|
Name |
Accession |
Description |
Interval |
E-value |
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
19-261 |
2.15e-113 |
|
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: 326.55 E-value: 2.15e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 19 QGERVVHIDKLWSIFGEgesqFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEG 98
Cdd:COG1127 1 MSEPMIEVRNLTKSFGD----RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 99 AA---SRVGMLFQQGALYSAFNVLDNVAFPLRELGTLPRALVDAAALVKLQMVGLkPEHAMRMPADLSGGMIKRVALARA 175
Cdd:COG1127 77 LYelrRRIGMLFQGGALFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGL-PGAADKMPSELSGGMRKRVALARA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 176 LIMDPPLLLLDEPTAGLDPNGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEVAVFPHP 255
Cdd:COG1127 156 LALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASDDP 235
|
....*.
gi 2788666989 256 FVAQFF 261
Cdd:COG1127 236 WVRQFL 241
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
42-260 |
3.05e-101 |
|
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: 295.57 E-value: 3.05e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 42 VHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAAS---RVGMLFQQGALYSAFNV 118
Cdd:cd03261 15 VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRlrrRMGMLFQSGALFDSLTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 119 LDNVAFPLRELGTLPRALVDAAALVKLQMVGLKPEHAmRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSD 198
Cdd:cd03261 95 FENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAED-LYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASG 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2788666989 199 DFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEVAVFPHPFVAQF 260
Cdd:cd03261 174 VIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASDDPLVRQF 235
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
44-249 |
5.34e-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: 192.93 E-value: 5.34e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQ----QgaLYSAfNVL 119
Cdd:COG1122 18 DDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLVFQnpddQ--LFAP-TVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 120 DNVAFPLRELGtLPRALVDAAALVKLQMVGLKpEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDD 199
Cdd:COG1122 95 EDVAFGPENLG-LPREEIRERVEEALELVGLE-HLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2788666989 200 FCALLRELHAElDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEV 249
Cdd:COG1122 173 LLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
41-255 |
2.54e-59 |
|
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: 196.66 E-value: 2.54e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 41 AVHqDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAA---SRVGMLFQ--QGALYSA 115
Cdd:COG1123 280 AVD-DVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRelrRRVQMVFQdpYSSLNPR 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 116 FNVLDNVAFPLRELGTLPRALVDAAALVKLQMVGLKPEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPN 195
Cdd:COG1123 359 MTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVS 438
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 196 GSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEvaVFPHP 255
Cdd:COG1123 439 VQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEE--VFANP 496
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
23-255 |
1.45e-58 |
|
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: 186.63 E-value: 1.45e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 23 VVHIDKLWSIFGEGESQFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGE---GA 99
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKelrKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 100 ASRVGMLFQQGALYSAFNVLDNVAFPLrELGTLPRALVDAAALVKLQMVGLKpEHAMRMPADLSGGMIKRVALARALIMD 179
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPL-EIAGVPKAEIEERVLELLELVGLE-DKADAYPAQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2788666989 180 PPLLLLDEPTAGLDPNGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEvaVFPHP 255
Cdd:cd03258 159 PKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEE--VFANP 232
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
19-236 |
4.47e-58 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 186.45 E-value: 4.47e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 19 QGERVVHIDKLWSIFGEGESQFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGeg 98
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 99 aasRVGMLFQQGALYSAFNVLDNVAFPLRELGtLPRALVDAAALVKLQMVGLKpEHAMRMPADLSGGMIKRVALARALIM 178
Cdd:COG1116 81 ---DRGVVFQEPALLPWLTVLDNVALGLELRG-VPKAERRERARELLELVGLA-GFEDAYPHQLSGGMRQRVAIARALAN 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2788666989 179 DPPLLLLDEPTAGLDpngsddfcALLRE--------LHAELDLTVVMVTHDLDTLFALSSRVAVLA 236
Cdd:COG1116 156 DPEVLLMDEPFGALD--------ALTRErlqdellrLWQETGKTVLFVTHDVDEAVFLADRVVVLS 213
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
24-235 |
7.01e-58 |
|
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: 184.60 E-value: 7.01e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 24 VHIDKLWSIFGEGESQFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPaaamgGEGAASRV 103
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEP-----VTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 104 GMLFQQGALYSAFNVLDNVAFPLrELGTLPRALVDAAALVKLQMVGLKpEHAMRMPADLSGGMIKRVALARALIMDPPLL 183
Cdd:cd03293 76 GYVFQQDALLPWLTVLDNVALGL-ELQGVPKAEARERAEELLELVGLS-GFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 184 LLDEPTAGLDpngsddfcALLRE-LHAEL-------DLTVVMVTHDLDTLFALSSRVAVL 235
Cdd:cd03293 154 LLDEPFSALD--------ALTREqLQEELldiwretGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
24-261 |
7.28e-58 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 188.77 E-value: 7.28e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 24 VHIDKLWSIFGEgesQFAVHqDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPaaamggegaASR- 102
Cdd:COG3842 6 LELENVSKRYGD---VTALD-DVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRD---------VTGl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 103 ------VGMLFQQGALYSAFNVLDNVAFPLRELGtLPRAlvDAAALVK--LQMVGLkPEHAMRMPADLSGGMIKRVALAR 174
Cdd:COG3842 73 ppekrnVGMVFQDYALFPHLTVAENVAFGLRMRG-VPKA--EIRARVAelLELVGL-EGLADRYPHQLSGGQQQRVALAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 175 ALIMDPPLLLLDEPTAGLDPNGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEVAVFP- 253
Cdd:COG3842 149 ALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPa 228
|
....*...
gi 2788666989 254 HPFVAQFF 261
Cdd:COG3842 229 TRFVADFI 236
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
24-240 |
2.72e-57 |
|
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: 183.07 E-value: 2.72e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 24 VHIDKLWSIFGEGESQFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAAS-- 101
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAfr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 102 --RVGMLFQQGALYSAFNVLDNVAFPLReLGTLPRALVDAAALVKLQMVGLKpEHAMRMPADLSGGMIKRVALARALIMD 179
Cdd:cd03255 81 rrHIGFVFQSFNLLPDLTALENVELPLL-LAGVPKKERRERAEELLERVGLG-DRLNHYPSELSGGQQQRVAIARALAND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2788666989 180 PPLLLLDEPTAGLDPNGSDDFCALLRELHAELDLTVVMVTHDLDtLFALSSRVAVLAEKKV 240
Cdd:cd03255 159 PKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPE-LAEYADRIIELRDGKI 218
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
24-244 |
4.10e-57 |
|
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: 182.33 E-value: 4.10e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 24 VHIDKLWSIFGegeSQFAVhQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAasRV 103
Cdd:cd03259 1 LELKGLSKTYG---SVRAL-DDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERR--NI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 104 GMLFQQGALYSAFNVLDNVAFPLRELGtLPRALVDAAALVKLQMVGLkPEHAMRMPADLSGGMIKRVALARALIMDPPLL 183
Cdd:cd03259 75 GMVFQDYALFPHLTVAENIAFGLKLRG-VPKAEIRARVRELLELVGL-EGLLNRYPHELSGGQQQRVALARALAREPSLL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2788666989 184 LLDEPTAGLDPNGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTG 244
Cdd:cd03259 153 LLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
44-239 |
1.18e-56 |
|
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: 181.13 E-value: 1.18e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQ----QgalYSAFNVL 119
Cdd:cd03225 18 DDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQnpddQ---FFGPTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 120 DNVAFPLRELGtLPRALVDAAALVKLQMVGLKpEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDD 199
Cdd:cd03225 95 EEVAFGLENLG-LPEEEIEERVEEALELVGLE-GLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2788666989 200 FCALLRELHAElDLTVVMVTHDLDTLFALSSRVAVLAEKK 239
Cdd:cd03225 173 LLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
24-249 |
3.58e-55 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 177.95 E-value: 3.58e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 24 VHIDKLWSIFGegeSQFAVHqDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAaSRV 103
Cdd:COG1131 1 IEVRGLTKRYG---DKTALD-GVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVR-RRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 104 GMLFQQGALYSAFNVLDNVAFpLRELGTLPRALVDAAALVKLQMVGLkPEHAMRMPADLSGGMIKRVALARALIMDPPLL 183
Cdd:COG1131 76 GYVPQEPALYPDLTVRENLRF-FARLYGLPRKEARERIDELLELFGL-TDAADRKVGTLSGGMKQRLGLALALLHDPELL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2788666989 184 LLDEPTAGLDPNGSDDFCALLRELHAElDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEV 249
Cdd:COG1131 154 ILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
39-260 |
1.13e-54 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 176.66 E-value: 1.13e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 39 QFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGaaSRVGMLFQQGALYSAFNV 118
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK--RPVNTVFQNYALFPHLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 119 LDNVAFPLReLGTLPRALVDAAALVKLQMVGLKpEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSD 198
Cdd:cd03300 90 FENIAFGLR-LKKLPKAEIKERVAEALDLVQLE-GYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRK 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2788666989 199 DFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEvaVFPHP---FVAQF 260
Cdd:cd03300 168 DMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEE--IYEEPanrFVADF 230
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
23-232 |
1.58e-54 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 176.00 E-value: 1.58e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 23 VVHIDKLWSIFGEGESQFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAA-- 100
Cdd:COG1136 4 LLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELArl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 101 --SRVGMLFQQGALYSAFNVLDNVAFPLReLGTLPRALVDAAALVKLQMVGLKpEHAMRMPADLSGGMIKRVALARALIM 178
Cdd:COG1136 84 rrRHIGFVFQFFNLLPELTALENVALPLL-LAGVSRKERRERARELLERVGLG-DRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2788666989 179 DPPLLLLDEPTAGLDPNGSDDFCALLRELHAELDLTVVMVTHDLDtLFALSSRV 232
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPE-LAARADRV 214
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
45-249 |
2.86e-53 |
|
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: 174.56 E-value: 2.86e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 45 DLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQ---PAAAMGGEGAASRVGMLFQQgALYSAF--NVL 119
Cdd:TIGR04521 23 DVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRditAKKKKKLKDLRKKVGLVFQF-PEHQLFeeTVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 120 DNVAFPLRELGtLPRALVDAAALVKLQMVGLKPEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDD 199
Cdd:TIGR04521 102 KDIAFGPKNLG-LSEEEAEERVKEALELVGLDEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKE 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2788666989 200 FCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEV 249
Cdd:TIGR04521 181 ILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREV 230
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
24-237 |
7.60e-53 |
|
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: 170.06 E-value: 7.60e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 24 VHIDKLWSIFGEgesQFAVHqDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASR- 102
Cdd:cd03229 1 LELKNVSKRYGQ---KTVLN-DVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 103 -VGMLFQQGALYSAFNVLDNVAFPLrelgtlpralvdaaalvklqmvglkpehamrmpadlSGGMIKRVALARALIMDPP 181
Cdd:cd03229 77 rIGMVFQDFALFPHLTVLENIALGL------------------------------------SGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2788666989 182 LLLLDEPTAGLDPNGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAE 237
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
24-263 |
7.92e-53 |
|
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: 173.21 E-value: 7.92e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 24 VHIDKLWSIFG-----------EGESQFAVH---------QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGT 83
Cdd:cd03294 1 IKIKGLYKIFGknpqkafkllaKGKSKEEILkktgqtvgvNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 84 VEVLGQPAAAMGGEGAAS----RVGMLFQQGALYSAFNVLDNVAFPLrELGTLPRALVDAAALVKLQMVGLKP-EHamRM 158
Cdd:cd03294 81 VLIDGQDIAAMSRKELRElrrkKISMVFQSFALLPHRTVLENVAFGL-EVQGVPRAEREERAAEALELVGLEGwEH--KY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 159 PADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEK 238
Cdd:cd03294 158 PDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDG 237
|
250 260
....*....|....*....|....*.
gi 2788666989 239 KVLVTGTPQEVAVFP-HPFVAQFFQG 263
Cdd:cd03294 238 RLVQVGTPEEILTNPaNDYVREFFRG 263
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
33-235 |
3.31e-52 |
|
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: 170.38 E-value: 3.31e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 33 FGEGESQFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASR---VGMLFQQ 109
Cdd:cd03257 11 FPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRrkeIQMVFQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 110 GalYSAFN----VLDNVAFPLRELGTLPR-ALVDAAALVKLQMVGLKPEHAMRMPADLSGGMIKRVALARALIMDPPLLL 184
Cdd:cd03257 91 P--MSSLNprmtIGEQIAEPLRIHGKLSKkEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARALALNPKLLI 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2788666989 185 LDEPTAGLDPNGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVL 235
Cdd:cd03257 169 ADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVM 219
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
33-269 |
6.96e-52 |
|
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: 169.98 E-value: 6.96e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 33 FGEGESQFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQGal 112
Cdd:COG1124 11 YGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDP-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 113 YSAFN----VLDNVAFPLRELGTLPRalvDAAALVKLQMVGLKPEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEP 188
Cdd:COG1124 89 YASLHprhtVDRILAEPLRIHGLPDR---EERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 189 TAGLDPNGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEVAVFP-HPFVAQFFQGERGR 267
Cdd:COG1124 166 TSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPkHPYTRELLAASLAF 245
|
..
gi 2788666989 268 RA 269
Cdd:COG1124 246 ER 247
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
45-263 |
5.16e-50 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 166.09 E-value: 5.16e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 45 DLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQ---PAAAMGGEGAASRVGMLFQQGALYSAFNVLDN 121
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEnipAMSRSRLYTVRKRMSMLFQSGALFTDMNVFDN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 122 VAFPLRELGTLPRALVDAAALVKLQMVGLKPEhAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDFC 201
Cdd:PRK11831 105 VAYPLREHTQLPAPLLHSTVMMKLEAVGLRGA-AKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLV 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2788666989 202 ALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEVAVFPHPFVAQFFQG 263
Cdd:PRK11831 184 KLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPRVRQFLDG 245
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
36-265 |
2.14e-49 |
|
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: 163.63 E-value: 2.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 36 GESQFAVhQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQGALYSA 115
Cdd:cd03295 11 GGGKKAV-NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQQIGLFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 116 FNVLDNVAFPLRELGtLPRALVDAAALVKLQMVGLKPEH-AMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDP 194
Cdd:cd03295 90 MTVEENIALVPKLLK-WPKEKIRERADELLALVGLDPAEfADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDP 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2788666989 195 NGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEVAVFPHP-FVAQFFQGER 265
Cdd:cd03295 169 ITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANdFVAEFVGADR 240
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
22-260 |
2.81e-49 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 166.48 E-value: 2.81e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 22 RVVHIDKlwsIFGegesQFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQpAAAMGGEGAAS 101
Cdd:COG1118 4 EVRNISK---RFG----SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGR-DLFTNLPPRER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 102 RVGMLFQQGALYSAFNVLDNVAFPLRELGtLPRALVDAAALVKLQMVGLkPEHAMRMPADLSGGMIKRVALARALIMDPP 181
Cdd:COG1118 76 RVGFVFQHYALFPHMTVAENIAFGLRVRP-PSKAEIRARVEELLELVQL-EGLADRYPSQLSGGQRQRVALARALAVEPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 182 LLLLDEPTAGLDPNGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEvaVFPHP---FVA 258
Cdd:COG1118 154 VLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDE--VYDRPatpFVA 231
|
..
gi 2788666989 259 QF 260
Cdd:COG1118 232 RF 233
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
24-261 |
5.55e-49 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 165.63 E-value: 5.55e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 24 VHIDKLWSIFGEgesQFAVHqDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVE-----VLGQPAAAmggeg 98
Cdd:COG3839 4 LELENVSKSYGG---VEALK-DIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILiggrdVTDLPPKD----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 99 aasR-VGMLFQQGALYSAFNVLDNVAFPLRELGtLPRALVD-----AAALVKLQmvglkpEHAMRMPADLSGGMIKRVAL 172
Cdd:COG3839 75 ---RnIAMVFQSYALYPHMTVYENIAFPLKLRK-VPKAEIDrrvreAAELLGLE------DLLDRKPKQLSGGQRQRVAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 173 ARALIMDPPLLLLDEPTAGLDPNGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEvaVF 252
Cdd:COG3839 145 GRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEE--LY 222
|
250
....*....|..
gi 2788666989 253 PHP---FVAQFF 261
Cdd:COG3839 223 DRPanlFVAGFI 234
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
23-277 |
6.76e-49 |
|
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: 169.31 E-value: 6.76e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 23 VVHIDKLWSIFGEGEsQFAVHqDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPG---KGTVEVLGQPAAAMGGEGA 99
Cdd:COG1123 4 LLEVRDLSVRYPGGD-VPAVD-GVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 100 ASRVGMLFQQGAlySAFN---VLDNVAFPLRELGtLPRALVDAAALVKLQMVGLkPEHAMRMPADLSGGMIKRVALARAL 176
Cdd:COG1123 82 GRRIGMVFQDPM--TQLNpvtVGDQIAEALENLG-LSRAEARARVLELLEAVGL-ERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 177 IMDPPLLLLDEPTAGLDPNGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEVAVFPHPF 256
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQAL 237
|
250 260
....*....|....*....|.
gi 2788666989 257 VAQFFQGERGRRAMAPAPSGP 277
Cdd:COG1123 238 AAVPRLGAARGRAAPAAAAAE 258
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
44-249 |
1.01e-48 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 161.80 E-value: 1.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGgegaaSRVGMLFQQGALYSAF--NVLDN 121
Cdd:COG1121 23 EDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRAR-----RRIGYVPQRAEVDWDFpiTVRDV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 122 VAFPL-RELGTLP------RALVDAAalvkLQMVGLKpEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDP 194
Cdd:COG1121 98 VLMGRyGRRGLFRrpsradREAVDEA----LERVGLE-DLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2788666989 195 NGSDDFCALLRELHAElDLTVVMVTHDLDTLFALSSRVAVLAeKKVLVTGTPQEV 249
Cdd:COG1121 173 ATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLN-RGLVAHGPPEEV 225
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
44-240 |
5.47e-48 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 159.06 E-value: 5.47e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAAS---RVGMLFQQGALYSAFNVLD 120
Cdd:COG2884 19 SDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYlrrRIGVVFQDFRLLPDRTVYE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 121 NVAFPLRELGTLPRAL---VDAAalvkLQMVGLKpEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGS 197
Cdd:COG2884 99 NVALPLRVTGKSRKEIrrrVREV----LDLVGLS-DKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2788666989 198 DDFCALLRELHAeLDLTVVMVTHDLDTLFALSSRVAVLAEKKV 240
Cdd:COG2884 174 WEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
23-268 |
2.05e-47 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 158.23 E-value: 2.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 23 VVHIDKLWSIFGEgesqFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAA-- 100
Cdd:COG1126 1 MIEIENLHKSFGD----LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKlr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 101 SRVGMLFQQGALYSAFNVLDNVAFPLRELGTLPRALVDAAALVKLQMVGLkPEHAMRMPADLSGGMIKRVALARALIMDP 180
Cdd:COG1126 77 RKVGMVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGL-ADKADAYPAQLSGGQQQRVAIARALAMEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 181 PLLLLDEPTAGLDPNGSDDFCALLRELhAELDLTVVMVTHDLDtlFA--LSSRVAVLAEKKVLVTGTPQEvaVFPHPfva 258
Cdd:COG1126 156 KVMLFDEPTSALDPELVGEVLDVMRDL-AKEGMTMVVVTHEMG--FAreVADRVVFMDGGRIVEEGPPEE--FFENP--- 227
|
250
....*....|
gi 2788666989 259 qffQGERGRR 268
Cdd:COG1126 228 ---QHERTRA 234
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
22-260 |
8.25e-47 |
|
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: 156.73 E-value: 8.25e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 22 RVVHIDKlwsIFGegesQFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQpaAAMGGEGAAS 101
Cdd:cd03296 4 EVRNVSK---RFG----DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGE--DATDVPVQER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 102 RVGMLFQQGALYSAFNVLDNVAFPLRE---LGTLPRALVDAAALVKLQMVGLKpEHAMRMPADLSGGMIKRVALARALIM 178
Cdd:cd03296 75 NVGFVFQHYALFRHMTVFDNVAFGLRVkprSERPPEAEIRAKVHELLKLVQLD-WLADRYPAQLSGGQRQRVALARALAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 179 DPPLLLLDEPTAGLDPNGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEVAVFP-HPFV 257
Cdd:cd03296 154 EPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPaSPFV 233
|
...
gi 2788666989 258 AQF 260
Cdd:cd03296 234 YSF 236
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
35-249 |
1.52e-46 |
|
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: 156.82 E-value: 1.52e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 35 EGESQFAVhQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLG-QPAAAMGGEGAASRVGMLFQ----Q 109
Cdd:TIGR04520 11 PESEKPAL-KNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGlDTLDEENLWEIRKKVGMVFQnpdnQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 110 --GALysafnVLDNVAFPLRELGtLPRA----LVDAAalvkLQMVGLKpEHAMRMPADLSGGMIKRVALARALIMDPPLL 183
Cdd:TIGR04520 90 fvGAT-----VEDDVAFGLENLG-VPREemrkRVDEA----LKLVGME-DFRDREPHLLSGGQKQRVAIAGVLAMRPDII 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2788666989 184 LLDEPTAGLDPNGSDDFCALLRELHAELDLTVVMVTHDLDTLfALSSRVAVLAEKKVLVTGTPQEV 249
Cdd:TIGR04520 159 ILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREI 223
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
22-255 |
3.39e-46 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 157.93 E-value: 3.39e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 22 RVVHIDKlwsIFGEGESQFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGE---G 98
Cdd:COG1135 3 ELENLSK---TFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERelrA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 99 AASRVGMLFQQGALYSAFNVLDNVAFPLRELGTlPRAlvDAAALVK--LQMVGLKpEHAMRMPADLSGGMIKRVALARAL 176
Cdd:COG1135 80 ARRKIGMIFQHFNLLSSRTVAENVALPLEIAGV-PKA--EIRKRVAelLELVGLS-DKADAYPSQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2788666989 177 IMDPPLLLLDEPTAGLDPNGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEvaVFPHP 255
Cdd:COG1135 156 ANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLD--VFANP 232
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
39-266 |
4.68e-46 |
|
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: 158.28 E-value: 4.68e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 39 QFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQpaaamggegAASRV-------GMLFQQGA 111
Cdd:TIGR03265 16 AFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGR---------DITRLppqkrdyGIVFQSYA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 112 LYSAFNVLDNVAFPLRELGtLPRALVDAAALVKLQMVGLkPEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAG 191
Cdd:TIGR03265 87 LFPNLTVADNIAYGLKNRG-MGRAEVAERVAELLDLVGL-PGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 192 LDPNGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEVAVFP-HPFVAQF------FQGE 264
Cdd:TIGR03265 165 LDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPaTPFVADFvgevnwLPGT 244
|
..
