|
Name |
Accession |
Description |
Interval |
E-value |
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-239 |
4.31e-125 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 355.90 E-value: 4.31e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 2 STLKVENLSKQY-GDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGS--------QT 71
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERgEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALrgralrrlRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 72 EIGMIFQQHNLVDGVSAYLNALTGSLNRVSMLKSMLQWQSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARA 151
Cdd:COG3638 81 RIGMIFQQFNLVPRLSVLTNVLAGRLGRTSTWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 152 LVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGRKLFDVGRDELTPELID 231
Cdd:COG3638 161 LVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAELTDAVLR 240
|
....*...
gi 493478014 232 DLYGSVET 239
Cdd:COG3638 241 EIYGGEAE 248
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-234 |
2.35e-111 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 321.05 E-value: 2.35e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGD-VTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQT--------EI 73
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPgEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGkalrqlrrQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 74 GMIFQQHNLVDGVSAYLNALTGSLNRVSMLKSMLQWQSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALV 153
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRLGRRSTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 154 QDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGRKLFDVGRDELTPELIDDL 233
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEVLDEI 240
|
.
gi 493478014 234 Y 234
Cdd:cd03256 241 Y 241
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-235 |
6.05e-98 |
|
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: 286.89 E-value: 6.05e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYG-DVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQ--------TEI 73
Cdd:TIGR02315 2 LEVENLSKVYPnGKQALKNINLNINPgEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRgkklrklrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 74 GMIFQQHNLVDGVSAYLNALTGSLNRVSMLKSMLQWQSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALV 153
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVLHGRLGYKPTWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 154 QDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGRKLFDVGRDELTPELIDDL 233
Cdd:TIGR02315 162 QQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDEVLRHI 241
|
..
gi 493478014 234 YG 235
Cdd:TIGR02315 242 YG 243
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-215 |
2.47e-71 |
|
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: 218.51 E-value: 2.47e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGD----VTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITG-SQTE----- 72
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKgEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKlSEKElaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 73 ---IGMIFQQHNLVDGVSAYLNaltgslnrVSMLKSMLQWQSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIA 149
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALEN--------VELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493478014 150 RALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFgDRFIGLRDGR 215
Cdd:cd03255 153 RALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYA-DRIIELRDGK 217
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-215 |
8.96e-71 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 217.22 E-value: 8.96e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 1 MST-LKVENLSKQYGD----VTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITG-SQTE- 72
Cdd:COG1136 1 MSPlLELRNLTKSYGTgegeVTALRGVSLSIEAgEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlSEREl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 73 -------IGMIFQQHNLVDGVSAYLN-ALTGSLNRVSmlksmlqwqSREDKLRALEALETVGLLDESHQRVSQMSGGQQQ 144
Cdd:COG1136 81 arlrrrhIGFVFQFFNLLPELTALENvALPLLLAGVS---------RKERRERARELLERVGLGDRLDHRPSQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493478014 145 RVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFgDRFIGLRDGR 215
Cdd:COG1136 152 RVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARA-DRVIRLRDGR 221
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-235 |
4.56e-70 |
|
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: 216.45 E-value: 4.56e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITG-SQTE----IGMIF 77
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPgEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlSRRElarrIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 78 QQHNLVDGVSAYLNALTGslnRVSMLkSMLQWQSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDPR 157
Cdd:COG1120 82 QEPPAPFGLTVRELVALG---RYPHL-GLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493478014 158 LLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGRKLFDVGRDE-LTPELIDDLYG 235
Cdd:COG1120 158 LLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEvLTPELLEEVYG 236
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-240 |
2.00e-60 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 191.46 E-value: 2.00e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 1 MSTLKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTEIGMIFQQ 79
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPgEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIGYVPQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 80 HNlVDG---VSAYLNALTGSLNRVSMLKsmlqWQSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDP 156
Cdd:COG1121 84 AE-VDWdfpITVRDVVLMGRYGRRGLFR----RPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 157 RLLLADEPVASLDPSSAETVMGYLRKaAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGRKLFDVGRDELTPELIDDLYGS 236
Cdd:COG1121 159 DLLLLDEPFAGVDAATEEALYELLRE-LRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAHGPPEEVLTPENLSRAYGG 237
|
....
gi 493478014 237 VETV 240
Cdd:COG1121 238 PVAL 241
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-215 |
1.13e-59 |
|
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: 188.50 E-value: 1.13e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITG---SQTEIGMIFQQ 79
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPgEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGvppERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 80 HNLVDGVSAYLNALTGslnrvsmLKSMLqWQSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDPRLL 159
Cdd:cd03259 81 YALFPHLTVAENIAFG-------LKLRG-VPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 493478014 160 LADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGR 215
Cdd:cd03259 153 LLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGR 208
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
2-240 |
4.41e-59 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 188.68 E-value: 4.41e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 2 STLKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGL----------------TDPTEGSISLDde 64
Cdd:PRK09984 3 TIIRVEKLAKTFNQHQALHAVDLNIHHgEMVALLGPSGSGKSTLLRHLSGLitgdksagshiellgrTVQREGRLARD-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 65 pITGSQTEIGMIFQQHNLVDGVSAYLNALTGSLNRVSMLKSMLQWQSREDKLRALEALETVGLLDESHQRVSQMSGGQQQ 144
Cdd:PRK09984 81 -IRKSRANTGYIFQQFNLVNRLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 145 RVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGRKLFDVGRDE 224
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
|
250
....*....|....*.
gi 493478014 225 LTPELIDDLYGSVETV 240
Cdd:PRK09984 240 FDNERFDHLYRSINRV 255
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-234 |
1.58e-58 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 186.42 E-value: 1.58e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTE----IGMIFQ 78
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPgEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEvrrrIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 79 QHNLVDGVSAYLN-ALTGSLNRVSmlksmlqwqSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDPR 157
Cdd:COG1131 81 EPALYPDLTVRENlRFFARLYGLP---------RKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493478014 158 LLLADEPVASLDPSSAETVMGYLRKAAKEhDVTALVSLHQVNIAAHFGDRFIGLRDGRKLFDVGRDELTPELIDDLY 234
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLLEDVF 227
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-215 |
2.67e-57 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 183.27 E-value: 2.67e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQT-------EIGM 75
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKgEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKdinklrrKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 76 IFQQHNLVdgvsAYLNAL---TGSLNRVsmLKsmlqwQSRED-KLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARA 151
Cdd:COG1126 82 VFQQFNLF----PHLTVLenvTLAPIKV--KK-----MSKAEaEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493478014 152 LVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHdVTALVSLHQVNIAAHFGDRFIGLRDGR 215
Cdd:COG1126 151 LAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEG-MTMVVVTHEMGFAREVADRVVFMDGGR 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-207 |
2.87e-57 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 183.75 E-value: 2.87e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 1 MST----LKVENLSKQY----GDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQT 71
Cdd:COG1116 1 MSAaapaLELRGVSKRFptggGGVTALDDVSLTVAAgEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 72 EIGMIFQQHNLVDGVSAYLNALTGsLNRVSMLKsmlqwqsREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARA 151
Cdd:COG1116 81 DRGVVFQEPALLPWLTVLDNVALG-LELRGVPK-------AERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 493478014 152 LVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTAL-VSlHQVNIAAHFGDR 207
Cdd:COG1116 153 LANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLfVT-HDVDEAVFLADR 208
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-215 |
3.58e-57 |
|
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: 181.96 E-value: 3.58e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTEI-------GM 75
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKgEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNInelrqkvGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 76 IFQQHNLVDGVSAyLNALTGSLNRVsmlksmLQWQSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQD 155
Cdd:cd03262 81 VFQQFNLFPHLTV-LENITLAPIKV------KGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 156 PRLLLADEPVASLDPSSAETVMGYLRKAAKEHdVTALVSLHQVNIAAHFGDRFIGLRDGR 215
Cdd:cd03262 154 PKVMLFDEPTSALDPELVGEVLDVMKDLAEEG-MTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-207 |
4.87e-56 |
|
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: 179.27 E-value: 4.87e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 5 KVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTEIGMIFQQHNlV 83
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPgEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGYVPQRRS-I 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 84 D---GVSAYLNALTGSLNRvsmlKSMLQWQSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDPRLLL 160
Cdd:cd03235 80 DrdfPISVRDVVLMGLYGH----KGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 493478014 161 ADEPVASLDPSSAETVMGYLRKaAKEHDVTALVSLHQVNIAAHFGDR 207
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRE-LRREGMTILVVTHDLGLVLEYFDR 201
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-221 |
2.07e-55 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 177.66 E-value: 2.07e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGD----VTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTEIGMIFQ 78
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEgEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 79 QHNLVDGVSAYLNALTG-SLNRVSMlksmlqwqsREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDPR 157
Cdd:cd03293 81 QDALLPWLTVLDNVALGlELQGVPK---------AEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493478014 158 LLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGL--RDGR--KLFDVG 221
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRivAEVEVD 219
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-222 |
1.76e-53 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 172.93 E-value: 1.76e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQY-GDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITG-SQTE-------I 73
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKgEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlKRREipylrrrI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 74 GMIFQQHNLVDGVSAYLN-AL----TGslnrvsmlksmlqWQSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGI 148
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENvALplrvTG-------------KSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493478014 149 ARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEhDVTALVSLHQVNIAAHFGDRFIGLRDGRKLFDVGR 222
Cdd:COG2884 149 ARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRLVRDEAR 221
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-192 |
2.56e-53 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 176.44 E-value: 2.56e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 1 MSTLKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTE---IGMI 76
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPgEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEkrnVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 77 FQQHNL------VDGVsAYlnaltGslnrvsmLKsMLQWQSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIAR 150
Cdd:COG3842 83 FQDYALfphltvAENV-AF-----G-------LR-MRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALAR 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 493478014 151 ALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTAL 192
Cdd:COG3842 149 ALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFI 190
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-246 |
8.86e-53 |
|
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: 171.96 E-value: 8.86e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGS----QTEIGMIFQ 78
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDgEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEpreaRRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 79 QHNLVDGVSAYLNaltgsLNRVSMLKSMlqwQSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDPRL 158
Cdd:COG4555 82 ERGLYDRLTVREN-----IRYFAELYGL---FDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 159 LLADEPVASLDPSSAETVMGYLRkAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGRKLF----DVGRDELTPELIDDLY 234
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILR-ALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAqgslDELREEIGEENLEDAF 232
|
250
....*....|..
gi 493478014 235 gsVETVGLADQE 246
Cdd:COG4555 233 --VALIGSEEGE 242
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-215 |
4.05e-52 |
|
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: 168.00 E-value: 4.05e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 5 KVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITgsqteigmifqqhnlv 83
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAgEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 84 dgvsaylnaltgslnrvsmlksmlQWQSRED-KLRAL--EALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDPRLLL 160
Cdd:cd03214 65 ------------------------SLSPKELaRKIAYvpQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 493478014 161 ADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGR 215
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGR 175
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-215 |
1.08e-51 |
|
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: 166.98 E-value: 1.08e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITG-------SQTEIGM 75
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAgEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDledelppLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 76 IFQQHNLVDGvsaylnaltgslnrvsmlksmlqwqsredklraLEALETVGLLdeshqrvsqMSGGQQQRVGIARALVQD 155
Cdd:cd03229 81 VFQDFALFPH---------------------------------LTVLENIALG---------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 156 PRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGR 215
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-231 |
2.66e-51 |
|
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: 175.09 E-value: 2.66e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQY-----GDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGS-------- 69
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRgETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLsrrslrel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 70 QTEIGMIFQQHNlvdgvsaylnaltGSLN-RVSMLKSM------LQWQSRED-KLRALEALETVGLLDESHQR-VSQMSG 140
Cdd:COG1123 341 RRRVQMVFQDPY-------------SSLNpRMTVGDIIaeplrlHGLLSRAErRERVAELLERVGLPPDLADRyPHELSG 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 141 GQQQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGR----- 215
Cdd:COG1123 408 GQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRivedg 487
|
250
....*....|....*....
gi 493478014 216 ---KLFDVGRDELTPELID 231
Cdd:COG1123 488 pteEVFANPQHPYTRALLA 506
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-197 |
7.56e-51 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 169.87 E-value: 7.56e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQY----GDVTALEDVSFQIED-E-FAVLlGESGAGKSTLLRCINGLTDPTEGSISLDDEPITG-SQTE---- 72
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKgEiFGII-GYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlSERElraa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 73 ---IGMIFQQHNLVDGVSAYLN-ALTGSLNRVSmlksmlqwqSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGI 148
Cdd:COG1135 81 rrkIGMIFQHFNLLSSRTVAENvALPLEIAGVP---------KAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 493478014 149 ARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQ 197
Cdd:COG1135 152 ARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHE 200
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-219 |
1.57e-49 |
|
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: 163.38 E-value: 1.57e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITG------SQTEIGMI 76
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPgEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGlppheiARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 77 FQQHNLVDGVSAYLNALTGSLNRVSMLKSMLQWQSREDKLR--ALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQ 154
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQARTGSGLLLARARREEREARerAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493478014 155 DPRLLLADEPVASLDPSSAETVMGYLRKaAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGRKLFD 219
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRE-LRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAE 224
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-215 |
1.76e-49 |
|
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: 163.14 E-value: 1.76e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGD----VTALEDVSFQIE--DEFAVLlGESGAGKSTLLRCINGLTDPTEGSISLDDEPITG--------S 69
Cdd:cd03258 2 IELKNVSKVFGDtggkVTALKDVSLSVPkgEIFGII-GRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlsgkelrkA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 70 QTEIGMIFQQHNLVDGVSAYLN-ALTGSLNRVSMlksmlqwqsREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGI 148
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENvALPLEIAGVPK---------AEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493478014 149 ARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGR 215
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGE 218
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-215 |
2.74e-49 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 166.02 E-value: 2.74e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 1 MSTLKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTE---IGMI 76
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDgEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKdrnIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 77 FQQHNLVDGVSAYLN---ALtgSLNRVSmlksmlqwqSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALV 153
Cdd:COG3839 81 FQSYALYPHMTVYENiafPL--KLRKVP---------KAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493478014 154 QDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLH-QVNiAAHFGDRFIGLRDGR 215
Cdd:COG3839 150 REPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHdQVE-AMTLADRIAVMNDGR 211
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-225 |
3.38e-49 |
|
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: 162.46 E-value: 3.38e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTE--------IG 74
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRgEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyelrrrIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 75 MIFQQhnlvdgvsaylNALTGSLN---------RvsMLKSMLQWQSREdklRALEALETVGLLDESHQRVSQMSGGQQQR 145
Cdd:COG1127 86 MLFQG-----------GALFDSLTvfenvafplR--EHTDLSEAEIRE---LVLEKLELVGLPGAADKMPSELSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 146 VGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGRKLFDVGRDEL 225
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL 229
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-215 |
1.11e-48 |
|
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: 160.75 E-value: 1.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQY----GDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQ-------- 70
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKgETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlrkirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 71 TEIGMIFQqhnlvdgvsaylNALTgSLNRV---------SMLKSMLQWQSREDKLRALEALETVGLLDE-SHQRVSQMSG 140
Cdd:cd03257 82 KEIQMVFQ------------DPMS-SLNPRmtigeqiaePLRIHGKLSKKEARKEAVLLLLVGVGLPEEvLNRYPHELSG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493478014 141 GQQQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGR 215
Cdd:cd03257 149 GQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGK 223
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-231 |
2.00e-48 |
|
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: 160.74 E-value: 2.00e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYG----DVTALEDVSFQIED--EFAvLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQ-----TE 72
Cdd:COG1124 2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPgeSFG-LVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRrkafrRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 73 IGMIFQQhnlvdgvsAYlnaltGSLN-RVSMLKSM---LQWQSREDKL-RALEALETVGLlDES--HQRVSQMSGGQQQR 145
Cdd:COG1124 81 VQMVFQD--------PY-----ASLHpRHTVDRILaepLRIHGLPDREeRIAELLEQVGL-PPSflDRYPHQLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 146 VGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTAL-VSlHQVNIAAHFGDRFIGLRDGR--------K 216
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLfVS-HDLAVVAHLCDRVAVMQNGRiveeltvaD 225
|
250
....*....|....*
gi 493478014 217 LFDVGRDELTPELID 231
Cdd:COG1124 226 LLAGPKHPYTRELLA 240
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-215 |
1.89e-47 |
|
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: 157.73 E-value: 1.89e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTD-----PTEGSISLDDEPITGSQ------- 70
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIpKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDvdvlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 71 TEIGMIFQQHNLVDGvSAYLNALTGslnrvsmLKSMLQWQSREDKLRALEALETVGLLDESHQR--VSQMSGGQQQRVGI 148
Cdd:cd03260 81 RRVGMVFQKPNPFPG-SIYDNVAYG-------LRLHGIKLKEELDERVEEALRKAALWDEVKDRlhALGLSGGQQQRLCL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493478014 149 ARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHdvTALVSLHQVNIAAHFGDRFIGLRDGR 215
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGR 217
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-219 |
2.27e-47 |
|
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: 158.28 E-value: 2.27e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 1 MSTLKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTE------I 73
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERgEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHriarlgI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 74 GMIFQQHNLVDGVSAYLNALTGSLNRV--SMLKSMLQW-----QSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRV 146
Cdd:COG0411 82 ARTFQNPRLFPELTVLENVLVAAHARLgrGLLAALLRLprarrEEREARERAEELLERVGLADRADEPAGNLSYGQQRRL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493478014 147 GIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGRKLFD 219
Cdd:COG0411 162 EIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAE 234
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-219 |
5.38e-47 |
|
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: 156.72 E-value: 5.38e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQY-GDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQ-----TEIGMI 76
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKgEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNlrelrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 77 FQQ--HNLV-----DGVsAYlnaltGSLNrvsmlksmlQWQSRED-KLRALEALETVGLLDESHQRVSQMSGGQQQRVGI 148
Cdd:COG1122 81 FQNpdDQLFaptveEDV-AF-----GPEN---------LGLPREEiRERVEEALELVGLEHLADRPPHELSGGQKQRVAI 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493478014 149 ARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHdVTALVSLHQVNIAAHFGDRFIGLRDGRKLFD 219
Cdd:COG1122 146 AGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEG-KTVIIVTHDLDLVAELADRVIVLDDGRIVAD 215
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-225 |
1.31e-46 |
|
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: 155.74 E-value: 1.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 6 VENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITG-SQTE-------IGMI 76
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRgEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlSEAElyrlrrrMGML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 77 FQQHNLVDGVSAYLN-ALtgslnrvsMLKSMLQWQSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQD 155
