 30 LPAGGLGLLAGAPGTGKTTLALDLAaAVATGKPWLGGPRVPEQGKVlyvSAEGPADELRRRLRA----AGADLDLPARLL 105
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 492088662 103 VLDNVLLGCLGRMPRWRGSLALFnREEKQRAMAALDRVGL 142
Cdd:pfam13481 106 FLSLVESLPLFFLDRGGPLLDAD-VDALEAALEEVEDPDL 144
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
15-51 |
3.95e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 37.84 E-value: 3.95e-03
10 20 30
....*....|....*....|....*....|....*...
gi 492088662 15 SHKSALVDLALSIQPGE-MVALIGASGSGKSTLLRHLA 51
Cdd:COG3267 27 SHREALARLEYALAQGGgFVVLTGEVGTGKTTLLRRLL 64
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
11-209 |
4.79e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 38.17 E-value: 4.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 11 NKTFSHKSALVDLALSIQPGEMVALIGASGSGKSTLLRHLAGLAycDRSnGGQVQVLGREVQSSGRL----NG-----QV 81
Cdd:PRK10982 255 NLTSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIR--EKS-AGTITLHGKKINNHNANeainHGfalvtEE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 82 RRLRADIGYIFQQFNlvnrlSVLDNvllgclgrMPRWRGSLALF-NREEKQRAMAALD--RVGLADLATQRAStLSGGQQ 158
Cdd:PRK10982 332 RRSTGIYAYLDIGFN-----SLISN--------IRNYKNKVGLLdNSRMKSDTQWVIDsmRVKTPGHRTQIGS-LSGGNQ 397
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 492088662 159 QRVAIARALTQRAEVILADEPIASLDPESARRVMEILADINRSDGKTVVVT 209
Cdd:PRK10982 398 QKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIIS 448
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
25-47 |
5.01e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 34.50 E-value: 5.01e-03
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
22-208 |
7.60e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 37.46 E-value: 7.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 22 DLALSIQPGEMVALIGASGSGKSTLLRHLAGLAYcDRSNGGQVQVLGREVQSSGrlngqVRR-LRADIGYIFQ---QFNL 97
Cdd:NF040905 278 DVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSY-GRNISGTVFKDGKEVDVST-----VSDaIDAGLAYVTEdrkGYGL 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492088662 98 VNRLSVLDNVLLGCLGRMPRwRGSLalfnREEKQRAMAALDRvglADLAT------QRASTLSGGQQQRVAIARALTQRA 171
Cdd:NF040905 352 NLIDDIKRNITLANLGKVSR-RGVI----DENEEIKVAEEYR---KKMNIktpsvfQKVGNLSGGNQQKVVLSKWLFTDP 423
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 492088662 172 EVILADEPIASLDpesarrV---MEILADINR--SDGKTVVV 208
Cdd:NF040905 424 DVLILDEPTRGID------VgakYEIYTIINElaAEGKGVIV 459
|
|
| |