gi 2788666989 265 RG 266
Cdd:TIGR03265 245 RG 246
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
40-260 |
1.13e-45 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 153.80 E-value: 1.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 40 FAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQpaAAMGGEGAASRVGMLFQQGALYSAFNVL 119
Cdd:TIGR00968 13 FQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQ--DATRVHARDRKIGFVFQHYALFKHLTVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 120 DNVAFPLrELGTLPRALVDAAALVKLQMVGLkpEH-AMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSD 198
Cdd:TIGR00968 91 DNIAFGL-EIRKHPKAKIKARVEELLELVQL--EGlGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALDAKVRK 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2788666989 199 DFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEVAVFP-HPFVAQF 260
Cdd:TIGR00968 168 ELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPaNPFVMSF 230
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
44-244 |
1.18e-45 |
|
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: 153.07 E-value: 1.18e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGgegaaSRVGMLFQQGALYSAF--NVLDN 121
Cdd:cd03235 16 EDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER-----KRIGYVPQRRSIDRDFpiSVRDV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 122 VA-------FPLRELGTLPRALVDAAalvkLQMVGLKpEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDP 194
Cdd:cd03235 91 VLmglyghkGLFRRLSKADKAKVDEA----LERVGLS-ELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2788666989 195 NGSDDFCALLRELHAElDLTVVMVTHDLDTLFALSSRVAVLAeKKVLVTG 244
Cdd:cd03235 166 KTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLN-RTVVASG 213
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
24-240 |
1.96e-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: 151.01 E-value: 1.96e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 24 VHIDKLWSIFGEGEsqfAVHqDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAaSRV 103
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALD-DISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVK-RRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 104 GMLFQQGALYSAFNVLDNVafplrelgtlpralvdaaalvklqmvglkpehamrmpaDLSGGMIKRVALARALIMDPPLL 183
Cdd:cd03230 76 GYLPEEPSLYENLTVRENL--------------------------------------KLSGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2788666989 184 LLDEPTAGLDPNGSDDFCALLRELHAElDLTVVMVTHDLDTLFALSSRVAVLAEKKV 240
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
41-249 |
2.59e-45 |
|
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: 153.27 E-value: 2.59e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 41 AVhQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAaSRVGML--FQQGALYSAFNV 118
Cdd:COG0411 19 AV-DDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRI-ARLGIArtFQNPRLFPELTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 119 LDNVA---------FPLRELGTLPRALVDAAALVK-----LQMVGLKpEHAMRMPADLSGGMIKRVALARALIMDPPLLL 184
Cdd:COG0411 97 LENVLvaaharlgrGLLAALLRLPRARREEREAREraeelLERVGLA-DRADEPAGNLSYGQQRRLEIARALATEPKLLL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2788666989 185 LDEPTAGLDPNGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEV 249
Cdd:COG0411 176 LDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEV 240
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
24-264 |
6.86e-45 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 155.24 E-value: 6.86e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 24 VHIDKLWSIFGEGEsqfaVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQpaAAMGGEGAASRV 103
Cdd:PRK10851 3 IEIANIKKSFGRTQ----VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT--DVSRLHARDRKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 104 GMLFQQGALYSAFNVLDNVAFPLRelgTLPR------ALVDAAALVKLQMVGLkpEH-AMRMPADLSGGMIKRVALARAL 176
Cdd:PRK10851 77 GFVFQHYALFRHMTVFDNIAFGLT---VLPRrerpnaAAIKAKVTQLLEMVQL--AHlADRYPAQLSGGQKQRVALARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 177 IMDPPLLLLDEPTAGLDPNGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEVAVFPHP- 255
Cdd:PRK10851 152 AVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATr 231
|
250
....*....|....*
gi 2788666989 256 FVAQF------FQGE 264
Cdd:PRK10851 232 FVLEFmgevnrLQGT 246
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
42-249 |
1.20e-44 |
|
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: 151.73 E-value: 1.20e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 42 VHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQGALYSAFNVLDN 121
Cdd:COG1120 16 VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQEPPAPFGLTVREL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 122 VA---FPLRELGTLP----RALVDAAalvkLQMVGLKpEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDP 194
Cdd:COG1120 96 VAlgrYPHLGLFGRPsaedREAVEEA----LERTGLE-HLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2788666989 195 NGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEV 249
Cdd:COG1120 171 AHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
44-249 |
1.57e-44 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 150.98 E-value: 1.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAA---SRVGMLFQQGALYSAFNVLD 120
Cdd:COG3638 20 DDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRrlrRRIGMIFQQFNLVPRLSVLT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 121 NV--------AFPLRELGTLPRALVDAAaLVKLQMVGLkPEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGL 192
Cdd:COG3638 100 NVlagrlgrtSTWRSLLGLFPPEDRERA-LEALERVGL-ADKAYQRADQLSGGQQQRVAIARALVQEPKLILADEPVASL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2788666989 193 DPNGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEV 249
Cdd:COG3638 178 DPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
36-271 |
1.39e-43 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 150.24 E-value: 1.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 36 GESQFAVhQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQGALYSA 115
Cdd:COG1125 12 PDGTVAV-DDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVELRRRIGYVIQQIGLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 116 FNVLDNVAFPLRELGTlPRALVDAAALVKLQMVGLKPE-HAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDP 194
Cdd:COG1125 91 MTVAENIATVPRLLGW-DKERIRARVDELLELVGLDPEeYRDRYPHELSGGQQQRVGVARALAADPPILLMDEPFGALDP 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2788666989 195 NGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEVAVFP-HPFVAQFFQGERGRRAMA 271
Cdd:COG1125 170 ITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPaNDFVADFVGADRGLRRLS 247
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
45-260 |
1.41e-42 |
|
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: 145.56 E-value: 1.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 45 DLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQpaAAMGGEGAASRVGMLFQQGALYSAFNVLDNVAF 124
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGK--DITNLPPEKRDISYVPQNYALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 125 PLRELgTLPRALVDAAALVKLQMVGLkpEHAM-RMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDFCAL 203
Cdd:cd03299 95 GLKKR-KVDKKEIERKVLEIAEMLGI--DHLLnRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 204 LRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEvaVFPHP---FVAQF 260
Cdd:cd03299 172 LKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEE--VFKKPkneFVAEF 229
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
32-255 |
3.45e-42 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 147.64 E-value: 3.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 32 IFGEGESQFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAAS---RVGMLFQ 108
Cdd:PRK11153 10 VFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKarrQIGMIFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 109 QGALYSAFNVLDNVAFPLrELGTLPRALVDAAALVKLQMVGLKpEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEP 188
Cdd:PRK11153 90 HFNLLSSRTVFDNVALPL-ELAGTPKAEIKARVTELLELVGLS-DKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2788666989 189 TAGLDPNGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEvaVFPHP 255
Cdd:PRK11153 168 TSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSE--VFSHP 232
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
24-232 |
4.24e-42 |
|
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: 143.82 E-value: 4.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 24 VHIDKLWSIFGEgesqFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAA--S 101
Cdd:cd03262 1 IEIKNLHKSFGD----FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINElrQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 102 RVGMLFQQGALYSAFNVLDNVAFPLRELGTLPRALVDAAALVKLQMVGLkPEHAMRMPADLSGGMIKRVALARALIMDPP 181
Cdd:cd03262 77 KVGMVFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGL-ADKADAYPAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2788666989 182 LLLLDEPTAGLDPNGSDDFCALLRELhAELDLTVVMVTHDLDtlFA--LSSRV 232
Cdd:cd03262 156 VMLFDEPTSALDPELVGEVLDVMKDL-AEEGMTMVVVTHEMG--FAreVADRV 205
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
45-265 |
6.75e-42 |
|
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: 147.69 E-value: 6.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 45 DLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTV----EVLGQPAAAMGGEGAASRVGMLFQQGALYSAFNVLD 120
Cdd:TIGR01186 11 DADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIfidgENIMKQSPVELREVRRKKIGMVFQQFALFPHMTILQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 121 NVAFPLrELGTLPRALVDAAALVKLQMVGLkPEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDF 200
Cdd:TIGR01186 91 NTSLGP-ELLGWPEQERKEKALELLKLVGL-EEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLIRDSM 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2788666989 201 CALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEVAVFP-HPFVAQFFQGER 265
Cdd:TIGR01186 169 QDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPaNEYVEEFIGKVD 234
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
44-240 |
8.69e-42 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 142.65 E-value: 8.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQGALYSAfNVLDNVA 123
Cdd:COG4619 17 SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQEPALWGG-TVRDNLP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 124 FP--LRELGTLPRALVDAaalvkLQMVGLkPEHAMRMPAD-LSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDF 200
Cdd:COG4619 96 FPfqLRERKFDRERALEL-----LERLGL-PPDILDKPVErLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRV 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2788666989 201 CALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKV 240
Cdd:COG4619 170 EELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
39-249 |
1.68e-41 |
|
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: 142.70 E-value: 1.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 39 QFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGL--LQPGK---GTVEVLGQPAAAMGGEGAASR--VGMLFQQGA 111
Cdd:cd03260 12 DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndLIPGApdeGEVLLDGKDIYDLDVDVLELRrrVGMVFQKPN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 112 LYSAfNVLDNVAFPLRELGTLPRALVDAAALVKLQMVGLKPEHAMRMPA-DLSGGMIKRVALARALIMDPPLLLLDEPTA 190
Cdd:cd03260 92 PFPG-SIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRLHAlGLSGGQQQRLCLARALANEPEVLLLDEPTS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2788666989 191 GLDPNGSDDFCALLRELHAEldLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEV 249
Cdd:cd03260 171 ALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
24-248 |
1.79e-41 |
|
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: 142.26 E-value: 1.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 24 VHIDKLWSIFGEGeSQFAVhQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAaSRV 103
Cdd:cd03263 1 LQIRNLTKTYKKG-TKPAV-DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAAR-QSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 104 GMLFQQGALYSAFNVLDNVAFPLReLGTLPRALVDAAALVKLQMVGLKPeHAMRMPADLSGGMIKRVALARALIMDPPLL 183
Cdd:cd03263 78 GYCPQFDALFDELTVREHLRFYAR-LKGLPKSEIKEEVELLLRVLGLTD-KANKRARTLSGGMKRKLSLAIALIGGPSVL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2788666989 184 LLDEPTAGLDPNGSDDFCALLRELHAEldLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQE 248
Cdd:cd03263 156 LLDEPTSGLDPASRRAIWDLILEVRKG--RSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
44-249 |
2.62e-41 |
|
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: 142.71 E-value: 2.62e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAA---SRVGMLFQQGALYSAFNVLD 120
Cdd:cd03256 18 KDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRqlrRQIGMIFQQFNLIERLSVLE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 121 NVAFPLreLGTLP--RALVD-------AAALVKLQMVGLKpEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAG 191
Cdd:cd03256 98 NVLSGR--LGRRStwRSLFGlfpkeekQRALAALERVGLL-DKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVAS 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2788666989 192 LDPNGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEV 249
Cdd:cd03256 175 LDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
23-263 |
6.00e-41 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 145.63 E-value: 6.00e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 23 VVHIDKLWSIFG-----------EGESQFAVH---------QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKG 82
Cdd:COG4175 3 KIEVRNLYKIFGkrperalklldQGKSKDEILektgqtvgvNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 83 TVEVLGQPAAAMGGEGAA----SRVGMLFQQGALYSAFNVLDNVAFPLrELGTLPRALVDAAALVKLQMVGLKpEHAMRM 158
Cdd:COG4175 83 EVLIDGEDITKLSKKELRelrrKKMSMVFQHFALLPHRTVLENVAFGL-EIQGVPKAERRERAREALELVGLA-GWEDSY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 159 PADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPngsddfcaLLR--------ELHAELDLTVVMVTHDLDTLFALSS 230
Cdd:COG4175 161 PDELSGGMQQRVGLARALATDPDILLMDEAFSALDP--------LIRremqdellELQAKLKKTIVFITHDLDEALRLGD 232
|
250 260 270
....*....|....*....|....*....|....*.
gi 2788666989 231 RVAVLAEKKVLVTGTPQEvaVFPHP---FVAQFFQG 263
Cdd:COG4175 233 RIAIMKDGRIVQIGTPEE--ILTNPandYVADFVED 266
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
22-260 |
7.18e-41 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 144.45 E-value: 7.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 22 RVVHIDKLWSifgegesQFAVHqDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAAs 101
Cdd:NF040840 3 RIENLSKDWK-------EFKLR-DISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRG- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 102 rVGMLFQQGALYSAFNVLDNVAFPLrELGTLPRALVDAAalVKLQMVGLKPEH-AMRMPADLSGGMIKRVALARALIMDP 180
Cdd:NF040840 74 -IAYVYQNYMLFPHKTVFENIAFGL-KLRKVPKEEIERK--VKEIMELLGISHlLHRKPRTLSGGEQQRVALARALIIEP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 181 PLLLLDEPTAGLDPNGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEvaVFPHP---FV 257
Cdd:NF040840 150 KLLLLDEPLSALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVRE--VFRRPkneFV 227
|
...
gi 2788666989 258 AQF 260
Cdd:NF040840 228 ARF 230
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
47-248 |
1.20e-40 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 140.66 E-value: 1.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 47 DLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGaasR-VGMLFQQGALYSAFNVLDNVAFP 125
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE---RpVSMLFQENNLFPHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 126 LR---ELGTLPRALVDAAAlvklQMVGLKpEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDFCA 202
Cdd:COG3840 96 LRpglKLTAEQRAQVEQAL----ERVGLA-GLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2788666989 203 LLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQE 248
Cdd:COG3840 171 LVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAA 216
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
44-250 |
2.99e-40 |
|
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: 139.49 E-value: 2.99e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASR-VGMLFQQGALYSAFNVLDNV 122
Cdd:cd03219 17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgIGRTFQIPRLFPELTVLENV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 123 A----FPLRELGTLPRALVDAAALVK-----LQMVGLkPEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLD 193
Cdd:cd03219 97 MvaaqARTGSGLLLARARREEREAREraeelLERVGL-ADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLN 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2788666989 194 PNGSDDFCALLRELhAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEVA 250
Cdd:cd03219 176 PEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVR 231
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
25-267 |
2.59e-39 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 138.07 E-value: 2.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 25 HIDKLWSIFGEGESQFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGgegaaSRVG 104
Cdd:COG4525 5 TVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG-----ADRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 105 MLFQQGALYSAFNVLDNVAFPLReLGTLPRALVDAAALVKLQMVGLKpEHAMRMPADLSGGMIKRVALARALIMDPPLLL 184
Cdd:COG4525 80 VVFQKDALLPWLNVLDNVAFGLR-LRGVPKAERRARAEELLALVGLA-DFARRRIWQLSGGMRQRVGIARALAADPRFLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 185 LDEPTAGLDpngsddfcALLRELHAELDLT--------VVMVTHDLD-TLFalssrvavLAEKKVLVTGTP-QEVAVFPH 254
Cdd:COG4525 158 MDEPFGALD--------ALTREQMQELLLDvwqrtgkgVFLITHSVEeALF--------LATRLVVMSPGPgRIVERLEL 221
|
250
....*....|...
gi 2788666989 255 PFVAQFFQGERGR 267
Cdd:COG4525 222 DFSRRFLAGEDAR 234
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
24-244 |
3.02e-39 |
|
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: 136.23 E-value: 3.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 24 VHIDKLWSIFGEgesqFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQpaAAMGGEGAASRV 103
Cdd:cd03301 1 VELENVTKRFGN----VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGR--DVTDLPPKDRDI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 104 GMLFQQGALYSAFNVLDNVAFPLReLGTLPRALVDAAALVKLQMVGLkpEHAM-RMPADLSGGMIKRVALARALIMDPPL 182
Cdd:cd03301 75 AMVFQNYALYPHMTVYDNIAFGLK-LRKVPKDEIDERVREVAELLQI--EHLLdRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 183 LLLDEPTAGLDpngsddfcALLRE--------LHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTG 244
Cdd:cd03301 152 FLMDEPLSNLD--------AKLRVqmraelkrLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
38-249 |
3.38e-39 |
|
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: 137.30 E-value: 3.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 38 SQFAVhQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAaSRVGMLFQQGALYSAFN 117
Cdd:COG4555 13 KVPAL-KDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREAR-RQIGVLPDERGLYDRLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 118 VLDNVAFpLRELGTLPRALVDAAALVKLQMVGLkPEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGS 197
Cdd:COG4555 91 VRENIRY-FAELYGLFDEELKKRIEELIELLGL-EEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMAR 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2788666989 198 DDFCALLRELHAElDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEV 249
Cdd:COG4555 169 RLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
41-235 |
3.94e-39 |
|
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: 139.03 E-value: 3.94e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 41 AVHqDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPG---KGTVEVLGQPAAAMGGEGA----ASRVGMLFQQGalY 113
Cdd:COG0444 20 AVD-GVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKELrkirGREIQMIFQDP--M 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 114 SAFN----VLDNVAFPLRELGTLPRALVDAAALVKLQMVGL-KPEHAMRM-PADLSGGMIKRVALARALIMDPPLLLLDE 187
Cdd:COG0444 97 TSLNpvmtVGDQIAEPLRIHGGLSKAEARERAIELLERVGLpDPERRLDRyPHELSGGMRQRVMIARALALEPKLLIADE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2788666989 188 PTAGLDPNGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVL 235
Cdd:COG0444 177 PTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVM 224
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
44-190 |
4.99e-39 |
|
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: 133.93 E-value: 4.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQGALYSAFNVLDNVA 123
Cdd:pfam00005 2 KNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENLR 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2788666989 124 FPLRELGTLPRALVD--AAALVKLQMVGLKPEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTA 190
Cdd:pfam00005 82 LGLLLKGLSKREKDAraEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
45-255 |
5.48e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 137.84 E-value: 5.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 45 DLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTV----EVLGQPAAAMGGEGAASRVGMLFQ--QGALYSAfNV 118
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVtigeRVITAGKKNKKLKPLRKKVGIVFQfpEHQLFEE-TV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 119 LDNVAFPLRELGtLPRAlvDAAALVK--LQMVGLKPEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNG 196
Cdd:PRK13634 104 EKDICFGPMNFG-VSEE--DAKQKARemIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2788666989 197 SDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEvaVFPHP 255
Cdd:PRK13634 181 RKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPRE--IFADP 237
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
45-260 |
1.14e-38 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 139.31 E-value: 1.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 45 DLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQpaAAMGGEGAASRVGMLFQQGALYSAFNVLDNVAF 124
Cdd:PRK09452 32 NLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQ--DITHVPAENRHVNTVFQSYALFPHMTVFENVAF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 125 PLReLGTLPRALVDAAALVKLQMVGLKpEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDFCALL 204
Cdd:PRK09452 110 GLR-MQKTPAAEITPRVMEALRMVQLE-EFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNEL 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2788666989 205 RELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEVAVFP-HPFVAQF 260
Cdd:PRK09452 188 KALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPkNLFVARF 244
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
44-239 |
1.17e-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: 133.14 E-value: 1.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQqgalysafnvldnva 123
Cdd:cd00267 16 DNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ--------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 124 fplrelgtlpralvdaaalvklqmvglkpehamrmpadLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDFCAL 203
Cdd:cd00267 81 --------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLEL 122
|
170 180 190
....*....|....*....|....*....|....*.
gi 2788666989 204 LRELHAElDLTVVMVTHDLDTLFALSSRVAVLAEKK 239
Cdd:cd00267 123 LRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
58-260 |
2.62e-38 |
|
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: 137.24 E-value: 2.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 58 IVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAAsrVGMLFQQGALYSAFNVLDNVAFPLRELGTlPRALV 137
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRH--INMVFQSYALFPHMTVEENVAFGLKMRKV-PRAEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 138 DAAALVKLQMVGLKpEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDFCALLRELHAELDLTVVM 217
Cdd:TIGR01187 78 KPRVLEALRLVQLE-EFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVF 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2788666989 218 VTHDLDTLFALSSRVAVLAEKKVLVTGTPQEvaVFPHP---FVAQF 260
Cdd:TIGR01187 157 VTHDQEEAMTMSDRIAIMRKGKIAQIGTPEE--IYEEPanlFVARF 200
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
35-249 |
5.11e-38 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 135.14 E-value: 5.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 35 EGESQFAVhQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQ----- 109
Cdd:PRK13635 16 PDAATYAL-KDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQNpdnqf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 110 -GAlysafNVLDNVAFPLRELGtLPRAL----VDAAalvkLQMVGLKpEHAMRMPADLSGGMIKRVALARALIMDPPLLL 184
Cdd:PRK13635 95 vGA-----TVQDDVAFGLENIG-VPREEmverVDQA----LRQVGME-DFLNREPHRLSGGQKQRVAIAGVLALQPDIII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2788666989 185 LDEPTAGLDPNGSDDFCALLRELHAELDLTVVMVTHDLDTLfALSSRVAVLAEKKVLVTGTPQEV 249
Cdd:PRK13635 164 LDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEEGTPEEI 227
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
44-244 |
8.02e-38 |
|
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: 131.40 E-value: 8.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAmggegaasrvgMLFQQGAlysafnvldnva 123
Cdd:cd03214 16 DDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLAS-----------LSPKELA------------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 124 fplRELGTLPRAL--VDAAALvklqmvglkpehAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDFC 201
Cdd:cd03214 73 ---RKIAYVPQALelLGLAHL------------ADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELL 137
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2788666989 202 ALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTG 244
Cdd:cd03214 138 ELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
43-241 |
2.52e-37 |
|
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: 131.26 E-value: 2.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 43 HQDLDLDIyRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAAS----RVGMLFQQGALYSAFNV 118
Cdd:cd03297 14 TLKIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPpqqrKIGLVFQQYALFPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 119 LDNVAFPLRELGTLPRALVDAAALVKLQMVGLKpehaMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSD 198
Cdd:cd03297 93 RENLAFGLKRKRNREDRISVDELLDLLGLDHLL----NRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2788666989 199 DFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVL 241
Cdd:cd03297 169 QLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
44-225 |
2.79e-37 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 131.06 E-value: 2.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAaSRVGMLFQQGALYSAFNVLDNVA 123
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYR-RRLAYLGHADGLKPELTVRENLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 124 FpLRELGTLPRALVDAAALvkLQMVGLkPEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDFCAL 203
Cdd:COG4133 98 F-WAALYGLRADREAIDEA--LEAVGL-AGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAEL 173
|
170 180
....*....|....*....|..
gi 2788666989 204 LRElHAELDLTVVMVTHDLDTL 225
Cdd:COG4133 174 IAA-HLARGGAVLLTTHQPLEL 194
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
45-249 |
1.71e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 131.32 E-value: 1.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 45 DLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASR--VGMLFQQGAlYSAF--NVLD 120
Cdd:PRK13637 25 NVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIRkkVGLVFQYPE-YQLFeeTIEK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 121 NVAFPLRELGtLPRALVDAAALVKLQMVGLKPE-HAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDD 199
Cdd:PRK13637 104 DIAFGPINLG-LSEEEIENRVKRAMNIVGLDYEdYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2788666989 200 FCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEV 249
Cdd:PRK13637 183 ILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
41-234 |
2.72e-36 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 131.78 E-value: 2.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 41 AVhQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAAS---RVGMLFQQGalYSAFN 117
Cdd:COG4608 33 AV-DGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPlrrRMQMVFQDP--YASLN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 118 ----VLDNVAFPLRELGTLPRALVDAAALVKLQMVGLKPEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLD 193
Cdd:COG4608 110 prmtVGDIIAEPLRIHGLASKAERRERVAELLELVGLRPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2788666989 194 P-------NgsddfcaLLRELHAELDLTVVMVTHDLDTLFALSSRVAV 234
Cdd:COG4608 190 VsiqaqvlN-------LLEDLQDELGLTYLFISHDLSVVRHISDRVAV 230
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
45-240 |
3.36e-36 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 128.68 E-value: 3.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 45 DLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAA---SRVGMLFQQGALYSAFNVLDN 121
Cdd:cd03292 19 GINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPylrRKIGVVFQDFRLLPDRNVYEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 122 VAFPLRELGTLPRalvDAAALVK--LQMVGLKPEHAmRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDD 199
Cdd:cd03292 99 VAFALEVTGVPPR---EIRKRVPaaLELVGLSHKHR-ALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2788666989 200 FCALLRELHAElDLTVVMVTHDLDTLFALSSRVAVLAEKKV 240
Cdd:cd03292 175 IMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
33-222 |
4.34e-36 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 128.62 E-value: 4.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 33 FGEGESQFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAAS----RVGMLFQ 108
Cdd:TIGR02211 11 YQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKlrnkKLGFIYQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 109 QGALYSAFNVLDNVAFPLReLGTLPRALVDAAALVKLQMVGLkpEHAM-RMPADLSGGMIKRVALARALIMDPPLLLLDE 187
Cdd:TIGR02211 91 FHHLLPDFTALENVAMPLL-IGKKSVKEAKERAYEMLEKVGL--EHRInHRPSELSGGERQRVAIARALVNQPSLVLADE 167
|
170 180 190
....*....|....*....|....*....|....*
gi 2788666989 188 PTAGLDPNGSDDFCALLRELHAELDLTVVMVTHDL 222
Cdd:TIGR02211 168 PTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDL 202
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
23-221 |
4.64e-36 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 128.21 E-value: 4.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 23 VVHIDKLWSIFGEGESQFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAAS- 101
Cdd:TIGR02982 1 VISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 102 --RVGMLFQQGALYSAFNVLDNVAFPLRELGTLPRALVDAAALVKLQMVGLKpEHAMRMPADLSGGMIKRVALARALIMD 179
Cdd:TIGR02982 81 rrRIGYIFQAHNLLGFLTARQNVQMALELQPNLSYQEARERARAMLEAVGLG-DHLNYYPHNLSGGQKQRVAIARALVHH 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2788666989 180 PPLLLLDEPTAGLDPNGSDDFCALLRELHAELDLTVVMVTHD 221
Cdd:TIGR02982 160 PKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHD 201
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
33-249 |
7.85e-36 |
|
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: 135.73 E-value: 7.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 33 FGEGESQFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQGAL 112
Cdd:COG2274 481 FRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFL 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 113 YSAfNVLDNVafplrelgTLPRALVDAAALVK-LQMVGLKpEHAMRMP-----------ADLSGGMIKRVALARALIMDP 180
Cdd:COG2274 561 FSG-TIRENI--------TLGDPDATDEEIIEaARLAGLH-DFIEALPmgydtvvgeggSNLSGGQRQRLAIARALLRNP 630
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2788666989 181 PLLLLDEPTAGLDPNGSDDFCALLRELHAelDLTVVMVTHDLDTLfALSSRVAVLAEKKVLVTGTPQEV 249
Cdd:COG2274 631 RILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTI-RLADRIIVLDKGRIVEDGTHEEL 696
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
44-249 |
2.41e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 128.43 E-value: 2.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASR--VGMLFQQ--GALYSAfNVL 119
Cdd:PRK13636 23 KGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKLResVGMVFQDpdNQLFSA-SVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 120 DNVAFPLRELGtLPRALVDAAALVKLQMVGL-----KPEHAmrmpadLSGGMIKRVALARALIMDPPLLLLDEPTAGLDP 194
Cdd:PRK13636 102 QDVSFGAVNLK-LPEDEVRKRVDNALKRTGIehlkdKPTHC------LSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDP 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2788666989 195 NGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEV 249
Cdd:PRK13636 175 MGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
23-259 |
3.59e-35 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 127.23 E-value: 3.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 23 VVHIDKLWSIFGEGESQfAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAAS- 101
Cdd:TIGR02769 8 VTHTYRTGGLFGAKQRA-PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 102 --RVGMLFQQGalYSAFN----VLDNVAFPLRELGTLPRALVDAAALVKLQMVGLKPEHAMRMPADLSGGMIKRVALARA 175
Cdd:TIGR02769 87 rrDVQLVFQDS--PSAVNprmtVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 176 LIMDPPLLLLDEPTAGLDPNGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEVAVFPHP 255
Cdd:TIGR02769 165 LAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLSFKHP 244
|
....
gi 2788666989 256 FVAQ 259
Cdd:TIGR02769 245 AGRN 248
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
23-222 |
4.81e-35 |
|
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: 126.01 E-value: 4.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 23 VVHIDKLWSIFGEGESQFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAA----MGGEG 98
Cdd:COG4181 8 IIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAldedARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 99 AASRVGMLFQQGALYSAFNVLDNVAFPLrELGTLPRALVDAAALvkLQMVGLKpEHAMRMPADLSGGMIKRVALARALIM 178
Cdd:COG4181 88 RARHVGFVFQSFQLLPTLTALENVMLPL-ELAGRRDARARARAL--LERVGLG-HRLDHYPAQLSGGEQQRVALARAFAT 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2788666989 179 DPPLLLLDEPTAGLDPNGSDDFCALLRELHAELDLTVVMVTHDL 222
Cdd:COG4181 164 EPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDP 207
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
38-249 |
8.02e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 127.51 E-value: 8.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 38 SQFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVE----------------------VLGQPAAAMG 95
Cdd:PRK13651 18 TELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifkdeknkkktkekekvleklVIQKTRFKKI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 96 GEGAA--SRVGMLFQqGALYSAF--NVLDNVAFPLRELGTLPR-ALVDAAALVKlqMVGLKPEHAMRMPADLSGGMIKRV 170
Cdd:PRK13651 98 KKIKEirRRVGVVFQ-FAEYQLFeqTIEKDIIFGPVSMGVSKEeAKKRAAKYIE--LVGLDESYLQRSPFELSGGQKRRV 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2788666989 171 ALARALIMDPPLLLLDEPTAGLDPNGSDDFCALLRELHAElDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEV 249
Cdd:PRK13651 175 ALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDI 252
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
45-249 |
8.90e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 126.77 E-value: 8.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 45 DLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQ------GAlysafNV 118
Cdd:PRK13650 25 DVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQNpdnqfvGA-----TV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 119 LDNVAFPLRELGtLPRALVDAAALVKLQMVGLKpEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSD 198
Cdd:PRK13650 100 EDDVAFGLENKG-IPHEEMKERVNEALELVGMQ-DFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2788666989 199 DFCALLRELHAELDLTVVMVTHDLDTLfALSSRVAVLAEKKVLVTGTPQEV 249
Cdd:PRK13650 178 ELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPREL 227
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
45-249 |
2.35e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 126.00 E-value: 2.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 45 DLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEV----LGQPAAAMGGEGAASRVGMLFQ--QGALYSAfNV 118
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivVSSTSKQKEIKPVRKKVGVVFQfpESQLFEE-TV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 119 LDNVAFPLRELGtLPRALVDAAALVKLQMVGLKPEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSD 198
Cdd:PRK13643 103 LKDVAFGPQNFG-IPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARI 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2788666989 199 DFCALLRELHaELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEV 249
Cdd:PRK13643 182 EMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDV 231
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
37-260 |
2.43e-34 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 127.64 E-value: 2.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 37 ESQFAVhQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAAsrVGMLFQQGALYSAF 116
Cdd:PRK11607 30 DGQHAV-DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRP--INMMFQSYALFPHM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 117 NVLDNVAFPLRElGTLPRALVDAAALVKLQMVGLKpEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNG 196
Cdd:PRK11607 107 TVEQNIAFGLKQ-DKLPKAEIASRVNEMLGLVHMQ-EFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKL 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2788666989 197 SDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEvaVFPHP---FVAQF 260
Cdd:PRK11607 185 RDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEE--IYEHPttrYSAEF 249
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
23-273 |
3.47e-34 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 124.80 E-value: 3.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 23 VVHIDKLWSIFGEGESQfAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAAS- 101
Cdd:PRK10419 9 LSHHYAHGGLSGKHQHQ-TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 102 --RVGMLFQQ--GALYSAFNVLDNVAFPLRELGTLPRALVDAAALVKLQMVGLKPEHAMRMPADLSGGMIKRVALARALI 177
Cdd:PRK10419 88 rrDIQMVFQDsiSAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 178 MDPPLLLLDEPTAGLDPNGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEVAVFPHPfV 257
Cdd:PRK10419 168 VEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLTFSSP-A 246
|
250
....*....|....*.