Cdd:cd03261 83 FQSGALFDSLTVFENvAF--------PLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 156 PRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGRKLFDVGRDEL 225
Cdd:cd03261 155 PELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-169 |
2.84e-46 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 155.79 E-value: 2.84e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 1 MSTLKVENLSKQYG----DVTALEDVSFQIE-DEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTEIGM 75
Cdd:COG4525 1 MSMLTVRHVSVRYPgggqPQPALQDVSLTIEsGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 76 IFQQHNLVDGVSAYLNALTGslnrvsmLKsmLQWQSREDKL-RALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQ 154
Cdd:COG4525 81 VFQKDALLPWLNVLDNVAFG-------LR--LRGVPKAERRaRAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAA 151
|
170
....*....|....*
gi 493478014 155 DPRLLLADEPVASLD 169
Cdd:COG4525 152 DPRFLLMDEPFGALD 166
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-215 |
9.58e-46 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 152.66 E-value: 9.58e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQ-----TEIGMIF 77
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAgECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPppewrRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 78 QQHNLVDG-VSAYLNaltgslnrvsmlksmLQWQSREDKL---RALEALETVGLlDES--HQRVSQMSGGQQQRVGIARA 151
Cdd:COG4619 81 QEPALWGGtVRDNLP---------------FPFQLRERKFdreRALELLERLGL-PPDilDKPVERLSGGERQRLALIRA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493478014 152 LVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGR 215
Cdd:COG4619 145 LLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-215 |
9.03e-45 |
|
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: 150.48 E-value: 9.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITG---SQTEIGMIFQQ 79
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADgEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDlppKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 80 HNLVDGVSAYLN-ALTGSLNRVSmlksmlqwqSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDPRL 158
Cdd:cd03301 81 YALYPHMTVYDNiAFGLKLRKVP---------KDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 493478014 159 LLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGR 215
Cdd:cd03301 152 FLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQ 208
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
8-225 |
2.50e-44 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 150.24 E-value: 2.50e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 8 NLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQT-------EIGMIFQQ 79
Cdd:PRK09493 6 NVSKHFGPTQVLHNIDLNIDQgEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVderlirqEAGMVFQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 80 HNLVDGVSAYLNALTGSLnRVsmlksmlQWQSRED-KLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDPRL 158
Cdd:PRK09493 86 FYLFPHLTALENVMFGPL-RV-------RGASKEEaEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493478014 159 LLADEPVASLDPSSAETVMGYLRKAAKEhDVTALVSLHQVNIAAHFGDRFIGLRDGRKLFDVGRDEL 225
Cdd:PRK09493 158 MLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVL 223
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
7-215 |
6.83e-44 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 148.17 E-value: 6.83e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 7 ENLSKQY-GDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPIT---GSQT-----EIGMI 76
Cdd:TIGR02673 5 HNVSKAYpGGVAALHDVSLHIRKgEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNrlrGRQLpllrrRIGVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 77 FQQHNLVDGVSAYLNaltgslnrVSMLKSMLQWQSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDP 156
Cdd:TIGR02673 85 FQDFRLLPDRTVYEN--------VALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 493478014 157 RLLLADEPVASLDPSSAETVMGYLRKAAKeHDVTALVSLHQVNIAAHFGDRFIGLRDGR 215
Cdd:TIGR02673 157 PLLLADEPTGNLDPDLSERILDLLKRLNK-RGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-169 |
8.94e-44 |
|
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: 148.54 E-value: 8.94e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITG---SQTEIGMIFQQ 79
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEgEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlppHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 80 HNLVDGVSAYLNALTGslnrvsmLKsMLQWQSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDPRLL 159
Cdd:cd03300 81 YALFPHLTVFENIAFG-------LR-LKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVL 152
|
170
....*....|
gi 493478014 160 LADEPVASLD 169
Cdd:cd03300 153 LLDEPLGALD 162
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-215 |
9.71e-44 |
|
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: 147.61 E-value: 9.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 5 KVENLSKQYGDVT--ALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQT-----EIGMI 76
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKgEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLkelrrKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 77 FQ--QHNLVdGVSAYLNALTGSLNrvsmlksmLQWQSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQ 154
Cdd:cd03225 81 FQnpDDQFF-GPTVEEEVAFGLEN--------LGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493478014 155 DPRLLLADEPVASLDPSSAETVMGYLRKAAKEHdVTALVSLHQVNIAAHFGDRFIGLRDGR 215
Cdd:cd03225 152 DPDILLLDEPTAGLDPAGRRELLELLKKLKAEG-KTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
7-230 |
1.23e-43 |
|
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: 149.33 E-value: 1.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 7 ENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGS---------QTEIGMI 76
Cdd:cd03294 28 EEILKKTGQTVGVNDVSLDVREgEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMsrkelrelrRKKISMV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 77 FQQHNLVDGVSAYLNALTGslnrvsmLKsmLQWQSREDKL-RALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQD 155
Cdd:cd03294 108 FQSFALLPHRTVLENVAFG-------LE--VQGVPRAEREeRAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVD 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493478014 156 PRLLLADEPVASLDPS-SAETVMGYLRKAAKEHDVTALVSlHQVNIAAHFGDRFIGLRDGRkLFDVGrdelTPELI 230
Cdd:cd03294 179 PDILLMDEAFSALDPLiRREMQDELLRLQAELQKTIVFIT-HDLDEALRLGDRIAIMKDGR-LVQVG----TPEEI 248
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-225 |
1.83e-43 |
|
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: 154.29 E-value: 1.83e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 1 MST-LKVENLSKQY--GDVTALEDVSFQIE-DEFAVLLGESGAGKSTLLRCINGLTDPT---EGSISLDDEPITGS---- 69
Cdd:COG1123 1 MTPlLEVRDLSVRYpgGDVPAVDGVSLTIApGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELseal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 70 -QTEIGMIFQQhnlvdgVSAYLNALTGSLNRVSMLksMLQWQSRED-KLRALEALETVGLLDESHQRVSQMSGGQQQRVG 147
Cdd:COG1123 81 rGRRIGMVFQD------PMTQLNPVTVGDQIAEAL--ENLGLSRAEaRARVLELLEAVGLERRLDRYPHQLSGGQRQRVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493478014 148 IARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGRKLFDVGRDEL 225
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-225 |
2.82e-43 |
|
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: 146.81 E-value: 2.82e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTE------IGMI 76
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEgEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHeraragIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 77 FQQHNLVDGVSAYLNALTGSLNRvsmlksmlqwqSREDKLRALE-ALETVGLLDE-SHQRVSQMSGGQQQRVGIARALVQ 154
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYAR-----------RRAKRKARLErVYELFPRLKErRKQLAGTLSGGEQQMLAIARALMS 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493478014 155 DPRLLLADEPVASLDPSSAETVMGYLRKAAKEhDVTALVSLHQVNIAAHFGDRFIGLRDGRKLFDVGRDEL 225
Cdd:cd03224 150 RPKLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-215 |
7.88e-43 |
|
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: 143.54 E-value: 7.88e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 5 KVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITgsqteigmifqqhnlv 83
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAgEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 84 dgvsaylnaltgslnrvsmlksmlqwqsredKLRALEALETVGLldeshqrVSQMSGGQQQRVGIARALVQDPRLLLADE 163
Cdd:cd00267 65 -------------------------------KLPLEELRRRIGY-------VPQLSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 493478014 164 PVASLDPSSAETVMGYLRKAAKEHdVTALVSLHQVNIAAHFGDRFIGLRDGR 215
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAEEG-RTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-215 |
1.02e-42 |
|
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: 143.69 E-value: 1.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTE----IGMIFQ 78
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKgEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEvkrrIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 79 QHNLvdgvsaYlnaltgslnrvsmlksmlqwqsreDKLRALEALEtvglldeshqrvsqMSGGQQQRVGIARALVQDPRL 158
Cdd:cd03230 81 EPSL------Y------------------------ENLTVRENLK--------------LSGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 493478014 159 LLADEPVASLDPSSAETVMGYLRKAAKEhDVTALVSLHQVNIAAHFGDRFIGLRDGR 215
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-166 |
1.15e-42 |
|
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: 142.79 E-value: 1.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 19 LEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITG-----SQTEIGMIFQQHNLVDGVSAYLNA 92
Cdd:pfam00005 1 LKNVSLTLnPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDderksLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493478014 93 LTGSLnrvsmlksMLQWQSREDKLRALEALETVGLLDESHQRV----SQMSGGQQQRVGIARALVQDPRLLLADEPVA 166
Cdd:pfam00005 81 RLGLL--------LKGLSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-215 |
1.98e-42 |
|
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: 144.88 E-value: 1.98e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGD----VTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTE------ 72
Cdd:COG4181 9 IELRGLTKTVGTgageLTILKGISLEVEAgESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDararlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 73 ---IGMIFQQHNLVDGVSAylnaltgsLNRVSM---LKSMlqwqsREDKLRALEALETVGLLDESHQRVSQMSGGQQQRV 146
Cdd:COG4181 89 arhVGFVFQSFQLLPTLTA--------LENVMLpleLAGR-----RDARARARALLERVGLGHRLDHYPAQLSGGEQQRV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493478014 147 GIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHfGDRFIGLRDGR 215
Cdd:COG4181 156 ALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGR 223
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-207 |
3.27e-42 |
|
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: 146.74 E-value: 3.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQY----GDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDP---TEGSISLDDEPITG-SQTE-- 72
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRgETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKlSEKElr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 73 ------IGMIFQqhnlvdgvsaylNALTgSLN---RVS-----MLKSMLQWQSREDKLRALEALETVGLlDESHQRVS-- 136
Cdd:COG0444 82 kirgreIQMIFQ------------DPMT-SLNpvmTVGdqiaePLRIHGGLSKAEARERAIELLERVGL-PDPERRLDry 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493478014 137 --QMSGGQQQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTAL-VSlHQVNIAAHFGDR 207
Cdd:COG0444 148 phELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILfIT-HDLGVVAEIADR 220
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-235 |
3.50e-42 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 144.91 E-value: 3.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 3 TLKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTE-----IGMI 76
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPgEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAelarrRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 77 FQQHNL-----VDGVsaylnaltgslnrVSMlkSMLQWQSREDKLRAL--EALETVGLLDESHQRVSQMSGGQQQRVGIA 149
Cdd:PRK13548 82 PQHSSLsfpftVEEV-------------VAM--GRAPHGLSRAEDDALvaAALAQVDLAHLAGRDYPQLSGGEQQRVQLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 150 RALVQ------DPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGRKLFDvG-- 221
Cdd:PRK13548 147 RVLAQlwepdgPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVAD-Gtp 225
|
250
....*....|....
gi 493478014 222 RDELTPELIDDLYG 235
Cdd:PRK13548 226 AEVLTPETLRRVYG 239
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-219 |
3.55e-42 |
|
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: 143.49 E-value: 3.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQIEDEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTE----IGMIFQQ 79
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKlrrrIGYLPQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 80 HNLVDGVSAYlnaltGSLNRVSMLKSMlqwQSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDPRLL 159
Cdd:cd03264 81 FGVYPNFTVR-----EFLDYIAWLKGI---PSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSIL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 160 LADEPVASLDPSSAETVMGYLRKAAKEHDVtaLVSLHQVNIAAHFGDRFIGLRDGRKLFD 219
Cdd:cd03264 153 IVDEPTAGLDPEERIRFRNLLSELGEDRIV--ILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-224 |
5.64e-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: 144.02 E-value: 5.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTaLEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTE---IGMIFQQ 79
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERgDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEkrdISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 80 HNLVDGVSAYLNALTGSLNRVSMLKsmlqwqsrEDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDPRLL 159
Cdd:cd03299 80 YALFPHMTVYKNIAYGLKKRKVDKK--------EIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKIL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493478014 160 LADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGrKLFDVGRDE 224
Cdd:cd03299 152 LLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNG-KLIQVGKPE 215
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-235 |
2.15e-41 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 142.95 E-value: 2.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTE-----IGMIF 77
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPgELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWelarrRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 78 QQHNL-----VDGVsaylnaltgslnrVSMLKSMLQWQSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARAL 152
Cdd:COG4559 82 QHSSLafpftVEEV-------------VALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 153 VQ-------DPRLLLADEPVASLDPSSAETVMGYLRKAAKEhDVTALVSLHQVNIAAHFGDRFIGLRDGRkLFDVGRDE- 224
Cdd:COG4559 149 AQlwepvdgGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGR-LVAQGTPEe 226
|
250
....*....|..
gi 493478014 225 -LTPELIDDLYG 235
Cdd:COG4559 227 vLTDELLERVYG 238
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
4-215 |
7.99e-41 |
|
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: 144.02 E-value: 7.99e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITG---SQTEIGMIFQQ 79
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVkKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRlppQKRDYGIVFQS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 80 HNLVDGVSAYLNALTGSLNRvSMLKSmlqwqsrEDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDPRLL 159
Cdd:TIGR03265 85 YALFPNLTVADNIAYGLKNR-GMGRA-------EVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 493478014 160 LADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGR 215
Cdd:TIGR03265 157 LLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGV 212
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-235 |
1.33e-40 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 140.28 E-value: 1.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTAleDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITG---SQTEIGMIFQQ 79
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAgERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTAlppAERPVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 80 HNLVDGVSAYLN---ALTGSLNRvsmlksmlqwqSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDP 156
Cdd:COG3840 80 NNLFPHLTVAQNiglGLRPGLKL-----------TAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 157 RLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGRKLFDVGRDELT----PELIDD 232
Cdd:COG3840 149 PILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLdgepPPALAA 228
|
...
gi 493478014 233 LYG 235
Cdd:COG3840 229 YLG 231
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-197 |
1.36e-40 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 143.02 E-value: 1.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 5 KVENLSKQY----GDVTALEDVSFQIE--DEFAVLlGESGAGKSTLLRCINGLTDPTEGSISLDDEPITG-SQTE----- 72
Cdd:PRK11153 3 ELKNISKVFpqggRTIHALNNVSLHIPagEIFGVI-GASGAGKSTLIRCINLLERPTSGRVLVDGQDLTAlSEKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 73 --IGMIFQQHNLVDGVSAYLN-ALTGSLNRVSmlksmlqwqSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIA 149
Cdd:PRK11153 82 rqIGMIFQHFNLLSSRTVFDNvALPLELAGTP---------KAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 493478014 150 RALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQ 197
Cdd:PRK11153 153 RALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHE 200
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
3-215 |
1.86e-40 |
|
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: 139.38 E-value: 1.86e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 3 TLKVENLSKQYGDVTA----LEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITG-SQTE---- 72
Cdd:TIGR02982 1 VISIRNLNHYYGHGSLrkqvLFDINLEINPgEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGaSKKQlvql 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 73 ---IGMIFQQHNLvdgvsayLNALTGSLNrVSMLKSMLQWQSRED-KLRALEALETVGLLDESHQRVSQMSGGQQQRVGI 148
Cdd:TIGR02982 81 rrrIGYIFQAHNL-------LGFLTARQN-VQMALELQPNLSYQEaRERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 149 ARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQ---VNIAahfgDRFIGLRDGR 215
Cdd:TIGR02982 153 ARALVHHPKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDnriLDVA----DRILQMEDGK 218
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-230 |
2.39e-40 |
|
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: 139.74 E-value: 2.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVT-ALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGS-----QTEIGMI 76
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKgEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQdpvelRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 77 FQQHNLvdgvsayLNALTGSLNrVSMLKSMLQWQSREDKLRALEALETVGLLDESH-QRV-SQMSGGQQQRVGIARALVQ 154
Cdd:cd03295 81 IQQIGL-------FPHMTVEEN-IALVPKLLKWPKEKIRERADELLALVGLDPAEFaDRYpHELSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493478014 155 DPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRfIGLRDGRKLFDVGrdelTPELI 230
Cdd:cd03295 153 DPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADR-IAIMKNGEIVQVG----TPDEI 223
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
7-215 |
4.79e-40 |
|
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: 138.31 E-value: 4.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 7 ENLSKQY-GDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPIT---GSQT-----EIGMI 76
Cdd:cd03292 4 INVTKTYpNGTAALDGINISISAgEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSdlrGRAIpylrrKIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 77 FQQHNLVDGVSAYLNaltgslnrVSMLKSMLQWQSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDP 156
Cdd:cd03292 84 FQDFRLLPDRNVYEN--------VAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 493478014 157 RLLLADEPVASLDPSSAETVMGYLRKAAKEhDVTALVSLHQVNIAAHFGDRFIGLRDGR 215
Cdd:cd03292 156 TILIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGK 213
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
7-170 |
2.28e-39 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 139.07 E-value: 2.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 7 ENLSKQYGDVT-ALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTE-----IGMIFQQ 79
Cdd:COG1125 5 ENVTKRYPDGTvAVDDLSLTIPAgEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVelrrrIGYVIQQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 80 HNLvdgvsayLNALTGSLNrVSMLKSMLQWQSREDKLRALEALETVGLLDES--HQRVSQMSGGQQQRVGIARALVQDPR 157
Cdd:COG1125 85 IGL-------FPHMTVAEN-IATVPRLLGWDKERIRARVDELLELVGLDPEEyrDRYPHELSGGQQQRVGVARALAADPP 156
|
170
....*....|...
gi 493478014 158 LLLADEPVASLDP 170
Cdd:COG1125 157 ILLMDEPFGALDP 169
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-197 |
3.81e-39 |
|
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: 135.68 E-value: 3.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTEIgmiFQQHNL 82
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAgEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY---RRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 83 VDGVSAYLNALTGSLNrVSMLKSMlqWQSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDPRLLLAD 162
Cdd:COG4133 80 LGHADGLKPELTVREN-LRFWAAL--YGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLD 156
|
170 180 190
....*....|....*....|....*....|....*
gi 493478014 163 EPVASLDPSSAETVMGYLRkAAKEHDVTALVSLHQ 197
Cdd:COG4133 157 EPFTALDAAGVALLAELIA-AHLARGGAVLLTTHQ 190
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
3-215 |
4.70e-39 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 136.85 E-value: 4.70e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 3 TLKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPI------TGSQ----- 70
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKgDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkpdrDGELvpadr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 71 -------TEIGMIFQQHNLVDGVSAYLNALTGSlnrVSMLKsmlqwQSRED-KLRALEALETVGLLDESHQRVSQMSGGQ 142
Cdd:COG4598 88 rqlqrirTRLGMVFQSFNLWSHMTVLENVIEAP---VHVLG-----RPKAEaIERAEALLAKVGLADKRDAYPAHLSGGQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493478014 143 QQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDvTALVSLHQVNIAAHFGDRFIGLRDGR 215
Cdd:COG4598 160 QQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGR-TMLVVTHEMGFARDVSSHVVFLHQGR 231
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-186 |
1.16e-38 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 134.28 E-value: 1.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 6 VENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDE---PITGSQT------EIGM 75
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKgKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQetpPLNSKKAskfrreKLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 76 IFQQHNLVDGVSAYLN---ALTGS-LNRVSMLKSMLqwqsredklralEALETVGLLDESHQRVSQMSGGQQQRVGIARA 151
Cdd:TIGR03608 81 LFQNFALIENETVEENldlGLKYKkLSKKEKREKKK------------EALEKVGLNLKLKQKIYELSGGEQQRVALARA 148
|
170 180 190
....*....|....*....|....*....|....*
gi 493478014 152 LVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKE 186
Cdd:TIGR03608 149 ILKPPPLILADEPTGSLDPKNRDEVLDLLLELNDE 183
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-170 |
1.60e-38 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 138.70 E-value: 1.60e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 1 MSTLKVENLSKQYGD------------------------VTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPT 55
Cdd:COG4175 1 MPKIEVRNLYKIFGKrperalklldqgkskdeilektgqTVGVNDASFDVEEgEIFVIMGLSGSGKSTLVRCLNRLIEPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 56 EGSISLDDEPITGS---------QTEIGMIFQQHNL------VDGVsAYlnaltGslnrvsmLKsmLQWQSREDKL-RAL 119
Cdd:COG4175 81 AGEVLIDGEDITKLskkelrelrRKKMSMVFQHFALlphrtvLENV-AF-----G-------LE--IQGVPKAERReRAR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 493478014 120 EALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDPRLLLADEPVASLDP 170
Cdd:COG4175 146 EALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDP 196
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-225 |
3.87e-38 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 135.62 E-value: 3.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 3 TLKVENLSKQYGDVTALEDVSFQIEDE--FAvLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTE-IG----- 74
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGeiFG-LLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRrIGylpee 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 75 ------M-IFQQhnLVdgvsaYLNALTGsLNRvsmlksmlqwqsREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVG 147
Cdd:COG4152 80 rglypkMkVGEQ--LV-----YLARLKG-LSK------------AEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493478014 148 IARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEhDVTALVSLHQVNIAAHFGDRFIGLRDGRKLFDVGRDEL 225
Cdd:COG4152 140 LIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-215 |
6.37e-38 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 136.43 E-value: 6.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 1 MStLKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQT----EIGM 75
Cdd:COG1118 1 MS-IEVRNISKRFGSFTLLDDVSLEIASgELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPprerRVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 76 IFQQHNL------VDGVSAYLNALTGSlnrvsmlksmlqwqSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIA 149
Cdd:COG1118 80 VFQHYALfphmtvAENIAFGLRVRPPS--------------KAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493478014 150 RALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGR 215
Cdd:COG1118 146 RALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGR 211
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-235 |
7.36e-38 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 133.67 E-value: 7.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQIE-DEFAVLLGESGAGKSTLLRCINGLTDPTEG-SISLDDEPITGS-----QTEIGMI 76
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKpGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEdvwelRKRIGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 77 --FQQHNLVDGVSAY---LNALTGSLNRvsmlksmlqWQ--SREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIA 149
Cdd:COG1119 84 spALQLRFPRDETVLdvvLSGFFDSIGL---------YRepTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 150 RALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTA-LVSlHQVN-IAAHFgDRFIGLRDGRKLFDVGRDE-LT 226
Cdd:COG1119 155 RALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLvLVT-HHVEeIPPGI-THVLLLKDGRVVAAGPKEEvLT 232
|
....*....