gi 2788666989 258 AQFFQgergrRAMAPA 273
Cdd:PRK10419 247 GRVLQ-----NAVLPA 257
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
45-249 |
3.79e-34 |
|
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: 123.95 E-value: 3.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 45 DLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAAS---RVGMLFQQGALYSAFNVLDN 121
Cdd:TIGR02315 20 NINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKlrrRIGMIFQHYNLIERLTVLEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 122 VAFP-------LRE-LGTLPRAlvDAA-ALVKLQMVGLKPEHAMRmpAD-LSGGMIKRVALARALIMDPPLLLLDEPTAG 191
Cdd:TIGR02315 100 VLHGrlgykptWRSlLGRFSEE--DKErALSALERVGLADKAYQR--ADqLSGGQQQRVAIARALAQQPDLILADEPIAS 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2788666989 192 LDPNGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEV 249
Cdd:TIGR02315 176 LDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
39-262 |
6.66e-34 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 123.28 E-value: 6.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 39 QFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASR--VGMLFQQGALYSAF 116
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRqeAGMVFQQFYLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 117 NVLDNVAF-PLRELGTlPRALVDAAALVKLQMVGLKpEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPN 195
Cdd:PRK09493 93 TALENVMFgPLRVRGA-SKEEAEKQARELLAKVGLA-ERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2788666989 196 GSDDFCALLRELhAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQE-VAVFPHPFVAQFFQ 262
Cdd:PRK09493 171 LRHEVLKVMQDL-AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVlIKNPPSQRLQEFLQ 237
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
22-260 |
7.72e-34 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 123.20 E-value: 7.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 22 RVVHIDKLWsifgeGESQfaVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRqILGLLQ-PGKGTVEVLG------QPAAAM 94
Cdd:COG4161 4 QLKNINCFY-----GSHQ--ALFDINLECPSGETLVLLGPSGAGKSSLLR-VLNLLEtPDSGQLNIAGhqfdfsQKPSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 95 GGEGAASRVGMLFQQGALYSAFNVLDN-VAFPLRELGTLPRALVDAAA--LVKLQMVglkpEHAMRMPADLSGGMIKRVA 171
Cdd:COG4161 76 AIRLLRQKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMklLARLRLT----DKADRFPLHLSGGQQQRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 172 LARALIMDPPLLLLDEPTAGLDPNGSDDFCALLRELhAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTpqeVAV 251
Cdd:COG4161 152 IARALMMEPQVLLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD---ASH 227
|
....*....
gi 2788666989 252 FPHPFVAQF 260
Cdd:COG4161 228 FTQPQTEAF 236
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
36-262 |
1.60e-33 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 122.43 E-value: 1.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 36 GESQfAVHqDLDLDIYRGEMLSIVGGSGTGKTVLLRqILGLLQ-PGKGTVEV------LGQPAAAMGGEGAASRVGMLFQ 108
Cdd:PRK11124 13 GAHQ-ALF-DITLDCPQGETLVLLGPSGAGKSSLLR-VLNLLEmPRSGTLNIagnhfdFSKTPSDKAIRELRRNVGMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 109 QGALYSAFNVLDN-VAFPLRELG-TLPRALVDAAALVK-LQMVglkpEHAMRMPADLSGGMIKRVALARALIMDPPLLLL 185
Cdd:PRK11124 90 QYNLWPHLTVQQNlIEAPCRVLGlSKDQALARAEKLLErLRLK----PYADRFPLHLSGGQQQRVAIARALMMEPQVLLF 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2788666989 186 DEPTAGLDPNGSDDFCALLRELhAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEvavFPHPFVAQFFQ 262
Cdd:PRK11124 166 DEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC---FTQPQTEAFKN 238
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
44-239 |
2.01e-33 |
|
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: 119.80 E-value: 2.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQGALYSAfNVLDNVa 123
Cdd:cd03228 19 KDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAYVPQDPFLFSG-TIRENI- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 124 fplrelgtlpralvdaaalvklqmvglkpehamrmpadLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDFCAL 203
Cdd:cd03228 97 --------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEA 138
|
170 180 190
....*....|....*....|....*....|....*.
gi 2788666989 204 LRELHAelDLTVVMVTHDLDTLfALSSRVAVLAEKK 239
Cdd:cd03228 139 LRALAK--GKTVIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
42-260 |
5.61e-33 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 123.68 E-value: 5.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 42 VHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQpaaAMGGEGAASR-VGMLFQQGALYSAFNVLD 120
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGE---DVTHRSIQQRdICMVFQSYALFPHMSLGE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 121 NVAFPLRELGtLPRALV-----DAAALVKLQmvGLKPehamRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPN 195
Cdd:PRK11432 98 NVGYGLKMLG-VPKEERkqrvkEALELVDLA--GFED----RYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDAN 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2788666989 196 GSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEVAVFPHP-FVAQF 260
Cdd:PRK11432 171 LRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASrFMASF 236
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
45-244 |
6.82e-33 |
|
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: 119.91 E-value: 6.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 45 DLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAAsrVGMLFQQGALYSAFNVLDNVAF 124
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP--VSMLFQENNLFAHLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 125 ---PLRELGTLPRALVDAAalvkLQMVGLKpEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDFC 201
Cdd:cd03298 94 glsPGLKLTAEDRQAIEVA----LARVGLA-GLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2788666989 202 ALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTG 244
Cdd:cd03298 169 DLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
33-240 |
7.71e-33 |
|
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: 119.28 E-value: 7.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 33 FGEGESQFAVhQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEgaaSRVGMLFQ--QG 110
Cdd:cd03226 7 FSYKKGTEIL-DDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERR---KSIGYVMQdvDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 111 ALYSAfNVLDNVAFPLRELgtlPRALVDAAALVK-LQMVGLKPEHamrmPADLSGGMIKRVALARALIMDPPLLLLDEPT 189
Cdd:cd03226 83 QLFTD-SVREELLLGLKEL---DAGNEQAETVLKdLDLYALKERH----PLSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2788666989 190 AGLDPNGSDDFCALLRELHAElDLTVVMVTHDLDTLFALSSRVAVLAEKKV 240
Cdd:cd03226 155 SGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
46-249 |
1.05e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 120.95 E-value: 1.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 46 LDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASR--VGMLFQQ--GALYsAFNVLDN 121
Cdd:PRK13639 21 INFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVRktVGIVFQNpdDQLF-APTVEED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 122 VAFPLRELGtLPRALVDAAALVKLQMVGLKpEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDFC 201
Cdd:PRK13639 100 VAFGPLNLG-LSKEEVEKRVKEALKAVGME-GFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIM 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2788666989 202 ALLRELHAElDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEV 249
Cdd:PRK13639 178 KLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
45-249 |
1.30e-32 |
|
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: 122.52 E-value: 1.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 45 DLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAAS----RVGMLFQQGALYSAFNVLD 120
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFLPphrrRIGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 121 NVAFPLRELGTLPRAlVDAAALVklQMVGLkpEHAM-RMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDD 199
Cdd:COG4148 97 NLLYGRKRAPRAERR-ISFDEVV--ELLGI--GHLLdRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2788666989 200 FCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEV 249
Cdd:COG4148 172 ILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEV 221
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
45-244 |
2.78e-32 |
|
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: 118.06 E-value: 2.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 45 DLDLDIYRGeMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAaSRVGMLFQQGALYSAFNVLDNVAF 124
Cdd:cd03264 18 GVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLR-RRIGYLPQEFGVYPNFTVREFLDY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 125 pLRELGTLPRALVDAAALVKLQMVGLKpEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDFCALL 204
Cdd:cd03264 96 -IAWLKGIPSKEVKARVDEVLELVNLG-DRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2788666989 205 RELHAelDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTG 244
Cdd:cd03264 174 SELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
42-223 |
2.87e-32 |
|
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: 117.52 E-value: 2.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 42 VHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASR--VGMLFQ--QGALYSAfN 117
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKGLLERRqrVGLVFQdpDDQLFAA-D 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 118 VLDNVAFPLRELGtLPRALVDAAALVKLQMVGLKpEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGS 197
Cdd:TIGR01166 86 VDQDVAFGPLNLG-LSEAEVERRVREALTAVGAS-GLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGR 163
|
170 180
....*....|....*....|....*.
gi 2788666989 198 DDFCALLRELHAElDLTVVMVTHDLD 223
Cdd:TIGR01166 164 EQMLAILRRLRAE-GMTVVISTHDVD 188
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
35-249 |
3.46e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 119.85 E-value: 3.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 35 EGESQFavhqDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGG----EGAASRVGMLFQ-- 108
Cdd:PRK13649 19 EGRALF----DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdiKQIRKKVGLVFQfp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 109 QGALYSAfNVLDNVAFPLRELGTLPRAlVDAAALVKLQMVGLKPEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEP 188
Cdd:PRK13649 95 ESQLFEE-TVLKDVAFGPQNFGVSQEE-AEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2788666989 189 TAGLDPNGSDDFCALLRELHaELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEV 249
Cdd:PRK13649 173 TAGLDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
33-272 |
4.43e-32 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 119.13 E-value: 4.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 33 FGEGEsqfaVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAA------------ 100
Cdd:COG4598 18 FGDLE----VLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDGElvpadrrqlqri 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 101 -SRVGMLFQQGALYSAFNVLDNVAF-PLRELGtLPRALVDAAALVKLQMVGLkPEHAMRMPADLSGGMIKRVALARALIM 178
Cdd:COG4598 94 rTRLGMVFQSFNLWSHMTVLENVIEaPVHVLG-RPKAEAIERAEALLAKVGL-ADKRDAYPAHLSGGQQQRAAIARALAM 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 179 DPPLLLLDEPTAGLDPNGSDDFCALLRELhAELDLTVVMVTHDLDtlFA--LSSRVAVLAEKKVLVTGTPQEvaVFPHPf 256
Cdd:COG4598 172 EPEVMLFDEPTSALDPELVGEVLKVMRDL-AEEGRTMLVVTHEMG--FArdVSSHVVFLHQGRIEEQGPPAE--VFGNP- 245
|
250
....*....|....*.
gi 2788666989 257 vaqffQGERGRRAMAP 272
Cdd:COG4598 246 -----KSERLRQFLSS 256
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
46-249 |
9.07e-32 |
|
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: 122.99 E-value: 9.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 46 LDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEV-LGQPAAAMGGEGAASR------VGMLFQQGALYSAFNV 118
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrVGDEWVDMTKPGPDGRgrakryIGILHQEYDLYPHRTV 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 119 LDNV--AFPLRelgtLPRALVDAAALVKLQMVGLKPEHAM----RMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGL 192
Cdd:TIGR03269 383 LDNLteAIGLE----LPDELARMKAVITLKMVGFDEEKAEeildKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTM 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2788666989 193 DPNGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEV 249
Cdd:TIGR03269 459 DPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
47-244 |
1.19e-31 |
|
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: 116.50 E-value: 1.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 47 DLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQpaAAMGGEGAASRVGMLFQQGALYSAFNVLDNVAFPL 126
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQ--SHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 127 R---ELGTLPRALVDAAAlvklQMVGLKpEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDFCAL 203
Cdd:TIGR01277 96 HpglKLNAEQQEKVVDAA----QQVGIA-DYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLAL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2788666989 204 LRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTG 244
Cdd:TIGR01277 171 VKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
23-222 |
2.23e-31 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 116.45 E-value: 2.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 23 VVHIDKLWSIFGEGESQFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAAS- 101
Cdd:PRK11629 5 LLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAEl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 102 ---RVGMLFQQGALYSAFNVLDNVAFPLReLGTLPRALVDAAALVKLQMVGLKPEHAMRmPADLSGGMIKRVALARALIM 178
Cdd:PRK11629 85 rnqKLGFIYQFHHLLPDFTALENVAMPLL-IGKKKPAEINSRALEMLAAVGLEHRANHR-PSELSGGERQRVAIARALVN 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2788666989 179 DPPLLLLDEPTAGLDPNGSDDFCALLRELHAELDLTVVMVTHDL 222
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDL 206
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
45-250 |
4.33e-31 |
|
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: 118.68 E-value: 4.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 45 DLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAAS----RVGMLFQQGALYSAFNVLD 120
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPpekrRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 121 NVAFPLRELGTLPRALVDAAALvklQMVGLKPeHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDF 200
Cdd:TIGR02142 95 NLRYGMKRARPSERRISFERVI---ELLGIGH-LLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEI 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2788666989 201 CALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEVA 250
Cdd:TIGR02142 171 LPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVW 220
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
44-263 |
9.35e-31 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 118.60 E-value: 9.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLG----QPAAAMGGEGAASRVGMLFQQGALYSAFNVL 119
Cdd:PRK10070 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiaKISDAELREVRRKKIAMVFQSFALMPHMTVL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 120 DNVAFPLrELGTLPRALVDAAALVKLQMVGLKpEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDD 199
Cdd:PRK10070 125 DNTAFGM-ELAGINAEERREKALDALRQVGLE-NYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2788666989 200 FCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEVAVFP-HPFVAQFFQG 263
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPaNDYVRTFFRG 267
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
33-263 |
1.09e-30 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 115.45 E-value: 1.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 33 FGEGEsqfaVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAM-------------GGEGA 99
Cdd:PRK10619 15 YGEHE----VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQLRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 100 ASRVGMLFQQGALYSAFNVLDNV-AFPLRELGtLPRALVDAAALVKLQMVGLKPEHAMRMPADLSGGMIKRVALARALIM 178
Cdd:PRK10619 91 RTRLTMVFQHFNLWSHMTVLENVmEAPIQVLG-LSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 179 DPPLLLLDEPTAGLDPNGSDDFCALLRELhAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEVAVFPH-PFV 257
Cdd:PRK10619 170 EPEVLLFDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQsPRL 248
|
....*.
gi 2788666989 258 AQFFQG 263
Cdd:PRK10619 249 QQFLKG 254
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
41-255 |
1.13e-30 |
|
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: 119.79 E-value: 1.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 41 AVHqDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLqPGKGTVEVLGQPAAAMGGEGAA---SRVGMLFQQ--GALYSA 115
Cdd:COG4172 301 AVD-GVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRALRplrRRMQVVFQDpfGSLSPR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 116 FNVLDNVAFPLRELGT-LPRALVDAAALVKLQMVGLKPEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDP 194
Cdd:COG4172 379 MTVGQIIAEGLRVHGPgLSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDV 458
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2788666989 195 NGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEvaVFPHP 255
Cdd:COG4172 459 SVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQ--VFDAP 517
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
45-248 |
1.70e-30 |
|
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: 115.95 E-value: 1.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 45 DLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLG-----QPAAAMggegaaSRVGMLFQQGALYSAFNVL 119
Cdd:TIGR01188 11 GVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGydvvrEPRKVR------RSIGIVPQYASVDEDLTGR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 120 DNVAFPLRELGtLPRALVDAAALVKLQMVGLKpEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDD 199
Cdd:TIGR01188 85 ENLEMMGRLYG-LPKDEAEERAEELLELFELG-EAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2788666989 200 FCALLRELHaELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQE 248
Cdd:TIGR01188 163 IWDYIRALK-EEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEE 210
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
47-251 |
1.71e-30 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 114.29 E-value: 1.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 47 DLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGegaaSR--VGMLFQQGALYSAFNVLDNVAf 124
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPP----SRrpVSMLFQENNLFSHLTVAQNIG- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 125 plreLGTLPRALVDAAALVKLQ----MVGLKpEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDF 200
Cdd:PRK10771 94 ----LGLNPGLKLNAAQREKLHaiarQMGIE-DLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEM 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2788666989 201 CALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKV--------LVTGTPQEVAV 251
Cdd:PRK10771 169 LTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIawdgptdeLLSGKASASAL 227
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
44-255 |
2.63e-30 |
|
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: 113.71 E-value: 2.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAasrvgMLFQQGALYSAFNVLDNVA 123
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPWLTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 124 FPLRE-LGTLPRALVDAAALVKLQMVGLKpEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDFCA 202
Cdd:TIGR01184 77 LAVDRvLPDLSKSERRAIVEEHIALVGLT-EAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQE 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2788666989 203 LLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEVAvFPHP 255
Cdd:TIGR01184 156 ELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVP-FPRP 207
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
33-248 |
3.32e-30 |
|
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: 118.72 E-value: 3.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 33 FGEGESQFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQGAL 112
Cdd:COG4987 341 FRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 113 YSAfNVLDNVAFPLRELGtlPRALVDAAALVKLQ------------MVGlkpEHAMRmpadLSGGMIKRVALARALIMDP 180
Cdd:COG4987 421 FDT-TLRENLRLARPDAT--DEELWAALERVGLGdwlaalpdgldtWLG---EGGRR----LSGGERRRLALARALLRDA 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2788666989 181 PLLLLDEPTAGLDPNGSDDFCALLRELHAelDLTVVMVTHDLDTLfALSSRVAVLAEKKVLVTGTPQE 248
Cdd:COG4987 491 PILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGL-ERMDRILVLEDGRIVEQGTHEE 555
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
34-249 |
4.89e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 114.03 E-value: 4.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 34 GEGESQFAVhQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGE-GAASRVGMLFQQ--G 110
Cdd:PRK13633 18 EESTEKLAL-DDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwDIRNKAGMVFQNpdN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 111 ALYSAFnVLDNVAFPLRELGTLP---RALVDAAaLVKLQMVGLKpEHAmrmPADLSGGMIKRVALARALIMDPPLLLLDE 187
Cdd:PRK13633 97 QIVATI-VEEDVAFGPENLGIPPeeiRERVDES-LKKVGMYEYR-RHA---PHLLSGGQKQRVAIAGILAMRPECIIFDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2788666989 188 PTAGLDPNGSDDFCALLRELHAELDLTVVMVTHDLDTLfALSSRVAVLAEKKVLVTGTPQEV 249
Cdd:PRK13633 171 PTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGTPKEI 231
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
46-264 |
5.70e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 113.68 E-value: 5.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 46 LDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQ--GALYSAfNVLDNVA 123
Cdd:PRK13647 24 LSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDpdDQVFSS-TVWDDVA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 124 FPLRELGtLPRALVDAAALVKLQMVGLKpEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDFCAL 203
Cdd:PRK13647 103 FGPVNMG-LDKDEVERRVEEALKAVRMW-DFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEI 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2788666989 204 LRELHAElDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQ--------EVAVFPHPFVAQFFQGE 264
Cdd:PRK13647 181 LDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSlltdedivEQAGLRLPLVAQIFEDL 248
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
44-249 |
6.04e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 113.55 E-value: 6.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQ------GAlysafN 117
Cdd:PRK13632 26 KNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIFQNpdnqfiGA-----T 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 118 VLDNVAFPLrELGTLPR----ALVDAAAlvklQMVGLKpEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLD 193
Cdd:PRK13632 101 VEDDIAFGL-ENKKVPPkkmkDIIDDLA----KKVGME-DYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2788666989 194 PNGSDDFCALLRELHAELDLTVVMVTHDLDTLFaLSSRVAVLAEKKVLVTGTPQEV 249
Cdd:PRK13632 175 PKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEI 229
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
39-248 |
9.64e-30 |
|
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: 111.69 E-value: 9.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 39 QFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQpAAAMGGEGAASRVGMLFQQGALYSAFNV 118
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGH-DVVREPREVRRRIGIVFQDLSVDDELTG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 119 LDNVAFPLRELGtLPRALVDAAALVKLQMVGLKpEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSD 198
Cdd:cd03265 91 WENLYIHARLYG-VPGAERRERIDELLDFVGLL-EAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2788666989 199 DFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQE 248
Cdd:cd03265 169 HVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
41-248 |
1.19e-29 |
|
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: 117.17 E-value: 1.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 41 AVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQGALYSAfNVLD 120
Cdd:COG4988 351 PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAG-TIRE 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 121 NVAFPLRELGtlPRALVDAAALVKLQmvglkpEHAMRMPAD-----------LSGGMIKRVALARALIMDPPLLLLDEPT 189
Cdd:COG4988 430 NLRLGRPDAS--DEELEAALEAAGLD------EFVAALPDGldtplgeggrgLSGGQAQRLALARALLRDAPLLLLDEPT 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2788666989 190 AGLDPNGSDDFCALLRELHAelDLTVVMVTHDLDTLfALSSRVAVLAEKKVLVTGTPQE 248
Cdd:COG4988 502 AHLDAETEAEILQALRRLAK--GRTVILITHRLALL-AQADRILVLDDGRIVEQGTHEE 557
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
44-249 |
1.55e-29 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 112.13 E-value: 1.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQGALYSAFNVLDNVA 123
Cdd:COG4559 18 DDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLPQHSSLAFPFTVEEVVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 124 F---PLRELGTLPRALVDAAalvkLQMVGLkPEHAMRMPADLSGGMIKRVALARALI-------MDPPLLLLDEPTAGLD 193
Cdd:COG4559 98 LgraPHGSSAAQDRQIVREA----LALVGL-AHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2788666989 194 PNGSDDFCALLRELhAELDLTVVMVTHDLDtLFAL-SSRVAVLAEKKVLVTGTPQEV 249
Cdd:COG4559 173 LAHQHAVLRLARQL-ARRGGGVVAVLHDLN-LAAQyADRILLLHQGRLVAQGTPEEV 227
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
42-249 |
1.90e-29 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 112.41 E-value: 1.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 42 VHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASR--VGMLFQ---QGALYSaf 116
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALRqqVATVFQdpeQQIFYT-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 117 NVLDNVAFPLRELGT----LPRALVDAAALVKLQMVGLKPEHAmrmpadLSGGMIKRVALARALIMDPPLLLLDEPTAGL 192
Cdd:PRK13638 94 DIDSDIAFSLRNLGVpeaeITRRVDEALTLVDAQHFRHQPIQC------LSHGQKKRVAIAGALVLQARYLLLDEPTAGL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2788666989 193 DPNGSDDFCALLRELHAELDlTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEV 249
Cdd:PRK13638 168 DPAGRTQMIAIIRRIVAQGN-HVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV 223
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
44-248 |
2.36e-29 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 110.65 E-value: 2.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPG---KGTVEVLGQPAAAMGGEGaaSRVGMLFQQGALYSAFNVLD 120
Cdd:COG4136 18 APLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQ--RRIGILFQDDLLFPHLSVGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 121 NVAFPLRElgTLPRALVDAAALVKLQMVGLkPEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDF 200
Cdd:COG4136 96 NLAFALPP--TIGRAQRRARVEQALEEAGL-AGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQF 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2788666989 201 CALLRELHAELDLTVVMVTHDLDtlfalssrvAVLAEKKVLVTGTPQE 248
Cdd:COG4136 173 REFVFEQIRQRGIPALLVTHDEE---------DAPAAGRVLDLGNWQH 211
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
45-255 |
4.00e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 111.02 E-value: 4.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 45 DLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQGALYSAFNVLDNVAF 124
Cdd:PRK13548 20 DVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLSFPFTVEEVVAM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 125 ---PLRELGTLPRALVDAAalvkLQMVGLkpEH-AMRMPADLSGGMIKRVALARALI------MDPPLLLLDEPTAGLDP 194
Cdd:PRK13548 100 graPHGLSRAEDDALVAAA----LAQVDL--AHlAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2788666989 195 NGSDDFCALLRELHAELDLTVVMVTHDLDtLFAL-SSRVAVLAEKKVLVTGTPQEV--------------AVFPHP 255
Cdd:PRK13548 174 AHQHHVLRLARQLAHERGLAVIVVLHDLN-LAARyADRIVLLHQGRLVADGTPAEVltpetlrrvygadvLVQPHP 248
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
42-244 |
4.94e-29 |
|
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: 109.61 E-value: 4.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 42 VHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQpaAAMGGEGAASRVGMLFQQGALYSAFNVLDN 121
Cdd:cd03268 15 VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK--SYQKNIEALRRIGALIEAPGFYPNLTAREN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 122 VAFPLRELGtLPRALVDAAalvkLQMVGLKpEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDFC 201
Cdd:cd03268 93 LRLLARLLG-IRKKRIDEV----LDVVGLK-DSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2788666989 202 ALLRELHAElDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTG 244
Cdd:cd03268 167 ELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
20-254 |
5.42e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 112.25 E-value: 5.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 20 GERVVHIDKLWSIFGEG-ESQFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEV----LGQPAAAM 94
Cdd:PRK13631 18 DDIILRVKNLYCVFDEKqENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKNNH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 95 GGEGAAS------------RVGMLFQQGAlYSAF--NVLDNVAFPLRELGTlprALVDAAALVK--LQMVGLKPEHAMRM 158
Cdd:PRK13631 98 ELITNPYskkiknfkelrrRVSMVFQFPE-YQLFkdTIEKDIMFGPVALGV---KKSEAKKLAKfyLNKMGLDDSYLERS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 159 PADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDFCALLRELHAElDLTVVMVTHDLDTLFALSSRVAVLAEK 238
Cdd:PRK13631 174 PFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKG 252
|
250
....*....|....*.
gi 2788666989 239 KVLVTGTPQEVAVFPH 254
Cdd:PRK13631 253 KILKTGTPYEIFTDQH 268
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
41-249 |
5.86e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 111.74 E-value: 5.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 41 AVHqDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPaaamGGEGAASRVGMLFQQGALYSAFNVLD 120
Cdd:COG4152 16 AVD-DVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEP----LDPEDRRRIGYLPEERGLYPKMKVGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 121 NVAFpLRELGTLPRALVDAAALVKLQMVGLkPEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDF 200
Cdd:COG4152 91 QLVY-LARLKGLSKAEAKRRADEWLERLGL-GDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2788666989 201 CALLRELHAElDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEV 249
Cdd:COG4152 169 KDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
52-249 |
6.14e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 111.05 E-value: 6.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 52 RGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQ--GALYSAfNVLDNVAFPLREL 129
Cdd:PRK13652 29 RNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNpdDQIFSP-TVEQDIAFGPINL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 130 GtLPRALVDAAALVKLQMVGLKpEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDFCALLRELHA 209
Cdd:PRK13652 108 G-LDEETVAHRVSSALHMLGLE-ELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPE 185
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2788666989 210 ELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEV 249
Cdd:PRK13652 186 TYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
21-250 |
1.89e-28 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 108.71 E-value: 1.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 21 ERVVHIDKLWSIFGEGESQFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAA----MGG 96
Cdd:PRK10584 4 ENIVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmdeeARA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 97 EGAASRVGMLFQQGALYSAFNVLDNVAFPLRELGTLPR-ALVDAAALVKLQMVGLKPEHamrMPADLSGGMIKRVALARA 175
Cdd:PRK10584 84 KLRAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRqSRNGAKALLEQLGLGKRLDH---LPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2788666989 176 LIMDPPLLLLDEPTAGLDPNGSDDFCALLRELHAELDLTVVMVTHDldtlfalsSRVAVLAEKKV-LVTGTPQEVA 250
Cdd:PRK10584 161 FNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD--------LQLAARCDRRLrLVNGQLQEEA 228
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
24-244 |
2.10e-28 |
|
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: 108.14 E-value: 2.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 24 VHIDKLWSIFGEgesqFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPaaamGGEGAASRV 103
Cdd:cd03269 1 LEVENVTKRFGR----VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKP----LDIAARNRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 104 GMLFQQGALYSAFNVLDNVAFpLRELGTLPRALVDAAALVKLQMVGLKpEHAMRMPADLSGGMIKRVALARALIMDPPLL 183
Cdd:cd03269 73 GYLPEERGLYPKMKVIDQLVY-LAQLKGLKKEEARRRIDEWLERLELS-EYANKRVEELSKGNQQKVQFIAAVIHDPELL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2788666989 184 LLDEPTAGLDPNGSDDFCALLRELhAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTG 244
Cdd:cd03269 151 ILDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
45-256 |
4.14e-28 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 110.18 E-value: 4.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 45 DLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGE---GAASRVGMLFQQ--GALYSAFNVL 119
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDewrAVRSDIQMIFQDplASLNPRMTIG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 120 DNVAFPLREL-GTLPRALVDAAalVKLQM--VGLKPEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNG 196
Cdd:PRK15079 119 EIIAEPLRTYhPKLSRQEVKDR--VKAMMlkVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSI 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2788666989 197 SDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEVAVFP-HPF 256
Cdd:PRK15079 197 QAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPlHPY 257
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
44-267 |
7.86e-28 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 107.86 E-value: 7.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGgegaaSRVGMLFQQGALYSAFNVLDNVA 123
Cdd:PRK11248 18 EDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-----AERGVVFQNEGLLPWRNVQDNVA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 124 FPLrELGTLPRALVDAAALVKLQMVGLKPEHAmRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDFCAL 203
Cdd:PRK11248 93 FGL-QLAGVEKMQRLEIAHQMLKKVGLEGAEK-RYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2788666989 204 LRELHAELDLTVVMVTHDLDTLFALSSRVAVLAekkvlvTGTPQEVAVFPHPFVAQFFQGERGR 267
Cdd:PRK11248 171 LLKLWQETGKQVLLITHDIEEAVFMATELVLLS------PGPGRVVERLPLNFARRFVAGESSR 228
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
24-244 |
8.32e-28 |
|
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: 106.68 E-value: 8.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 24 VHIDKLWSIFGEGESQFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLG-----QPAAAMggeg 98
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvkEPAEAR---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 99 aaSRVGMLFQQGALYSAFNVLDNVAFPLRELGTLPRALVDAAALV--KLQMvglkPEHAMRMPADLSGGMIKRVALARAL 176
Cdd:cd03266 78 --RRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELadRLGM----EELLDRRVGGFSTGMRQKVAIARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2788666989 177 IMDPPLLLLDEPTAGLDPNGSDDFCALLRELHAElDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTG 244
Cdd:cd03266 152 VHDPPVLLLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
34-250 |
9.54e-28 |
|
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: 106.36 E-value: 9.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 34 GEGESQfaVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASR-VGMLFQQGAL 112
Cdd:cd03224 9 GYGKSQ--ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYVPEGRRI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 113 YSAFNVLDNVafplrELGTLPRALVDAAALVKlQMVGLKP---EHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPT 189
Cdd:cd03224 87 FPELTVEENL-----LLGAYARRRAKRKARLE-RVYELFPrlkERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2788666989 190 AGLDPNGSDDFCALLRELHAElDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEVA 250
Cdd:cd03224 161 EGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
36-222 |
1.34e-27 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 107.04 E-value: 1.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 36 GESQfAVHqDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGL--LQPG---KGTVEVLGQPAAAMGGEGAA--SRVGMLFQ 108
Cdd:COG1117 22 GDKQ-ALK-DINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGarvEGEILLDGEDIYDPDVDVVElrRRVGMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 109 QGALYsAFNVLDNVAFPLRELGTLPRALVDAAALVKLQMVGLKPE--HAMRMPA-DLSGGMIKRVALARALIMDPPLLLL 185
Cdd:COG1117 100 KPNPF-PKSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALWDEvkDRLKKSAlGLSGGQQQRLCIARALAVEPEVLLM 178
|
170 180 190
....*....|....*....|....*....|....*..
gi 2788666989 186 DEPTAGLDPNGSDDFCALLRELhAElDLTVVMVTHDL 222
Cdd:COG1117 179 DEPTSALDPISTAKIEELILEL-KK-DYTIVIVTHNM 213
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
44-223 |
1.54e-27 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 105.01 E-value: 1.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGqpaaamggegaASRVGMLFQQGALYSAF--NVLDN 121
Cdd:NF040873 9 HGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRSEVPDSLplTVRDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 122 VAF-------PLRELGTLPRALVDAAalvkLQMVGLKpEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDP 194
Cdd:NF040873 78 VAMgrwarrgLWRRLTRDDRAAVDDA----LERVGLA-DLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180
....*....|....*....|....*....
gi 2788666989 195 NGSDDFCALLRELHAElDLTVVMVTHDLD 223
Cdd:NF040873 153 ESRERIIALLAEEHAR-GATVVVVTHDLE 180
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
37-255 |
2.04e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 107.19 E-value: 2.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 37 ESQFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQP---GKGTVEVLGQPAAAMGGEGAASRVGMLFQQ---- 109
Cdd:PRK13640 17 DSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIREKVGIVFQNpdnq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 110 --GAlysafNVLDNVAFPLRELGtLPRALVDAAALVKLQMVGLKpEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDE 187
Cdd:PRK13640 97 fvGA-----TVGDDVAFGLENRA-VPRPEMIKIVRDVLADVGML-DYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2788666989 188 PTAGLDPNGSDDFCALLRELHAELDLTVVMVTHDLDTLfALSSRVAVLAEKKVLVTGTPQEvaVFPHP 255
Cdd:PRK13640 170 STSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVE--IFSKV 234
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
42-240 |
6.17e-27 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 105.53 E-value: 6.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 42 VHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGgegaaSRVGMLFQQGALYSAFNVLDN 121
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAR-----EDTRLMFQDARLLPWKKVIDN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 122 VAFPLRelGTLpralvDAAALVKLQMVGLKpEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDFC 201
Cdd:PRK11247 102 VGLGLK--GQW-----RDAALQALAAVGLA-DRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQ 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 2788666989 202 ALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKV 240
Cdd:PRK11247 174 DLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
36-240 |
6.41e-27 |
|
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: 103.06 E-value: 6.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 36 GESQFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQGALYSA 115
Cdd:cd03246 11 PGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQDDELFSG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 116 fNVLDNVafplrelgtlpralvdaaalvklqmvglkpehamrmpadLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPN 195
Cdd:cd03246 91 -SIAENI---------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVE 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2788666989 196 GSDDFCALLRELHAElDLTVVMVTHDLDTLfALSSRVAVLAEKKV 240
Cdd:cd03246 131 GERALNQAIAALKAA-GATRIVIAHRPETL-ASADRILVLEDGRV 173
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
39-249 |
7.70e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 105.86 E-value: 7.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 39 QFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLL-----QPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQGAlY 113
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIisetgQTIVGDYAIPANLKKIKEVKRLRKEIGLVFQFPE-Y 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 114 SAFN--VLDNVAFPLRELGTLPRALVDAAALVkLQMVGLKPEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAG 191
Cdd:PRK13645 102 QLFQetIEKDIAFGPVNLGENKQEAYKKVPEL-LKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2788666989 192 LDPNGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEV 249
Cdd:PRK13645 181 LDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEI 238
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
45-249 |
7.97e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 105.68 E-value: 7.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 45 DLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAAS----RVGMLFQ--QGALYSAfNV 118
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKklrkKVSLVFQfpEAQLFEN-TV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 119 LDNVAFPLRELGTLPRAlVDAAALVKLQMVGLKPEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSD 198
Cdd:PRK13641 104 LKDVEFGPKNFGFSEDE-AKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRK 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2788666989 199 DFCALLRELHAElDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEV 249
Cdd:PRK13641 183 EMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
41-249 |
1.11e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 106.45 E-value: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 41 AVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAaSRVGMLFQQGALYSAFNVLD 120
Cdd:PRK13536 55 AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLAR-ARIGVVPQFDNLDLEFTVRE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 121 NVAFPLRELGTLPRAlVDAAALVKLQMVGLKPEHAMRMpADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDF 200
Cdd:PRK13536 134 NLLVFGRYFGMSTRE-IEAVIPSLLEFARLESKADARV-SDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLI 211
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2788666989 201 CALLRELHAeLDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEV 249
Cdd:PRK13536 212 WERLRSLLA-RGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
45-249 |
2.36e-26 |
|
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: 103.63 E-value: 2.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 45 DLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKG-TVEVLGQPAAAMGGEGAASRVGML--FQQGALYSAFNVLDN 121
Cdd:COG1119 21 DISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRIGLVspALQLRFPRDETVLDV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 122 VA-------FPLRELGTLPRALVDAAalvkLQMVGLKpEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDP 194
Cdd:COG1119 101 VLsgffdsiGLYREPTDEQRERAREL----LELLGLA-HLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2788666989 195 NGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEV 249
Cdd:COG1119 176 GARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
44-253 |
6.05e-26 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 102.06 E-value: 6.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPG----KGTVEVLGQPAAAMGGEGAAsrVGMLFQQGAlySAFNVL 119
Cdd:TIGR02770 3 QDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGltqtSGEILLDGRPLLPLSIRGRH--IATIMQNPR--TAFNPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 120 DNVAFPLRE---LGTLPRALVDAAALVKLQMVGLK-PEHAMRM-PADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDP 194
Cdd:TIGR02770 79 FTMGNHAIEtlrSLGKLSKQARALILEALEAVGLPdPEEVLKKyPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2788666989 195 NGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEVAVFP 253
Cdd:TIGR02770 159 VNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNP 217
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
35-249 |
7.35e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 102.86 E-value: 7.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 35 EGESQFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQ-GALY 113
Cdd:PRK13642 15 EKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNpDNQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 114 SAFNVLDNVAFPLRELGtLPR----ALVDAAaLVKLQMVGLKpehaMRMPADLSGGMIKRVALARALIMDPPLLLLDEPT 189
Cdd:PRK13642 95 VGATVEDDVAFGMENQG-IPReemiKRVDEA-LLAVNMLDFK----TREPARLSGGQKQRVAVAGIIALRPEIIILDEST 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 190 AGLDPNGSDDFCALLRELHAELDLTVVMVTHDLDTLfALSSRVAVLAEKKVLVTGTPQEV 249
Cdd:PRK13642 169 SMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEIIKEAAPSEL 227
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
21-248 |
7.51e-26 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 102.78 E-value: 7.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 21 ERVVHIDKLWSIFGEGESQFAVhqdlDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGT---VEVLG---QPAAAM 94
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHAV----DLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAgshIELLGrtvQREGRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 95 GGEGAASR--VGMLFQQGALYSAFNVLDNVAfpLRELGTLP---------RALVDAAALVKLQMVGLKpEHAMRMPADLS 163
Cdd:PRK09984 78 ARDIRKSRanTGYIFQQFNLVNRLSVLENVL--IGALGSTPfwrtcfswfTREQKQRALQALTRVGMV-HFAHQRVSTLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 164 GGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVT 243
Cdd:PRK09984 155 GGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYD 234
|
....*
gi 2788666989 244 GTPQE 248
Cdd:PRK09984 235 GSSQQ 239
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
41-260 |
7.61e-26 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 104.73 E-value: 7.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 41 AVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQpaAAMGGEGAASRVGMLFQQGALYSAFNVLD 120
Cdd:PRK11000 17 VISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK--RMNDVPPAERGVGMVFQSYALYPHLSVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 121 NVAFPLRELGTLPRAL---VDAAALVkLQMvglkpEHAM-RMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDpng 196
Cdd:PRK11000 95 NMSFGLKLAGAKKEEInqrVNQVAEV-LQL-----AHLLdRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD--- 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2788666989 197 sddfcALLR--------ELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEVAVFP-HPFVAQF 260
Cdd:PRK11000 166 -----AALRvqmrieisRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPaNRFVAGF 233
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
45-249 |
9.17e-26 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 104.92 E-value: 9.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 45 DLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQGALYSAFNVLDNVaf 124
Cdd:PRK09536 21 GVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLSFEFDVRQVV-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 125 plrELGTLP------------RALVDAAalvkLQMVGLKpEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGL 192
Cdd:PRK09536 99 ---EMGRTPhrsrfdtwtetdRAAVERA----MERTGVA-QFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2788666989 193 DPNGSDDFCALLRELhAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEV 249
Cdd:PRK09536 171 DINHQVRTLELVRRL-VDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
41-249 |
1.74e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 102.17 E-value: 1.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 41 AVHqDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEV----LGQPAAAMGGEGAASRVGMLFQ--QGALYS 114
Cdd:PRK13646 22 AIH-DVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVdditITHKTKDKYIRPVRKRIGMVFQfpESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 115 afnvlDNVAfplRELGTLPRAL------VDAAALVKLQMVGLKPEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEP 188
Cdd:PRK13646 101 -----DTVE---REIIFGPKNFkmnldeVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2788666989 189 TAGLDPNGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEV 249
Cdd:PRK13646 173 TAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
46-268 |
2.83e-25 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 100.59 E-value: 2.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 46 LDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEV------LGQPAAAMGGEGAASR--VGMLFQQGALYSAFN 117
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidTARSLSQQKGLIRQLRqhVGFVFQNFNLFPHRT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 118 VLDNV-AFPLRELGTlPRALVDAAALVKLQMVGLKPEHAmRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNG 196
Cdd:PRK11264 102 VLENIiEGPVIVKGE-PKEEATARARELLAKVGLAGKET-SYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPEL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2788666989 197 SDDFCALLRELhAELDLTVVMVTHDLDTLFALSSRvAVLAEKKVLVTGTPQEvAVFPHPfvaqffQGERGRR 268
Cdd:PRK11264 180 VGEVLNTIRQL-AQEKRTMVIVTHEMSFARDVADR-AIFMDQGRIVEQGPAK-ALFADP------QQPRTRQ 242
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
41-222 |
3.58e-25 |
|
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: 104.36 E-value: 3.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 41 AVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQGALYSAfNVLD 120
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDT-TVRE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 121 NVAFPlRELGTlpralvDAAALVKLQMVGLKpEHAMRMP-----------ADLSGGMIKRVALARALIMDPPLLLLDEPT 189
Cdd:TIGR02868 428 NLRLA-RPDAT------DEELWAALERVGLA-DWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDEPT 499
|
170 180 190
....*....|....*....|....*....|....
gi 2788666989 190 AGLDPNGSDdfcALLRELHAELD-LTVVMVTHDL 222
Cdd:TIGR02868 500 EHLDAETAD---ELLEDLLAALSgRTVVLITHHL 530
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
47-249 |
6.53e-25 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 100.06 E-value: 6.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 47 DLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAaSRVGML--FQQGALYSAFNVLDN--V 122
Cdd:PRK11300 25 NLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQI-ARMGVVrtFQHVRLFREMTVIENllV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 123 AfPLRELGT--------LP---RALVDAA--ALVKLQMVGLKpEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPT 189
Cdd:PRK11300 104 A-QHQQLKTglfsgllkTPafrRAESEALdrAATWLERVGLL-EHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 190 AGLDPNGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEV 249
Cdd:PRK11300 182 AGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 241
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
37-255 |
1.21e-24 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 99.53 E-value: 1.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 37 ESQFAVHqDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQGAlySAF 116
Cdd:COG4167 24 QQFEAVK-PVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCKHIRMIFQDPN--TSL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 117 N-------VLDnvaFPLReLGTLpralVDAAALVK-----LQMVGLKPEHAMRMPADLSGGMIKRVALARALIMDPPLLL 184
Cdd:COG4167 101 NprlnigqILE---EPLR-LNTD----LTAEEREErifatLRLVGLLPEHANFYPHMLSSGQKQRVALARALILQPKIII 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2788666989 185 LDEPTAGLDPNGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEvaVFPHP 255
Cdd:COG4167 173 ADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAE--VFANP 241
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
45-256 |
2.45e-24 |
|
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: 98.36 E-value: 2.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 45 DLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVL---GQPAAAMGGEGAASRVGMLFQQGALYSafNVLD- 120
Cdd:TIGR02323 21 DVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYImrsGAELELYQLSEAERRRLMRTEWGFVHQ--NPRDg 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 121 ---------NVAFPLRELGTLPRALVDAAALVKLQMVGLKPEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAG 191
Cdd:TIGR02323 99 lrmrvsagaNIGERLMAIGARHYGNIRATAQDWLEEVEIDPTRIDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDEPTGG 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2788666989 192 LDPNGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEVAVFP-HPF 256
Cdd:TIGR02323 179 LDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPqHPY 244
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
42-255 |
4.95e-24 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 100.94 E-value: 4.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 42 VHQDLDLDIYRGEMLSIVGGSGTGKTV----LLRQIlgllqPGKGTVEVLGQPAAAMGGEGAA---SRVGMLFQ--QGAL 112
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLLpvrHRIQVVFQdpNSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 113 YSAFNVLDNVAFPLR-ELGTLPRALVDAAALVKLQMVGLKPEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAG 191
Cdd:PRK15134 376 NPRLNVLQIIEEGLRvHQPTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSS 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2788666989 192 LDPNGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQevAVFPHP 255
Cdd:PRK15134 456 LDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCE--RVFAAP 517
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
42-249 |
4.96e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 98.72 E-value: 4.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 42 VHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAaSRVGMLFQQGALYSAFNVLDN 121
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHAR-QRVGVVPQFDNLDPDFTVREN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 122 VAFPLRELGtLPRALVDAAALVKLQMVGLKPEHAMRMpADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDFC 201
Cdd:PRK13537 101 LLVFGRYFG-LSAAAARALVPPLLEFAKLENKADAKV-GELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMW 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2788666989 202 ALLRELHAElDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEV 249
Cdd:PRK13537 179 ERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
33-277 |
5.59e-24 |
|
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: 100.91 E-value: 5.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 33 FGEGESQFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPG----KGTVEVLGQPAAAMGGEGAA----SRVG 104
Cdd:COG4172 16 FGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPaahpSGSILFDGQDLLGLSERELRrirgNRIA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 105 MLFQQ--GALYSAFNVLDNVAFPLRELGTLPRALVDAAALVKLQMVGLkPEHAMRM---PADLSGGMIKRVALARALIMD 179
Cdd:COG4172 96 MIFQEpmTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGI-PDPERRLdayPHQLSGGQRQRVMIAMALANE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 180 PPLLLLDEPTAGLDPNGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEVAVFP-HPFVA 258
Cdd:COG4172 175 PDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAAPqHPYTR 254
|
250
....*....|....*....
gi 2788666989 259 QFFQGERGRRAMAPAPSGP 277
Cdd:COG4172 255 KLLAAEPRGDPRPVPPDAP 273
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
41-240 |
7.22e-24 |
|
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: 95.19 E-value: 7.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 41 AVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRvGMLF-----QQGALYSA 115
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRA-GIAYvpedrKREGLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 116 FNVLDNVAFPLRelgtlpralvdaaalvklqmvglkpehamrmpadLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPN 195
Cdd:cd03215 93 LSVAENIALSSL----------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2788666989 196 GSDDFCALLRELhAELDLTVVMVTHDLDTLFALSSRVAVLAEKKV 240
Cdd:cd03215 139 AKAEIYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
44-244 |
1.11e-23 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 96.53 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAA-SRVGMLF-------QQGA---L 112
Cdd:PRK11701 23 RDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSeAERRRLLrtewgfvHQHPrdgL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 113 YSAFNVLDNVAFPLRELGTLPRALVDAAALVKLQMVGLKPEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGL 192
Cdd:PRK11701 103 RMQVSAGGNIGERLMAVGARHYGDIRATAGDWLERVEIDAARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2788666989 193 DPNGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTG 244
Cdd:PRK11701 183 DVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
40-260 |
1.24e-23 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 98.38 E-value: 1.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 40 FAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQpaaamggegaasRVG----------MLFQQ 109
Cdd:PRK11650 17 TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGR------------VVNelepadrdiaMVFQN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 110 GALYSAFNVLDNVAFPLRELGTlPRALVD-----AAALVKLQmvglkpEHAMRMPADLSGGMIKRVALARALIMDPPLLL 184
Cdd:PRK11650 85 YALYPHMSVRENMAYGLKIRGM-PKAEIEervaeAARILELE------PLLDRKPRELSGGQRQRVAMGRAIVREPAVFL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2788666989 185 LDEPTAGLDPNGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEvaVFPHP---FVAQF 260
Cdd:PRK11650 158 FDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVE--VYEKPastFVASF 234
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
44-248 |
1.52e-23 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 99.85 E-value: 1.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQGALYSAfNVLDNVA 123
Cdd:COG1132 357 KDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSG-TIRENIR 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 124 FPLRELgtlPRALVDAAAlvklQMVGLKpEHAMRMP-----------ADLSGGMIKRVALARALIMDPPLLLLDEPTAGL 192
Cdd:COG1132 436 YGRPDA---TDEEVEEAA----KAAQAH-EFIEALPdgydtvvgergVNLSGGQRQRIAIARALLKDPPILILDEATSAL 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2788666989 193 DPnGSDdfcALLRELHAEL--DLTVVMVTHDLDTLfALSSRVAVLAEKKVLVTGTPQE 248
Cdd:COG1132 508 DT-ETE---ALIQEALERLmkGRTTIVIAHRLSTI-RNADRILVLDDGRIVEQGTHEE 560
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
44-249 |
1.54e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 96.59 E-value: 1.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASR-VGMLFQQGAL-YSAFNVLDN 121
Cdd:PRK13644 19 ENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKlVGIVFQNPETqFVGRTVEED 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 122 VAFPLRELGTLP---RALVDAAalvkLQMVGLKpEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSD 198
Cdd:PRK13644 99 LAFGPENLCLPPieiRKRVDRA----LAEIGLE-KYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2788666989 199 DFCALLRELHaELDLTVVMVTHDLDTLFAlSSRVAVLAEKKVLVTGTPQEV 249
Cdd:PRK13644 174 AVLERIKKLH-EKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENV 222
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
35-249 |
1.62e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 96.36 E-value: 1.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 35 EGESQFAVhQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQ----- 109
Cdd:PRK13648 18 QSDASFTL-KDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQNpdnqf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 110 -GALYsAFNV---LDNVAFPLRELGT-LPRALVDAAALvklqmvglkpEHAMRMPADLSGGMIKRVALARALIMDPPLLL 184
Cdd:PRK13648 97 vGSIV-KYDVafgLENHAVPYDEMHRrVSEALKQVDML----------ERADYEPNALSGGQKQRVAIAGVLALNPSVII 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2788666989 185 LDEPTAGLDPNGSDDFCALLRELHAELDLTVVMVTHDLDTLfALSSRVAVLAEKKVLVTGTPQEV 249
Cdd:PRK13648 166 LDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEA-MEADHVIVMNKGTVYKEGTPTEI 229
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
46-220 |
1.83e-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: 1.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 46 LDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASrVGMLFQQGALYSAFNVLDNVAFP 125
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHEN-ILYLGHLPGLKPELSALENLHFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 126 LRELGTLPRALVDAAALVKLQmvglkpEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDFCALLR 205
Cdd:TIGR01189 98 AAIHGGAQRTIEDALAAVGLT------GFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLR 171
|
170
....*....|....*
gi 2788666989 206 ElHAELDLTVVMVTH 220
Cdd:TIGR01189 172 A-HLARGGIVLLTTH 185
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
44-225 |
1.88e-23 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 99.28 E-value: 1.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQGALYSAfNVLDNVA 123
Cdd:TIGR02857 339 RPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAG-TIAENIR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 124 fpLRELGTLPRALVDAAALVKL-QMVGLKPEHAMRM----PADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSD 198
Cdd:TIGR02857 418 --LARPDASDAEIREALERAGLdEFVAALPQGLDTPigegGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEA 495
|
170 180
....*....|....*....|....*..
gi 2788666989 199 DFCALLRELHAelDLTVVMVTHDLDTL 225
Cdd:TIGR02857 496 EVLEALRALAQ--GRTVLLVTHRLALA 520
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
44-235 |
3.21e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 98.55 E-value: 3.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASR-VGMLFQQGALYSAFNVLDNV 122
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAgIAIIHQELNLVPNLSVAENI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 123 AfplreLGTLPRA--LVDAAALVK-----LQMVGLkPEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPN 195
Cdd:COG1129 101 F-----LGREPRRggLIDWRAMRRrarelLARLGL-DIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTER 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2788666989 196 GSDDFCALLRELHAElDLTVVMVTHDLDTLFALSSRVAVL 235
Cdd:COG1129 175 EVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVL 213
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
41-220 |
4.14e-23 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 93.79 E-value: 4.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 41 AVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGmlfQQGALYSAFNVLD 120
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG---HRNAMKPALTVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 121 NVAFPLRELGTLPRALVDAAALVKLQmvglkpeHAMRMPA-DLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDD 199
Cdd:PRK13539 93 NLEFWAAFLGGEELDIAAALEAVGLA-------PLAHLPFgYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVAL 165
|
170 180
....*....|....*....|.
gi 2788666989 200 FCALLRElHAELDLTVVMVTH 220
Cdd:PRK13539 166 FAELIRA-HLAQGGIVIAATH 185
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
22-235 |
4.50e-23 |
|
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: 92.49 E-value: 4.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 22 RVVHIDKlwsIFGegesqfAVH--QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPaaamggega 99
Cdd:cd03216 2 ELRGITK---RFG------GVKalDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKE--------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 100 asrvgmlfqqgalysafnvldnVAFplrelgtlpRALVDAAALvKLQMVglkpehamrmpADLSGGMIKRVALARALIMD 179
Cdd:cd03216 64 ----------------------VSF---------ASPRDARRA-GIAMV-----------YQLSVGERQMVEIARALARN 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2788666989 180 PPLLLLDEPTAGLDPNGSDDFCALLRELHAElDLTVVMVTHDLDTLFALSSRVAVL 235
Cdd:cd03216 101 ARLLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVL 155
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
44-244 |
5.00e-23 |
|
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: 94.32 E-value: 5.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQpAAAMGGEGAASRVGMLF-QQGALYSAFNVLDNV 122
Cdd:cd03267 38 KGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL-VPWKRRKKFLRRIGVVFgQKTQLWWDLPVIDSF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 123 AFpLRELGTLP--RALVDAAALVKLqmvgLKPEHAMRMPA-DLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDD 199
Cdd:cd03267 117 YL-LAAIYDLPpaRFKKRLDELSEL----LDLEELLDTPVrQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQEN 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2788666989 200 FCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTG 244
Cdd:cd03267 192 IRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
36-221 |
5.80e-23 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 98.26 E-value: 5.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 36 GESQFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLrQILGLL-QPGKGTVEVLGQPAAA----MGGEGAASRVGMLFQQG 110
Cdd:PRK10535 17 GEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLM-NILGCLdKPTSGTYRVAGQDVATldadALAQLRREHFGFIFQRY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 111 ALYSAFNVLDNVAFPLRELGtLPRALVDAAALVKLQMVGLKpEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTA 190
Cdd:PRK10535 96 HLLSHLTAAQNVEVPAVYAG-LERKQRLLRAQELLQRLGLE-DRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTG 173
|
170 180 190
....*....|....*....|....*....|.
gi 2788666989 191 GLDPNGSDDFCALLRELHaELDLTVVMVTHD 221
Cdd:PRK10535 174 ALDSHSGEEVMAILHQLR-DRGHTVIIVTHD 203
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-253 |
6.44e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 94.73 E-value: 6.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 20 GERVVHIDKLWSIFGEGesqfAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQ------PGKGTVEVLGQPAAA 93
Cdd:PRK14246 7 AEDVFNISRLYLYINDK----AILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 94 MGGEGAASRVGMLFQQGALYSAFNVLDNVAFPLRELGTLPRALVDAAALVKLQMVGLKPEHAMRM--PAD-LSGGMIKRV 170
Cdd:PRK14246 83 IDAIKLRKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLnsPASqLSGGQQQRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 171 ALARALIMDPPLLLLDEPTAGLDPNGSDDFCALLRELHAEldLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEVA 250
Cdd:PRK14246 163 TIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIF 240
|
...