gi 493478014 227 PELIDDLYG 235
Cdd:COG1119 233 SENLSEAFG 241
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
3-215 |
2.09e-37 |
|
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: 132.08 E-value: 2.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 3 TLKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITG---SQTEIGMIFQ 78
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSgELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDvpvQERNVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 79 QHNLVDGVSAYLNALTGslnrVSMLKSMLQWQSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDPRL 158
Cdd:cd03296 82 HYALFRHMTVFDNVAFG----LRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 493478014 159 LLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGR 215
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGR 214
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-230 |
2.79e-37 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 137.46 E-value: 2.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTE------IGMI 76
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPgEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRdaqaagIAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 77 FQQHNLVDGVSAYLNALtgsLNRVSMLKSMLQWqsREDKLRALEALETVGL-LDeSHQRVSQMSGGQQQRVGIARALVQD 155
Cdd:COG1129 85 HQELNLVPNLSVAENIF---LGREPRRGGLIDW--RAMRRRARELLARLGLdID-PDTPVGDLSVAQQQLVEIARALSRD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493478014 156 PRLLLADEPVASLDPSSAETVMGYLRKaAKEHDVTAL-VS--LHQV-NIAahfgDRFIGLRDGRKLFDVGRDELTPELI 230
Cdd:COG1129 159 ARVLILDEPTASLTEREVERLFRIIRR-LKAQGVAIIyIShrLDEVfEIA----DRVTVLRDGRLVGTGPVAELTEDEL 232
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
21-219 |
3.62e-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: 130.88 E-value: 3.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 21 DVSFQIEDEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGS---------QTEIGMIFQQHNLVDGVSAYLN 91
Cdd:cd03297 16 KIDFDLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSrkkinlppqQRKIGLVFQQYALFPHLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 92 ALTGslnrvsmlksMLQWQSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDPRLLLADEPVASLDPS 171
Cdd:cd03297 96 LAFG----------LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 493478014 172 SAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGRKLFD 219
Cdd:cd03297 166 LRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYI 213
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-215 |
3.98e-37 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 131.29 E-value: 3.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 1 MStLKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQT-------- 71
Cdd:COG4161 1 MS-IQLKNINCFYGSHQALFDINLECPSgETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKpsekairl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 72 ---EIGMIFQQHNLVDGVSAYLNALTGSLNRVSMLKSmlqwQSREdklRALEALETVGLLDESHQRVSQMSGGQQQRVGI 148
Cdd:COG4161 80 lrqKVGMVFQQYNLWPHLTVMENLIEAPCKVLGLSKE----QARE---KAMKLLARLRLTDKADRFPLHLSGGQQQRVAI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493478014 149 ARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAkEHDVTALVSLHQVNIAAHFGDRFIGLRDGR 215
Cdd:COG4161 153 ARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGR 218
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-216 |
6.94e-37 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 129.71 E-value: 6.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGS-QTEIGMIFQQHN 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKgEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAaRNRIGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 82 L-----VDGVSAYLNALTGsLNRvsmlksmlqwqsREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDP 156
Cdd:cd03269 81 LypkmkVIDQLVYLAQLKG-LKK------------EEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDP 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 157 RLLLADEPVASLDPSSAETVMGYLRkAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGRK 216
Cdd:cd03269 148 ELLILDEPFSGLDPVNVELLKDVIR-ELARAGKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-235 |
9.26e-37 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 130.59 E-value: 9.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 5 KVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTE----IGMIFQQ 79
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKgGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRelakRLAILRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 80 HNlvdgvsaYLNA-LT--------------GSLNRvsmlksmlqwqsrEDKLRALEALETVGLLDESHQRVSQMSGGQQQ 144
Cdd:COG4604 83 EN-------HINSrLTvrelvafgrfpyskGRLTA-------------EDREIIDEAIAYLDLEDLADRYLDELSGGQRQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 145 RVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGRKLFDVGRDE 224
Cdd:COG4604 143 RAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEE 222
|
250
....*....|..
gi 493478014 225 -LTPELIDDLYG 235
Cdd:COG4604 223 iITPEVLSDIYD 234
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
3-215 |
1.57e-36 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 129.75 E-value: 1.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 3 TLKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQT---------- 71
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQgETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTpsdkairelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 72 -EIGMIFQQHNLVDGVSAYLNALTGSLNRVSMLKSmlqwqsrEDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIAR 150
Cdd:PRK11124 82 rNVGMVFQQYNLWPHLTVQQNLIEAPCRVLGLSKD-------QALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493478014 151 ALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAkEHDVTALVSLHQVNIAAHFGDRFIGLRDGR 215
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGH 218
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-219 |
1.64e-36 |
|
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: 130.65 E-value: 1.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYG-----DVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTE----- 72
Cdd:TIGR04521 1 IKLKNVSYIYQpgtpfEKKALDDVSLTIEDgEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKklkdl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 73 ---IGMIFQQ------------------HNLvdGVSAYlnaltgslnrvsmlksmlqwqsrEDKLRALEALETVGLlDES 131
Cdd:TIGR04521 81 rkkVGLVFQFpehqlfeetvykdiafgpKNL--GLSEE-----------------------EAEERVKEALELVGL-DEE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 132 HQRVS--QMSGGQQQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTA-LVSlHQVNIAAHFGDRF 208
Cdd:TIGR04521 135 YLERSpfELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTViLVT-HSMEDVAEYADRV 213
|
250
....*....|.
gi 493478014 209 IGLRDGRKLFD 219
Cdd:TIGR04521 214 IVMHKGKIVLD 224
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-216 |
1.80e-36 |
|
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: 127.16 E-value: 1.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSqteigmifqqhnl 82
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRgEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFA------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 83 vdgvsaylnaltgslnrvsmlksmlqwqSREDKLRAlealetvGLldeshQRVSQMSGGQQQRVGIARALVQDPRLLLAD 162
Cdd:cd03216 68 ----------------------------SPRDARRA-------GI-----AMVYQLSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 493478014 163 EPVASLDPSSAETVMGYLRKAAKEHDVTALVSlHQVNIAAHFGDRFIGLRDGRK 216
Cdd:cd03216 108 EPTAALTPAEVERLFKVIRRLRAQGVAVIFIS-HRLDEVFEIADRVTVLRDGRV 160
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-207 |
9.12e-36 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 127.49 E-value: 9.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 6 VENLSKQYGDVTALEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTE----IGMIFQQH 80
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVrRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREvrrrIGIVFQDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 81 NLVDGVSAYLNaltgslnrVSMLKSMLQWQSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDPRLLL 160
Cdd:cd03265 83 SVDDELTGWEN--------LYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLF 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 493478014 161 ADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDR 207
Cdd:cd03265 155 LDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDR 201
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
4-230 |
9.33e-36 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 128.18 E-value: 9.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTD-----PTEGSISLDDEPITGSQ------- 70
Cdd:TIGR00972 2 IEIENLNLFYGEKEALKNINLDIpKNQVTALIGPSGCGKSTLLRSLNRMNDlvpgvRIEGKVLFDGQDIYDKKidvvelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 71 TEIGMIFQQHNLVDgVSAYLNALTGSlnRVSMLKSmlqwqSREDKLRALEALETVGLLDESHQRVSQ----MSGGQQQRV 146
Cdd:TIGR00972 82 RRVGMVFQKPNPFP-MSIYDNIAYGP--RLHGIKD-----KKELDEIVEESLKKAALWDEVKDRLHDsalgLSGGQQQRL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 147 GIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKehDVTALVSLHQVNIAAHFGDRFIGLRDGR--------KLF 218
Cdd:TIGR00972 154 CIARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKK--KYTIVIVTHNMQQAARISDRTAFFYDGElveygpteQIF 231
|
250
....*....|..
gi 493478014 219 DVGRDELTPELI 230
Cdd:TIGR00972 232 TNPKEKRTEDYI 243
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-244 |
1.99e-35 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 127.51 E-value: 1.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYG-----DVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTE----- 72
Cdd:COG1101 2 LELKNLSKTFNpgtvnEKRALDGLNLTIEEgDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYkraky 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 73 IGMIFQqhnlvdgvsaylNALTGSLNRVSMLKSM-----------LQW-QSREDKLRALEALETV--GLLDESHQRVSQM 138
Cdd:COG1101 82 IGRVFQ------------DPMMGTAPSMTIEENLalayrrgkrrgLRRgLTKKRRELFRELLATLglGLENRLDTKVGLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 139 SGGQQQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGRKLF 218
Cdd:COG1101 150 SGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIIL 229
|
250 260
....*....|....*....|....*....
gi 493478014 219 DVGRDE---LTPELIDDLYGSVETVGLAD 244
Cdd:COG1101 230 DVSGEEkkkLTVEDLLELFEEIRGEELAD 258
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-169 |
4.10e-35 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 126.74 E-value: 4.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTEIGMIFQQHNL 82
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESgELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGVVFQNEGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 83 VDGVSAYLNALTGSlnrvsMLKSMLQWQSREdklRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDPRLLLAD 162
Cdd:PRK11248 82 LPWRNVQDNVAFGL-----QLAGVEKMQRLE---IAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLD 153
|
....*..
gi 493478014 163 EPVASLD 169
Cdd:PRK11248 154 EPFGALD 160
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
8-169 |
5.04e-35 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 129.30 E-value: 5.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 8 NLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITG---SQTEIGMIFQQHNLV 83
Cdd:PRK09452 19 GISKSFDGKEVISNLDLTINNgEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHvpaENRHVNTVFQSYALF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 84 DGVSAYLNALTGslnrvsmLKsMLQWQSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDPRLLLADE 163
Cdd:PRK09452 99 PHMTVFENVAFG-------LR-MQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDE 170
|
....*.
gi 493478014 164 PVASLD 169
Cdd:PRK09452 171 SLSALD 176
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-207 |
7.96e-35 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 127.54 E-value: 7.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQY-----------GDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITG-SQ 70
Cdd:COG4608 8 LEVRDLKKHFpvrgglfgrtvGVVKAVDGVSFDIRRgETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGlSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 71 TE-------IGMIFQqhnlvDgvsAYlnaltGSLN-------------RVSMLKSMlqwQSREDklRALEALETVGLLDE 130
Cdd:COG4608 88 RElrplrrrMQMVFQ-----D---PY-----ASLNprmtvgdiiaeplRIHGLASK---AERRE--RVAELLELVGLRPE 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493478014 131 SHQRVSQM-SGGQQQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDR 207
Cdd:COG4608 150 HADRYPHEfSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDR 227
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-243 |
2.07e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 125.55 E-value: 2.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 1 MStLKVENLSKQYGDVT-----ALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQT--- 71
Cdd:PRK13637 1 MS-IKIENLTHIYMEGTpfekkALDNVNIEIEDgEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVkls 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 72 ----EIGMIFQ--QHNLVDGvSAYLNALTGSLNrvsmlksmLQWQSREDKLRALEALETVGLLDESHQRVS--QMSGGQQ 143
Cdd:PRK13637 80 dirkKVGLVFQypEYQLFEE-TIEKDIAFGPIN--------LGLSEEEIENRVKRAMNIVGLDYEDYKDKSpfELSGGQK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 144 QRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGRKLFDVGRD 223
Cdd:PRK13637 151 RRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPR 230
|
250 260
....*....|....*....|
gi 493478014 224 ELTPElIDDLygsvETVGLA 243
Cdd:PRK13637 231 EVFKE-VETL----ESIGLA 245
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-225 |
2.13e-34 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 123.94 E-value: 2.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 1 MSTLKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTE------I 73
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEgEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHriarlgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 74 GM------IFQQ----HNLVdgVSAYLnaltgslnrvsmlksmlqwqsREDKLRALEALETV-GL---LDE-SHQRVSQM 138
Cdd:COG0410 81 GYvpegrrIFPSltveENLL--LGAYA---------------------RRDRAEVRADLERVyELfprLKErRRQRAGTL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 139 SGGQQQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEhDVTALVSLHQVNIAAHFGDRFIGLRDGRKLF 218
Cdd:COG0410 138 SGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVL 216
|
....*..
gi 493478014 219 DVGRDEL 225
Cdd:COG0410 217 EGTAAEL 223
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
11-230 |
2.33e-34 |
|
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: 127.28 E-value: 2.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 11 KQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPIT---------GSQTEIGMIFQQH 80
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKgEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMkqspvelreVRRKKIGMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 81 NLVDGVSAylnaltgsLNRVSMLKSMLQWQSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDPRLLL 160
Cdd:TIGR01186 81 ALFPHMTI--------LQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 161 ADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGrKLFDVGrdelTPELI 230
Cdd:TIGR01186 153 MDEAFSALDPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAG-EIVQVG----TPDEI 217
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
4-215 |
2.68e-34 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 123.29 E-value: 2.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVT----ALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITG---SQ----- 70
Cdd:NF038007 2 LNMQNAEKCYITKTiktkVLNHLNFSVEKgDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNlsySQkiilr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 71 -TEIGMIFQQHNLVDGVSAYLN-ALTGSLNRVSmlksmlqwqSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGI 148
Cdd:NF038007 82 rELIGYIFQSFNLIPHLSIFDNvALPLKYRGVA---------KKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493478014 149 ARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHdvTALVSLHQVNIAAHFGDRFIGLRDGR 215
Cdd:NF038007 153 ARAMVSNPALLLADEPTGNLDSKNARAVLQQLKYINQKG--TTIIMVTHSDEASTYGNRIINMKDGK 217
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
2-215 |
4.73e-34 |
|
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: 126.37 E-value: 4.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 2 STLKVeNLSKQYGDVTaLeDVSFQIEDE-FAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTE-------- 72
Cdd:COG4148 1 MMLEV-DFRLRRGGFT-L-DVDFTLPGRgVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGiflpphrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 73 -IGMIFQQHNL-----VDGvsaylNALTGslnrvsmLKSMLQWQSREDKLRALEALETVGLLDeshQRVSQMSGGQQQRV 146
Cdd:COG4148 78 rIGYVFQEARLfphlsVRG-----NLLYG-------RKRAPRAERRISFDEVVELLGIGHLLD---RRPATLSGGERQRV 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 147 GIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTAL-VSlHQVNIAAHFGDRFIGLRDGR 215
Cdd:COG4148 143 AIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILyVS-HSLDEVARLADHVVLLEQGR 211
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-196 |
5.07e-34 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 125.99 E-value: 5.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGS---QTEIGMIFQQ 79
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIkQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRsiqQRDICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 80 HNLVDGVSAYLNALTGslnrvsmLKsMLQWQSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDPRLL 159
Cdd:PRK11432 87 YALFPHMSLGENVGYG-------LK-MLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVL 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 493478014 160 LADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLH 196
Cdd:PRK11432 159 LFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTH 195
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-176 |
6.95e-34 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 123.22 E-value: 6.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTD--P---TEGSISLDDEPITGSQTE----- 72
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPEnKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDIYDPDVDvvelr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 73 --IGMIFQQHNLV-----DGVsAYLNALTGSLNRvsmlksmlqwqsreDKLRAL--EALETVGLLDES----HQRVSQMS 139
Cdd:COG1117 92 rrVGMVFQKPNPFpksiyDNV-AYGLRLHGIKSK--------------SELDEIveESLRKAALWDEVkdrlKKSALGLS 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 493478014 140 GGQQQRVGIARALVQDPRLLLADEPVASLDPSSAETV 176
Cdd:COG1117 157 GGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKI 193
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-215 |
9.88e-34 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 120.57 E-value: 9.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGD--VTALEDVSFQIE-DEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTE-----IGM 75
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKpGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLEslrknIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 76 IFQQHNLVDGvsaylnaltgslnrvsmlksmlqwqsredklralealeTVG--LLdeshqrvsqmSGGQQQRVGIARALV 153
Cdd:cd03228 81 VPQDPFLFSG--------------------------------------TIRenIL----------SGGQRQRIAIARALL 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493478014 154 QDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHdvTALVSLHQVNIAAHFgDRFIGLRDGR 215
Cdd:cd03228 113 RDPPILILDEATSALDPETEALILEALRALAKGK--TVIVIAHRLSTIRDA-DRIIVLDDGR 171
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-215 |
1.67e-33 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 122.48 E-value: 1.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTEIGMIFQQHNL 82
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIpAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRLMFQDARL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 83 ------VDGVSAylnALTGslnrvsmlksmlQWQSRedklrALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDP 156
Cdd:PRK11247 93 lpwkkvIDNVGL---GLKG------------QWRDA-----ALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 493478014 157 RLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGR 215
Cdd:PRK11247 153 GLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
4-215 |
2.01e-33 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 121.46 E-value: 2.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGD----VTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQT------- 71
Cdd:PRK11629 6 LQCDNLCKRYQEgsvqTDVLHNVSFSIGEgEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakaelr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 72 --EIGMIFQQHNLVDGVSAylnaltgsLNRVSMLKSMLQWQSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIA 149
Cdd:PRK11629 86 nqKLGFIYQFHHLLPDFTA--------LENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493478014 150 RALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFgDRFIGLRDGR 215
Cdd:PRK11629 158 RALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGR 222
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-214 |
2.19e-33 |
|
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: 121.42 E-value: 2.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 19 LEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTEIGMIFQQHNLVDGVSAYLN-ALtgS 96
Cdd:TIGR01184 1 LKGVNLTIqQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVFQNYSLLPWLTVRENiAL--A 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 97 LNRVsmlksMLQWQSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDPRLLLADEPVASLDPSSAETV 176
Cdd:TIGR01184 79 VDRV-----LPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 493478014 177 MGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDG 214
Cdd:TIGR01184 154 QEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-228 |
4.95e-33 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 125.91 E-value: 4.95e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTE------IGMI 76
Cdd:COG3845 6 LELRGITKRFGGVVANDDVSLTVRPgEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRdaialgIGMV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 77 FQQHNLVDGVSAYLNALTGSLNRVSMLksmLQWQSREDKLRALeaLETVGL-LDeSHQRVSQMSGGQQQRVGIARALVQD 155
Cdd:COG3845 86 HQHFMLVPNLTVAENIVLGLEPTKGGR---LDRKAARARIREL--SERYGLdVD-PDAKVEDLSVGEQQRVEILKALYRG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 156 PRLLLADEPVASLDPSSAETVMGYLRKAAKE-----------HDVTALvslhqvniaahfGDRFIGLRDGRKLFDVGRDE 224
Cdd:COG3845 160 ARILILDEPTAVLTPQEADELFEILRRLAAEgksiifithklREVMAI------------ADRVTVLRRGKVVGTVDTAE 227
|
....