gi 2788666989 251 VFP 253
Cdd:PRK14246 241 TSP 243
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
44-249 |
7.10e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 94.31 E-value: 7.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQGALYSAFNVLDNVA 123
Cdd:PRK11231 19 NDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGITVRELVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 124 F---PLR----ELGTLPRALVDAAaLVKLQMVGLkpehAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNG 196
Cdd:PRK11231 99 YgrsPWLslwgRLSAEDNARVNQA-MEQTRINHL----ADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINH 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2788666989 197 SDDFCALLRELHAElDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEV 249
Cdd:PRK11231 174 QVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
33-244 |
2.46e-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: 91.22 E-value: 2.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 33 FGEGESQFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMggegaasrvgmlfqQGAL 112
Cdd:cd03247 8 FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL--------------EKAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 113 YSAFNVLDNvafplrelgtlpRALVDAAALvkLQMVGLKpehamrmpadLSGGMIKRVALARALIMDPPLLLLDEPTAGL 192
Cdd:cd03247 74 SSLISVLNQ------------RPYLFDTTL--RNNLGRR----------FSGGERQRLALARILLQDAPIVLLDEPTVGL 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2788666989 193 DPNGSDdfcALLRELHAEL-DLTVVMVTHDLDTLFALsSRVAVLAEKKVLVTG 244
Cdd:cd03247 130 DPITER---QLLSLIFEVLkDKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
44-244 |
2.96e-22 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 91.95 E-value: 2.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGK---GTVEVLGQPAAAMGGEgaaSRVGMLFQQGALYSAFNVLD 120
Cdd:cd03234 24 NDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKPDQFQ---KCVAYVRQDDILLPGLTVRE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 121 NVAF--PLRelgtLPRALVDA-----AALVKLQMVGLKPEHAMRMPAdLSGGMIKRVALARALIMDPPLLLLDEPTAGLD 193
Cdd:cd03234 101 TLTYtaILR----LPRKSSDAirkkrVEDVLLRDLALTRIGGNLVKG-ISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2788666989 194 PNGSDDFCALLRELhAELDLTVVMVTH----DldtLFALSSRVAVLAEKKVLVTG 244
Cdd:cd03234 176 SFTALNLVSTLSQL-ARRNRIVILTIHqprsD---LFRLFDRILLLSSGEIVYSG 226
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
42-266 |
2.99e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 92.60 E-value: 2.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 42 VHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPG-----KGTVEVLGQPAAAMGGEGAASR--VGMLFQQGALYS 114
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDPIEVRreVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 115 AFNVLDNVAFPLRELGTL-PRALVDAAALVKLQMVGLKPEHAMRM---PADLSGGMIKRVALARALIMDPPLLLLDEPTA 190
Cdd:PRK14267 99 HLTIYDNVAIGVKLNGLVkSKKELDERVEWALKKAALWDEVKDRLndyPSNLSGGQRQRLVIARALAMKPKILLMDEPTA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2788666989 191 GLDPNGSDDFCALLRELHAelDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEVAVFP-HPFVAQFFQGERG 266
Cdd:PRK14267 179 NIDPVGTAKIEELLFELKK--EYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPeHELTEKYVTGALG 253
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
36-250 |
3.47e-22 |
|
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: 91.97 E-value: 3.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 36 GESQfaVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASR-VGMLFQQGALYS 114
Cdd:COG0410 14 GGIH--VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgIGYVPEGRRIFP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 115 AFNVLDNVafplrELGTLPRALVDAAALVKLQMVGLKP---EHAMRMPADLSGG---MikrVALARALIMDPPLLLLDEP 188
Cdd:COG0410 92 SLTVEENL-----LLGAYARRDRAEVRADLERVYELFPrlkERRRQRAGTLSGGeqqM---LAIGRALMSRPKLLLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2788666989 189 TAGLDPNGSDDFCALLRELHAElDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEVA 250
Cdd:COG0410 164 SLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELL 224
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
45-249 |
3.65e-22 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 92.46 E-value: 3.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 45 DLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPG----KGTVEVLGQPAAAMGGEGAAsrVGMLFQqgALYSAFNVLD 120
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGKPVAPCALRGRK--IATIMQ--NPRSAFNPLH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 121 NVAFPLRE-LGTLPRALVDAAALVKLQMVGLK-PEHAMRM-PADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGS 197
Cdd:PRK10418 97 TMHTHAREtCLALGKPADDATLTAALEAVGLEnAARVLKLyPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2788666989 198 DDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEV 249
Cdd:PRK10418 177 ARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
44-254 |
4.03e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 92.79 E-value: 4.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQI--LGLLQPG---KGTVEVLGQPAAAMGGEGAASR--VGMLFQQGALYSaF 116
Cdd:PRK14258 24 EGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrMNELESEvrvEGRVEFFNQNIYERRVNLNRLRrqVSMVHPKPNLFP-M 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 117 NVLDNVAFPLRELGTLPRALVDAAALVKLQMVGLKPE--HAMRMPA-DLSGGMIKRVALARALIMDPPLLLLDEPTAGLD 193
Cdd:PRK14258 103 SVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEikHKIHKSAlDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLD 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2788666989 194 PNGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVT-----GTPQEVAVFPH 254
Cdd:PRK14258 183 PIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENRIGqlvefGLTKKIFNSPH 248
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
39-271 |
5.82e-22 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 91.71 E-value: 5.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 39 QFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQpaaamggegaaSRVGMLFQQGALysafnv 118
Cdd:PRK09544 16 QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK-----------LRIGYVPQKLYL------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 119 ldNVAFPL--RELGTLPRALVDAAALVKLQMVglKPEHAMRMPAD-LSGGMIKRVALARALIMDPPLLLLDEPTAGLDPN 195
Cdd:PRK09544 79 --DTTLPLtvNRFLRLRPGTKKEDILPALKRV--QAGHLIDAPMQkLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVN 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2788666989 196 GSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLaEKKVLVTGTPQEVAVFPHpFVAQFfqGERGRRAMA 271
Cdd:PRK09544 155 GQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEVVSLHPE-FISMF--GPRGAEQLG 226
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
44-235 |
1.11e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 94.32 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASR-VGMLFQQGALYSAFNVLDNV 122
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALgIGMVHQHFMLVPNLTVAENI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 123 AFPLRELGTLPRALVDAAALVK--LQMVGLK--PEhamRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSD 198
Cdd:COG3845 102 VLGLEPTKGGRLDRKAARARIRelSERYGLDvdPD---AKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEAD 178
|
170 180 190
....*....|....*....|....*....|....*..
gi 2788666989 199 DFCALLRELhAELDLTVVMVTHDLDTLFALSSRVAVL 235
Cdd:COG3845 179 ELFEILRRL-AAEGKSIIFITHKLREVMAIADRVTVL 214
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
44-236 |
1.12e-21 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 89.86 E-value: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPaaamggegaASRVGMLFQQGALY--------SA 115
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEP---------IRRQRDEYHQDLLYlghqpgikTE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 116 FNVLDNVAFPLRelgtLPRALVDAAALVKLQMVGLKP-EHAmrmPAD-LSGGMIKRVALARALIMDPPLLLLDEPTAGLD 193
Cdd:PRK13538 89 LTALENLRFYQR----LHGPGDDEALWEALAQVGLAGfEDV---PVRqLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2788666989 194 PNGSDDFCALLRElHAELDLTVVMVTHdlDTLFALSSRVAVLA 236
Cdd:PRK13538 162 KQGVARLEALLAQ-HAEQGGMVILTTH--QDLPVASDKVRKLR 201
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
36-232 |
1.20e-21 |
|
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: 90.57 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 36 GESQFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQGALY-S 114
Cdd:COG4778 20 GGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDLAQASPREILALRRRTIGYvS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 115 AF-NV------LDNVAFPLRELGT-LPRALVDAAALvkLQMVGLkPEHAMRM-PADLSGGMIKRVALARALIMDPPLLLL 185
Cdd:COG4778 100 QFlRViprvsaLDVVAEPLLERGVdREEARARAREL--LARLNL-PERLWDLpPATFSGGEQQRVNIARGFIADPPLLLL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2788666989 186 DEPTAGLDPNGSDDFCALLRELHAElDLTVVMVTHDLDTLFALSSRV 232
Cdd:COG4778 177 DEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRV 222
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
44-237 |
1.28e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 90.32 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGA---ASRVGMLFQQGALYSAFNVLD 120
Cdd:PRK10908 19 QGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVpflRRQIGMIFQDHHLLMDRTVYD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 121 NVAFPLRELGTLP---RALVDAAalvkLQMVGLKpEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGS 197
Cdd:PRK10908 99 NVAIPLIIAGASGddiRRRVSAA----LDKVGLL-DKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2788666989 198 DDFCALLRELHaELDLTVVMVTHDLDTLFALSSRVAVLAE 237
Cdd:PRK10908 174 EGILRLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSD 212
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
44-249 |
1.31e-21 |
|
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: 94.04 E-value: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTV------------EVLGQpaaamggegaasRVGMLFQQGA 111
Cdd:COG4618 349 RGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVrldgadlsqwdrEELGR------------HIGYLPQDVE 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 112 LYSAfNVLDNVAfplReLGTLPRALVDAAAlvklQMVGLkpeHAM--RMP-----------ADLSGGMIKRVALARALIM 178
Cdd:COG4618 417 LFDG-TIAENIA---R-FGDADPEKVVAAA----KLAGV---HEMilRLPdgydtrigeggARLSGGQRQRIGLARALYG 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2788666989 179 DPPLLLLDEPTAGLDPNGSDDFCALLRELHAElDLTVVMVTHDLdTLFALSSRVAVLAEKKVLVTGTPQEV 249
Cdd:COG4618 485 DPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGPRDEV 553
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
44-221 |
1.39e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.98 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQpaaamggegaaSRVGMLFQQGALYSAFNVLDNVA 123
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG-----------LRIGYLPQEPPLDDDLTVLDTVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 124 FPLRELGTLPRAL-----------VDAAALVKLQM--------------------VGLKPEHAMRMPADLSGGMIKRVAL 172
Cdd:COG0488 84 DGDAELRALEAELeeleaklaepdEDLERLAELQEefealggweaearaeeilsgLGFPEEDLDRPVSELSGGWRRRVAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2788666989 173 ARALIMDPPLLLLDEPTAGLDPNGsddfCALLRELHAELDLTVVMVTHD 221
Cdd:COG0488 164 ARALLSEPDLLLLDEPTNHLDLES----IEWLEEFLKNYPGTVLVVSHD 208
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
52-222 |
1.40e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 92.33 E-value: 1.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 52 RGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASR---VGMLFQQGalYSAFN----VLDNVAF 124
Cdd:PRK11308 40 RGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLrqkIQIVFQNP--YGSLNprkkVGQILEE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 125 PLRELGTLPRALVDAAALVKLQMVGLKPEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDFCALL 204
Cdd:PRK11308 118 PLLINTSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLM 197
|
170
....*....|....*...
gi 2788666989 205 RELHAELDLTVVMVTHDL 222
Cdd:PRK11308 198 MDLQQELGLSYVFISHDL 215
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
42-249 |
1.63e-21 |
|
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: 90.24 E-value: 1.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 42 VHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQGALYSAfNVLDN 121
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQENVLFNR-SIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 122 VAfpLRELGTLPRALVDAAALVKLQmvglkpEHAMRMP-----------ADLSGGMIKRVALARALIMDPPLLLLDEPTA 190
Cdd:cd03252 96 IA--LADPGMSMERVIEAAKLAGAH------DFISELPegydtivgeqgAGLSGGQRQRIAIARALIHNPRILIFDEATS 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 191 GLDPNGSDdfcALLRELHAELD-LTVVMVTHDLDTLFAlSSRVAVLAEKKVLVTGTPQEV 249
Cdd:cd03252 168 ALDYESEH---AIMRNMHDICAgRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDEL 223
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
40-263 |
3.61e-21 |
|
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: 92.94 E-value: 3.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 40 FAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGL--LQPGKGTV----------------EVLGQP----------- 90
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpSKVGEPcpvcggtlepe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 91 ------AAAMGGEGAASRVGMLFQQG-ALYSAFNVLDNVAFPLRELGTLPRALVDAAALVkLQMVGLkpEHAMRMPA-DL 162
Cdd:TIGR03269 93 evdfwnLSDKLRRRIRKRIAIMLQRTfALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDL-IEMVQL--SHRITHIArDL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 163 SGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLV 242
Cdd:TIGR03269 170 SGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIKE 249
|
250 260
....*....|....*....|.
gi 2788666989 243 TGTPQEVavfphpfVAQFFQG 263
Cdd:TIGR03269 250 EGTPDEV-------VAVFMEG 263
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
36-249 |
3.78e-21 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 90.05 E-value: 3.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 36 GESQFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQGALYSA 115
Cdd:PRK10253 16 GYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 116 FNVLDNVA---FPLRELGTLPRALVDAAALVKLQMVGLKpeHAMRMPAD-LSGGMIKRVALARALIMDPPLLLLDEPTAG 191
Cdd:PRK10253 96 ITVQELVArgrYPHQPLFTRWRKEDEEAVTKAMQATGIT--HLADQSVDtLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2788666989 192 LDPNGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEV 249
Cdd:PRK10253 174 LDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
37-235 |
4.16e-21 |
|
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: 88.80 E-value: 4.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 37 ESQFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQGALYSAf 116
Cdd:cd03245 14 NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQDVTLFYG- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 117 NVLDNVAFPLRELGTlpRALVDAAALVKL-QMVGLKPeHAMRMP-----ADLSGGMIKRVALARALIMDPPLLLLDEPTA 190
Cdd:cd03245 93 TLRDNITLGAPLADD--ERILRAAELAGVtDFVNKHP-NGLDLQigergRGLSGGQRQAVALARALLNDPPILLLDEPTS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2788666989 191 GLDPNGSDDFCALLRELHAelDLTVVMVTHDLdTLFALSSRVAVL 235
Cdd:cd03245 170 AMDMNSEERLKERLRQLLG--DKTLIIITHRP-SLLDLVDRIIVM 211
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
26-277 |
1.38e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 90.92 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 26 IDKLWSIFGEGESQFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQ------PGkGTVEVLGQPAAAMGGEGA 99
Cdd:PRK15134 8 IENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPsppvvyPS-GDIRFHGESLLHASEQTL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 100 A----SRVGMLFQQGALysAFNVLDNVAFPLRELGTLPRALVDAAA----LVKLQMVGLKpEHAMRM---PADLSGGMIK 168
Cdd:PRK15134 87 RgvrgNKIAMIFQEPMV--SLNPLHTLEKQLYEVLSLHRGMRREAArgeiLNCLDRVGIR-QAAKRLtdyPHQLSGGERQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 169 RVALARALIMDPPLLLLDEPTAGLDPNGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQE 248
Cdd:PRK15134 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAAT 243
|
250 260 270
....*....|....*....|....*....|.
gi 2788666989 249 VAVFP-HPFVAQFFQGE-RGRRAMAPAPSGP 277
Cdd:PRK15134 244 LFSAPtHPYTQKLLNSEpSGDPVPLPEPASP 274
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
21-256 |
2.71e-20 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 90.30 E-value: 2.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 21 ERVVHIDKLWSIFGEGESQFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEV-------------- 86
Cdd:PRK10261 10 RDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCdkmllrrrsrqvie 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 87 LGQPAAAMGGEGAASRVGMLFQQ--GALYSAFNVLDNVAFPLRELGTLPRALVDAAALVKLQMVGLKPEHAM--RMPADL 162
Cdd:PRK10261 90 LSEQSAAQMRHVRGADMAMIFQEpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTIlsRYPHQL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 163 SGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLV 242
Cdd:PRK10261 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVE 249
|
250
....*....|....*
gi 2788666989 243 TGTPQEVAVFP-HPF 256
Cdd:PRK10261 250 TGSVEQIFHAPqHPY 264
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
42-274 |
2.87e-20 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 90.30 E-value: 2.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 42 VH--QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAAS---RVGMLFQQ--GALYS 114
Cdd:PRK10261 337 VHavEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQAlrrDIQFIFQDpyASLDP 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 115 AFNVLDNVAFPLRELGTLPRALVDAAALVKLQMVGLKPEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDP 194
Cdd:PRK10261 417 RQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 195 NGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGtPQEvAVFPHPfvaqffQGERGRRAMAPAP 274
Cdd:PRK10261 497 SIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG-PRR-AVFENP------QHPYTRKLMAAVP 568
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
33-264 |
6.18e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 86.51 E-value: 6.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 33 FGEGEsqfaVHQDLDLDIYRGEMLSIVGGSGTGKTVLLR---QILGLLQPGKGTVEVL--GQPAAAMGGEGAASRVGMLF 107
Cdd:PRK14247 13 FGQVE----VLDGVNLEIPDNTITALMGPSGSGKSTLLRvfnRLIELYPEARVSGEVYldGQDIFKMDVIELRRRVQMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 108 QQGALYSAFNVLDNVAFPLReLGTLPRALVDAAALVK--LQMVGLKPEHAMRMPA---DLSGGMIKRVALARALIMDPPL 182
Cdd:PRK14247 89 QIPNPIPNLSIFENVALGLK-LNRLVKSKKELQERVRwaLEKAQLWDEVKDRLDApagKLSGGQQQRLCIARALAFQPEV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 183 LLLDEPTAGLDPNGSDDFCALLRELHAelDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEVAVFP-HPFVAQFF 261
Cdd:PRK14247 168 LLADEPTANLDPENTAKIESLFLELKK--DMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPrHELTEKYV 245
|
...
gi 2788666989 262 QGE 264
Cdd:PRK14247 246 TGR 248
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
33-248 |
7.58e-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: 85.75 E-value: 7.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 33 FGEGESQFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQGAL 112
Cdd:cd03251 8 FRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVSQDVFL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 113 YSAfNVLDNVAFPLRELGtlPRALVDAAALVKLQmvglkpEHAMRMP-----------ADLSGGMIKRVALARALIMDPP 181
Cdd:cd03251 88 FND-TVAENIAYGRPGAT--REEVEEAARAANAH------EFIMELPegydtvigergVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2788666989 182 LLLLDEPTAGLDPNGSDDFCALLRELHAelDLTVVMVTHDLDTLfALSSRVAVLAEKKVLVTGTPQE 248
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTI-ENADRIVVLEDGKIVERGTHEE 222
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
46-246 |
8.24e-20 |
|
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: 89.30 E-value: 8.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 46 LDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASrVGMLFQQGALYSAFNVLDNVAFP 125
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQS-LGMCPQHNILFHHLTVAEHILFY 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 126 LRELG-TLPRALVDAAALvkLQMVGLkpEHAMRMPA-DLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDFCAL 203
Cdd:TIGR01257 1028 AQLKGrSWEEAQLEMEAM--LEDTGL--HHKRNEEAqDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDL 1103
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2788666989 204 LreLHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTP 246
Cdd:TIGR01257 1104 L--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
36-241 |
8.88e-20 |
|
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: 84.52 E-value: 8.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 36 GESQFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPG--KGTVEVLGQPAAAMGGEgaaSRVGMLFQQGALY 113
Cdd:cd03213 18 SKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPLDKRSFR---KIIGYVPQDDILH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 114 SAFNVldnvafplRElgtlprALVDAAALVKLqmvglkpehamrmpadlSGGMIKRVALARALIMDPPLLLLDEPTAGLD 193
Cdd:cd03213 95 PTLTV--------RE------TLMFAAKLRGL-----------------SGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2788666989 194 PNGSDDFCALLRELhAELDLTVVMVTHDL-DTLFALSSRVAVLAEKKVL 241
Cdd:cd03213 144 SSSALQVMSLLRRL-ADTGRTIICSIHQPsSEIFELFDKLLLLSQGRVI 191
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
42-250 |
1.28e-19 |
|
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: 84.90 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 42 VHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEvLGQPAAAMGGEGAASRVGM--LFQQGALYSAFNVL 119
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIL-LDGQDITKLPMHKRARLGIgyLPQEASIFRKLTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 120 DNVAFPLrELGTLPRALVDAAALVKLQMVGLkpEHAMRMPAD-LSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSD 198
Cdd:cd03218 94 ENILAVL-EIRGLSKKEREEKLEELLEEFHI--THLRKSKASsLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQ 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2788666989 199 DFCALLRELhAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEVA 250
Cdd:cd03218 171 DIQKIIKIL-KDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| GldA_ABC_ATP |
TIGR03522 |
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein ... |
22-252 |
1.33e-19 |
|
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldA is an ABC transporter ATP-binding protein (pfam00005) linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae and Cytophaga hutchinsonii. Knockouts of GldA abolish the gliding phenotype. Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. Bacteroidetes with members of this protein family appear to have all of the genes associated with gliding motility.
Pssm-ID: 132561 [Multi-domain] Cd Length: 301 Bit Score: 86.37 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 22 RVVHIDKlwsIFGEgesQFAVHQdLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAAS 101
Cdd:TIGR03522 4 RVSSLTK---LYGT---QNALDE-VSFEAQKGRIVGFLGPNGAGKSTTMKIITGYLPPDSGSVQVCGEDVLQNPKEVQRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 102 rVGMLFQQGALYSAFNVLDNVAFPLRELGTLPRALVDAAALVkLQMVGLKPEHAMRMPAdLSGGMIKRVALARALIMDPP 181
Cdd:TIGR03522 77 -IGYLPEHNPLYLDMYVREYLQFIAGIYGMKGQLLKQRVEEM-IELVGLRPEQHKKIGQ-LSKGYRQRVGLAQALIHDPK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2788666989 182 LLLLDEPTAGLDPNGSDDFCALLRELHAelDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEVAVF 252
Cdd:TIGR03522 154 VLILDEPTTGLDPNQLVEIRNVIKNIGK--DKTIILSTHIMQEVEAICDRVIIINKGKIVADKKLDELSAA 222
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
53-253 |
1.35e-19 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 85.61 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 53 GEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQGAlySAFN-------VLDnvaFP 125
Cdd:PRK15112 39 GQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPS--TSLNprqrisqILD---FP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 126 LR---ELGTLPRalvDAAALVKLQMVGLKPEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDFCA 202
Cdd:PRK15112 114 LRlntDLEPEQR---EKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLIN 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2788666989 203 LLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEVAVFP 253
Cdd:PRK15112 191 LMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASP 241
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
42-240 |
1.43e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 88.15 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 42 VHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEG-AASRVGML----FQQGaLYSAF 116
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGIAYVpedrKGEG-LVLDL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 117 NVLDNVAFP----LRELGTLPRALVDAAALVKLQMVGLKPEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGL 192
Cdd:COG1129 346 SIRENITLAsldrLSRGGLLDRRRERALAEEYIKRLRIKTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGI 425
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2788666989 193 DPNGSDDFCALLRELhAELDLTVVMVTHDLDTLFALSSRVAVLAEKKV 240
Cdd:COG1129 426 DVGAKAEIYRLIREL-AAEGKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
44-233 |
2.11e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 84.83 E-value: 2.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQI--LGLLQPG---KGTVEVLGQPAAAMGGEGAASR--VGMLFQQGALYSaF 116
Cdd:PRK14239 22 NSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIYSPRTDTVDLRkeIGMVFQQPNPFP-M 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 117 NVLDNVAFPLRELGTLPRALVDAAALVKLQMVGLKPEHAMRMPAD---LSGGMIKRVALARALIMDPPLLLLDEPTAGLD 193
Cdd:PRK14239 101 SIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRLHDSalgLSGGQQQRVCIARVLATSPKIILLDEPTSALD 180
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2788666989 194 PNGSDDFCALLRELHAelDLTVVMVTHDLDTLFALSSRVA 233
Cdd:PRK14239 181 PISAGKIEETLLGLKD--DYTMLLVTRSMQQASRISDRTG 218
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
45-256 |
2.67e-19 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 85.93 E-value: 2.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 45 DLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPG---KGTV-----EVLGQPAAAMGGEGAaSRVGMLFQQGAlySAF 116
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSAtfngrEILNLPEKELNKLRA-EQISMIFQDPM--TSL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 117 NVLDNVAFPLRELGTLPRALVDAAAL---VK-LQMVGLkPEHAMRM---PADLSGGMIKRVALARALIMDPPLLLLDEPT 189
Cdd:PRK09473 111 NPYMRVGEQLMEVLMLHKGMSKAEAFeesVRmLDAVKM-PEARKRMkmyPHEFSGGMRQRVMIAMALLCRPKLLIADEPT 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2788666989 190 AGLDPNGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEVAVFP-HPF 256
Cdd:PRK09473 190 TALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPsHPY 257
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
41-220 |
3.19e-19 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 83.31 E-value: 3.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 41 AVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGtvEVLGQPAAAMGGEGAASRvGMLF--QQGALYSAFNV 118
Cdd:cd03231 14 ALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAG--RVLLNGGPLDFQRDSIAR-GLLYlgHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 119 LDNVAFPLRELGTlpRALVDAAALVKLQMVGLKPEHAmrmpadLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSD 198
Cdd:cd03231 91 LENLRFWHADHSD--EQVEEALARVGLNGFEDRPVAQ------LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
170 180
....*....|....*....|..
gi 2788666989 199 DFCALLRElHAELDLTVVMVTH 220
Cdd:cd03231 163 RFAEAMAG-HCARGGMVVLTTH 183
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
44-244 |
4.77e-19 |
|
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: 83.35 E-value: 4.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPaaamggegaasrVGMLFQQGALYSAFNVLDNVA 123
Cdd:cd03220 39 KDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV------------SSLLGLGGGFNPELTGRENIY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 124 FPLRELGtLPRALVDA-----AALVKLQMVGLKPehaMRMpadLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSD 198
Cdd:cd03220 107 LNGRLLG-LSRKEIDEkideiIEFSELGDFIDLP---VKT---YSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2788666989 199 DFCALLRELHAELDlTVVMVTHDLDTLFALSSRVAVLAEKKVLVTG 244
Cdd:cd03220 180 KCQRRLRELLKQGK-TVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
26-256 |
6.28e-19 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 84.79 E-value: 6.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 26 IDKLWSIFGEGESQFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQ-PGKGTVEVL---GQPAAAMGGEGAAS 101
Cdd:PRK11022 6 VDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPGRVMAEKLefnGQDLQRISEKERRN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 102 RVG----MLFQQGAlySAFNVLDNVAFPLREL------GTlpRALVDAAALVKLQMVGLkPEHAMRM---PADLSGGMIK 168
Cdd:PRK11022 86 LVGaevaMIFQDPM--TSLNPCYTVGFQIMEAikvhqgGN--KKTRRQRAIDLLNQVGI-PDPASRLdvyPHQLSGGMSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 169 RVALARALIMDPPLLLLDEPTAGLDPNGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQE 248
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHD 240
|
....*....
gi 2788666989 249 VAVFP-HPF 256
Cdd:PRK11022 241 IFRAPrHPY 249
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
45-249 |
6.89e-19 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 84.93 E-value: 6.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 45 DLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTV----EVLGQPAAAMGGEGAASRVGMLFQQGALYSAFNVLD 120
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIvlngRVLFDAEKGICLPPEKRRIGYVFQDARLFPHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 121 NVAFPLRElgtlpralVDAAALVKL-QMVGLKPeHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDD 199
Cdd:PRK11144 96 NLRYGMAK--------SMVAQFDKIvALLGIEP-LLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2788666989 200 FCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEV 249
Cdd:PRK11144 167 LLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
44-249 |
1.05e-18 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 82.66 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQGALYSAfNVLDNVA 123
Cdd:cd03254 20 KDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDTFLFSG-TIMENIR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 124 fplreLGTL--PRALVDAAAlvklQMVGLKPEhAMRMP-----------ADLSGGMIKRVALARALIMDPPLLLLDEPTA 190
Cdd:cd03254 99 -----LGRPnaTDEEVIEAA----KEAGAHDF-IMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKILILDEATS 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2788666989 191 GLDPNGSDDFCALLRELHAelDLTVVMVTHDLDTLfALSSRVAVLAEKKVLVTGTPQEV 249
Cdd:cd03254 169 NIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTI-KNADKILVLDDGKIIEEGTHDEL 224
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
57-266 |
1.13e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 83.61 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 57 SIVGGSGTGKTVLLRQILGLLQPGKG---TVEVL--GQPAAAMGGEGA-ASRVGMLFQQGALYSaFNVLDNVAFPLRELG 130
Cdd:PRK14271 51 SLMGPTGSGKTTFLRTLNRMNDKVSGyrySGDVLlgGRSIFNYRDVLEfRRRVGMLFQRPNPFP-MSIMDNVLAGVRAHK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 131 TLPRALVDAAALVKLQMVGLKPEHAMRM---PADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDFCALLREL 207
Cdd:PRK14271 130 LVPRKEFRGVAQARLTEVGLWDAVKDRLsdsPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSL 209
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 208 HAEldLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEVAVFP-HPFVAQFFQGERG 266
Cdd:PRK14271 210 ADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPkHAETARYVAGLSG 267
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
44-237 |
1.78e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 84.86 E-value: 1.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVlgqPaaamggegaaSRVGMLF-------QQGALYSAf 116
Cdd:COG4178 380 EDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR---P----------AGARVLFlpqrpylPLGTLREA- 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 117 nvldnVAFPLRelgtlPRALVDAAALVKLQMVGLkPEHAMRM--PAD----LSGGMIKRVALARALIMDPPLLLLDEPTA 190
Cdd:COG4178 446 -----LLYPAT-----AEAFSDAELREALEAVGL-GHLAERLdeEADwdqvLSLGEQQRLAFARLLLHKPDWLFLDEATS 514
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2788666989 191 GLDPNGSDDFCALLRElhaEL-DLTVVMVTHDlDTLFALSSRVAVLAE 237
Cdd:COG4178 515 ALDEENEAALYQLLRE---ELpGTTVISVGHR-STLAAFHDRVLELTG 558
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
44-223 |
2.64e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 81.30 E-value: 2.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQGALYSAfNVLDNVA 123
Cdd:PRK10247 24 NNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGD-TVYDNLI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 124 FP--LRELGTLPRALVDaaalvKLQMVGLkPEHAMRMP-ADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDF 200
Cdd:PRK10247 103 FPwqIRNQQPDPAIFLD-----DLERFAL-PDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNV 176
|
170 180
....*....|....*....|...
gi 2788666989 201 CALLRELHAELDLTVVMVTHDLD 223
Cdd:PRK10247 177 NEIIHRYVREQNIAVLWVTHDKD 199
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
42-248 |
3.38e-18 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 81.12 E-value: 3.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 42 VHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQGALysaFN--VL 119
Cdd:cd03253 16 VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQDTVL---FNdtIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 120 DNVAFplrelGTL---PRALVDAAALVKLQmvglkpEHAMRMP-----------ADLSGGMIKRVALARALIMDPPLLLL 185
Cdd:cd03253 93 YNIRY-----GRPdatDEEVIEAAKAAQIH------DKIMRFPdgydtivgergLKLSGGEKQRVAIARAILKNPPILLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2788666989 186 DEPTAGLDPNGSDDFCALLRELHAelDLTVVMVTHDLDTLfALSSRVAVLAEKKVLVTGTPQE 248
Cdd:cd03253 162 DEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTI-VNADKIIVLKDGRIVERGTHEE 221
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
44-249 |
5.32e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 80.90 E-value: 5.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGqpaaamggegaasRVGMLFQQGAlysAFN----VL 119
Cdd:COG1134 43 KDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-------------RVSALLELGA---GFHpeltGR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 120 DNVAFPLRELGtLPRALVDAaalvKLQMV----GLkpEHAMRMPA-DLSGGMIKRVALARALIMDPPLLLLDEPTAGldp 194
Cdd:COG1134 107 ENIYLNGRLLG-LSRKEIDE----KFDEIvefaEL--GDFIDQPVkTYSSGMRARLAFAVATAVDPDILLVDEVLAV--- 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2788666989 195 nGSDDF---C-ALLRELHAELDlTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEV 249
Cdd:COG1134 177 -GDAAFqkkClARIRELRESGR-TVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEV 233
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
50-252 |
1.02e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 82.79 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 50 IYRGEMLSIVGGSGTGKTVLLRQILGLLQPG---KGTVEVLGQPAAAMGGEGaasRVGMLFQQGALYSAFNVLDNVAF-- 124
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRA---ISAYVQQDDLFIPTLTVREHLMFqa 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 125 ----PLRELGTLPRALVDAAalvkLQMVGLKPEHAMRM--PAD---LSGGMIKRVALARALIMDPPLLLLDEPTAGLDPN 195
Cdd:TIGR00955 125 hlrmPRRVTKKEKRERVDEV----LQALGLRKCANTRIgvPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSF 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2788666989 196 GSDDFCALLRELhAELDLTVVMVTHD-LDTLFALSSRVAVLAEKKVLVTGTPQEVAVF 252
Cdd:TIGR00955 201 MAYSVVQVLKGL-AQKGKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQAVPF 257
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
44-222 |
1.12e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 80.52 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQGALYSAFN--VLDN 121
Cdd:COG1101 23 DGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQDPMMGTAPSmtIEEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 122 VAFPLR--ELGTLPRALVDA------AALVKLQMvGLkpEHAMRMPAD-LSGGmiKRVALAraLIM----DPPLLLLDEP 188
Cdd:COG1101 103 LALAYRrgKRRGLRRGLTKKrrelfrELLATLGL-GL--ENRLDTKVGlLSGG--QRQALS--LLMatltKPKLLLLDEH 175
|
170 180 190
....*....|....*....|....*....|....
gi 2788666989 189 TAGLDPNGSDDFCALLRELHAELDLTVVMVTHDL 222
Cdd:COG1101 176 TAALDPKTAALVLELTEKIVEENNLTTLMVTHNM 209
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
39-240 |
1.15e-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: 79.75 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 39 QFAVhQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGegaaSRVGMLFQQGALYSAFNV 118
Cdd:TIGR03740 13 QTAV-NNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKDL----HKIGSLIESPPLYENLTA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 119 LDNVafplrELGTLPRALVDAAALVKLQMVGLkpEHAMRMPA-DLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGS 197
Cdd:TIGR03740 88 RENL-----KVHTTLLGLPDSRIDEVLNIVDL--TNTGKKKAkQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLDPIGI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2788666989 198 DDFCALLRELHAElDLTVVMVTHDLDTLFALSSRVAVLAEKKV 240
Cdd:TIGR03740 161 QELRELIRSFPEQ-GITVILSSHILSEVQQLADHIGIISEGVL 202
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
42-225 |
3.10e-17 |
|
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: 78.67 E-value: 3.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 42 VHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQGALYSAfNVLDN 121
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVLFAR-SLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 122 VAFPLR--ELGTLPRALVDAAALVKLQMVGLKP-EHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSD 198
Cdd:cd03248 108 IAYGLQscSFECVKEAAQKAHAHSFISELASGYdTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQ 187
|
170 180
....*....|....*....|....*..
gi 2788666989 199 DFCALLRELHAelDLTVVMVTHDLDTL 225
Cdd:cd03248 188 QVQQALYDWPE--RRTVLVIAHRLSTV 212
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
42-248 |
4.20e-17 |
|
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: 78.35 E-value: 4.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 42 VHQDLDLDIYRGEMLSIVGGSGTGKTVllrqILGLLQ----PGKGTVEVLGQPAAAMGGEGAASRVGMLFQQGALYSAfN 117
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKST----VVSLLErfydPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFDG-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 118 VLDNVAF--PLRELGTLPRALVDAAA---LVKL-----QMVGlkpEHAmrmpADLSGGMIKRVALARALIMDPPLLLLDE 187
Cdd:cd03249 93 IAENIRYgkPDATDEEVEEAAKKANIhdfIMSLpdgydTLVG---ERG----SQLSGGQKQRIAIARALLRNPKILLLDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2788666989 188 PTAGLDpNGSDdfcallRELHAELDL-----TVVMVTHDLDTLFAlSSRVAVLAEKKVLVTGTPQE 248
Cdd:cd03249 166 ATSALD-AESE------KLVQEALDRamkgrTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDE 223
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
42-248 |
7.74e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 80.15 E-value: 7.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 42 VHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQGALYSAfNVLDN 121
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSG-SVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 122 VAFPLRELgtlPRALVDAAAlvklQMVGLKpEHAMRMPAD-----------LSGGMIKRVALARALIMDPPLLLLDEPTA 190
Cdd:TIGR00958 575 IAYGLTDT---PDEEIMAAA----KAANAH-DFIMEFPNGydtevgekgsqLSGGQKQRIAIARALVRKPRVLILDEATS 646
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2788666989 191 GLDPNGSddfcALLRELHAELDLTVVMVTHDLDTLfALSSRVAVLAEKKVLVTGTPQE 248
Cdd:TIGR00958 647 ALDAECE----QLLQESRSRASRTVLLIAHRLSTV-ERADQILVLKKGSVVEMGTHKQ 699
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
45-249 |
1.08e-16 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 77.43 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 45 DLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQGALYSAFNVLDNVAF 124
Cdd:COG4604 19 DVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQENHINSRLTVRELVAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 125 plrelGTLP----------RALVDAAalvkLQMVGLKP-EHamRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLD 193
Cdd:COG4604 99 -----GRFPyskgrltaedREIIDEA----IAYLDLEDlAD--RYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2788666989 194 PNGSDDFCALLRELHAELDLTVVMVTHDLDtlFA--LSSRVAVLAEKKVLVTGTPQEV 249
Cdd:COG4604 168 MKHSVQMMKLLRRLADELGKTVVIVLHDIN--FAscYADHIVAMKDGRVVAQGTPEEI 223
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
46-249 |
1.23e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 77.28 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 46 LDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLqPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQGAlySAFNV-----LD 120
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQQT--PPFAMpvfqyLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 121 NVAFPLRELGTLPRALVDAAALVKLQMvglKPEhamRMPADLSGGMIKRVALARALIMDPP-------LLLLDEPTAGLD 193
Cdd:PRK03695 92 LHQPDKTRTEAVASALNEVAEALGLDD---KLG---RSVNQLSGGEWQRVRLAAVVLQVWPdinpagqLLLLDEPMNSLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2788666989 194 PNGSDDFCALLRELhAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEV 249
Cdd:PRK03695 166 VAQQAALDRLLSEL-CQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
44-221 |
1.64e-16 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 74.41 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVlgqpaaamggeGAASRVGmLFQQgalysafnvldnva 123
Cdd:cd03221 17 KDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-----------GSTVKIG-YFEQ-------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 124 fplrelgtlpralvdaaalvklqmvglkpehamrmpadLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGsddfCAL 203
Cdd:cd03221 71 --------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLES----IEA 108
|
170
....*....|....*...
gi 2788666989 204 LRELHAELDLTVVMVTHD 221
Cdd:cd03221 109 LEEALKEYPGTVILVSHD 126
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
33-262 |
1.81e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 79.10 E-value: 1.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 33 FGEGESQFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAmggegaasrvgmlFQQGAL 112
Cdd:PRK11160 346 FTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAD-------------YSEAAL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 113 YSAFNVL------------DNVAFplrelgTLPRAlVDAAALVKLQMVGLKPEHAMRMPAD---------LSGGMIKRVA 171
Cdd:PRK11160 413 RQAISVVsqrvhlfsatlrDNLLL------AAPNA-SDEALIEVLQQVGLEKLLEDDKGLNawlgeggrqLSGGEQRRLG 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 172 LARALIMDPPLLLLDEPTAGLDPNGSDDFCALLRElHAElDLTVVMVTHDLdTLFALSSRVAVLAEKKVLVTGTPQEVaV 251
Cdd:PRK11160 486 IARALLHDAPLLLLDEPTEGLDAETERQILELLAE-HAQ-NKTVLMITHRL-TGLEQFDRICVMDNGQIIEQGTHQEL-L 561
|
250
....*....|.
gi 2788666989 252 FPHPFVAQFFQ 262
Cdd:PRK11160 562 AQQGRYYQLKQ 572
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
20-237 |
2.23e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.53 E-value: 2.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 20 GERVVHIDKLWSIFGEGESqfAVHqDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGA 99
Cdd:COG3845 254 GEVVLEVENLSVRDDRGVP--ALK-DVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRER 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 100 ASRvGMLF-----QQGALYSAFNVLDNVAF------PLRELGTLPRALVDAAALVKLQMVGLKPEHAMRMPADLSGGMIK 168
Cdd:COG3845 331 RRL-GVAYipedrLGRGLVPDMSVAENLILgryrrpPFSRGGFLDRKAIRAFAEELIEEFDVRTPGPDTPARSLSGGNQQ 409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2788666989 169 RVALARALIMDPPLLLLDEPTAGLDPNGSDDFCALLRELHAElDLTVVMVTHDLDTLFALSSRVAVLAE 237
Cdd:COG3845 410 KVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYE 477
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
46-196 |
1.05e-15 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 74.11 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 46 LDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLfqqGALYSAFNVLDNVAFP 125
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHL---PGLKADLSTLENLHFL 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2788666989 126 LRELGTLPRALVDAAalvkLQMVGLKpEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNG 196
Cdd:PRK13543 107 CGLHGRRAKQMPGSA----LAIVGLA-GYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEG 172
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
34-225 |
1.09e-15 |
|
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: 73.66 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 34 GEGESQFAVHqDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGqpaaamggegaasRVGMLFQQGALY 113
Cdd:cd03250 13 GEQETSFTLK-DINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------SIAYVSQEPWIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 114 SAfNVLDNVAF--PLRElgTLPRALVDAAALVK---------LQMVGLKPehamrmpADLSGGMIKRVALARALIMDPPL 182
Cdd:cd03250 79 NG-TIRENILFgkPFDE--ERYEKVIKACALEPdleilpdgdLTEIGEKG-------INLSGGQKQRISLARAVYSDADI 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2788666989 183 LLLDEPTAGLDPNGSDD-----FCALLRElhaelDLTVVMVTHDLDTL 225
Cdd:cd03250 149 YLLDDPLSAVDAHVGRHifencILGLLLN-----NKTRILVTHQLQLL 191
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
19-256 |
1.13e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 76.81 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 19 QGERVVHIDKLWSIFGEGESQFAvHQD------LDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLqPGKGTVEVLGQPAA 92
Cdd:PRK11174 337 QGEKELASNDPVTIEAEDLEILS-PDGktlagpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELR 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 93 AMGGEGAASRVGMLFQQGALYSAfNVLDNVAF--PLRELGTLPRALVDAAAL--VKLQMVGLKPEHAMRMpADLSGGMIK 168
Cdd:PRK11174 415 ELDPESWRKHLSWVGQNPQLPHG-TLRDNVLLgnPDASDEQLQQALENAWVSefLPLLPQGLDTPIGDQA-AGLSVGQAQ 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 169 RVALARALIMDPPLLLLDEPTAGLDPNGSDdfcALLREL-HAELDLTVVMVTHDLDTLFALsSRVAVLAEKKVLVTGTPQ 247
Cdd:PRK11174 493 RLALARALLQPCQLLLLDEPTASLDAHSEQ---LVMQALnAASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYA 568
|
....*....
gi 2788666989 248 EVAVFPHPF 256
Cdd:PRK11174 569 ELSQAGGLF 577
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
44-245 |
1.30e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 74.92 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPaaaMGGEGAASRVGMLFQQGALYSAFNVL--DN 121
Cdd:PRK15056 24 RDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQP---TRQALQKNLVAYVPQSEEVDWSFPVLveDV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 122 VAFP-------LRELGTLPRALVDaAALVKLQMVglkpEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDP 194
Cdd:PRK15056 101 VMMGryghmgwLRRAKKRDRQIVT-AALARVDMV----EFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2788666989 195 NGSDDFCALLRELHAElDLTVVMVTHDLDTlfalssrVAVLAEKKVLVTGT 245
Cdd:PRK15056 176 KTEARIISLLRELRDE-GKTMLVSTHNLGS-------VTEFCDYTVMVKGT 218
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
41-241 |
1.77e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 75.12 E-value: 1.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 41 AVhQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLG-QPAAAMGGEGaaSRVGMLF-QQGALYSAFNV 118
Cdd:COG4586 37 AV-DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyVPFKRRKEFA--RRIGVVFgQRSQLWWDLPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 119 LDNVAFpLRELGTLPRALVDA--AALVKLqmvgLKPEHAMRMPA-DLSGG--MikRVALARALIMDPPLLLLDEPTAGLD 193
Cdd:COG4586 114 IDSFRL-LKAIYRIPDAEYKKrlDELVEL----LDLGELLDTPVrQLSLGqrM--RCELAAALLHRPKILFLDEPTIGLD 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2788666989 194 PNGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVL 241
Cdd:COG4586 187 VVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRII 234
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
45-248 |
2.45e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 75.93 E-value: 2.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 45 DLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAaSRVGMLFQQGALYSAFNVLDNVAF 124
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATR-RRVGYMSQAFSLYGELTVRQNLEL 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 125 PLReLGTLPRAlvDAAALVKlQMV---GLKpEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDFC 201
Cdd:NF033858 363 HAR-LFHLPAA--EIAARVA-EMLerfDLA-DVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFW 437
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2788666989 202 ALLRELHAELDLTVVMVTHdldtlF----ALSSRVAVLAEKKVLVTGTPQE 248
Cdd:NF033858 438 RLLIELSREDGVTIFISTH-----FmneaERCDRISLMHAGRVLASDTPAA 483
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
44-255 |
2.50e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 74.05 E-value: 2.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRqILGLLQ-PGKGTVEVLGQPAAAMGGEGAASRVGMLFQQGALYSAFNVLDNV 122
Cdd:PRK10575 28 HPLSLTFPAGKVTGLIGHNGSGKSTLLK-MLGRHQpPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGMTVRELV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 123 A---FP----LRELGTLPRALVDAAalvkLQMVGLKPeHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPN 195
Cdd:PRK10575 107 AigrYPwhgaLGRFGAADREKVEEA----ISLVGLKP-LAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIA 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2788666989 196 GSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEV--------------AVFPHP 255
Cdd:PRK10575 182 HQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELmrgetleqiygipmGILPHP 255
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
42-249 |
3.30e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 73.39 E-value: 3.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 42 VHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASR-VGMLFQQGALYSAFNVLD 120
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgIGYLPQEASIFRRLSVYD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 121 NVAFPL---RELGTLPRALVDAAALVKLQMVGLKPEhamrMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGS 197
Cdd:PRK10895 98 NLMAVLqirDDLSAEQREDRANELMEEFHIEHLRDS----MGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2788666989 198 DDFCALLRELHaELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEV 249
Cdd:PRK10895 174 IDIKRIIEHLR-DSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
44-225 |
5.90e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 74.33 E-value: 5.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEvLGQPAaamggegaasRVGMLFQ-QGALYSAFNVLDNV 122
Cdd:COG0488 332 DDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK-LGETV----------KIGYFDQhQEELDPDKTVLDEL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 123 AfPLRELGTL--PRALvdaaalvkLQMVGLKPEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPngsdDF 200
Cdd:COG0488 401 R-DGAPGGTEqeVRGY--------LGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDI----ET 467
|
170 180
....*....|....*....|....*...
gi 2788666989 201 CALLRELHAELDLTVVMVTHD---LDTL 225
Cdd:COG0488 468 LEALEEALDDFPGTVLLVSHDryfLDRV 495
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
45-248 |
8.12e-15 |
|
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: 73.98 E-value: 8.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 45 DLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQGALysaFN--VLDNV 122
Cdd:TIGR02203 350 SISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVL---FNdtIANNI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 123 AFPlrELGTLPRALVDAAalvkLQMVGLKpEHAMRMP-----------ADLSGGMIKRVALARALIMDPPLLLLDEPTAG 191
Cdd:TIGR02203 427 AYG--RTEQADRAEIERA----LAAAYAQ-DFVDKLPlgldtpigengVLLSGGQRQRLAIARALLKDAPILILDEATSA 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2788666989 192 LDpNGSDdfcallRELHAELD-----LTVVMVTHDLDTLfALSSRVAVLAEKKVLVTGTPQE 248
Cdd:TIGR02203 500 LD-NESE------RLVQAALErlmqgRTTLVIAHRLSTI-EKADRIVVMDDGRIVERGTHNE 553
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
41-249 |
1.34e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 72.17 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 41 AVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPG--------KGTVEVLGQPAAAMGGEGAASRVGMLFQQGAL 112
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 113 YSAFNVLDNVA---FP-LRELGTLPR----------ALVDAAALVKlqmvglkpehamRMPADLSGGMIKRVALARAL-- 176
Cdd:PRK13547 95 AFAFSAREIVLlgrYPhARRAGALTHrdgeiawqalALAGATALVG------------RDVTTLSGGELARVQFARVLaq 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 177 -------IMDPPLLLLDEPTAGLDPNGSDDFCALLRELHAELDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEV 249
Cdd:PRK13547 163 lwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
44-233 |
1.45e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 71.74 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLR--QILGLLQPG---KGTVEVLGQPAAAMGG--EGAASRVGMLFQQGALYSAf 116
Cdd:PRK14243 27 KNVWLDIPKNQITAFIGPSGCGKSTILRcfNRLNDLIPGfrvEGKVTFHGKNLYAPDVdpVEVRRRIGMVFQKPNPFPK- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 117 NVLDNVAFPLRELG-------TLPRALVDAA----ALVKLQMVGLKpehamrmpadLSGGMIKRVALARALIMDPPLLLL 185
Cdd:PRK14243 106 SIYDNIAYGARINGykgdmdeLVERSLRQAAlwdeVKDKLKQSGLS----------LSGGQQQRLCIARAIAVQPEVILM 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2788666989 186 DEPTAGLDPNGSDDFCALLRELHAelDLTVVMVTHDLDTlfalSSRVA 233
Cdd:PRK14243 176 DEPCSALDPISTLRIEELMHELKE--QYTIIIVTHNMQQ----AARVS 217
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
44-226 |
2.61e-14 |
|
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: 69.10 E-value: 2.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPaaamggegaasrvGMLF--QQGalYsafnvldn 121
Cdd:cd03223 18 KDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE-------------DLLFlpQRP--Y-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 122 vaFPLrelGTLPRALVdaaalvklqmvglKPEHAMrmpadLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDFC 201
Cdd:cd03223 75 --LPL---GTLREQLI-------------YPWDDV-----LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLY 131
|
170 180
....*....|....*....|....*..