gi 493478014 225 LTPE 228
Cdd:COG3845 228 TSEE 231
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
4-215 |
6.47e-33 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 119.98 E-value: 6.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQY-GDVTALEDVSFQIE-DEFAVLLGESGAGKSTLLRCINGLTDPTEGSI--------SLDDEPITGSQTEI 73
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRpGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsghditRLKNREVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 74 GMIFQQHNLVDGVSAYLNAltgslnrvsMLKSMLQWQSRED-KLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARAL 152
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNV---------AIPLIIAGASGDDiRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493478014 153 VQDPRLLLADEPVASLDPSSAETVMgYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGR 215
Cdd:PRK10908 153 VNKPAVLLADEPTGNLDDALSEGIL-RLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGH 214
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-215 |
2.34e-32 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 119.69 E-value: 2.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQIE-DEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPIT------GS------- 69
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANaGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdGQlkvadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 70 -----QTEIGMIFQQHNLVDGVSAYLNALTGSLNRVSMLKSmlqwqsrEDKLRALEALETVGLLDESHQRV-SQMSGGQQ 143
Cdd:PRK10619 86 qlrllRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQ-------EARERAVKYLAKVGIDERAQGKYpVHLSGGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493478014 144 QRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDvTALVSLHQVNIAAHFGDRFIGLRDGR 215
Cdd:PRK10619 159 QRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSSHVIFLHQGK 229
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
8-215 |
2.55e-32 |
|
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: 121.76 E-value: 2.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 8 NLSKQYGDVTAleDVSFQIE-DEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGS---------QTEIGMIF 77
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPgQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSrkgiflppeKRRIGYVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 78 QQHNLVDGVSAYLNALTGslnrvsMLKSML-QWQSREDKLRALEALETvgLLDeshQRVSQMSGGQQQRVGIARALVQDP 156
Cdd:TIGR02142 82 QEARLFPHLSVRGNLRYG------MKRARPsERRISFERVIELLGIGH--LLG---RLPGRLSGGEKQRVAIGRALLSSP 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 493478014 157 RLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGR 215
Cdd:TIGR02142 151 RLLLMDEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGR 209
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-215 |
3.31e-32 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 118.70 E-value: 3.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 1 MSTLKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDD------EPITGSQTEI 73
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPgEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDitidtaRSLSQQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 74 -------GMIFQQHNLVDGVSAYLNALTGSLnrvsmlksMLQWQSREDKL-RALEALETVGLLDESHQRVSQMSGGQQQR 145
Cdd:PRK11264 81 rqlrqhvGFVFQNFNLFPHRTVLENIIEGPV--------IVKGEPKEEATaRARELLAKVGLAGKETSYPRRLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 146 VGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSlHQVNIAAHFGDRFIGLRDGR 215
Cdd:PRK11264 153 VAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVT-HEMSFARDVADRAIFMDQGR 221
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-215 |
4.81e-32 |
|
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: 124.56 E-value: 4.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGD--VTALEDVSFQIE-DEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITG-------SQteI 73
Cdd:COG2274 474 IELENVSFRYPGdsPPVLDNISLTIKpGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQidpaslrRQ--I 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 74 GMIFQQHNLvdgvsaylnaLTGSL--NrVSMlksmlqWQSREDKLRALEALETVGLLD--ESH---------QRVSQMSG 140
Cdd:COG2274 552 GVVLQDVFL----------FSGTIreN-ITL------GDPDATDEEIIEAARLAGLHDfiEALpmgydtvvgEGGSNLSG 614
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493478014 141 GQQQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKehDVTALVSLHQVNIAAHFgDRFIGLRDGR 215
Cdd:COG2274 615 GQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRLA-DRIIVLDKGR 686
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-219 |
5.19e-32 |
|
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: 117.32 E-value: 5.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEpitGSQTEIGMIFQQHNL 82
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKgEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK---SYQKNIEALRRIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 83 VDGVSAYLNaLTGSLN-RVSMLKSMLqwqsreDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDPRLLLA 161
Cdd:cd03268 78 IEAPGFYPN-LTARENlRLLARLLGI------RKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 493478014 162 DEPVASLDPSSAETVMGYLRKAAKEhDVTALVSLHQVNIAAHFGDRFIGLRDGRKLFD 219
Cdd:cd03268 151 DEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
11-270 |
6.53e-32 |
|
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: 119.42 E-value: 6.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 11 KQYGDVTALEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTE----IGMIFQQHNLVDG 85
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVrEGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKvrrsIGIVPQYASVDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 86 vsaylnaLTGSLNRVSM--LKSMLQWQSREdklRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDPRLLLADE 163
Cdd:TIGR01188 81 -------LTGRENLEMMgrLYGLPKDEAEE---RAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 164 PVASLDPSSAETVMGYLRkAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGRKLFDVGRDELTPELIDDlygSVETVGLA 243
Cdd:TIGR01188 151 PTTGLDPRTRRAIWDYIR-ALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGKD---TLESRPRD 226
|
250 260
....*....|....*....|....*..
gi 493478014 244 DQEKTVEEALDAIGDDPSEGAAEDAQR 270
Cdd:TIGR01188 227 IQSLKVEVSMLIAELGETGLGLLAVTV 253
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-219 |
6.61e-32 |
|
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: 118.30 E-value: 6.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQY--GDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSI------SLDDEPITGSQTEIG 74
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKgEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVtvdgldTLDEENLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 75 MIFQQHNlvdgvsaylNALTGSL----------NrvsmlksmLQWQSREDKLRALEALETVGLLDESHQRVSQMSGGQQQ 144
Cdd:TIGR04520 81 MVFQNPD---------NQFVGATveddvafgleN--------LGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493478014 145 RVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHfGDRFIGLRDGRKLFD 219
Cdd:TIGR04520 144 RVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAE 217
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
2-235 |
6.93e-32 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 118.19 E-value: 6.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 2 STLKVENLSKQYGDVTALEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTE-----IGM 75
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLpTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRqlarrLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 76 IFQQHNLVDGV----------SAYLNaLTGSLnrvsmlksmlqwqSREDKLRALEALETVGLLDESHQRVSQMSGGQQQR 145
Cdd:PRK11231 81 LPQHHLTPEGItvrelvaygrSPWLS-LWGRL-------------SAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 146 VGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDvTALVSLHQVNIAAHFGDRFIGLRDGRKLFDVGRDE- 224
Cdd:PRK11231 147 AFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGK-TVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEv 225
|
250
....*....|.
gi 493478014 225 LTPELIDDLYG 235
Cdd:PRK11231 226 MTPGLLRTVFD 236
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-242 |
4.19e-31 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 116.65 E-value: 4.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVT--ALEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTDPTEGSIS-----LDDEPITGSQTEIGM 75
Cdd:PRK13635 6 IRVEHISFRYPDAAtyALKDVSFSVyEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITvggmvLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 76 IFQQ-HNLVDGVSAYLNALTGSLN----RVSMLKsmlqwqsredklRALEALETVGLLDESHQRVSQMSGGQQQRVGIAR 150
Cdd:PRK13635 86 VFQNpDNQFVGATVQDDVAFGLENigvpREEMVE------------RVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 151 ALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAhFGDRFIGLRDGRKLfdvgrDELTPELI 230
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAA-QADRVIVMNKGEIL-----EEGTPEEI 227
|
250
....*....|..
gi 493478014 231 DDLYGSVETVGL 242
Cdd:PRK13635 228 FKSGHMLQEIGL 239
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-230 |
5.30e-31 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 114.93 E-value: 5.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQIE-DEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTE------IG-- 74
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPkGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHeraragIAyv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 75 ----MIFQQhnlvdgVSAYLNALTGslnrvsmlksmLQWQSREDKLRALEALETVGLLDE-SHQRVSQMSGGQQQRVGIA 149
Cdd:TIGR03410 81 pqgrEIFPR------LTVEENLLTG-----------LAALPRRSRKIPDEIYELFPVLKEmLGRRGGDLSGGQQQQLAIA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 150 RALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGRKLFDVGRDELTPEL 229
Cdd:TIGR03410 144 RALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDK 223
|
.
gi 493478014 230 I 230
Cdd:TIGR03410 224 V 224
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
3-196 |
1.15e-30 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 113.73 E-value: 1.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 3 TLKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDP---TEGSISLDDEPITGSQTE---IGM 75
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPgEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEqrrIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 76 IFQQHNLVDGVSAYLN---ALTGSLNRvsmlksmlqwqsREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARAL 152
Cdd:COG4136 81 LFQDDLLFPHLSVGENlafALPPTIGR------------AQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 493478014 153 VQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLH 196
Cdd:COG4136 149 LAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTH 192
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-226 |
1.17e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 115.01 E-value: 1.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 1 MSTLKVENLSKQYGDVTALEDVSFQIEDE-FAVLLGESGAGKSTLLRCINGLTD-----PTEGSISLDDE-----PITGS 69
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNtITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQdifkmDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 70 QTEIGMIFQQHNLVDGVSAYLN-ALTGSLNRVSMLKSMLQWQSREdklraleALETVGLLDESHQRV----SQMSGGQQQ 144
Cdd:PRK14247 81 RRRVQMVFQIPNPIPNLSIFENvALGLKLNRLVKSKKELQERVRW-------ALEKAQLWDEVKDRLdapaGKLSGGQQQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 145 RVGIARALVQDPRLLLADEPVASLDPSSA---ETVMGYLRKaakehDVTALVSLHQVNIAAHFGDRFIGLRDG------- 214
Cdd:PRK14247 154 RLCIARALAFQPEVLLADEPTANLDPENTakiESLFLELKK-----DMTIVLVTHFPQQAARISDYVAFLYKGqivewgp 228
|
250
....*....|...
gi 493478014 215 -RKLFDVGRDELT 226
Cdd:PRK14247 229 tREVFTNPRHELT 241
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-241 |
1.80e-30 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 117.64 E-value: 1.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 1 MSTLKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITG-SQTEIGMifQ 78
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREgSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEAlSARAASR--R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 79 QHNLVDGVSAYLN---ALTGSLNRVSMLKSMLQWQSREDklRALE-ALETVGLLDESHQRVSQMSGGQQQRVGIARALVQ 154
Cdd:PRK09536 79 VASVPQDTSLSFEfdvRQVVEMGRTPHRSRFDTWTETDR--AAVErAMERTGVAQFADRPVTSLSGGERQRVLLARALAQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 155 DPRLLLADEPVASLDPSSAETVMGYLRKAAkEHDVTALVSLHQVNIAAHFGDRFIGLRDGRkLFDVGRDE--LTPELIDD 232
Cdd:PRK09536 157 ATPVLLLDEPTASLDINHQVRTLELVRRLV-DDGKTAVAAIHDLDLAARYCDELVLLADGR-VRAAGPPAdvLTADTLRA 234
|
....*....
gi 493478014 233 LYGSVETVG 241
Cdd:PRK09536 235 AFDARTAVG 243
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
33-230 |
4.78e-30 |
|
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: 114.90 E-value: 4.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 33 LLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTE---IGMIFQQHNLVDGVSAYLNALTGslnrvsmLKsMLQW 109
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHlrhINMVFQSYALFPHMTVEENVAFG-------LK-MRKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 110 QSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDV 189
Cdd:TIGR01187 73 PRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGI 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 493478014 190 TALVSLHQVNIAAHFGDRFIGLRDGrKLFDVGrdelTPELI 230
Cdd:TIGR01187 153 TFVFVTHDQEEAMTMSDRIAIMRKG-KIAQIG----TPEEI 188
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-214 |
8.24e-30 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 113.01 E-value: 8.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 1 MSTL-KVENLSKQY---------GDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGS 69
Cdd:COG4167 1 MSALlEVRNLSKTFkyrtglfrrQQFEAVKPVSFTLEAgQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 70 QTE-----IGMIFQQHNlvdgvsaylNALTGSLNRVSMLKSML----QWQSREDKLRALEALETVGLLDEsHQRV--SQM 138
Cdd:COG4167 81 DYKyrckhIRMIFQDPN---------TSLNPRLNIGQILEEPLrlntDLTAEEREERIFATLRLVGLLPE-HANFypHML 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493478014 139 SGGQQQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDG 214
Cdd:COG4167 151 SSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQG 226
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-183 |
1.22e-29 |
|
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: 111.37 E-value: 1.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 1 MST-LKVENLSKQY-----GDVT--ALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISL--DDEPITGS 69
Cdd:COG4778 1 MTTlLEVENLSKTFtlhlqGGKRlpVLDGVSFSVAAgECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 70 Q-----------TEIGMifqqhnlvdgVSAYLNALTgslnRVSML----KSMLQWQSRED--KLRALEALETVGLlDESH 132
Cdd:COG4778 81 QaspreilalrrRTIGY----------VSQFLRVIP----RVSALdvvaEPLLERGVDREeaRARARELLARLNL-PERL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 493478014 133 QRVS--QMSGGQQQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKA 183
Cdd:COG4778 146 WDLPpaTFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA 198
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
4-207 |
1.32e-29 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 112.18 E-value: 1.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTD-----PTEGSISLDDEPITGSQT------ 71
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFyPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYSPRTdtvdlr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 72 -EIGMIFQQHNLVDgVSAYLNALTGslnrvsmlksmLQWQSREDKLRALEALET----VGLLDESHQRVSQ----MSGGQ 142
Cdd:PRK14239 86 kEIGMVFQQPNPFP-MSIYENVVYG-----------LRLKGIKDKQVLDEAVEKslkgASIWDEVKDRLHDsalgLSGGQ 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493478014 143 QQRVGIARALVQDPRLLLADEPVASLDPSSA----ETVMGYlrkaakEHDVTALVSLHQVNIAAHFGDR 207
Cdd:PRK14239 154 QQRVCIARVLATSPKIILLDEPTSALDPISAgkieETLLGL------KDDYTMLLVTRSMQQASRISDR 216
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-215 |
1.44e-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: 116.78 E-value: 1.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 2 STLKVENLSKQYGD-VTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTE-----IG 74
Cdd:COG4988 335 PSIELEDVSFSYPGgRPALDGLSLTIPPgERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAswrrqIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 75 MIFQQhnlvdgvsAYLnaLTGSLnRVSMLksMLQWQSREDKLRAleALETVGLLDESHQ-----------RVSQMSGGQQ 143
Cdd:COG4988 415 WVPQN--------PYL--FAGTI-RENLR--LGRPDASDEELEA--ALEAAGLDEFVAAlpdgldtplgeGGRGLSGGQA 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493478014 144 QRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHdvTALVSLHQVNIAAHFgDRFIGLRDGR 215
Cdd:COG4988 480 QRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLAQA-DRILVLDDGR 548
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-225 |
1.65e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 112.63 E-value: 1.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVT-ALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGS-------QTEIG 74
Cdd:PRK13636 6 LKVEELNYNYSDGThALKGININIKKgEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSrkglmklRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 75 MIFQQ-HNLVDGVSAYLNALTGSLNrvsmlksmLQWQSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALV 153
Cdd:PRK13636 86 MVFQDpDNQLFSASVYQDVSFGAVN--------LKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493478014 154 QDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGRKLFDVGRDEL 225
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
29-215 |
9.56e-29 |
|
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: 108.73 E-value: 9.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 29 EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITG---SQTEIGMIFQQHNLVDGVSAYLNAltgSLNRVSMLKS 105
Cdd:cd03298 25 EITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAappADRPVSMLFQENNLFAHLTVEQNV---GLGLSPGLKL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 106 MLQWQSREDKlraleALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAK 185
Cdd:cd03298 102 TAEDRQAIEV-----ALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHA 176
|
170 180 190
....*....|....*....|....*....|
gi 493478014 186 EHDVTALVSLHQVNIAAHFGDRFIGLRDGR 215
Cdd:cd03298 177 ETKMTVLMVTHQPEDAKRLAQRVVFLDNGR 206
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
29-215 |
1.38e-28 |
|
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: 108.41 E-value: 1.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 29 EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGS---QTEIGMIFQQHNLVDGVSAYLNALTGslnrvsmLKS 105
Cdd:TIGR01277 25 EIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLapyQRPVSMLFQENNLFAHLTVRQNIGLG-------LHP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 106 MLQWQSrEDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAK 185
Cdd:TIGR01277 98 GLKLNA-EQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCS 176
|
170 180 190
....*....|....*....|....*....|
gi 493478014 186 EHDVTALVSLHQVNIAAHFGDRFIGLRDGR 215
Cdd:TIGR01277 177 ERQRTLLMVTHHLSDARAIASQIAVVSQGK 206
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-215 |
1.43e-28 |
|
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: 108.36 E-value: 1.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGD--VTALEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGS----QTEIGMI 76
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVyKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDrkaaRQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 77 FQQHNLVDGVSAYLNaltgsLNRVSMLKSMLQWQSREDklrALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDP 156
Cdd:cd03263 81 PQFDALFDELTVREH-----LRFYARLKGLPKSEIKEE---VELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 493478014 157 RLLLADEPVASLDPSSAETVMGYLRKAAKEHdvTALVSLHQVNIAAHFGDRFIGLRDGR 215
Cdd:cd03263 153 SVLLLDEPTSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGK 209
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-169 |
1.63e-28 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 111.66 E-value: 1.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 1 MSTLKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDE---PITGSQTEIGMI 76
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEgEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmnDVPPAERGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 77 FQQHNLVDGVSAYLNALTGsLNRVSMLKSmlQWQSREDKlrALEALETVGLLDeshQRVSQMSGGQQQRVGIARALVQDP 156
Cdd:PRK11000 81 FQSYALYPHLSVAENMSFG-LKLAGAKKE--EINQRVNQ--VAEVLQLAHLLD---RKPKALSGGQRQRVAIGRTLVAEP 152
|
170
....*....|...
gi 493478014 157 RLLLADEPVASLD 169
Cdd:PRK11000 153 SVFLLDEPLSNLD 165
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-215 |
1.78e-28 |
|
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: 113.71 E-value: 1.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 3 TLKVENLSKQY--GDVTALEDVSFQIE-DEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTE-----IG 74
Cdd:COG4987 333 SLELEDVSFRYpgAGRPVLDGLSLTLPpGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDdlrrrIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 75 MIFQQHNLVDGvSAYLNALTGSLNrVSmlksmlqwqsrEDKLRAleALETVGL--------------LDESHQRVSqmsG 140
Cdd:COG4987 413 VVPQRPHLFDT-TLRENLRLARPD-AT-----------DEELWA--ALERVGLgdwlaalpdgldtwLGEGGRRLS---G 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493478014 141 GQQQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHdvTALVSLHQVNIAAHFgDRFIGLRDGR 215
Cdd:COG4987 475 GERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLAGLERM-DRILVLEDGR 546
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-215 |
3.67e-28 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 108.62 E-value: 3.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 1 MSTLKVENLSKQYGDV---------TALEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQ 70
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGglsgkhqhqTVLNNVSLSLkSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 71 TE--------IGMIFQ--------QHNLVDGVSAYLNALTgSLNRvsmlksmlqwqsREDKLRALEALETVGLLDESHQR 134
Cdd:PRK10419 81 RAqrkafrrdIQMVFQdsisavnpRKTVREIIREPLRHLL-SLDK------------AERLARASEMLRAVDLDDSVLDK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 135 V-SQMSGGQQQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRD 213
Cdd:PRK10419 148 RpPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDN 227
|
..
gi 493478014 214 GR 215
Cdd:PRK10419 228 GQ 229
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
4-211 |
4.88e-28 |
|
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: 107.10 E-value: 4.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQIE-DEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTE-IGMIFQQHN 81
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPkNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKDLHkIGSLIESPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 82 LVDGVSAYLNaltgsLNRVSMLKSMlqwqsreDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDPRLLLA 161
Cdd:TIGR03740 81 LYENLTAREN-----LKVHTTLLGL-------PDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLIL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 493478014 162 DEPVASLDPSSAETVMGYLRkAAKEHDVTALVSLHQVNIAAHFGDrFIGL 211
Cdd:TIGR03740 149 DEPTNGLDPIGIQELRELIR-SFPEQGITVILSSHILSEVQQLAD-HIGI 196
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-235 |
4.97e-28 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 108.15 E-value: 4.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 2 STLKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTE-----IGM 75
Cdd:PRK10253 6 ARLRGEQLTLGYGKYTVAENLTVEIPDgHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKevarrIGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 76 IFQQHNLVDGVSAYLNALTGSLNRVSMLKsmlQWQsREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQD 155
Cdd:PRK10253 86 LAQNATTPGDITVQELVARGRYPHQPLFT---RWR-KEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 156 PRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGRKLFDVGRDEL-TPELIDDLY 234
Cdd:PRK10253 162 TAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIvTAELIERIY 241
|
.
gi 493478014 235 G 235
Cdd:PRK10253 242 G 242
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
4-217 |
1.25e-27 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 107.00 E-value: 1.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITG-SQTEI---GMI-- 76
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVrEQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGlPGHQIarmGVVrt 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 77 FQQHNLVDGVSAYLNALTGSLNRVS------MLKSMLQWQSREDKL-RALEALETVGLLDESHQRVSQMSGGQQQRVGIA 149
Cdd:PRK11300 86 FQHVRLFREMTVIENLLVAQHQQLKtglfsgLLKTPAFRRAESEALdRAATWLERVGLLEHANRQAGNLAYGQQRRLEIA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493478014 150 RALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGRKL 217
Cdd:PRK11300 166 RCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPL 233
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-169 |
1.55e-27 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 108.78 E-value: 1.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 1 MSTLKVENLSKQY-GDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITG---SQTEIGM 75
Cdd:PRK11650 1 MAGLKLQAVRKSYdGKTQVIKGIDLDVADgEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNElepADRDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 76 IFQQHNLVDGVSAYLNALTGSLNRvSMLKSmlqwQSREDKLRALEALETVGLLDeshQRVSQMSGGQQQRVGIARALVQD 155
Cdd:PRK11650 81 VFQNYALYPHMSVRENMAYGLKIR-GMPKA----EIEERVAEAARILELEPLLD---RKPRELSGGQRQRVAMGRAIVRE 152
|
170
....*....|....
gi 493478014 156 PRLLLADEPVASLD 169
Cdd:PRK11650 153 PAVFLFDEPLSNLD 166
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-225 |
1.57e-27 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 110.64 E-value: 1.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDD------EPITGSQTEIGMI 76
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVyPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinynklDHKLAAQLGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 77 FQQHNLVDGVSAYLNALTGSL-NRVSMLKSMLQWqsREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQD 155
Cdd:PRK09700 86 YQELSVIDELTVLENLYIGRHlTKKVCGVNIIDW--REMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493478014 156 PRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSlHQVNIAAHFGDRFIGLRDG-----RKLFDVGRDEL 225
Cdd:PRK09700 164 AKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYIS-HKLAEIRRICDRYTVMKDGssvcsGMVSDVSNDDI 237
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
4-215 |
3.30e-27 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 110.20 E-value: 3.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQY----GDVTALEDVSFQIE-DEFAVLLGESGAGKSTLLRCINGLTDPTEGS--------ISLDDEPITGSQ 70
Cdd:PRK10535 5 LELKDIRRSYpsgeEQVEVLKGISLDIYaGEMVAIVGASGSGKSTLMNILGCLDKPTSGTyrvagqdvATLDADALAQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 71 TE-IGMIFQQHNLVDGVSAYLN----ALTGSLNRvsmlksmlqwqsREDKLRALEALETVGLLDESHQRVSQMSGGQQQR 145
Cdd:PRK10535 85 REhFGFIFQRYHLLSHLTAAQNvevpAVYAGLER------------KQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 146 VGIARALVQDPRLLLADEPVASLDPSSAETVMGYLrKAAKEHDVTALVSLHQVNIAAHfGDRFIGLRDGR 215
Cdd:PRK10535 153 VSIARALMNGGQVILADEPTGALDSHSGEEVMAIL-HQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGE 220
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
4-171 |
9.77e-27 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 106.20 E-value: 9.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQY----------GDVTALEDVSFQIE--DEFAVLlGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQT 71
Cdd:PRK11308 6 LQAIDLKKHYpvkrglfkpeRLVKALDGVSFTLErgKTLAVV-GESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 72 E--------IGMIFQqhnlvdgvSAYlnaltGSLN---RV-SMLKSMLQWQSR----EDKLRALEALETVGLLDESHQRV 135
Cdd:PRK11308 85 EaqkllrqkIQIVFQ--------NPY-----GSLNprkKVgQILEEPLLINTSlsaaERREKALAMMAKVGLRPEHYDRY 151
|
170 180 190
....*....|....*....|....*....|....*..
gi 493478014 136 SQM-SGGQQQRVGIARALVQDPRLLLADEPVASLDPS 171
Cdd:PRK11308 152 PHMfSGGQRQRIAIARALMLDPDVVVADEPVSALDVS 188
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-256 |
1.30e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 104.82 E-value: 1.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVT-ALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGS-----QTEIGMI 76
Cdd:PRK13647 5 IEVEDLHFRYKDGTkALKGLSLSIPEgSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAEnekwvRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 77 FQQ-HNLVDGVSAYLNALTGSLNrvsmlksmLQWQSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQD 155
Cdd:PRK13647 85 FQDpDDQVFSSTVWDDVAFGPVN--------MGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 156 PRLLLADEPVASLDPSSAETVMGYLRKAAKEhDVTALVSLHQVNIAAHFGDRFIGLRDGRKLFD-----------VGRDE 224
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEgdkslltdediVEQAG 235
|
250 260 270
....*....|....*....|....*....|..
gi 493478014 225 LTPELIDDLYGSVETVGLADQEKTVEEALDAI 256
Cdd:PRK13647 236 LRLPLVAQIFEDLPELGQSKLPLTVKEAVQII 267
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-256 |
1.49e-26 |
|
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: 107.97 E-value: 1.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTD--PTEGSI----------------SLDDE 64
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEgEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyhvalcekcgyverpSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 65 PIT---GSQTEIGMIFQqhNLVDGVSAYLN-----------ALTGSlNRV--SMLKSM--LQWQSREDKLRALEALETVG 126
Cdd:TIGR03269 81 PCPvcgGTLEPEEVDFW--NLSDKLRRRIRkriaimlqrtfALYGD-DTVldNVLEALeeIGYEGKEAVGRAVDLIEMVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 127 LLDESHQRVSQMSGGQQQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGD 206
Cdd:TIGR03269 158 LSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSD 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 493478014 207 RFIGLRDGrKLFDVGrdelTPELIDDLYgsVETVGLADQEKTVEEALDAI 256
Cdd:TIGR03269 238 KAIWLENG-EIKEEG----TPDEVVAVF--MEGVSEVEKECEVEVGEPII 280
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
4-206 |
1.84e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 104.09 E-value: 1.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTD--PT---EGSISLDDEPITGSQTE----- 72
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIpKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNLYAPDVDpvevr 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 73 --IGMIFQQHN-----LVDGVS--AYLNALTGSLNRV--SMLKSMLQWQSREDKLRalealetvglldeshQRVSQMSGG 141
Cdd:PRK14243 91 rrIGMVFQKPNpfpksIYDNIAygARINGYKGDMDELveRSLRQAALWDEVKDKLK---------------QSGLSLSGG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493478014 142 QQQRVGIARALVQDPRLLLADEPVASLDPSSA---ETVMGYLRKaakehDVTALVSLHQVNIAAHFGD 206
Cdd:PRK14243 156 QQQRLCIARAIAVQPEVILMDEPCSALDPISTlriEELMHELKE-----QYTIIIVTHNMQQAARVSD 218
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-170 |
2.32e-26 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 103.19 E-value: 2.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 1 MSTLKVENLSKQYGDVTALEDVSFQIEDEFAV-LLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITG------SQTEI 73
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVgLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlpmhkrARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 74 GMIFQQHNLVDGVSAYLNaltgslnrvsmLKSMLQWQ--SREDKLRALEAletvgLLDE------SHQRVSQMSGGQQQR 145
Cdd:COG1137 81 GYLPQEASIFRKLTVEDN-----------ILAVLELRklSKKEREERLEE-----LLEEfgithlRKSKAYSLSGGERRR 144
|
170 180
....*....|....*....|....*
gi 493478014 146 VGIARALVQDPRLLLADEPVASLDP 170
Cdd:COG1137 145 VEIARALATNPKFILLDEPFAGVDP 169
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-169 |
2.51e-26 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 105.69 E-value: 2.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGS---QTEIGMIFQQ 79
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIyKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVppyQRPINMMFQS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 80 HNLVDGVSAYLNALTGsLNRVSMLKSmlqwqsrEDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDPRLL 159
Cdd:PRK11607 100 YALFPHMTVEQNIAFG-LKQDKLPKA-------EIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLL 171
|
170
....*....|
gi 493478014 160 LADEPVASLD 169
Cdd:PRK11607 172 LLDEPMGALD 181
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
18-267 |
2.55e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 104.33 E-value: 2.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 18 ALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTE---------IGMIFQ--QHNLVDG 85
Cdd:PRK13634 22 ALYDVNVSIPSgSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNkklkplrkkVGIVFQfpEHQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 86 VSAYLNALtGSLN-RVSmlksmlqwqSREDKLRALEALETVGLLDESHQRVS-QMSGGQQQRVGIARALVQDPRLLLADE 163
Cdd:PRK13634 102 TVEKDICF-GPMNfGVS---------EEDAKQKAREMIELVGLPEELLARSPfELSGGQMRRVAIAGVLAMEPEVLVLDE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 164 PVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGrKLFDVGrdelTPELI----DDL----YG 235
Cdd:PRK13634 172 PTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKG-TVFLQG----TPREIfadpDELeaigLD 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 493478014 236 SVETVGLADQ-EK-----------TVEEALDAIGDDPSEGAAED 267
Cdd:PRK13634 247 LPETVKFKRAlEEkfgisfpkpclTLEELAHEVVQLLRKGGHES 290
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
11-219 |
2.76e-26 |
|
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: 102.80 E-value: 2.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 11 KQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEpITGSQTE-----IGMIFQQHNLV- 83
Cdd:cd03267 29 RKYREVEALKGISFTIEKgEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL-VPWKRRKkflrrIGVVFGQKTQLw 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 84 -DgvsayLNALTGslnrVSMLKSMLQWQSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDPRLLLAD 162
Cdd:cd03267 108 wD-----LPVIDS----FYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 493478014 163 EPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGRKLFD 219
Cdd:cd03267 179 EPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYD 235
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3-215 |
3.66e-26 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 107.17 E-value: 3.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 3 TLKVENLSKQY-GDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITG-SQTE----IGM 75
Cdd:COG1132 339 EIEFENVSFSYpGDRPVLKDISLTIPPgETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDlTLESlrrqIGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 76 IFQQHNLVDGvSAYLNALTGSLNRvsmlksmlqwqSREDKLRALEA-------------LET-VGlldeshQRVSQMSGG 141
Cdd:COG1132 419 VPQDTFLFSG-TIRENIRYGRPDA-----------TDEEVEEAAKAaqahefiealpdgYDTvVG------ERGVNLSGG 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493478014 142 QQQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKehDVTALVSLHQVNIAAHFgDRFIGLRDGR 215
Cdd:COG1132 481 QRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRNA-DRILVLDDGR 551
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-219 |
4.06e-26 |
|
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: 102.06 E-value: 4.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGD----VTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLD-----DEPITgSQTEI 73
Cdd:cd03266 2 ITADALTKRFRDvkktVQAVDGVSFTVKPgEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDgfdvvKEPAE-ARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 74 GMIFQQHNLVDGVSA-----YLNALTGsLNRvSMLKSMLQWQSreDKLRALEALEtvglldeshQRVSQMSGGQQQRVGI 148
Cdd:cd03266 81 GFVSDSTGLYDRLTArenleYFAGLYG-LKG-DELTARLEELA--DRLGMEELLD---------RRVGGFSTGMRQKVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493478014 149 ARALVQDPRLLLADEPVASLDPSSAETVMGYLRkAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGRKLFD 219
Cdd:cd03266 148 ARALVHDPPVLLLDEPTTGLDVMATRALREFIR-QLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-215 |
5.78e-26 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 101.78 E-value: 5.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 2 STLKVENLSKQYGD----VTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTE---- 72
Cdd:PRK10584 5 NIVEVHHLKKSVGQgeheLSILTGVELVVKRgETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEarak 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 73 -----IGMIFQQHNLVdgvsAYLNALTgSLNRVSMLKSMLQWQSREdklRALEALETVGLLDESHQRVSQMSGGQQQRVG 147
Cdd:PRK10584 85 lrakhVGFVFQSFMLI----PTLNALE-NVELPALLRGESSRQSRN---GAKALLEQLGLGKRLDHLPAQLSGGEQQRVA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493478014 148 IARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFgDRFIGLRDGR 215
Cdd:PRK10584 157 LARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARC-DRRLRLVNGQ 223
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-230 |
6.61e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 104.14 E-value: 6.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 1 MSTLKVE--NLSKQYGDVTALEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITG----SQTEI 73
Cdd:PRK13536 37 MSTVAIDlaGVSKSYGDKAVVNGLSFTVaSGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPArarlARARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 74 GMIFQQHNLVDGVSAYLNALT-GSLNRVSmlksmlqwqSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARAL 152
Cdd:PRK13536 117 GVVPQFDNLDLEFTVRENLLVfGRYFGMS---------TREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARAL 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493478014 153 VQDPRLLLADEPVASLDPSSAETVMGYLRkAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGRKLFDVGRDELTPELI 230
Cdd:PRK13536 188 INDPQLLILDEPTTGLDPHARHLIWERLR-SLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHI 264
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
18-235 |
6.94e-26 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 102.56 E-value: 6.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 18 ALEDVSFQIEDE---------FAV-----LLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQT-----EIGMIFQ 78
Cdd:PRK10575 13 ALRNVSFRVPGRtllhplsltFPAgkvtgLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSkafarKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 79 QHNLVDGVSAY-LNALT-----GSLNRVSmlksmlqwqsREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARAL 152
Cdd:PRK10575 93 QLPAAEGMTVReLVAIGrypwhGALGRFG----------AADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 153 VQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGRKLFDVGRDELT-PELID 231
Cdd:PRK10575 163 AQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMrGETLE 242
|
....
gi 493478014 232 DLYG 235
Cdd:PRK10575 243 QIYG 246
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-182 |
7.17e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 105.92 E-value: 7.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 6 VENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDdepitgSQTEIGMIFQQHNLVD 84
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPgDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP------KGLRIGYLPQEPPLDD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 85 GVSAY---------LNALTGSLNRVSM--------LKSMLQWQSREDKL-------RALEALETVGLLDESHQR-VSQMS 139
Cdd:COG0488 75 DLTVLdtvldgdaeLRALEAELEELEAklaepdedLERLAELQEEFEALggweaeaRAEEILSGLGFPEEDLDRpVSELS 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 493478014 140 GGQQQRVGIARALVQDPRLLLADEPVASLDpssAETVM---GYLRK 182
Cdd:COG0488 155 GGWRRRVALARALLSEPDLLLLDEPTNHLD---LESIEwleEFLKN 197
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-202 |
8.54e-26 |
|
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: 105.83 E-value: 8.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 2 STLKVENLSKQYGDVT-ALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGS-----QTEIG 74
Cdd:TIGR02857 320 SSLEFSGVSVAYPGRRpALRPVSFTVPPgERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADAdadswRDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 75 MIFQQHNLVDGVSAYLNALTGSLNRVSMLKSMLQWQSREDKLRALEA-LETvgLLDESHQRvsqMSGGQQQRVGIARALV 153
Cdd:TIGR02857 400 WVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQgLDT--PIGEGGAG---LSGGQAQRLALARAFL 474
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 493478014 154 QDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHdvTALVSLHQVNIAA 202
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRALAQGR--TVLLVTHRLALAA 521
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
4-181 |
1.00e-25 |
|
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: 100.51 E-value: 1.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITgsqteigmifQQHNL 82
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLnAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLA----------EQRDE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 83 VDGVSAYLNALTGSLNRVSMLKSMLQWQ--SREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDPRLLL 160
Cdd:TIGR01189 71 PHENILYLGHLPGLKPELSALENLHFWAaiHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWI 150
|
170 180
....*....|....*....|.
gi 493478014 161 ADEPVASLDPSSAETVMGYLR 181
Cdd:TIGR01189 151 LDEPTTALDKAGVALLAGLLR 171
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-215 |
1.05e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 102.08 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVT-ALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQT-------EIG 74
Cdd:PRK13639 2 LETRDLKYSYPDGTeALKGINFKAEKgEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKsllevrkTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 75 MIFQQHN------LVDGVSAYlnaltGSLNrvsmlksmLQWQSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGI 148
Cdd:PRK13639 82 IVFQNPDdqlfapTVEEDVAF-----GPLN--------LGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493478014 149 ARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEhDVTALVSLHQVNIAAHFGDRFIGLRDGR 215
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGK 214
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
4-225 |
1.74e-25 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 100.81 E-value: 1.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQIEDEFAVLlGESGAGKSTLLRCINGLTDPTEGSISLDDEPITG---SQTEIGMIFQQH 80
Cdd:PRK10771 2 LKLTDITWLYHHLPMRFDLTVERGERVAIL-GPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTtppSRRPVSMLFQEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 81 NLVDGVSAYLNALTGsLNRVSMLKSmlqwqSREDKLRALeaLETVGLLDESHQRVSQMSGGQQQRVGIARALVQDPRLLL 160
Cdd:PRK10771 81 NLFSHLTVAQNIGLG-LNPGLKLNA-----AQREKLHAI--ARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493478014 161 ADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGRKLFDVGRDEL 225
Cdd:PRK10771 153 LDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
14-201 |
1.95e-25 |
|
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: 99.42 E-value: 1.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 14 GDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPI-------TGSQTEIGMIFQqhnlvDG 85
Cdd:TIGR01166 3 GGPEVLKGLNFAAERgEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLdysrkglLERRQRVGLVFQ-----DP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 86 VSAYLNALTGSlnRVSMLKSMLQWQSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDPRLLLADEPV 165
Cdd:TIGR01166 78 DDQLFAADVDQ--DVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPT 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 493478014 166 ASLDPSSAETVMGYLRKaAKEHDVTALVSLHQVNIA 201
Cdd:TIGR01166 156 AGLDPAGREQMLAILRR-LRAEGMTVVISTHDVDLA 190
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-170 |
2.99e-25 |
|
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: 99.92 E-value: 2.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITG------SQTEIGMI 76
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVkQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKlpmhkrARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 77 FQQHNLVDGVSAYLNALtgslnrvSMLKSM-LQWQSREDKLRALeaLETVGLLDESHQRVSQMSGGQQQRVGIARALVQD 155
Cdd:cd03218 81 PQEASIFRKLTVEENIL-------AVLEIRgLSKKEREEKLEEL--LEEFHITHLRKSKASSLSGGERRRVEIARALATN 151
|
170
....*....|....*
gi 493478014 156 PRLLLADEPVASLDP 170
Cdd:cd03218 152 PKFLLLDEPFAGVDP 166
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
18-207 |
3.68e-25 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 102.09 E-value: 3.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 18 ALEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTDPTEGSIS--------LDDEPITGSQTEIGMIFQqhnlvDGVSa 88
Cdd:PRK15079 36 AVDGVTLRLyEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAwlgkdllgMKDDEWRAVRSDIQMIFQ-----DPLA- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 89 ylnaltgSLN-RVSM-------LKSMLQWQSRED-KLRALEALETVGLLDESHQRVS-QMSGGQQQRVGIARALVQDPRL 158
Cdd:PRK15079 110 -------SLNpRMTIgeiiaepLRTYHPKLSRQEvKDRVKAMMLKVGLLPNLINRYPhEFSGGQCQRIGIARALILEPKL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 493478014 159 LLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDR 207
Cdd:PRK15079 183 IICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDR 231
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-214 |
6.20e-25 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 101.70 E-value: 6.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 1 MStLKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITG---SQTEIGMI 76
Cdd:PRK10851 1 MS-IEIANIKKSFGRTQVLNDISLDIPSgQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRlhaRDRKVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 77 FQQHNLVDGVSAYLNALTGslnrVSMLKSMLQWQSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDP 156
Cdd:PRK10851 80 FQHYALFRHMTVFDNIAFG----LTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 493478014 157 RLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDG 214
Cdd:PRK10851 156 QILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQG 213
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
13-204 |
1.02e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 97.69 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 13 YGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISlddepiTGSQTEIGMIFQQHNLVDGVSAyln 91
Cdd:NF040873 2 YGGRPVLHGVDLTIPAgSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR------RAGGARVAYVPQRSEVPDSLPL--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 92 altgslnRVSMLKSMLQWQ--------SREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDPRLLLADE 163
Cdd:NF040873 73 -------TVRDLVAMGRWArrglwrrlTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 493478014 164 PVASLDPSSAETVMGYLRKAAKEhDVTALVSLHQVN-IAAHF 204
Cdd:NF040873 146 PTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLElVRRAD 186
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-215 |
1.14e-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: 102.46 E-value: 1.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQY-----------GDVTALEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTdPTEGSISLDDEPITGSQT 71
Cdd:COG4172 276 LEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLrRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 72 --------EIGMIFQQHNlvdgvsaylnaltGSLN-RVS--------MLKSMLQWQSREDKLRALEALETVGLLDESHQR 134
Cdd:COG4172 355 ralrplrrRMQVVFQDPF-------------GSLSpRMTvgqiiaegLRVHGPGLSAAERRARVAEALEEVGLDPAARHR 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 135 -VSQMSGGQQQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRD 213
Cdd:COG4172 422 yPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKD 501
|
..