gi 2788666989 202 ALLRELHAeldlTVVMVTH--DLDTLF 226
Cdd:cd03223 132 QLLKELGI----TVISVGHrpSLWKFH 154
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
44-251 |
4.06e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.12 E-value: 4.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASR-VGMLFQQGALYSAFNVLDNV 122
Cdd:PRK09700 22 KSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGIIYQELSVIDELTVLENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 123 ---AFPLRELGTLPraLVDAA-----ALVKLQMVGLKPEHAMRMpADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDP 194
Cdd:PRK09700 102 yigRHLTKKVCGVN--IIDWRemrvrAAMMLLRVGLKVDLDEKV-ANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTN 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2788666989 195 NGSDDFCALLRELHAElDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEVAV 251
Cdd:PRK09700 179 KEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSN 234
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
44-265 |
4.12e-14 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 70.06 E-value: 4.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEmlsIVG--G-SGTGKTVLLRQILGLLQPGKGTVEVLGQ-----PAAAMggegaaSRVGM--LFQQGaly 113
Cdd:COG1137 20 KDVSLEVNQGE---IVGllGpNGAGKTTTFYMIVGLVKPDSGRIFLDGEdithlPMHKR------ARLGIgyLPQEA--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 114 SAF---NVLDNVAFPLrELGTLPRALVDA--AALvkLQMVGLkpEHAMRMPAD-LSGGMIKRVALARALIMDPPLLLLDE 187
Cdd:COG1137 88 SIFrklTVEDNILAVL-ELRKLSKKEREErlEEL--LEEFGI--THLRKSKAYsLSGGERRRVEIARALATNPKFILLDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2788666989 188 PTAGLDPNGSDDFCALLRELhAELDLTVVMVTHDL-DTLfALSSRVAVLAEKKVLVTGTPQEVAVfpHPFVAQFFQGER 265
Cdd:COG1137 163 PFAGVDPIAVADIQKIIRHL-KERGIGVLITDHNVrETL-GICDRAYIISEGKVLAEGTPEEILN--NPLVRKVYLGED 237
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
45-245 |
6.69e-14 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 71.69 E-value: 6.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 45 DLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQGALYSAfNVLDNVAF 124
Cdd:TIGR01193 492 DISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSG-SILENLLL 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 125 PLRElGTLPRALVDAAALV-------KLQMvGLKPEHAMRmPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGS 197
Cdd:TIGR01193 571 GAKE-NVSQDEIWAACEIAeikddieNMPL-GYQTELSEE-GSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITE 647
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2788666989 198 DDFCALLRELHaelDLTVVMVTHDLdTLFALSSRVAVLAEKKVLVTGT 245
Cdd:TIGR01193 648 KKIVNNLLNLQ---DKTIIFVAHRL-SVAKQSDKIIVLDHGKIIEQGS 691
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
19-237 |
1.09e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 70.85 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 19 QGERVVHIDKLwsiFGEGesqFAvhqDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVeVLGQPAAAMGGEG 98
Cdd:PRK15439 264 AGAPVLTVEDL---TGEG---FR---NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRI-MLNGKEINALSTA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 99 AASRVGMLF-----QQGALY----SAFNVldnVAFPLRELGTLPRALVDAAALVKL-QMVGLKPEHAMRMPADLSGGMIK 168
Cdd:PRK15439 334 QRLARGLVYlpedrQSSGLYldapLAWNV---CALTHNRRGFWIKPARENAVLERYrRALNIKFNHAEQAARTLSGGNQQ 410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2788666989 169 RVALARALIMDPPLLLLDEPTAGLDPNGSDDFCALLRELhAELDLTVVMVTHDLDTLFALSSRVAVLAE 237
Cdd:PRK15439 411 KVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSI-AAQNVAVLFISSDLEEIEQMADRVLVMHQ 478
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
33-229 |
4.89e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 66.91 E-value: 4.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 33 FGEGES--QFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLL--QPGKGTVEVlgqpaaamggegaasrvgmlfQ 108
Cdd:COG2401 34 FGVELRvvERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDV---------------------P 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 109 QGALYSAFNVLDNVAfplrelgtLPRALVDAAALvkLQMVGLKPEHAM-RMPADLSGGMIKRVALARALIMDPPLLLLDE 187
Cdd:COG2401 93 DNQFGREASLIDAIG--------RKGDFKDAVEL--LNAVGLSDAVLWlRRFKELSTGQKFRFRLALLLAERPKLLVIDE 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2788666989 188 PTAGLDPNGSDDFCALLRELHAELDLTVVMVTHDLDTLFALS 229
Cdd:COG2401 163 FCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVIDDLQ 204
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
38-244 |
6.19e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 68.54 E-value: 6.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 38 SQFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPaAAMGGEGAASRVGMLF--QQGALYSA 115
Cdd:PRK15439 22 SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNP-CARLTPAKAHQLGIYLvpQEPLLFPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 116 FNVLDNVAFPL-RELGTLPRalvdAAALVKLQMVGLKPEhamrMPA---DLSGGMIkrVALARALIMDPPLLLLDEPTAG 191
Cdd:PRK15439 101 LSVKENILFGLpKRQASMQK----MKQLLAALGCQLDLD----SSAgslEVADRQI--VEILRGLMRDSRILILDEPTAS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2788666989 192 LDPNGSDDFCALLRELHAElDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTG 244
Cdd:PRK15439 171 LTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTIALSG 222
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
23-249 |
9.61e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 68.50 E-value: 9.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 23 VVHIDKLWSIFgEGESQFAVHQdLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQpaaamggeGAASR 102
Cdd:TIGR01257 1937 ILRLNELTKVY-SGTSSPAVDR-LCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGK--------SILTN 2006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 103 VGMLFQQGALYSAFNVLDNVA------FPLRELGTLPRALVDAAALVKLQMVGLKPeHAMRMPADLSGGMIKRVALARAL 176
Cdd:TIGR01257 2007 ISDVHQNMGYCPQFDAIDDLLtgrehlYLYARLRGVPAEEIEKVANWSIQSLGLSL-YADRLAGTYSGGNKRKLSTAIAL 2085
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2788666989 177 IMDPPLLLLDEPTAGLDPNGS----DDFCALLRELHAeldltVVMVTHDLDTLFALSSRVAVLAEKKVLVTGTPQEV 249
Cdd:TIGR01257 2086 IGCPPLVLLDEPTTGMDPQARrmlwNTIVSIIREGRA-----VVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
45-221 |
1.14e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 67.65 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 45 DLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGtvEVLGQPAAamggegaasRVGMLFQQGALYSAFNVLDNV-- 122
Cdd:TIGR03719 23 DISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG--EARPQPGI---------KVGYLPQEPQLDPTKTVRENVee 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 123 -------------------AFP-------LRELGTLpRALVDAAAL----VKLQMVGlkpeHAMRMP------ADLSGGM 166
Cdd:TIGR03719 92 gvaeikdaldrfneisakyAEPdadfdklAAEQAEL-QEIIDAADAwdldSQLEIAM----DALRCPpwdadvTKLSGGE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2788666989 167 IKRVALARALIMDPPLLLLDEPTAGLDpngSDDFCALLRELHaELDLTVVMVTHD 221
Cdd:TIGR03719 167 RRRVALCRLLLSKPDMLLLDEPTNHLD---AESVAWLERHLQ-EYPGTVVAVTHD 217
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
42-246 |
1.91e-12 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 65.21 E-value: 1.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 42 VHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQGALYSA---FNv 118
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQDPVLFSGtirSN- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 119 LDnvafPLRELGtlpralvDAAALVKLQMVGLKpEHAMRMP-----------ADLSGGMIKRVALARALIMDPPLLLLDE 187
Cdd:cd03244 98 LD----PFGEYS-------DEELWQALERVGLK-EFVESLPggldtvveeggENLSVGQRQLLCLARALLRKSKILVLDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2788666989 188 PTAGLDPNGSDDFCALLRELHAelDLTVVMVTHDLDTLFAlSSRVAVLAEKKVLVTGTP 246
Cdd:cd03244 166 ATASVDPETDALIQKTIREAFK--DCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDSP 221
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
33-231 |
3.72e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 66.15 E-value: 3.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 33 FGEGESQFAVhQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASrvgmLFQqgAL 112
Cdd:PRK10522 330 FAYQDNGFSV-GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRK----LFS--AV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 113 YSAFNVLDNVAFPlrELGTLPRALVDaAALVKLQMVG-LKPEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAG 191
Cdd:PRK10522 403 FTDFHLFDQLLGP--EGKPANPALVE-KWLERLKMAHkLELEDGRISNLKLSKGQKKRLALLLALAEERDILLLDEWAAD 479
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2788666989 192 LDPNGSDDFCALLRELHAELDLTVVMVTHDlDTLFALSSR 231
Cdd:PRK10522 480 QDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADR 518
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
38-225 |
5.38e-12 |
|
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: 63.89 E-value: 5.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 38 SQFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASR----VGMLFQQGALY 113
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 114 SAfNVLDNVAFPLRELGTLPRALVDAAAL---VKLQMVGLKPEHAMRmPADLSGGMIKRVALARALIMDPPLLLLDEPTA 190
Cdd:cd03290 92 NA-TVEENITFGSPFNKQRYKAVTDACSLqpdIDLLPFGDQTEIGER-GINLSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 2788666989 191 GLDPNGSDDFC-ALLRELHAELDLTVVMVTHDLDTL 225
Cdd:cd03290 170 ALDIHLSDHLMqEGILKFLQDDKRTLVLVTHKLQYL 205
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
53-244 |
6.88e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 65.29 E-value: 6.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 53 GEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQpaAAMGGEGAASRVGMLFQQGALYSAFNVLDNVAFP--LRELG 130
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILAN--NRKPTKQILKRTGFVTQDDILYPHLTVRETLVFCslLRLPK 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 131 TLPRALVDAAALVKLQMVGL-KPEHAM---RMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDFCALLRE 206
Cdd:PLN03211 172 SLTKQEKILVAESVISELGLtKCENTIignSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGS 251
|
170 180 190
....*....|....*....|....*....|....*....
gi 2788666989 207 LhAELDLTVVMVTHDLDT-LFALSSRVAVLAEKKVLVTG 244
Cdd:PLN03211 252 L-AQKGKTIVTSMHQPSSrVYQMFDSVLVLSEGRCLFFG 289
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
35-232 |
7.57e-12 |
|
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: 65.20 E-value: 7.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 35 EGESQFAVHQdLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGaasrvgmlFQQgaLYS 114
Cdd:COG4615 341 DGDEGFTLGP-IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREA--------YRQ--LFS 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 115 A-FNvlDNVAFPlRELGTLPRALVDAAA--LVKLQMvglkpEHAMRMPA------DLSGGMIKRVALARALIMDPPLLLL 185
Cdd:COG4615 410 AvFS--DFHLFD-RLLGLDGEADPARARelLERLEL-----DHKVSVEDgrfsttDLSQGQRKRLALLVALLEDRPILVF 481
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2788666989 186 DEPTAGLDPNGSDDF-CALLRELHAElDLTVVMVTHDlDTLFALSSRV 232
Cdd:COG4615 482 DEWAADQDPEFRRVFyTELLPELKAR-GKTVIAISHD-DRYFDLADRV 527
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
162-277 |
1.69e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 64.27 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 162 LSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDFCALLRELHAElDLTVVMVTHDLDTLFALSSRVAVLAEKKVL 241
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLA 214
|
90 100 110
....*....|....*....|....*....|....*.
gi 2788666989 242 VTGTPQEvaVFPHPFVAQFFQGERGRRAMAPAPSGP 277
Cdd:PRK10938 215 ETGEREE--ILQQALVAQLAHSEQLEGVQLPEPDEP 248
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
45-240 |
7.40e-11 |
|
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: 62.15 E-value: 7.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 45 DLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLqPGK--GTVEVLGQPAAAMGGEGAAS-----------RVGMLFQQGA 111
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAY-PGKfeGNVFINGKPVDIRNPAQAIRagiamvpedrkRHGIVPILGV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 112 LYS-AFNVLDNVAFplrelgtlpRALVDAAA-----LVKLQMVGLKPEHAMRMPADLSGGMIKRVALARALIMDPPLLLL 185
Cdd:TIGR02633 357 GKNiTLSVLKSFCF---------KMRIDAAAelqiiGSAIQRLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLIL 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2788666989 186 DEPTAGLDPNGSDDFCALLRELHAElDLTVVMVTHDLDTLFALSSRVAVLAEKKV 240
Cdd:TIGR02633 428 DEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
145-254 |
9.48e-11 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 61.36 E-value: 9.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 145 LQMVGLK-PEHAMR-MPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDFCALLRELHAELDLTVVMVTHDL 222
Cdd:PRK15093 140 LHRVGIKdHKDAMRsFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDL 219
|
90 100 110
....*....|....*....|....*....|..
gi 2788666989 223 DTLFALSSRVAVLAEKKVLVTGTPQEVAVFPH 254
Cdd:PRK15093 220 QMLSQWADKINVLYCGQTVETAPSKELVTTPH 251
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
44-235 |
1.07e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.85 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAA-AMGGEGAASRVGMLFQQGALYSAFNVLDNV 122
Cdd:PRK11288 21 DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAAGVAIIYQELHLVPEMTVAENL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 123 ---AFPLReLGTLPRALVDAAALVKLQMVGLKPEHAMRMpADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDD 199
Cdd:PRK11288 101 ylgQLPHK-GGIVNRRLLNYEAREQLEHLGVDIDPDTPL-KYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQ 178
|
170 180 190
....*....|....*....|....*....|....*.
gi 2788666989 200 FCALLRELHAElDLTVVMVTHDLDTLFALSSRVAVL 235
Cdd:PRK11288 179 LFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVF 213
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
45-249 |
2.25e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 60.91 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 45 DLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEgaaSRVG-----MlfQQGA---LYSAF 116
Cdd:NF033858 19 DVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHR---RAVCpriayM--PQGLgknLYPTL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 117 NVLDNVAFPLRELGtLPRALVDA--AALvkLQMVGLKPeHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDP 194
Cdd:NF033858 94 SVFENLDFFGRLFG-QDAAERRRriDEL--LRATGLAP-FADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2788666989 195 NGSDDFCALLRELHAEL-DLTVVMVT------HDLDTLFALSsrvavlaEKKVLVTGTPQEV 249
Cdd:NF033858 170 LSRRQFWELIDRIRAERpGMSVLVATaymeeaERFDWLVAMD-------AGRVLATGTPAEL 224
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
49-234 |
3.27e-10 |
|
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: 58.96 E-value: 3.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 49 DIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQpaaamggegaasRVGMLFQQGALYSAFNVLDNVAFPLRE 128
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELD------------TVSYKPQYIKADYEGTVRDLLSSITKD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 129 LGTLPRALVDAAAlvKLQMVGLKPehamRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDFCALLRELH 208
Cdd:cd03237 89 FYTHPYFKTEIAK--PLQIEQILD----REVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFA 162
|
170 180
....*....|....*....|....*.
gi 2788666989 209 AELDLTVVMVTHDLDTLFALSSRVAV 234
Cdd:cd03237 163 ENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
46-235 |
3.68e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 60.22 E-value: 3.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 46 LDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVL--GQPAAAMGGEGAASR-VGMLFQQGALYSAFNVLDNV 122
Cdd:TIGR02633 20 IDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYwsGSPLKASNIRDTERAgIVIIHQELTLVPELSVAENI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 123 aFPLRELgTLPRALVDAAALVK-----LQMVGLKPEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGS 197
Cdd:TIGR02633 100 -FLGNEI-TLPGGRMAYNAMYLraknlLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKET 177
|
170 180 190
....*....|....*....|....*....|....*...
gi 2788666989 198 DDFCALLRELHAElDLTVVMVTHDLDTLFALSSRVAVL 235
Cdd:TIGR02633 178 EILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVI 214
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
41-237 |
3.95e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 59.92 E-value: 3.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 41 AVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAAsRVGMLF------QQG--AL 112
Cdd:PRK11288 267 GLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAI-RAGIMLcpedrkAEGiiPV 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 113 YSafnVLDNVAFPLRELGTLPRALVDA---AALVKLQMVGLK-----PEHAMRmpaDLSGGMIKRVALARALIMDPPLLL 184
Cdd:PRK11288 346 HS---VADNINISARRHHLRAGCLINNrweAENADRFIRSLNiktpsREQLIM---NLSGGNQQKAILGRWLSEDMKVIL 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2788666989 185 LDEPTAGLDPNGSDDFCALLRELhAELDLTVVMVTHDLDTLFALSSRVAVLAE 237
Cdd:PRK11288 420 LDEPTRGIDVGAKHEIYNVIYEL-AAQGVAVLFVSSDLPEVLGVADRIVVMRE 471
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
44-225 |
5.95e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 59.65 E-value: 5.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQGALysaFN--VLDN 121
Cdd:PRK11176 360 RNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHL---FNdtIANN 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 122 VAFPLRElgTLPRALVDAAAlvklqmvglKPEHAM----RMP-----------ADLSGGMIKRVALARALIMDPPLLLLD 186
Cdd:PRK11176 437 IAYARTE--QYSREQIEEAA---------RMAYAMdfinKMDngldtvigengVLLSGGQRQRIAIARALLRDSPILILD 505
|
170 180 190
....*....|....*....|....*....|....*....
gi 2788666989 187 EPTAGLDPNGSDDFCALLRELHAelDLTVVMVTHDLDTL 225
Cdd:PRK11176 506 EATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTI 542
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
50-221 |
7.01e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.19 E-value: 7.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 50 IYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVevlgqpaaamggegaasRVGM-----LFQQ--GALYSAFNVLDNV 122
Cdd:PRK11147 342 VQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-----------------HCGTklevaYFDQhrAELDPEKTVMDNL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 123 AFPLREL---GtlpralVDAAALVKLQMVGLKPEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPngsdD 199
Cdd:PRK11147 405 AEGKQEVmvnG------RPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV----E 474
|
170 180
....*....|....*....|..
gi 2788666989 200 FCALLRELHAELDLTVVMVTHD 221
Cdd:PRK11147 475 TLELLEELLDSYQGTVLLVSHD 496
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
42-193 |
8.87e-10 |
|
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: 58.33 E-value: 8.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 42 VHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGqpaaamggegaasRVGMLFQQGALYSAfNVLDN 121
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPG-TIKEN 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2788666989 122 VAFPLRELGTLPRALVDAAALVklQMVGLKPEHAMRMPAD----LSGGMIKRVALARALIMDPPLLLLDEPTAGLD 193
Cdd:cd03291 118 IIFGVSYDEYRYKSVVKACQLE--EDITKFPEKDNTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
52-225 |
1.14e-09 |
|
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: 55.84 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 52 RGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVlgqpaaamggegaasrvgmlfqqgalysafnvldnvafplrelgt 131
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY--------------------------------------------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 132 lpralVDAAALVKLQMVGLKPEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDD-----FCALLRE 206
Cdd:smart00382 36 -----IDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALlllleELRLLLL 110
|
170
....*....|....*....
gi 2788666989 207 LHAELDLTVVMVTHDLDTL 225
Cdd:smart00382 111 LKSEKNLTVILTTNDEKDL 129
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
45-193 |
1.29e-09 |
|
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: 58.68 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 45 DLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQGALysaFN--VLDNV 122
Cdd:COG5265 376 GVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVL---FNdtIAYNI 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 123 AFPlrELGTLPRALVDAAALVKLQ------------MVG---LKpehamrmpadLSGGMIKRVALARALIMDPPLLLLDE 187
Cdd:COG5265 453 AYG--RPDASEEEVEAAARAAQIHdfieslpdgydtRVGergLK----------LSGGEKQRVAIARTLLKNPPILIFDE 520
|
....*.
gi 2788666989 188 PTAGLD 193
Cdd:COG5265 521 ATSALD 526
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
42-193 |
1.81e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 58.38 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 42 VHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGqpaaamggegaasRVGMLFQQGALYSAfNVLDN 121
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPG-TIKDN 506
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2788666989 122 VAFPLRELGTLPRALVDAAALVklQMVGLKPEHAMRMPAD----LSGGMIKRVALARALIMDPPLLLLDEPTAGLD 193
Cdd:TIGR01271 507 IIFGLSYDEYRYTSVIKACQLE--EDIALFPEKDKTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
145-193 |
1.97e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.04 E-value: 1.97e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2788666989 145 LQMVGLKPEHAMrmpADLSGGMIKRVALARALIMDPPLLLLDEPTAGLD 193
Cdd:PRK11147 143 LAQLGLDPDAAL---SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
45-223 |
2.27e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.82 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 45 DLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGtvEVLGQPAAamggegaasRVGMLFQQGALYSAFNVLDNV-- 122
Cdd:PRK11819 25 DISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG--EARPAPGI---------KVGYLPQEPQLDPEKTVRENVee 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 123 -------------------AFP-------LRELGTLpRALVDAAALVKL--QMvglkpEHAM---RMPAD------LSGG 165
Cdd:PRK11819 94 gvaevkaaldrfneiyaayAEPdadfdalAAEQGEL-QEIIDAADAWDLdsQL-----EIAMdalRCPPWdakvtkLSGG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2788666989 166 MIKRVALARALIMDPPLLLLDEPTAGLDpngsddfcA-----LLRELHaELDLTVVMVTHD---LD 223
Cdd:PRK11819 168 ERRRVALCRLLLEKPDMLLLDEPTNHLD--------AesvawLEQFLH-DYPGTVVAVTHDryfLD 224
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
52-240 |
3.96e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.86 E-value: 3.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 52 RGEMLSIVGGSGTGKTVLLRQILGLLqPGKGTVEVL--GQPAAAMGGEGAAS-----------RVGMLFQQG-------- 110
Cdd:PRK13549 287 RGEILGIAGLVGAGRTELVQCLFGAY-PGRWEGEIFidGKPVKIRNPQQAIAqgiamvpedrkRDGIVPVMGvgknitla 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 111 AL--YSAFNVLDNVAfplrELGTLPRALvdaaalvklQMVGLKPEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEP 188
Cdd:PRK13549 366 ALdrFTGGSRIDDAA----ELKTILESI---------QRLKVKTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEP 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2788666989 189 TAGLDPNGSDDFCALLRELhAELDLTVVMVTHDLDTLFALSSRVAVLAEKKV 240
Cdd:PRK13549 433 TRGIDVGAKYEIYKLINQL-VQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
44-250 |
9.56e-09 |
|
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: 54.07 E-value: 9.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLlqPG----KGTVEVLGQpAAAMGGEGAASRVG--MLFQQGALYSAFN 117
Cdd:cd03217 17 KGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH--PKyevtEGEILFKGE-DITDLPPEERARLGifLAFQYPPEIPGVK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 118 VLDnvaFpLRELGtlpralvdaaalvklqmVGLkpehamrmpadlSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGS 197
Cdd:cd03217 94 NAD---F-LRYVN-----------------EGF------------SGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDAL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2788666989 198 DDFCALLRELHAElDLTVVMVTHDLDTL-FALSSRVAVLAEKKVLVTGtPQEVA 250
Cdd:cd03217 141 RLVAEVINKLREE-GKSVLIITHYQRLLdYIKPDRVHVLYDGRIVKSG-DKELA 192
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
58-221 |
1.72e-08 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 53.38 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 58 IVGGSGTGKTVLLRQIL----GLLQPGK----------GTVEVLGQpaaamggegaasrVGMLFQ--QGALYSA---FNV 118
Cdd:cd03240 27 IVGQNGAGKTTIIEALKyaltGELPPNSkggahdpkliREGEVRAQ-------------VKLAFEnaNGKKYTItrsLAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 119 LDNVAFPLRElgtlpralvDAAALVklqmvglkpehaMRMPADLSGG------MIKRVALARALIMDPPLLLLDEPTAGL 192
Cdd:cd03240 94 LENVIFCHQG---------ESNWPL------------LDMRGRCSGGekvlasLIIRLALAETFGSNCGILALDEPTTNL 152
|
170 180 190
....*....|....*....|....*....|
gi 2788666989 193 DPNGSDD-FCALLRELHAELDLTVVMVTHD 221
Cdd:cd03240 153 DEENIEEsLAEIIEERKSQKNFQLIVITHD 182
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
44-248 |
1.97e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 54.79 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRvGMLF-----QQGALYSAFNV 118
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKK-GMAYitesrRDNGFFPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 119 LDNVAF-PLRELGTLPRA--LVDAAALVKL-----QMVGLKPEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTA 190
Cdd:PRK09700 359 AQNMAIsRSLKDGGYKGAmgLFHEVDEQRTaenqrELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTR 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2788666989 191 GLDPNGSDDFCALLRELhAELDLTVVMVTHDLDTLFALSSRVAV---------------LAEKKVLVTGTPQE 248
Cdd:PRK09700 439 GIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVfcegrltqiltnrddMSEEEIMAWALPQE 510
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
24-225 |
2.03e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 54.72 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 24 VHIDKLWSIFGEGESqfaVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRV 103
Cdd:PRK10790 341 IDIDNVSFAYRDDNL---VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGV 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 104 GMLfQQGALYSAFNVLDNVafplrelgTLPRALVDAAALVKLQMVGLKpEHAMRMPA-----------DLSGGMIKRVAL 172
Cdd:PRK10790 418 AMV-QQDPVVLADTFLANV--------TLGRDISEEQVWQALETVQLA-ELARSLPDglytplgeqgnNLSVGQKQLLAL 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2788666989 173 ARALIMDPPLLLLDEPTAGLDPNGSDDFCALLRELHAEldLTVVMVTHDLDTL 225
Cdd:PRK10790 488 ARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAHRLSTI 538
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
49-235 |
2.42e-08 |
|
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: 52.57 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 49 DIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEvlgqpaaamggegaasrvgmlfqqgalysafnvldnvafplre 128
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDE------------------------------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 129 lgtLPRAlvdaaalvklqMVGLKPEHAmrmpaDLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDFCALLRELH 208
Cdd:cd03222 58 ---WDGI-----------TPVYKPQYI-----DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLS 118
|
170 180
....*....|....*....|....*..
gi 2788666989 209 AELDLTVVMVTHDLDTLFALSSRVAVL 235
Cdd:cd03222 119 EEGKKTALVVEHDLAVLDYLSDRIHVF 145
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
153-249 |
4.03e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 53.59 E-value: 4.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 153 EHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDFCALLRELHAElDLTVVMVTHDLDTLFALSSRV 232
Cdd:NF000106 136 EAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHEL 214
|
90
....*....|....*..
gi 2788666989 233 AVLAEKKVLVTGTPQEV 249
Cdd:NF000106 215 TVIDRGRVIADGKVDEL 231
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
50-193 |
4.91e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.66 E-value: 4.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 50 IYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVE----VLGQPAAAMGGEGAasRVGMLfqqgaLYSAFNVLDN---- 121
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDpelkISYKPQYIKPDYDG--TVEDL-----LRSITDDLGSsyyk 434
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2788666989 122 --VAFPLRelgtLPRALvdaaalvklqmvglkpEHAMRmpaDLSGGMIKRVALARALIMDPPLLLLDEPTAGLD 193
Cdd:PRK13409 435 seIIKPLQ----LERLL----------------DKNVK---DLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
41-245 |
7.04e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 52.19 E-value: 7.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 41 AVHQdLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQGA-LYSAFNVL 119
Cdd:PRK11614 20 ALHE-VSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRrVFSRMTVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 120 DNVA----FPLREL---------GTLPRALvdaaalvklqmvglkpEHAMRMPADLSGGMIKRVALARALIMDPPLLLLD 186
Cdd:PRK11614 99 ENLAmggfFAERDQfqerikwvyELFPRLH----------------ERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2788666989 187 EPTAGLDPNGSDDFCALLRELHAElDLTVVMVTHDLDTLFALSSRVAVLAEKKVLVTGT 245
Cdd:PRK11614 163 EPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVVLEDT 220
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
33-273 |
1.03e-07 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 52.66 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 33 FGEGESQFAVHqDLDLDIYRGEMLSIVGGSGTGKTVLLrqilGLLQ----PGKGTVEVLGQPAAAMGGEGAASRVGMLFQ 108
Cdd:PRK13657 342 FSYDNSRQGVE-DVSFEAKPGQTVAIVGPTGAGKSTLI----NLLQrvfdPQSGRILIDGTDIRTVTRASLRRNIAVVFQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 109 QGALysaFN--VLDN--VAFPLRELGTLPRALVDAAAL--VKLQMVGLKpEHAMRMPADLSGGMIKRVALARALIMDPPL 182
Cdd:PRK13657 417 DAGL---FNrsIEDNirVGRPDATDEEMRAAAERAQAHdfIERKPDGYD-TVVGERGRQLSGGERQRLAIARALLKDPPI 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 183 LLLDEPTAGLDpngsddfCALLRELHAELDL-----TVVMVTHDLDTLfALSSRVAVLAEKKVLVTGTPQEVAVFPHPFV 257
Cdd:PRK13657 493 LILDEATSALD-------VETEAKVKAALDElmkgrTTFIIAHRLSTV-RNADRILVFDNGRVVESGSFDELVARGGRFA 564
|
250 260
....*....|....*....|
gi 2788666989 258 ----AQFFQGERGRRAMAPA 273
Cdd:PRK13657 565 allrAQGMLQEDERRKQPAA 584
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
45-250 |
1.30e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 52.67 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 45 DLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLgqpaaamggegaASRVGMLFQQGALYSAfNVLDNVAF 124
Cdd:PLN03232 635 DINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVI------------RGSVAYVPQVSWIFNA-TVRENILF 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 125 PLR-ELGTLPRAlVDAAALvkLQMVGLKPEHAM----RMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSD- 198
Cdd:PLN03232 702 GSDfESERYWRA-IDVTAL--QHDLDLLPGRDLteigERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHq 778
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2788666989 199 --DFCaLLRELHAEldlTVVMVTHDLDTLfALSSRVAVLAEKKVLVTGTPQEVA 250
Cdd:PLN03232 779 vfDSC-MKDELKGK---TRVLVTNQLHFL-PLMDRIILVSEGMIKEEGTFAELS 827
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
42-249 |
1.40e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 52.64 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 42 VHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQGALYSA---FNv 118
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGslrMN- 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 119 LDNVAFPLRELGTLPRALVDAAALVKLQMVGLKPEHAmRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSD 198
Cdd:TIGR00957 1380 LDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECA-EGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDN 1458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2788666989 199 DFCALLRELHAelDLTVVMVTHDLDTLFALsSRVAVLAEKKVLVTGTPQEV 249
Cdd:TIGR00957 1459 LIQSTIRTQFE--DCTVLTIAHRLNTIMDY-TRVIVLDKGEVAEFGAPSNL 1506
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
162-252 |
1.58e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 52.34 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 162 LSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDFCALLRELHAELDLTVVMVTHdldtlfalssRVAVLAEK-KV 240
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH----------RIASIKRSdKI 1428
|
90
....*....|..
gi 2788666989 241 LVTGTPQEVAVF 252
Cdd:PTZ00265 1429 VVFNNPDRTGSF 1440
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
161-264 |
1.64e-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: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 161 DLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDFCALLRELhAELDLTVVMVTHDLDTLFALSSRVAVLaekkv 240
Cdd:cd03236 139 QLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIREL-AEDDNYVLVVEHDLAVLDYLSDYIHCL----- 212
|
90 100
....*....|....*....|....*....
gi 2788666989 241 lvTGTPQEVAVFPHPF-----VAQFFQGE 264
Cdd:cd03236 213 --YGEPGAYGVVTLPKsvregINEFLDGY 239
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
44-225 |
1.80e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 50.01 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILgllqpgkgtvevlgqpaaamggegAASRVGMLFQQGALYSafnvlDNVA 123
Cdd:cd03238 12 QNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL------------------------YASGKARLISFLPKFS-----RNKL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 124 FPLRELGTLpralvdaaalVKLQMVGLKPEHAMrmpADLSGGMIKRVALARALIMDPP--LLLLDEPTAGLDPNGSDDFC 201
Cdd:cd03238 63 IFIDQLQFL----------IDVGLGYLTLGQKL---STLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLL 129
|
170 180
....*....|....*....|....*.