gi 493478014 214 GR 215
Cdd:COG4172 502 GK 503
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-214 |
1.81e-24 |
|
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: 97.33 E-value: 1.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 6 VENLSKQYGDVT-ALEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGS--QTEIGMIFQ--Q 79
Cdd:cd03226 2 IENISFSYKKGTeILDDLSLDLyAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKerRKSIGYVMQdvD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 80 HNLVdGVSAYLNALTGSLNrvsmlksmlqwqSREDKLRALEALETVGL--LDESHQRvsQMSGGQQQRVGIARALVQDPR 157
Cdd:cd03226 82 YQLF-TDSVREELLLGLKE------------LDAGNEQAETVLKDLDLyaLKERHPL--SLSGGQKQRLAIAAALLSGKD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 493478014 158 LLLADEPVASLDPSSAETVMGYLRKAAKEhDVTALVSLHQVNIAAHFGDRFIGLRDG 214
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-215 |
2.08e-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: 101.68 E-value: 2.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 1 MSTLKVENLS----KQYGDVTALEDVSFQIE-DEFAVLLGESGAGKS----TLLRCINGLTDPTEGSISLDDEPITG-SQ 70
Cdd:COG4172 4 MPLLSVEDLSvafgQGGGTVEAVKGVSFDIAaGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGlSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 71 TE--------IGMIFQQ--------HNLVDGVSAYLnALTGSLNRvsmlksmlqwqsREDKLRALEALETVGLlDESHQR 134
Cdd:COG4172 84 RElrrirgnrIAMIFQEpmtslnplHTIGKQIAEVL-RLHRGLSG------------AAARARALELLERVGI-PDPERR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 135 VS----QMSGGQQQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIG 210
Cdd:COG4172 150 LDayphQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAV 229
|
....*
gi 493478014 211 LRDGR 215
Cdd:COG4172 230 MRQGE 234
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-235 |
2.26e-24 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 101.53 E-value: 2.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 1 MSTLKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTE------I 73
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVKALDDISFDCRAgQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaalaagV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 74 GMIFQQHNLVDGVSAYLNALTGSL-NRVSMLKsmlqwqSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARAL 152
Cdd:PRK11288 82 AIIYQELHLVPEMTVAENLYLGQLpHKGGIVN------RRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 153 VQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSlHQVNIAAHFGDRFIGLRDGRK------LFDVGRDELT 226
Cdd:PRK11288 156 ARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVS-HRMEEIFALCDAITVFKDGRYvatfddMAQVDRDQLV 234
|
250
....*....|...
gi 493478014 227 PEL----IDDLYG 235
Cdd:PRK11288 235 QAMvgreIGDIYG 247
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
4-219 |
2.73e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 98.62 E-value: 2.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGD------VTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDD------EPITGSQ 70
Cdd:PRK13633 5 IKCKNVSYKYESneesteKLALDDVNLEVKKgEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsdeENLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 71 TEIGMIFQQHNlvdgvsaylNALTGSL--NRVSMLKSMLQWQSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGI 148
Cdd:PRK13633 85 NKAGMVFQNPD---------NQIVATIveEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493478014 149 ARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHfGDRFIGLRDGRKLFD 219
Cdd:PRK13633 156 AGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVME 225
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-224 |
4.73e-24 |
|
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: 101.03 E-value: 4.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQY-----GDVTALEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTDPTEGSIS--LDDEPI--------- 66
Cdd:TIGR03269 280 IKVRNVSKRYisvdrGVVKAVDNVSLEVkEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrVGDEWVdmtkpgpdg 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 67 TGSQTE-IGMIFQQHNLVDGvSAYLNALTGSLNrvsmlksmLQWQSREDKLRALEALETVGLLDESHQRV-----SQMSG 140
Cdd:TIGR03269 360 RGRAKRyIGILHQEYDLYPH-RTVLDNLTEAIG--------LELPDELARMKAVITLKMVGFDEEKAEEIldkypDELSE 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 141 GQQQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGrKLFDV 220
Cdd:TIGR03269 431 GERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDG-KIVKI 509
|
....
gi 493478014 221 GRDE 224
Cdd:TIGR03269 510 GDPE 513
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-217 |
8.69e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 97.57 E-value: 8.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 1 MST--LKVENLSKQYGDVTALEDVSFQIE-DEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITG----SQTEI 73
Cdd:PRK13537 3 MSVapIDFRNVEKRYGDKLVVDGLSFHVQrGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSrarhARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 74 GMIFQQHNLVDGVSAYLNALTgsLNRVSMLKSMlqwQSREdklRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALV 153
Cdd:PRK13537 83 GVVPQFDNLDPDFTVRENLLV--FGRYFGLSAA---AARA---LVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493478014 154 QDPRLLLADEPVASLDPSSAETVMGYLRK---AAKehdvTALVSLHQVNIAAHFGDRFIGLRDGRKL 217
Cdd:PRK13537 155 NDPDVLVLDEPTTGLDPQARHLMWERLRSllaRGK----TILLTTHFMEEAERLCDRLCVIEEGRKI 217
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
7-224 |
1.06e-23 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 100.33 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 7 ENLSKQY-GDVT-ALEDVSFQIE-DEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITgsQTE-------IGMI 76
Cdd:TIGR03375 467 RNVSFAYpGQETpALDNVSLTIRpGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIR--QIDpadlrrnIGYV 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 77 FQQHNLvdgvsaylnaLTGSLnrvsmlksmlqwqsRE---------DKLRALEALETVGLLD--ESH---------QRVS 136
Cdd:TIGR03375 545 PQDPRL----------FYGTL--------------RDnialgapyaDDEEILRAAELAGVTEfvRRHpdgldmqigERGR 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 137 QMSGGQQQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAkeHDVTALVSLHQVNIAAhFGDRFIGLRDGRK 216
Cdd:TIGR03375 601 SLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWL--AGKTLVLVTHRTSLLD-LVDRIIVMDNGRI 677
|
....*...
gi 493478014 217 LFDVGRDE 224
Cdd:TIGR03375 678 VADGPKDQ 685
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
3-172 |
2.09e-23 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 94.56 E-value: 2.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 3 TLKVENLSKQYGDVTALEDVSFQIEDEFAVLL-GESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQteigmifqqhn 81
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLtGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPD----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 82 lVDGVSAYL---NALTGSLnrvSMLKSMLQWQS--REDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDP 156
Cdd:PRK13539 71 -VAEACHYLghrNAMKPAL---TVAENLEFWAAflGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNR 146
|
170
....*....|....*.
gi 493478014 157 RLLLADEPVASLDPSS 172
Cdd:PRK13539 147 PIWILDEPTAALDAAA 162
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-215 |
2.19e-23 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 93.43 E-value: 2.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTA--LEDVSFQIE-DEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITgsqteigmifQQH 80
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEpGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADIS----------QWD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 81 nlvdgvSAYLNALTGSLnrvsmlksmLQwqsrEDKLRALEALETVglldeshqrvsqMSGGQQQRVGIARALVQDPRLLL 160
Cdd:cd03246 71 ------PNELGDHVGYL---------PQ----DDELFSGSIAENI------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 493478014 161 ADEPVASLDPSSAETVMGYLRkAAKEHDVTALVSLHQVNIAAHfGDRFIGLRDGR 215
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIA-ALKAAGATRIVIAHRPETLAS-ADRILVLEDGR 172
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1-218 |
2.33e-23 |
|
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: 94.15 E-value: 2.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 1 MSTLKVENLSKQ------YGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDP--TEGSISLDDEPITGS-- 69
Cdd:cd03213 1 GVTLSFRNLTVTvksspsKSGKQLLKNVSGKAKPgELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDKRsf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 70 QTEIGMIfQQHNLVdgvsayLNALTgslnrvsmLKSMLQWQSredKLRALealetvglldeshqrvsqmSGGQQQRVGIA 149
Cdd:cd03213 81 RKIIGYV-PQDDIL------HPTLT--------VRETLMFAA---KLRGL-------------------SGGERKRVSIA 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 150 RALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHdVTALVSLHQV-NIAAHFGDRFIGLRDGRKLF 218
Cdd:cd03213 124 LELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTG-RTIICSIHQPsSEIFELFDKLLLLSQGRVIY 192
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4-215 |
3.82e-23 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 98.08 E-value: 3.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQIE-DEFAVLLGESGAGKSTLLRCINGLTdPT---EGSISLDDEPITGS---QTE---I 73
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRaGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASnirDTEragI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 74 GMIFQQHNLVDGVSAYLNALTGS-------LNRVSMLksmlqwqsredkLRALEALETVGLLDESHQRVSQMSGGQQQRV 146
Cdd:PRK13549 85 AIIHQELALVKELSVLENIFLGNeitpggiMDYDAMY------------LRAQKLLAQLKLDINPATPVGNLGLGQQQLV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493478014 147 GIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKaAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGR 215
Cdd:PRK13549 153 EIAKALNKQARLLILDEPTASLTESETAVLLDIIRD-LKAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
18-215 |
6.30e-23 |
|
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: 93.42 E-value: 6.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 18 ALEDVSFQIE-DEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPItgSQTE-------IGMIFQQHNLVDGvSAY 89
Cdd:cd03245 19 ALDNVSLTIRaGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDI--RQLDpadlrrnIGYVPQDVTLFYG-TLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 90 LNALTGSLNrvsmlksmlqwqsrEDKLRALEALETVGLLD-----------ESHQRVSQMSGGQQQRVGIARALVQDPRL 158
Cdd:cd03245 96 DNITLGAPL--------------ADDERILRAAELAGVTDfvnkhpngldlQIGERGRGLSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 493478014 159 LLADEPVASLDPSSAETVMGYLRKAAKehDVTALVSLHQVNIAAhFGDRFIGLRDGR 215
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLLD-LVDRIIVMDSGR 215
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
2-242 |
7.53e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 94.43 E-value: 7.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 2 STLKVENLSKQY-GDVT-ALEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTE-----I 73
Cdd:PRK13648 6 SIIVFKNVSFQYqSDASfTLKDVSFNIpKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEklrkhI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 74 GMIFQ--QHNLVDGVSAYLNALtGSLNRVSMLKSMlqwqsredKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARA 151
Cdd:PRK13648 86 GIVFQnpDNQFVGSIVKYDVAF-GLENHAVPYDEM--------HRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 152 LVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHfGDRFIGLRDGrKLFDVGrdelTPELID 231
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKG-TVYKEG----TPTEIF 230
|
250
....*....|.
gi 493478014 232 DLYGSVETVGL 242
Cdd:PRK13648 231 DHAEELTRIGL 241
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
11-197 |
1.02e-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: 93.10 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 11 KQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGL---TDPTEGSISLDDEPITGSQT--EIGMIFQQHNLVD 84
Cdd:cd03234 15 NWNKYARILNDVSLHVESgQVMAILGSSGSGKTTLLDAISGRvegGGTTSGQILFNGQPRKPDQFqkCVAYVRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 85 GVSAYLNALTGSLNRVSMLKSmlqwQSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDPRLLLADEP 164
Cdd:cd03234 95 GLTVRETLTYTAILRLPRKSS----DAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190
....*....|....*....|....*....|...
gi 493478014 165 VASLDPSSAETVMGYLRKAAKEhDVTALVSLHQ 197
Cdd:cd03234 171 TSGLDSFTALNLVSTLSQLARR-NRIVILTIHQ 202
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-226 |
2.20e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 92.98 E-value: 2.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 1 MSTLKVENLSKQYGDVTALEDVSFQIEDE--FAvLLGESGAGKSTLLRCINGLTD-----PTEGSISL--------DDEP 65
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNgvFA-LMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLfgrniyspDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 66 ITgSQTEIGMIFQQHNLVDGVSAYLNALTG-SLNRvsMLKSmlqwqSREDKLRALEALETVGLLDESHQRV----SQMSG 140
Cdd:PRK14267 81 IE-VRREVGMVFQYPNPFPHLTIYDNVAIGvKLNG--LVKS-----KKELDERVEWALKKAALWDEVKDRLndypSNLSG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 141 GQQQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHdvTALVSLHQVNIAAHFGD--------RFIGLR 212
Cdd:PRK14267 153 GQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDyvaflylgKLIEVG 230
|
250
....*....|....
gi 493478014 213 DGRKLFDVGRDELT 226
Cdd:PRK14267 231 PTRKVFENPEHELT 244
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-215 |
3.23e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 92.94 E-value: 3.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 1 MSTLKVENLSKQY-GDVTALEDVSFQIEDEFAV-LLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTE-----I 73
Cdd:PRK13652 1 MHLIETRDLCYSYsGSKEALNNINFIAPRNSRIaVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIRevrkfV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 74 GMIFQQ-HNLVDGVSAYLNALTGSLNrvsmlksmLQWQSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARAL 152
Cdd:PRK13652 81 GLVFQNpDDQIFSPTVEQDIAFGPIN--------LGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493478014 153 VQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGR 215
Cdd:PRK13652 153 AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGR 215
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-230 |
5.08e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 92.03 E-value: 5.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 2 STLKVENLSKQY---GDVTALEDVSFQIEDEFAV-LLGESGAGKSTLLRCINGLTDPTEGSISLDDEPI----------- 66
Cdd:PRK14246 6 SAEDVFNISRLYlyiNDKAILKDITIKIPNNSIFgIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgkdifqida 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 67 TGSQTEIGMIFQQHNLVDGVSAYLNAltgslnrVSMLKSMLQWQSREDKLRALEALETVGLLDESHQRV----SQMSGGQ 142
Cdd:PRK14246 86 IKLRKEVGMVFQQPNPFPHLSIYDNI-------AYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLnspaSQLSGGQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 143 QQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEhdVTALVSLHQVNIAAHFGDRFIGLRDGR------- 215
Cdd:PRK14246 159 QQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGElvewgss 236
|
250
....*....|....*.
gi 493478014 216 -KLFDVGRDELTPELI 230
Cdd:PRK14246 237 nEIFTSPKNELTEKYV 252
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
4-232 |
5.77e-22 |
|
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: 91.82 E-value: 5.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEpiTGSQTEIGMI------ 76
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLyPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMR--SGAELELYQLseaerr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 77 --------FQQHNLVDGVSAYLNALTGSLNRVSMLKSMLQWQSREDKLRALEALETVglLDESHQRVSQMSGGQQQRVGI 148
Cdd:TIGR02323 82 rlmrtewgFVHQNPRDGLRMRVSAGANIGERLMAIGARHYGNIRATAQDWLEEVEID--PTRIDDLPRAFSGGMQQRLQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 149 ARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGRklfdVGRDELTPE 228
Cdd:TIGR02323 160 ARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGR----VVESGLTDQ 235
|
....
gi 493478014 229 LIDD 232
Cdd:TIGR02323 236 VLDD 239
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-234 |
6.96e-22 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 91.09 E-value: 6.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 1 MSTLKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQT------EI 73
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQgEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTakimreAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 74 GMIFQQHNLVDGVSAYLNALTGSLnrvsmLKSMLQWQSREDKLRALEALetvgLLDESHQRVSQMSGGQQQRVGIARALV 153
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMGGF-----FAERDQFQERIKWVYELFPR----LHERRIQRAGTMSGGEQQMLAIGRALM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 154 QDPRLLLADEPVASLDPSSAETVMGYLRKaAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGR-KLFDVGRDELTPELIDD 232
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQ-LREQGMTIFLVEQNANQALKLADRGYVLENGHvVLEDTGDALLANEAVRS 232
|
..
gi 493478014 233 LY 234
Cdd:PRK11614 233 AY 234
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
18-218 |
7.16e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 92.15 E-value: 7.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 18 ALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGS---------QTEIGMIFQ--QHNLV-D 84
Cdd:PRK13646 22 AIHDVNTEFEQgKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKtkdkyirpvRKRIGMVFQfpESQLFeD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 85 GVSAYLnaLTGSLNRVSMLKsmlqwqsrEDKLRALEALETVGL-LDESHQRVSQMSGGQQQRVGIARALVQDPRLLLADE 163
Cdd:PRK13646 102 TVEREI--IFGPKNFKMNLD--------EVKNYAHRLLMDLGFsRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493478014 164 PVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDG--------RKLF 218
Cdd:PRK13646 172 PTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGsivsqtspKELF 234
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4-181 |
8.34e-22 |
|
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: 90.24 E-value: 8.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTEIgmifqQHNL 82
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLaAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSI-----ARGL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 83 vdgvsAYLNALTGSLNRVSMLKSMLQWQSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDPRLLLAD 162
Cdd:cd03231 76 -----LYLGHAPGIKTTLSVLENLRFWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILD 150
|
170
....*....|....*....
gi 493478014 163 EPVASLDPSSAETVMGYLR 181
Cdd:cd03231 151 EPTTALDKAGVARFAEAMA 169
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
4-214 |
9.26e-22 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 93.56 E-value: 9.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITG---------SQTEI 73
Cdd:PRK10070 29 LSKEQILEKTGLSLGVKDASLAIEEgEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKisdaelrevRRKKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 74 GMIFQQHNLVDGVSAYLNALTGslnrvsMLKSMLQWQSREDKlrALEALETVGLLDESHQRVSQMSGGQQQRVGIARALV 153
Cdd:PRK10070 109 AMVFQSFALMPHMTVLDNTAFG------MELAGINAEERREK--ALDALRQVGLENYAHSYPDELSGGMRQRVGLARALA 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493478014 154 QDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDG 214
Cdd:PRK10070 181 INPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNG 241
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
4-225 |
9.66e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 91.69 E-value: 9.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQY---GDVTALEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQT-----EIG 74
Cdd:PRK13642 5 LEVENLVFKYekeSDVNQLNGVSFSItKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVwnlrrKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 75 MIFQQ-HNLVDGVSAYLNALTGSLNRVSMLKSMLQwqsredklRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALV 153
Cdd:PRK13642 85 MVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIK--------RVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493478014 154 QDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHfGDRFIGLRDGRKLFDVGRDEL 225
Cdd:PRK13642 157 LRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSEL 227
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1-215 |
1.07e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 91.81 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 1 MStLKVENLSKQYGDVTALE-----DVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITgSQT--- 71
Cdd:PRK13641 1 MS-IKFENVDYIYSPGTPMEkkgldNISFELEEgSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHIT-PETgnk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 72 -------EIGMIFQ--QHNLVDGvSAYLNALTGSLNrvsmlksmLQWQSREDKLRALEALETVGLLDESHQRVS-QMSGG 141
Cdd:PRK13641 79 nlkklrkKVSLVFQfpEAQLFEN-TVLKDVEFGPKN--------FGFSEDEAKEKALKWLKKVGLSEDLISKSPfELSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493478014 142 QQQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSlHQVNIAAHFGDRFIGLRDGR 215
Cdd:PRK13641 150 QMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVT-HNMDDVAEYADDVLVLEHGK 222
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-223 |
1.64e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 90.95 E-value: 1.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 1 MSTLKVENLSKQYGDVT---ALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQT----- 71
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQekyTLNDVSFHVKQgEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVwdirh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 72 EIGMIFQQ-HNLVDGVSAYLNALTGSLNRVSMLKSMlqwqsredKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIAR 150
Cdd:PRK13650 82 KIGMVFQNpDNQFVGATVEDDVAFGLENKGIPHEEM--------KERVNEALELVGMQDFKEREPARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 151 ALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAhFGDRFIGLRDG--------RKLFDVGR 222
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGqveststpRELFSRGN 232
|
.