gi 2788666989 202 ALLRELhaeLDL--TVVMVTHDLDTL 225
Cdd:cd03238 130 EVIKGL---IDLgnTVILIEHNLDVL 152
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
44-193 |
1.88e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 50.33 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEgaasrvgmlFQQGALYSAFNVLDNVA 123
Cdd:PRK13540 18 QQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCT---------YQKQLCFVGHRSGINPY 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2788666989 124 FPLRElGTLPRALVDAAALVKLQMVGL-KPEHAMRMPAD-LSGGMIKRVALARALIMDPPLLLLDEPTAGLD 193
Cdd:PRK13540 89 LTLRE-NCLYDIHFSPGAVGITELCRLfSLEHLIDYPCGlLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
46-221 |
2.01e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.78 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 46 LDLDiyrgEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVevlgqpaaamggeGAASRVGMlfqqgALYSAFNV--LDNVA 123
Cdd:PLN03073 532 IDLD----SRIAMVGPNGIGKSTILKLISGELQPSSGTV-------------FRSAKVRM-----AVFSQHHVdgLDLSS 589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 124 FPLRELGTLPRALVDAAALVKLQMVGLKPEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDdfcAL 203
Cdd:PLN03073 590 NPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVE---AL 666
|
170
....*....|....*...
gi 2788666989 204 LRELhAELDLTVVMVTHD 221
Cdd:PLN03073 667 IQGL-VLFQGGVLMVSHD 683
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
46-249 |
2.98e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 51.48 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 46 LDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQpaaamggegaasrVGMLFQQgALYSAFNVLDNVAF- 124
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAYVPQQ-AWIQNDSLRENILFg 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 125 -PLRElgTLPRALVDAAALV-KLQMV--GLKPEHAMRmPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPN-GSDD 199
Cdd:TIGR00957 723 kALNE--KYYQQVLEACALLpDLEILpsGDRTEIGEK-GVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHvGKHI 799
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2788666989 200 FCALLRELHAELDLTVVMVTHDLDTLfALSSRVAVLAEKKVLVTGTPQEV 249
Cdd:TIGR00957 800 FEHVIGPEGVLKNKTRILVTHGISYL-PQVDVIIVMSGGKISEMGSYQEL 848
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
44-240 |
3.47e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.88 E-value: 3.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLF----QQGALYS----A 115
Cdd:PRK10982 265 RDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHGFALVteerRSTGIYAyldiG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 116 FNVL-DNVAFPLRELGTLPRALVDAAALVKLQMVGLK-PEHAMRMpADLSGGMIKRVALARALIMDPPLLLLDEPTAGLD 193
Cdd:PRK10982 345 FNSLiSNIRNYKNKVGLLDNSRMKSDTQWVIDSMRVKtPGHRTQI-GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGID 423
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2788666989 194 PNGSDDFCALLRELhAELDLTVVMVTHDLDTLFALSSRVAVLAEKKV 240
Cdd:PRK10982 424 VGAKFEIYQLIAEL-AKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
42-246 |
5.51e-07 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 48.95 E-value: 5.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 42 VHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQGALYSafnvldn 121
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQDPTLFS------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 122 vafplrelGTLPRAL--------VDAAALVKLQMVGLkpehamrmpaDLSGGMIKRVALARALIMDPPLLLLDEPTAGLD 193
Cdd:cd03369 96 --------GTIRSNLdpfdeysdEEIYGALRVSEGGL----------NLSQGQRQLLCLARALLKRPRVLVLDEATASID 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2788666989 194 pNGSDdfcALLRE-LHAEL-DLTVVMVTHDLDTLfALSSRVAVLAEKKVLVTGTP 246
Cdd:cd03369 158 -YATD---ALIQKtIREEFtNSTILTIAHRLRTI-IDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
45-221 |
5.61e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 50.32 E-value: 5.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 45 DLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVlGQPAaamggegaasRVGMLFQQ-GALYSAFNVLDNVA 123
Cdd:TIGR03719 340 DLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------KLAYVDQSrDALDPNKTVWEEIS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 124 FPLRELgTLPRALVDAAALVKLqmVGLKPEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNgsddfcaL 203
Cdd:TIGR03719 409 GGLDII-KLGKREIPSRAYVGR--FNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVE-------T 478
|
170 180
....*....|....*....|.
gi 2788666989 204 LRELH-AELDL--TVVMVTHD 221
Cdd:TIGR03719 479 LRALEeALLNFagCAVVISHD 499
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
140-264 |
5.70e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 50.60 E-value: 5.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 140 AALVKLQMVGLKPEHAMrmpADLSGGMIKRVALARAL------IMdpplLLLDEPTAGLDPNGSDDFCALLRELHAELDl 213
Cdd:PRK00635 458 SILIDLGLPYLTPERAL---ATLSGGEQERTALAKHLgaeligIT----YILDEPSIGLHPQDTHKLINVIKKLRDQGN- 529
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2788666989 214 TVVMVTHDlDTLFALSSRV------AVLAEKKVLVTGTPQEVAVFPHPFVAQFFQGE 264
Cdd:PRK00635 530 TVLLVEHD-EQMISLADRIidigpgAGIFGGEVLFNGSPREFLAKSDSLTAKYLRQE 585
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
31-233 |
6.67e-07 |
|
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: 48.12 E-value: 6.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 31 SIFGEGESQFAVHQDLDLDiyRGEMLSIVGGSGTGKTVLLRQIlgllqpgkgtvevlgqpaaamggegaasrvgmlfqqg 110
Cdd:cd03227 1 KIVLGRFPSYFVPNDVTFG--EGSLTIITGPNGSGKSTILDAI------------------------------------- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 111 alysAFNVLDNVAFPLRELGTLPRALVdaaALVKLQMVGLKPEhamrmpadLSGGMIKRVALARAL----IMDPPLLLLD 186
Cdd:cd03227 42 ----GLALGGAQSATRRRSGVKAGCIV---AAVSAELIFTRLQ--------LSGGEKELSALALILalasLKPRPLYILD 106
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2788666989 187 EPTAGLDP-NGSDDFCALLRelHAELDLTVVMVTHDLDtLFALSSRVA 233
Cdd:cd03227 107 EIDRGLDPrDGQALAEAILE--HLVKGAQVIVITHLPE-LAELADKLI 151
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
45-237 |
1.14e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 49.23 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 45 DLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASR---------------VGMLFQQ 109
Cdd:PRK10762 270 DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANgivyisedrkrdglvLGMSVKE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 110 GALYSAFNVLDNVAFPLRelGTLPRALVDAaaLVKL---------QMVGLkpehamrmpadLSGGMIKRVALARALIMDP 180
Cdd:PRK10762 350 NMSLTALRYFSRAGGSLK--HADEQQAVSD--FIRLfniktpsmeQAIGL-----------LSGGNQQKVAIARGLMTRP 414
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2788666989 181 PLLLLDEPTAGLDPNGSDDFCALLRELHAElDLTVVMVTHDLDTLFALSSRVAVLAE 237
Cdd:PRK10762 415 KVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHE 470
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
161-235 |
2.30e-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: 48.63 E-value: 2.30e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2788666989 161 DLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDFCALLRELhAELDLTVVMVTHDLDTLFALSSRVAVL 235
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIREL-AEEGKYVLVVEHDLAILDYLADYVHIL 285
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
162-250 |
2.39e-06 |
|
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: 48.86 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 162 LSGGMIKRVALARAL---IMDPPLLLLDEPTAGLDpngSDDFCALLRELHAELDL--TVVMVTHDLDtlfalssrVAVLA 236
Cdd:TIGR00630 830 LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLH---FDDIKKLLEVLQRLVDKgnTVVVIEHNLD--------VIKTA 898
|
90 100
....*....|....*....|....*..
gi 2788666989 237 E-------------KKVLVTGTPQEVA 250
Cdd:TIGR00630 899 DyiidlgpeggdggGTVVASGTPEEVA 925
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
45-246 |
2.41e-06 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 47.75 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 45 DLDLDIYRGEMLSIVGGSGTGKTVLLRQILGL--LQPGKGTVEVLGQ------PAAamggegaasR----VGMLFQQgal 112
Cdd:COG0396 18 GVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEdilelsPDE---------RaragIFLAFQY--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 113 ysafnvldNVAFP-------LRE-LGTLPRALVDAAALVK-----LQMVGLKPEHAMR-MPADLSGGMIKRVALARALIM 178
Cdd:COG0396 86 --------PVEIPgvsvsnfLRTaLNARRGEELSAREFLKllkekMKELGLDEDFLDRyVNEGFSGGEKKRNEILQMLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2788666989 179 DPPLLLLDEPTAGLDpngSDdfcAL------LRELHAElDLTVVMVTHD---LDTLFAlsSRVAVLAEKKVLVTGTP 246
Cdd:COG0396 158 EPKLAILDETDSGLD---ID---ALrivaegVNKLRSP-DRGILIITHYqriLDYIKP--DFVHVLVDGRIVKSGGK 225
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
152-220 |
2.80e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.32 E-value: 2.80e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2788666989 152 PEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDpngsddfcallreLHAELDL---------TVVMVTH 220
Cdd:PLN03073 335 PEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD-------------LHAVLWLetyllkwpkTFIVVSH 399
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
133-235 |
4.21e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.48 E-value: 4.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 133 PRALVDAAALvkLQMVGLKPEHAMRMpADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDFCALLRELHAElD 212
Cdd:NF040905 114 NETNRRAREL--LAKVGLDESPDTLV-TDIGVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQ-G 189
|
90 100
....*....|....*....|...
gi 2788666989 213 LTVVMVTHDLDTLFALSSRVAVL 235
Cdd:NF040905 190 ITSIIISHKLNEIRRVADSITVL 212
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
162-223 |
5.73e-06 |
|
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: 46.45 E-value: 5.73e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2788666989 162 LSGGMIKRVALARALIMDPP---LLLLDEPTAGLDPngsDDFCALLRELHAELDL--TVVMVTHDLD 223
Cdd:cd03271 170 LSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHF---HDVKKLLEVLQRLVDKgnTVVVIEHNLD 233
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
160-231 |
7.30e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.33 E-value: 7.30e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2788666989 160 ADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDFCALLRELHAELDLTVVMVTHDL------DTLFALSSR 231
Cdd:PTZ00265 578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLstiryaNTIFVLSNR 655
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
49-193 |
9.34e-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: 46.70 E-value: 9.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 49 DIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEV----------LGQPAAAMGGEGAASRVGMLFQQGALYSafnv 118
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEdlkisykpqyISPDYDGTVEEFLRSANTDDFGSSYYKT---- 437
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2788666989 119 ldNVAFPLrelgtlpralvdaaalvklqmvGLKPEHAMRMpADLSGGMIKRVALARALIMDPPLLLLDEPTAGLD 193
Cdd:COG1245 438 --EIIKPL----------------------GLEKLLDKNV-KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
45-248 |
1.16e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 46.65 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 45 DLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLgqpaaamggegaASRVGMLFQQGALYSAfNVLDNVAF 124
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVI------------RGTVAYVPQVSWIFNA-TVRDNILF 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 125 PLR-ELGTLPRAlVDAAALVK-LQMV--GLKPEHAMRmPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPN-GSDD 199
Cdd:PLN03130 702 GSPfDPERYERA-IDVTALQHdLDLLpgGDLTEIGER-GVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHvGRQV 779
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2788666989 200 FCALLRElhaEL-DLTVVMVTHDLDTLFALsSRVAVLAEKKVLVTGTPQE 248
Cdd:PLN03130 780 FDKCIKD---ELrGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEE 825
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
45-235 |
2.10e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 45.69 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 45 DLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVL--GQPAAAMGGEGAASR-VGMLFQQGALYSAFNVLDN 121
Cdd:PRK13549 23 NVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTYEGEIIfeGEELQASNIRDTERAgIAIIHQELALVKELSVLEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 122 VaFPLRELGtlPRALVDAAALVK-----LQMVGLKPEHAMRMpADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNG 196
Cdd:PRK13549 103 I-FLGNEIT--PGGIMDYDAMYLraqklLAQLKLDINPATPV-GNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESE 178
|
170 180 190
....*....|....*....|....*....|....*....
gi 2788666989 197 SDDFCALLRELHAElDLTVVMVTHDLDTLFALSSRVAVL 235
Cdd:PRK13549 179 TAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVI 216
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
53-220 |
2.51e-05 |
|
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: 44.16 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 53 GEMLSIVGGSGTGKTVLL-----RQILGLLqpgKGTVEVLGQPAAAMGGEgaasRVGMLFQQGALYSAFNVldnvafplR 127
Cdd:cd03232 33 GTLTALMGESGAGKTTLLdvlagRKTAGVI---TGEILINGRPLDKNFQR----STGYVEQQDVHSPNLTV--------R 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 128 ElgtlprALVDAAALVklqmvGLKPEHAmrmpadlsggmiKRVALARALIMDPPLLLLDEPTAGLDPNGSDDFCALLREL 207
Cdd:cd03232 98 E------ALRFSALLR-----GLSVEQR------------KRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKL 154
|
170
....*....|...
gi 2788666989 208 hAELDLTVVMVTH 220
Cdd:cd03232 155 -ADSGQAILCTIH 166
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
31-237 |
2.62e-05 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 44.18 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 31 SIFGEGESQFAVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLqPGKGTVEvlgqpaaamggeGAASRVGMLFQQG 110
Cdd:cd03233 11 FTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRT-EGNVSVE------------GDIHYNGIPYKEF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 111 ALY----SAFNVLDNVAFPlrelgTLP-RALVDAAALVKlqmvglkpehAMRMPADLSGGMIKRVALARALIMDPPLLLL 185
Cdd:cd03233 78 AEKypgeIIYVSEEDVHFP-----TLTvRETLDFALRCK----------GNEFVRGISGGERKRVSIAEALVSRASVLCW 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2788666989 186 DEPTAGLDPNGSDDFCALLRELHAELDLTVVM-VTHDLDTLFALSSRVAVLAE 237
Cdd:cd03233 143 DNSTRGLDSSTALEILKCIRTMADVLKTTTFVsLYQASDEIYDLFDKVLVLYE 195
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
161-235 |
3.45e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.80 E-value: 3.45e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2788666989 161 DLSGGMIKRVALARALIMDPPLLLLDEPTAGLDP----NGSDdfcaLLRELhAElDLTVVMVTHDLDTLFALSSRVAVL 235
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIrqrlNVAR----LIREL-AE-GKYVLVVEHDLAVLDYLADNVHIA 284
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
48-240 |
3.75e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 44.61 E-value: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 48 LDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAA-AMGGEGAASRVGMLFQQGALYSAFNVLDNVaFPL 126
Cdd:PRK10762 25 LNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQEAGIGIIHQELNLIPQLTIAENI-FLG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 127 RE----LGTL--PRALVDAAALvkLQMVGLKpEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDF 200
Cdd:PRK10762 104 REfvnrFGRIdwKKMYAEADKL--LARLNLR-FSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2788666989 201 CALLRELHAElDLTVVMVTHDLDTLFALSSRVAVL------AEKKV 240
Cdd:PRK10762 181 FRVIRELKSQ-GRGIVYISHRLKEIFEICDDVTVFrdgqfiAEREV 225
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
26-88 |
6.23e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 44.11 E-value: 6.23e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2788666989 26 IDKLWSIF---GEGESQFAVHqDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLG 88
Cdd:PRK13545 21 FDKLKDLFfrsKDGEYHYALN-NISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG 85
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
42-249 |
8.31e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.81 E-value: 8.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 42 VHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQGALYSA---FNv 118
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGtvrFN- 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 119 LDnvafPLRELG------TLPRALVDAAalVKLQMVGLKPEhAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGL 192
Cdd:PLN03232 1330 ID----PFSEHNdadlweALERAHIKDV--IDRNPFGLDAE-VSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASV 1402
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2788666989 193 DPNGSDDFCALLRELHAEldLTVVMVTHDLDTLFAlSSRVAVLAEKKVLVTGTPQEV 249
Cdd:PLN03232 1403 DVRTDSLIQRTIREEFKS--CTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQEL 1456
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
41-226 |
8.93e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 43.75 E-value: 8.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 41 AVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPgKGTVEVLGqpaaamggegaASRVGMLFQQgaLYSAFNVLD 120
Cdd:TIGR01271 1233 AVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST-EGEIQIDG-----------VSWNSVTLQT--WRKAFGVIP 1298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 121 NVAFPLRelGTL-----PRALVDAAALVKL-QMVGLK------PEHAMRMPAD----LSGGMIKRVALARALIMDPPLLL 184
Cdd:TIGR01271 1299 QKVFIFS--GTFrknldPYEQWSDEEIWKVaEEVGLKsvieqfPDKLDFVLVDggyvLSNGHKQLMCLARSILSKAKILL 1376
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2788666989 185 LDEPTAGLDPNgsdDFCALLREL-HAELDLTVVMVTHDLDTLF 226
Cdd:TIGR01271 1377 LDEPSAHLDPV---TLQIIRKTLkQSFSNCTVILSEHRVEALL 1416
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
162-250 |
9.34e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.86 E-value: 9.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 162 LSGGMIKRVALARALIM---DPPLLLLDEPTAGLDPngsDDFCALLRELHAELDL--TVVMVTHDLDtlfalssrvaVLA 236
Cdd:COG0178 827 LSGGEAQRVKLASELSKrstGKTLYILDEPTTGLHF---HDIRKLLEVLHRLVDKgnTVVVIEHNLD----------VIK 893
|
90 100
....*....|....*....|....*....
gi 2788666989 237 -------------EK--KVLVTGTPQEVA 250
Cdd:COG0178 894 tadwiidlgpeggDGggEIVAEGTPEEVA 922
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
162-225 |
1.02e-04 |
|
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: 42.63 E-value: 1.02e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2788666989 162 LSGGMIKRVALARALIM--DPPLLLLDEPTAGLDPNGSDDFCALLRELHAeLDLTVVMVTHDLDTL 225
Cdd:cd03270 138 LSGGEAQRIRLATQIGSglTGVLYVLDEPSIGLHPRDNDRLIETLKRLRD-LGNTVLVVEHDEDTI 202
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
46-248 |
1.12e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 43.57 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 46 LDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQGALYSA---FNvLDnv 122
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGtvrFN-LD-- 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 123 afPLRELG------TLPRA-LVDAaalVKLQMVGLKPEHAmRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPn 195
Cdd:PLN03130 1335 --PFNEHNdadlweSLERAhLKDV---IRRNSLGLDAEVS-EAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDV- 1407
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2788666989 196 GSDdfcALLRELHAE--LDLTVVMVTHDLDTLFAlSSRVAVLAEKKVLVTGTPQE 248
Cdd:PLN03130 1408 RTD---ALIQKTIREefKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPEN 1458
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
161-194 |
1.21e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.08 E-value: 1.21e-04
10 20 30
....*....|....*....|....*....|....
gi 2788666989 161 DLSGGMIKRVALARALIMDPPLLLLDEPTAGLDP 194
Cdd:PRK10938 401 SLSWGQQRLALIVRALVKHPTLLILDEPLQGLDP 434
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
139-225 |
1.29e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.23 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 139 AAALvkLQMVGLKPEHAMRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLDPngsdDFCALLRELHAELDLTVVMV 218
Cdd:PRK10636 129 AASL--LHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDL----DAVIWLEKWLKSYQGTLILI 202
|
....*..
gi 2788666989 219 THDLDTL 225
Cdd:PRK10636 203 SHDRDFL 209
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
169-221 |
1.34e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.96 E-value: 1.34e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2788666989 169 RVALARALIMDPPLLLLDEPTAGLDPNgsddfcaLLRELHAEL---DLTVVMVTHD 221
Cdd:PRK15064 163 RVLLAQALFSNPDILLLDEPTNNLDIN-------TIRWLEDVLnerNSTMIIISHD 211
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
162-260 |
1.98e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 42.75 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 162 LSGGMIKRVALARALIMDP---PLLLLDEPTAGLDpngSDDFCALLRELHAELDL--TVVMVTHDLDTLfalssrvavla 236
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRStgkTLYILDEPTTGLH---FEDIRKLLEVLHRLVDKgnTVVVIEHNLDVI----------- 896
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2788666989 237 eK-----------------KVLVTGTPQEVAVFPHPFVAQF 260
Cdd:PRK00349 897 -KtadwiidlgpeggdgggEIVATGTPEEVAKVEASYTGRY 936
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
159-222 |
2.38e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 41.99 E-value: 2.38e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2788666989 159 PADLSGGMIKRVALARALIMDPP---LLLLDEPTAGLDPngsddfcALLREL------HAELDLTVVMVTHDL 222
Cdd:pfam13304 234 AFELSDGTKRLLALLAALLSALPkggLLLIDEPESGLHP-------KLLRRLlellkeLSRNGAQLILTTHSP 299
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
44-84 |
2.41e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.19 E-value: 2.41e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTV 84
Cdd:PRK15064 336 KNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
41-240 |
3.66e-04 |
|
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: 41.38 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 41 AVHQDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPgKGTVEVLGqpaaamggegaASRVGMLFQQgaLYSAFNVLD 120
Cdd:cd03289 18 AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDG-----------VSWNSVPLQK--WRKAFGVIP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 121 NVAFPLRelGTLPRAL------VDAAALVKLQMVGLK------PEHAMRMPAD----LSGGMIKRVALARALIMDPPLLL 184
Cdd:cd03289 84 QKVFIFS--GTFRKNLdpygkwSDEEIWKVAEEVGLKsvieqfPGQLDFVLVDggcvLSHGHKQLMCLARSVLSKAKILL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2788666989 185 LDEPTAGLDPNGSDDFCALLRelHAELDLTVVMVTHDLDTLFAlSSRVAVLAEKKV 240
Cdd:cd03289 162 LDEPSAHLDPITYQVIRKTLK--QAFADCTVILSEHRIEAMLE-CQRFLVIEENKV 214
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
145-265 |
3.96e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.92 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 145 LQMVGLKPEHAMRMPADLSGGMIKRVALAR----ALImdPPLLLLDEPTAGLDPNGSDDFCALLRELHaelDL--TVVMV 218
Cdd:TIGR00630 472 LIDVGLDYLSLSRAAGTLSGGEAQRIRLATqigsGLT--GVLYVLDEPSIGLHQRDNRRLINTLKRLR---DLgnTLIVV 546
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2788666989 219 THDLDTLfALSSRVAVLAEK------KVLVTGTPQEVAVFPHPFVAQFFQGER 265
Cdd:TIGR00630 547 EHDEDTI-RAADYVIDIGPGagehggEVVASGTPEEILANPDSLTGQYLSGRK 598
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
44-193 |
1.20e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 40.53 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVevlgqpaaamggeGAASRVGMLFQQGALYSAfNVLDNVA 123
Cdd:PTZ00243 677 RDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------WAERSIAYVPQQAWIMNA-TVRGNIL 742
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2788666989 124 FPLRELgtlPRALVDAAALVKLQM------VGLKPEHAmRMPADLSGGMIKRVALARALIMDPPLLLLDEPTAGLD 193
Cdd:PTZ00243 743 FFDEED---AARLADAVRVSQLEAdlaqlgGGLETEIG-EKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
162-237 |
1.28e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.77 E-value: 1.28e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2788666989 162 LSGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDFCALLRELHAElDLTVVMVTHDLDTLFALSSRVAVLAE 237
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVISSELPELLGMCDRIYVMNE 479
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
53-207 |
1.54e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 40.09 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 53 GEMLSIVGGSGTGKTVLLRQILGLLQPG---KGTVEVLGQPAAAMGGegaaSRVGMLFQQG----------AL-YSAFnv 118
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAERVTTGvitGGDRLVNGRPLDSSFQ----RSIGYVQQQDlhlptstvreSLrFSAY-- 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 119 ldnvafpLRELGTLPRA----LVD-----------AAALVKLQMVGLKPEHAmrmpadlsggmiKRVALARALIMDPPLL 183
Cdd:TIGR00956 863 -------LRQPKSVSKSekmeYVEevikllemesyADAVVGVPGEGLNVEQR------------KRLTIGVELVAKPKLL 923
|
170 180
....*....|....*....|....*
gi 2788666989 184 L-LDEPTAGLDPNGSDDFCALLREL 207
Cdd:TIGR00956 924 LfLDEPTSGLDSQTAWSICKLMRKL 948
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
146-232 |
1.74e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.03 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 146 QMVGLKPEHAMRMPADLSGG------MIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDFCALLRELHAE----LDLTV 215
Cdd:TIGR00606 1184 RVVMLKGDTALDMRGRCSAGqkvlasLIIRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEIIKSrsqqRNFQL 1263
|
90
....*....|....*....
gi 2788666989 216 VMVTHDLD--TLFALSSRV 232
Cdd:TIGR00606 1264 LVITHDEDfvELLGRSEYV 1282
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
45-86 |
2.09e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 39.33 E-value: 2.09e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2788666989 45 DLDLDIYRGEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEV 86
Cdd:PRK11819 342 DLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
53-250 |
2.49e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 39.38 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 53 GEMLSIVGGSGTGKTVLLRQILGLLQPGKGTVEVLGQPAAAMGGEGAASRVGMLFQQGALYSAfNVLDNVAfPLRELGTl 132
Cdd:PTZ00243 1336 REKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDG-TVRQNVD-PFLEASS- 1412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 133 prALVDAAalvkLQMVGLKpEHAmrmpADLSGGMIKRV---------------ALARALI-MDPPLLLLDEPTAGLDPng 196
Cdd:PTZ00243 1413 --AEVWAA----LELVGLR-ERV----ASESEGIDSRVleggsnysvgqrqlmCMARALLkKGSGFILMDEATANIDP-- 1479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2788666989 197 sddfcALLRELHAEL-----DLTVVMVTHDLDTLfALSSRVAVLAEKKVLVTGTPQEVA 250
Cdd:PTZ00243 1480 -----ALDRQIQATVmsafsAYTVITIAHRLHTV-AQYDKIIVMDHGAVAEMGSPRELV 1532
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
162-222 |
3.01e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.04 E-value: 3.01e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2788666989 162 LSGGMIKRVALARALIM---DPPLLLLDEPTAGLDpngSDDFCALLRELHAELDL--TVVMVTHDL 222
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLH---THDIKALIYVLQSLTHQghTVVIIEHNM 872
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
163-252 |
5.92e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 38.17 E-value: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 163 SGGMIKRVALARALIMDPPLLLLDEPTAGLDPNGSDDFCALLRELHAELDLTVVMVTHDL-DTLFALSSRVAVLAEKKVL 241
Cdd:TIGR00956 211 SGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCsQDAYELFDKVIVLYEGYQI 290
|
90
....*....|.
gi 2788666989 242 VTGTPQEVAVF 252
Cdd:TIGR00956 291 YFGPADKAKQY 301
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
44-220 |
7.94e-03 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 37.42 E-value: 7.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 44 QDLDLDIYRGEMLSIVGGSGTGKTVLLRqILGLLQPGKGTVevLGQPaaamggegaasRVGMLF--QQGALYSAFNVLDN 121
Cdd:TIGR00954 469 ESLSFEVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGGR--LTKP-----------AKGKLFyvPQRPYMTLGTLRDQ 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788666989 122 VAFPLRELGTLPRALVDAAALVKLQMVGLkpEH---------AMRMPAD-LSGGMIKRVALARALIMDPPLLLLDEPTAG 191
Cdd:TIGR00954 535 IIYPDSSEDMKRRGLSDKDLEQILDNVQL--THilereggwsAVQDWMDvLSGGEKQRIAMARLFYHKPQFAILDECTSA 612
|
170 180
....*....|....*....|....*....
gi 2788666989 192 LDPNGSDDFCALLRelhaELDLTVVMVTH 220
Cdd:TIGR00954 613 VSVDVEGYMYRLCR----EFGITLFSVSH 637
|
|
| |