gi 493478014 223 D 223
Cdd:PRK13650 233 D 233
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
4-214 |
1.82e-21 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 90.62 E-value: 1.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQY---------GDVTALEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPIT------ 67
Cdd:PRK15112 5 LEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLrEGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgdysy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 68 GSQtEIGMIFQQHnlvdgvsaylnalTGSLN---RVSM-------LKSMLQWQSREDklRALEALETVGLL-DESHQRVS 136
Cdd:PRK15112 85 RSQ-RIRMIFQDP-------------STSLNprqRISQildfplrLNTDLEPEQREK--QIIETLRQVGLLpDHASYYPH 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493478014 137 QMSGGQQQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDG 214
Cdd:PRK15112 149 MLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQG 226
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-172 |
2.29e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 89.95 E-value: 2.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 1 MSTLKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPIT------GSQTEI 73
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSgEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllplhaRARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 74 GMIFQQHNLVDGVSAYLNaltgsLNRVSMLKSMLQWQSREDklRALEALETVGLldeSHQRVS---QMSGGQQQRVGIAR 150
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDN-----LMAVLQIRDDLSAEQRED--RANELMEEFHI---EHLRDSmgqSLSGGERRRVEIAR 150
|
170 180
....*....|....*....|..
gi 493478014 151 ALVQDPRLLLADEPVASLDPSS 172
Cdd:PRK10895 151 ALAANPKFILLDEPFAGVDPIS 172
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-210 |
2.89e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 90.10 E-value: 2.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTD-----PTEGSISLDDEPITGSQT------ 71
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIyQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIYERRVnlnrlr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 72 -EIGMIFQQHNLVDgVSAYLNALTGSlnrvsmlkSMLQWQSREDKLRALE-ALETVGLLDES----HQRVSQMSGGQQQR 145
Cdd:PRK14258 88 rQVSMVHPKPNLFP-MSVYDNVAYGV--------KIVGWRPKLEIDDIVEsALKDADLWDEIkhkiHKSALDLSGGQQQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493478014 146 VGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALV---SLHQVNIAAHFGDRFIG 210
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIvshNLHQVSRLSDFTAFFKG 226
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-217 |
3.34e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 90.24 E-value: 3.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 2 STLKVENLSKQYGD--VTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGS--------ISLDDEPITGSQ 70
Cdd:PRK13640 4 NIVEFKHVSFTYPDskKPALNDISFSIPRgSWTALIGHNGSGKSTISKLINGLLLPDDNPnskitvdgITLTAKTVWDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 71 TEIGMIFQQ-HNLVDGVSAYLNALTGSLNRVSmlksmlqwqSREDKLRAL-EALETVGLLDESHQRVSQMSGGQQQRVGI 148
Cdd:PRK13640 84 EKVGIVFQNpDNQFVGATVGDDVAFGLENRAV---------PRPEMIKIVrDVLADVGMLDYIDSEPANLSGGQKQRVAI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493478014 149 ARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHfGDRFIGLRDGRKL 217
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLL 222
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
4-230 |
5.83e-21 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 91.77 E-value: 5.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTdPT---EGSISLDDEP-----ITGSQTE-I 73
Cdd:NF040905 2 LEMRGITKTFPGVKALDDVNLSVREgEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEVcrfkdIRDSEALgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 74 GMIFQQHNLVDGVSAYLNALTGslNRVSMlKSMLQWqsREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALV 153
Cdd:NF040905 81 VIIHQELALIPYLSIAENIFLG--NERAK-RGVIDW--NETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493478014 154 QDPRLLLADEPVASLDPSSAETVMGYLRKaAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGR--KLFDVGRDELTPELI 230
Cdd:NF040905 156 KDVKLLILDEPTAALNEEDSAALLDLLLE-LKAQGITSIIISHKLNEIRRVADSITVLRDGRtiETLDCRADEVTEDRI 233
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4-232 |
6.71e-21 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 88.83 E-value: 6.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGS------------- 69
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLyPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRdlyalseaerrrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 70 -QTEIGMIFQqhNLVDG----VSAYLNalTGSlnrvsmlKSMLQWQSREDKLR--ALEALETVGL-LDESHQRVSQMSGG 141
Cdd:PRK11701 87 lRTEWGFVHQ--HPRDGlrmqVSAGGN--IGE-------RLMAVGARHYGDIRatAGDWLERVEIdAARIDDLPTTFSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 142 QQQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGRklfdVG 221
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGR----VV 231
|
250
....*....|.
gi 493478014 222 RDELTPELIDD 232
Cdd:PRK11701 232 ESGLTDQVLDD 242
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
5-195 |
9.91e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 88.89 E-value: 9.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 5 KVENLSKQYGDVT--ALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLD-----DEPITGSQTEIGMI 76
Cdd:PRK13632 9 KVENVSFSYPNSEnnALKNVSFEINEgEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDgitisKENLKEIRKKIGII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 77 FQQ-HNLVDGVSAYLNALTGSLNRVSMLKSMlqwqsredKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQD 155
Cdd:PRK13632 89 FQNpDNQFIGATVEDDIAFGLENKKVPPKKM--------KDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 493478014 156 PRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTaLVSL 195
Cdd:PRK13632 161 PEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKT-LISI 199
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
7-215 |
1.76e-20 |
|
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: 87.29 E-value: 1.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 7 ENLSKQYGD-VTALEDVSFQIEDEFAV-LLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTE-----IGMIFQQ 79
Cdd:cd03253 4 ENVTFAYDPgRPVLKDVSFTIPAGKKVaIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDslrraIGVVPQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 80 HNLVDGVSAYlNALTGSLN--RVSMLKSMLQWQSREDKLRALEALET-VGlldeshQRVSQMSGGQQQRVGIARALVQDP 156
Cdd:cd03253 84 TVLFNDTIGY-NIRYGRPDatDEEVIEAAKAAQIHDKIMRFPDGYDTiVG------ERGLKLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 493478014 157 RLLLADEPVASLDPSSAETVMGYLRKAAKehDVTALVSLHQVNIAAHfGDRFIGLRDGR 215
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGR 212
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
4-230 |
2.11e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 90.15 E-value: 2.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQY-----------GDVTALEDVSFQIE-DEFAVLLGESGAGKST----LLRCINgltdpTEGSISLDDEPIT 67
Cdd:PRK15134 276 LDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRpGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLH 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 68 G--------SQTEIGMIFQQHNlvdgvsaylNALTGSLNRVSMLKSMLQ-----WQSREDKLRALEALETVGLLDESHQR 134
Cdd:PRK15134 351 NlnrrqllpVRHRIQVVFQDPN---------SSLNPRLNVLQIIEEGLRvhqptLSAAQREQQVIAVMEEVGLDPETRHR 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 135 V-SQMSGGQQQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRD 213
Cdd:PRK15134 422 YpAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQ 501
|
250 260
....*....|....*....|....*
gi 493478014 214 G--------RKLFDVGRDELTPELI 230
Cdd:PRK15134 502 GevveqgdcERVFAAPQQEYTRQLL 526
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
8-219 |
2.21e-20 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 89.16 E-value: 2.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 8 NLSKQYGDVTAleDVSFQIEDE-FAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTE---------IGMIF 77
Cdd:PRK11144 5 NFKQQLGDLCL--TVNLTLPAQgITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGiclppekrrIGYVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 78 QQHNL-----VDGvsaylNALTGslnrvsMLKSMlqwQSREDKLRALEALETvgLLDeshqRV-SQMSGGQQQRVGIARA 151
Cdd:PRK11144 83 QDARLfphykVRG-----NLRYG------MAKSM---VAQFDKIVALLGIEP--LLD----RYpGSLSGGEKQRVAIGRA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 152 LVQDPRLLLADEPVASLD-PSSAEtVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGR-KLFD 219
Cdd:PRK11144 143 LLTAPELLLMDEPLASLDlPRKRE-LLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKvKAFG 211
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-215 |
4.93e-20 |
|
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: 89.11 E-value: 4.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQIE-DEFAVLLGESGAGKSTLLRCINGL--TDPTEGSISLDDEPITGS---QTE---IG 74
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRpGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASnirDTEragIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 75 MIFQQHNLVDGVSAYLNALTGslNRVSMLKSMLQWQsrEDKLRALEALETVGLLDESHQR-VSQMSGGQQQRVGIARALV 153
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIFLG--NEITLPGGRMAYN--AMYLRAKNLLRELQLDADNVTRpVGDYGGGQQQLVEIAKALN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493478014 154 QDPRLLLADEPVASLDPSSAETVMGYLRKaAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGR 215
Cdd:TIGR02633 158 KQARLLILDEPSSSLTEKETEILLDIIRD-LKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
15-196 |
5.15e-20 |
|
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: 86.05 E-value: 5.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 15 DVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITG-------SQteIGMIFQQHNLVDGv 86
Cdd:cd03249 15 DVPILKGLSLTIPPgKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlnlrwlrSQ--IGLVSQEPVLFDG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 87 SAYLNALTGSLNRVSmlksmlqwQSREDKLRALEALETVGLLDESH-----QRVSQMSGGQQQRVGIARALVQDPRLLLA 161
Cdd:cd03249 92 TIAENIRYGKPDATD--------EEVEEAAKKANIHDFIMSLPDGYdtlvgERGSQLSGGQKQRIAIARALLRNPKILLL 163
|
170 180 190
....*....|....*....|....*....|....*
gi 493478014 162 DEPVASLDPSSAETVMGYLRKAAKehDVTALVSLH 196
Cdd:cd03249 164 DEATSALDAESEKLVQEALDRAMK--GRTTIVIAH 196
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-214 |
5.17e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 89.10 E-value: 5.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 2 STLKVENLSKQYGDVTAL-EDVSFQIEDEFAVLL-GESGAGKSTLLRCINGLTDPTEGSISLDDEpitgsqteIGMIF-- 77
Cdd:COG4178 361 GALALEDLTLRTPDGRPLlEDLSLSLKPGERLLItGPSGSGKSTLLRAIAGLWPYGSGRIARPAG--------ARVLFlp 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 78 QQhnlvdgvsAYLnaLTGSLnrvsmlKSML---QWQSREDKLRALEALETVGL------LDESHQRVSQMSGGQQQRVGI 148
Cdd:COG4178 433 QR--------PYL--PLGTL------REALlypATAEAFSDAELREALEAVGLghlaerLDEEADWDQVLSLGEQQRLAF 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493478014 149 ARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEhdvTALVSL-HQVNIAAHFgDRFIGLRDG 214
Cdd:COG4178 497 ARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPG---TTVISVgHRSTLAAFH-DRVLELTGD 559
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-215 |
7.56e-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: 7.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGD--VTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQ-----TEIGM 75
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAgETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTlaslrRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 76 IFQQHNLVDGVSAYlNALTGSLNrvsmlksmlqwQSREDKLRALE---ALETVGLLDESHQ-----RVSQMSGGQQQRVG 147
Cdd:cd03251 81 VSQDVFLFNDTVAE-NIAYGRPG-----------ATREEVEEAARaanAHEFIMELPEGYDtvigeRGVKLSGGQRQRIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493478014 148 IARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKehDVTALVSLHQVNIAAHfGDRFIGLRDGR 215
Cdd:cd03251 149 IARALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLEDGK 213
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
19-235 |
7.66e-20 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 86.42 E-value: 7.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 19 LEDVSFQIE-DEFAVLLGESGAGKSTLLRCING-LTDPTE-------GSISLDDEPITG--------------SQTEIGM 75
Cdd:PRK13547 17 LRDLSLRIEpGRVTALLGRNGAGKSTLLKALAGdLTGGGAprgarvtGDVTLNGEPLAAidaprlarlravlpQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 76 IFQQHNLVDgVSAYLNALTGSLnrvsmlksmlqwQSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQ- 154
Cdd:PRK13547 97 AFSAREIVL-LGRYPHARRAGA------------LTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQl 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 155 --------DPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGRKLFD-VGRDEL 225
Cdd:PRK13547 164 wpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHgAPADVL 243
|
250
....*....|
gi 493478014 226 TPELIDDLYG 235
Cdd:PRK13547 244 TPAHIARCYG 253
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-215 |
8.42e-20 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 84.29 E-value: 8.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYG--DVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPItgsqteigmifqqH 80
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQgEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPV-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 81 NLVDGVSAYLNALTgslNRVSMLKSMLqwqsredklraleaLETVGLldeshqrvsQMSGGQQQRVGIARALVQDPRLLL 160
Cdd:cd03247 68 DLEKALSSLISVLN---QRPYLFDTTL--------------RNNLGR---------RFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 493478014 161 ADEPVASLDPSSAETVMGYLRKAAKEHdvTALVSLHQVNIAAHFgDRFIGLRDGR 215
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDK--TLIWITHHLTGIEHM-DKILFLENGK 173
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
19-235 |
9.80e-20 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 85.66 E-value: 9.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 19 LEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTdPTEGSISLDDEPITG-SQTEI----GMIFQQHNLVDG--VSAYL 90
Cdd:COG4138 12 LGPISAQVNAgELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDwSAAELarhrAYLSQQQSPPFAmpVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 91 nALTGSLNRVSmlksmlqwqsrEDKLRALEAL-ETVGLLDESHQRVSQMSGGQQQRVGIARALVQ-------DPRLLLAD 162
Cdd:COG4138 91 -ALHQPAGASS-----------EAVEQLLAQLaEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493478014 163 EPVASLDPSSAETVMGYLRKAAkEHDVTALVSLHQVNIAAHFGDRFIGLRDGRKLFDVGRDE-LTPELIDDLYG 235
Cdd:COG4138 159 EPMNSLDVAQQAALDRLLRELC-QQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEvMTPENLSEVFG 231
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-215 |
1.54e-19 |
|
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: 87.85 E-value: 1.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYG--DVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPIT-----GSQTEIGM 75
Cdd:TIGR02203 331 VEFRNVTFRYPgrDRPALDSISLVIEPgETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLAdytlaSLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 76 IFQQHNLVDGVSAYlNALTGSLNRVSMLKSmlqwqsrEDKLRALEALETVGLLDES-HQRV----SQMSGGQQQRVGIAR 150
Cdd:TIGR02203 411 VSQDVVLFNDTIAN-NIAYGRTEQADRAEI-------ERALAAAYAQDFVDKLPLGlDTPIgengVLLSGGQRQRLAIAR 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493478014 151 ALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHdvTALVSLHQVNIAAHfGDRFIGLRDGR 215
Cdd:TIGR02203 483 ALLKDAPILILDEATSALDNESERLVQAALERLMQGR--TTLVIAHRLSTIEK-ADRIVVMDDGR 544
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
4-197 |
1.57e-19 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 84.09 E-value: 1.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTEigmiFQQhNL 82
Cdd:PRK13538 2 LEARNLACERDERILFSGLSFTLNAgELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE----YHQ-DL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 83 vdgvsAYLNALTG------SLNRVSMLKSMLQWQSREDklrALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDP 156
Cdd:PRK13538 77 -----LYLGHQPGikteltALENLRFYQRLHGPGDDEA---LWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 493478014 157 RLLLADEPVASLDPSSAETVMGYLRKAAkEHDVTALVSLHQ 197
Cdd:PRK13538 149 PLWILDEPFTAIDKQGVARLEALLAQHA-EQGGMVILTTHQ 188
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
4-211 |
4.16e-19 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 83.22 E-value: 4.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQIE-DEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTE-----IGMIF 77
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRaGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEiyrqqVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 78 QQHNLVdGVSAYLNALtgslnrvsmlksmLQWQSRE---DKLRALEALETVGLLDES-HQRVSQMSGGQQQRVGIARALV 153
Cdd:PRK10247 88 QTPTLF-GDTVYDNLI-------------FPWQIRNqqpDPAIFLDDLERFALPDTIlTKNIAELSGGEKQRISLIRNLQ 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 493478014 154 QDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHfGDRFIGL 211
Cdd:PRK10247 154 FMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKVITL 210
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-238 |
5.35e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 83.99 E-value: 5.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 8 NLSKQYGDVTALEDVSFQIEDEFAV-LLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGS-----------QTEIGM 75
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTsLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRsifnyrdvlefRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 76 IFQQHNLVDgVSAYLNALTGslnrvsmLKSMLQWQSREDKLRALEALETVGLLDESHQRVS----QMSGGQQQRVGIARA 151
Cdd:PRK14271 106 LFQRPNPFP-MSIMDNVLAG-------VRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSdspfRLSGGQQQLLCLART 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 152 LVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEhdVTALVSLHQVNIAAHFGDRFIGLRDGR--------KLFDVGRD 223
Cdd:PRK14271 178 LAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRlveegpteQLFSSPKH 255
|
250
....*....|....*
gi 493478014 224 ELTPELIDDLYGSVE 238
Cdd:PRK14271 256 AETARYVAGLSGDVK 270
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
3-183 |
6.70e-19 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 85.88 E-value: 6.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 3 TLKVENLSKQY-GDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPI-TGSQTEIGMI--- 76
Cdd:TIGR02868 334 TLELRDLSAGYpGAPPVLDGVSLDLPPgERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVsSLDQDEVRRRvsv 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 77 FQQHNLVDGVSAYLNALTGSLNrvsmlksmlqwQSREDklrALEALETVGLLD-----------ESHQRVSQMSGGQQQR 145
Cdd:TIGR02868 414 CAQDAHLFDTTVRENLRLARPD-----------ATDEE---LWAALERVGLADwlralpdgldtVLGEGGARLSGGERQR 479
|
170 180 190
....*....|....*....|....*....|....*...
gi 493478014 146 VGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKA 183
Cdd:TIGR02868 480 LALARALLADAPILLLDEPTEHLDAETADELLEDLLAA 517
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-174 |
7.61e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 85.89 E-value: 7.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQIE-DEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLddepitGSQTEIGmIFQQHNl 82
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDrGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL------GETVKIG-YFDQHQ- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 83 vdgvsAYLNaltgsLNrvsmlKSMLQWQSRE-DKLRALEALETVGLL----DESHQRVSQMSGGQQQRVGIARALVQDPR 157
Cdd:COG0488 388 -----EELD-----PD-----KTVLDELRDGaPGGTEQEVRGYLGRFlfsgDDAFKPVGVLSGGEKARLALAKLLLSPPN 452
|
170
....*....|....*..
gi 493478014 158 LLLADEPVASLDPSSAE 174
Cdd:COG0488 453 VLLLDEPTNHLDIETLE 469
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-215 |
9.31e-19 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 84.39 E-value: 9.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 1 MSTLKVENLSKQY----GDVTALEDVSFQIE-DEFAVLLGESGAGKSTLLRCINGLTDP---TEGSISLDDEPITGSQT- 71
Cdd:PRK09473 10 DALLDVKDLRVTFstpdGDVTAVNDLNFSLRaGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPEk 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 72 --------EIGMIFQqhnlvdgvsaylNALTgSLN---RVS-MLKSMLQWQSREDKLRALEalETVGLLD-----ESHQR 134
Cdd:PRK09473 90 elnklraeQISMIFQ------------DPMT-SLNpymRVGeQLMEVLMLHKGMSKAEAFE--ESVRMLDavkmpEARKR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 135 VS----QMSGGQQQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIG 210
Cdd:PRK09473 155 MKmyphEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLV 234
|
....*
gi 493478014 211 LRDGR 215
Cdd:PRK09473 235 MYAGR 239
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-182 |
1.13e-18 |
|
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: 80.19 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQIE-DEFAVLLGESGAGKSTLLRCINGLTDPTEGSIslddepITGSQTEIGmifqqhnl 82
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINpGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV------TWGSTVKIG-------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 83 vdgvsaYLnaltgslnrvsmlksmlqwqsredklralealetvglldeshqrvSQMSGGQQQRVGIARALVQDPRLLLAD 162
Cdd:cd03221 67 ------YF---------------------------------------------EQLSGGEKMRLALAKLLLENPNLLLLD 95
|
170 180
....*....|....*....|
gi 493478014 163 EPVASLDPSSAETVMGYLRK 182
Cdd:cd03221 96 EPTNHLDLESIEALEEALKE 115
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
17-200 |
1.29e-18 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 81.93 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 17 TALEDVSFQIED-EFAVLLGESGAGKSTLLRCING--LTDPTEGSISLDDEPITgsqteigmifQQHNLVDGVSaylnal 93
Cdd:COG2401 44 YVLRDLNLEIEPgEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVPDNQFG----------REASLIDAIG------ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 94 tgslnrvsmlksmlqwqSREDKLRALEALETVGLLDES--HQRVSQMSGGQQQRVGIARALVQDPRLLLADEPVASLDPS 171
Cdd:COG2401 108 -----------------RKGDFKDAVELLNAVGLSDAVlwLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180
....*....|....*....|....*....
gi 493478014 172 SAETVMGYLRKAAKEHDVTALVSLHQVNI 200
Cdd:COG2401 171 TAKRVARNLQKLARRAGITLVVATHHYDV 199
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
17-206 |
1.63e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 82.62 E-value: 1.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 17 TALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGS--QTEIGMIFQQHNlVDGVSAYLNAL 93
Cdd:PRK15056 21 TALRDASFTVPGgSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQAlqKNLVAYVPQSEE-VDWSFPVLVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 94 TGSLNRVSMLkSMLQWQSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDPRLLLADEPVASLDPSSA 173
Cdd:PRK15056 100 VVMMGRYGHM-GWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTE 178
|
170 180 190
....*....|....*....|....*....|...
gi 493478014 174 ETVMGYLRKAAKEHDvTALVSLHQVNIAAHFGD 206
Cdd:PRK15056 179 ARIISLLRELRDEGK-TMLVSTHNLGSVTEFCD 210
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-169 |
1.91e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 82.08 E-value: 1.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 1 MSTL-KVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDepitgsQTEIGMIFQ 78
Cdd:PRK09544 1 MTSLvSLENVSVSFGQRRVLSDVSLELKPgKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG------KLRIGYVPQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 79 QhnlvdgvsAYLNA-LTGSLNRVSMLKSMLQwqsREDKLRALEALETVGLLDESHQRvsqMSGGQQQRVGIARALVQDPR 157
Cdd:PRK09544 75 K--------LYLDTtLPLTVNRFLRLRPGTK---KEDILPALKRVQAGHLIDAPMQK---LSGGETQRVLLARALLNRPQ 140
|
170
....*....|..
gi 493478014 158 LLLADEPVASLD 169
Cdd:PRK09544 141 LLVLDEPTQGVD 152
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
18-215 |
2.06e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 82.48 E-value: 2.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 18 ALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGS---------QTEIGMIFQ--QHNLVDG 85
Cdd:PRK13649 22 ALFDVNLTIEDgSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkdikqiRKKVGLVFQfpESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 86 VsaylnaltgSLNRVSMLKSMLQWQSREDKLRALEALETVGLLDESHQRVS-QMSGGQQQRVGIARALVQDPRLLLADEP 164
Cdd:PRK13649 102 T---------VLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLFEKNPfELSGGQMRRVAIAGILAMEPKILVLDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 493478014 165 VASLDPSSAETVMGYLRKAAKEHDVTALVSlHQVNIAAHFGDRFIGLRDGR 215
Cdd:PRK13649 173 TAGLDPKGRKELMTLFKKLHQSGMTIVLVT-HLMDDVANYADFVYVLEKGK 222
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-215 |
2.11e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 82.98 E-value: 2.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLS-----KQYGDVTALEDVSFQIE-DEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDD---------EPITG 68
Cdd:PRK13631 22 LRVKNLYcvfdeKQENELVALNNISYTFEkNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigdkknnHELIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 69 SQTE------------IGMIFQ--QHNLvdgvsaylnaLTGSLNRVSMLKSMLQWQSRED-KLRALEALETVGLlDESHQ 133
Cdd:PRK13631 102 NPYSkkiknfkelrrrVSMVFQfpEYQL----------FKDTIEKDIMFGPVALGVKKSEaKKLAKFYLNKMGL-DDSYL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 134 RVS--QMSGGQQQRVGIARALVQDPRLLLADEPVASLDPsSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGL 211
Cdd:PRK13631 171 ERSpfGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDP-KGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVM 249
|
....
gi 493478014 212 RDGR 215
Cdd:PRK13631 250 DKGK 253
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
18-225 |
2.68e-18 |
|
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: 81.38 E-value: 2.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 18 ALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPI-----TGSQTEIGMIFQQHNLVDGVSAYLN 91
Cdd:cd03252 17 ILDNISLRIKPgEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLaladpAWLRRQVGVVLQENVLFNRSIRDNI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 92 ALTG---SLNRVSMLKSMLQWQSREDKLRalEALET-VGlldeshQRVSQMSGGQQQRVGIARALVQDPRLLLADEPVAS 167
Cdd:cd03252 97 ALADpgmSMERVIEAAKLAGAHDFISELP--EGYDTiVG------EQGAGLSGGQRQRIAIARALIHNPRILIFDEATSA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 493478014 168 LDPSSAETVMGYLRKAAKEHdvTALVSLHQVNiAAHFGDRFIGLRDGRKLFDVGRDEL 225
Cdd:cd03252 169 LDYESEHAIMRNMHDICAGR--TVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-208 |
4.41e-18 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 82.26 E-value: 4.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 1 MSTLKVENLS----KQYGDVTALEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTDP----TEGSISLDDE------- 64
Cdd:COG4170 1 MPLLDIRNLTieidTPQGRVKAVDRVSLTLnEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIdllklsp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 65 ----PITGSqtEIGMIFQQHnlvdgvSAYL--NALTGSLNRVSMLKSMLQ---WQSRED-KLRALEALETVGLLDesHQR 134
Cdd:COG4170 81 rerrKIIGR--EIAMIFQEP------SSCLdpSAKIGDQLIEAIPSWTFKgkwWQRFKWrKKRAIELLHRVGIKD--HKD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493478014 135 V-----SQMSGGQQQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRF 208
Cdd:COG4170 151 ImnsypHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTI 229
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-215 |
4.48e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 83.72 E-value: 4.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVT--ALEDVSFQIE-DEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITG---SQTEIGMIF 77
Cdd:PRK11160 339 LTLNNVSFTYPDQPqpVLKGLSLQIKaGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADyseAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 78 qqhnlvdgVSAYLNALTGSLnRVSMLksMLQWQSREDKLraLEALETVGL--LDESHQRVS--------QMSGGQQQRVG 147
Cdd:PRK11160 419 --------VSQRVHLFSATL-RDNLL--LAAPNASDEAL--IEVLQQVGLekLLEDDKGLNawlgeggrQLSGGEQRRLG 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493478014 148 IARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKehDVTALVSLHQVNIAAHFgDRFIGLRDGR 215
Cdd:PRK11160 486 IARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQF-DRICVMDNGQ 550
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
18-214 |
1.30e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 80.55 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 18 ALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGS--QTEIGMIFQQHNLVDGVSAYLNALT 94
Cdd:PRK13643 21 ALFDIDLEVKKgSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTskQKEIKPVRKKVGVVFQFPESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 95 GSLNRVSMLKSMLQWQSREDKLRALEALETVGLLDESHQRVS-QMSGGQQQRVGIARALVQDPRLLLADEPVASLDPSSA 173
Cdd:PRK13643 101 TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPfELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKAR 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 493478014 174 ETVMGYLRKAAKEHDVTALVSlHQVNIAAHFGDRFIGLRDG 214
Cdd:PRK13643 181 IEMMQLFESIHQSGQTVVLVT-HLMDDVADYADYVYLLEKG 220
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4-219 |
1.39e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 80.52 E-value: 1.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYG-----DVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSIS--LDDEPITGSQTEIGM 75
Cdd:PRK13651 3 IKVKNIVKIFNkklptELKALDNVSVEINQgEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwiFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 76 IFQQHNLVDGVSAYLNALTGSLNRVSMLKSMLQWQ--------------------SREDKLRALEALETVGLlDESHQRV 135
Cdd:PRK13651 83 VLEKLVIQKTRFKKIKKIKEIRRRVGVVFQFAEYQlfeqtiekdiifgpvsmgvsKEEAKKRAAKYIELVGL-DESYLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 136 S--QMSGGQQQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSlHQVNIAAHFGDRFIGLRD 213
Cdd:PRK13651 162 SpfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVT-HDLDNVLEWTKRTIFFKD 240
|
....*.
gi 493478014 214 GRKLFD 219
Cdd:PRK13651 241 GKIIKD 246
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
27-250 |
1.51e-17 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 82.37 E-value: 1.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 27 EDEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGS----QTEIGMIfQQHNLVdgvsayLNALTgsLNRVSM 102
Cdd:TIGR01257 955 ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNldavRQSLGMC-PQHNIL------FHHLT--VAEHIL 1025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 103 LKSMLQWQSREDKLRALEA-LETVGLLDESHQRVSQMSGGQQQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLR 181
Cdd:TIGR01257 1026 FYAQLKGRSWEEAQLEMEAmLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLL 1105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493478014 182 KAAKEHdvTALVSLHQVNIAAHFGDRFIGLRDGRkLFDVGrdelTPELIDDLYGSVETVGLADQEKTVE 250
Cdd:TIGR01257 1106 KYRSGR--TIIMSTHHMDEADLLGDRIAIISQGR-LYCSG----TPLFLKNCFGTGFYLTLVRKMKNIQ 1167
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
29-197 |
1.62e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 82.02 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 29 EFAVLLGESGAGKSTLL-----RCINGLTdpTEGSISLDDEPITGSQ-TEIGMIFQQHNLvdgvsaYLNALTG--SLNRV 100
Cdd:TIGR00955 52 ELLAVMGSSGAGKTTLMnalafRSPKGVK--GSGSVLLNGMPIDAKEmRAISAYVQQDDL------FIPTLTVreHLMFQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 101 SMLKSMLQWQSREDKLRALEALETVGLLDESHQRVSQ------MSGGQQQRVGIARALVQDPRLLLADEPVASLDPSSAE 174
Cdd:TIGR00955 124 AHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAY 203
|
170 180
....*....|....*....|...
gi 493478014 175 TVMGYLRKAAKEHDvTALVSLHQ 197
Cdd:TIGR00955 204 SVVQVLKGLAQKGK-TIICTIHQ 225
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
4-215 |
1.94e-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: 79.05 E-value: 1.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQY---GDVTALEDVSFQIE-DEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTE-----IG 74
Cdd:cd03248 12 VKFQNVTFAYptrPDTLVLQDVSFTLHpGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylhskVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 75 MIFQQHNLVDGVSAylNALTGSLNRVSM--LKSMLQWQSREDKLRALEAletvGLLDESHQRVSQMSGGQQQRVGIARAL 152
Cdd:cd03248 92 LVGQEPVLFARSLQ--DNIAYGLQSCSFecVKEAAQKAHAHSFISELAS----GYDTEVGEKGSQLSGGQKQRVAIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493478014 153 VQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHdvTALVSLHQVNIAAHfGDRFIGLRDGR 215
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVER-ADQILVLDGGR 225
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-215 |
5.22e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 80.52 E-value: 5.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 1 MSTLKVENLS---KQYGDV-TALEDVSFQIE-DEFAVLLGESGAGKS-TLLRCINGLTDP----TEGSISLD-------D 63
Cdd:PRK15134 3 QPLLAIENLSvafRQQQTVrTVVNDVSLQIEaGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHgesllhaS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 64 EP----ITGSQteIGMIFQQ--------HNLVDGVSAYLnaltgSLNRvsmlkSMLQWQSREDklrALEALETVG----- 126
Cdd:PRK15134 83 EQtlrgVRGNK--IAMIFQEpmvslnplHTLEKQLYEVL-----SLHR-----GMRREAARGE---ILNCLDRVGirqaa 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 127 --LLDESHQrvsqMSGGQQQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHF 204
Cdd:PRK15134 148 krLTDYPHQ----LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKL 223
|
250
....*....|.
gi 493478014 205 GDRFIGLRDGR 215
Cdd:PRK15134 224 ADRVAVMQNGR 234
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-230 |
5.43e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 80.07 E-value: 5.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLS-KQYGDVTALEDVSFQIedeFAvllGE-------SGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQT---- 71
Cdd:COG3845 258 LEVENLSvRDDRGVPALKDVSLEV---RA---GEilgiagvAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPrerr 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 72 EIGMIF-----QQHNLVDGVSAYLNALTGSLNRVSMLKS-MLQWqsredklRALEALeTVGLLDE-------SHQRVSQM 138
Cdd:COG3845 332 RLGVAYipedrLGRGLVPDMSVAENLILGRYRRPPFSRGgFLDR-------KAIRAF-AEELIEEfdvrtpgPDTPARSL 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 139 SGGQQQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHdvTA--LVS--LHQV-NIAahfgDRFIGLRD 213
Cdd:COG3845 404 SGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAG--AAvlLISedLDEIlALS----DRIAVMYE 477
|
250
....*....|....*..
gi 493478014 214 GRKLFDVGRDELTPELI 230
Cdd:COG3845 478 GRIVGEVPAAEATREEI 494
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
5-225 |
7.07e-17 |
|
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: 77.27 E-value: 7.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 5 KVENLSKQY-GDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGS-----QTEIGMIF 77
Cdd:cd03254 4 EFENVNFSYdEKKPVLKDINFSIKPgETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIsrkslRSMIGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 78 QQHNLVDGvSAYLNALTGSLNrvsmlksmlqwqSREDKLraLEALETVGLLD-----------ESHQRVSQMSGGQQQRV 146
Cdd:cd03254 84 QDTFLFSG-TIMENIRLGRPN------------ATDEEV--IEAAKEAGAHDfimklpngydtVLGENGGNLSQGERQLL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493478014 147 GIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKehDVTALVSLHQVNIAAHfGDRFIGLRDGRKLFDVGRDEL 225
Cdd:cd03254 149 AIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDEL 224
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-215 |
8.26e-17 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 77.15 E-value: 8.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGD--VTALEDVSFQIEDEFAV-LLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTE-----IGM 75
Cdd:cd03244 3 IEFKNVSLRYRPnlPPVLKNISFSIKPGEKVgIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHdlrsrISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 76 IFQQHNLVDG-VSAYLNALTgslnrvsmlksmlqwQSREDKLraLEALETVGLLDeshqRVSQMSG-------------- 140
Cdd:cd03244 83 IPQDPVLFSGtIRSNLDPFG---------------EYSDEEL--WQALERVGLKE----FVESLPGgldtvveeggenls 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493478014 141 -GQQQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKehDVTALVSLHQVNIAAHFgDRFIGLRDGR 215
Cdd:cd03244 142 vGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFK--DCTVLTIAHRLDTIIDS-DRILVLDKGR 214
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
15-201 |
1.71e-16 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 79.00 E-value: 1.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 15 DVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQ-----TEIGMIFQQHNLVDGvSA 88
Cdd:TIGR00958 493 DVPVLKGLTFTLHPgEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDhhylhRQVALVGQEPVLFSG-SV 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 89 YLNALTGsLNRVSMlkSMLQWQSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDPRLLLADEPVASL 168
Cdd:TIGR00958 572 RENIAYG-LTDTPD--EEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSAL 648
|
170 180 190
....*....|....*....|....*....|...
gi 493478014 169 DPSSAETVmGYLRKAAkehDVTALVSLHQVNIA 201
Cdd:TIGR00958 649 DAECEQLL-QESRSRA---SRTVLLIAHRLSTV 677
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-243 |
2.22e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 76.95 E-value: 2.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVT-ALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSI------SLDDEPITGSQTEIGM 75
Cdd:PRK13644 2 IRLENVSYSYPDGTpALENINLVIKKgEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlvsgidTGDFSKLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 76 IFQqhnlvdgvsaylNALTGSLNR-----VSMLKSMLQWQSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIAR 150
Cdd:PRK13644 82 VFQ------------NPETQFVGRtveedLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 151 ALVQDPRLLLADEPVASLDPSSAETVMGYLRKaAKEHDVTALVSLHQVNiAAHFGDRFIGLRDGRKLFdvgrdELTPE-L 229
Cdd:PRK13644 150 ILTMEPECLIFDEVTSMLDPDSGIAVLERIKK-LHEKGKTIVYITHNLE-ELHDADRIIVMDRGKIVL-----EGEPEnV 222
|
250
....*....|....
gi 493478014 230 IDDLygSVETVGLA 243
Cdd:PRK13644 223 LSDV--SLQTLGLT 234
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
4-215 |
3.54e-16 |
|
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: 77.87 E-value: 3.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQY--GDVTALEDVSFQIE-DEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITG-SQTEIGMIF-- 77
Cdd:COG4618 331 LSVENLTVVPpgSKRPILRGVSFSLEpGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQwDREELGRHIgy 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 78 --QQHNLVDGvsaylnalTGSLNrVSMLKSMlqwqsreDKLRALEALETVGLldesHQRVSQM---------------SG 140
Cdd:COG4618 411 lpQDVELFDG--------TIAEN-IARFGDA-------DPEKVVAAAKLAGV----HEMILRLpdgydtrigeggarlSG 470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493478014 141 GQQQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRkAAKEHDVTALVSLHQVNIAAHFgDRFIGLRDGR 215
Cdd:COG4618 471 GQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIR-ALKARGATVVVITHRPSLLAAV-DKLLVLRDGR 543
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
3-226 |
3.83e-16 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 77.77 E-value: 3.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 3 TLKVENLS--KQYGDVTALEDVSFQIE-DEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTE-----IG 74
Cdd:TIGR01842 316 HLSVENVTivPPGGKKPTLRGISFSLQaGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDREtfgkhIG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 75 MIFQQHNLVDGVSAylnaltgslNRVSMLKSMLQWQSREDKLRALEALETVGLLDESHQRV-----SQMSGGQQQRVGIA 149
Cdd:TIGR01842 396 YLPQDVELFPGTVA---------ENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVigpggATLSGGQRQRIALA 466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493478014 150 RALVQDPRLLLADEPVASLDPSSAETVMGYLrKAAKEHDVTALVSLHQVNIAAhFGDRFIGLRDGR-KLFDVGRDELT 226
Cdd:TIGR01842 467 RALYGDPKLVVLDEPNSNLDEEGEQALANAI-KALKARGITVVVITHRPSLLG-CVDKILVLQDGRiARFGERDEVLA 542
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
9-209 |
5.68e-16 |
|
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: 75.14 E-value: 5.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 9 LSKQYGDVT-ALEDVSFQiEDEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTEIGMIFQQHnlvdgVS 87
Cdd:cd03237 6 MKKTLGEFTlEVEGGSIS-ESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADYEGT-----VR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 88 AYLNALTGSLNRVSmlksmlQWQSRedklrALEALETVGLLDeshQRVSQMSGGQQQRVGIARALVQDPRLLLADEPVAS 167
Cdd:cd03237 80 DLLSSITKDFYTHP------YFKTE-----IAKPLQIEQILD---REVPELSGGELQRVAIAACLSKDADIYLLDEPSAY 145
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 493478014 168 LDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFI 209
Cdd:cd03237 146 LDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLI 187
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-219 |
6.40e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 76.28 E-value: 6.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 5 KVENLSKQY-------G--------------DVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLD 62
Cdd:COG4586 3 EVENLSKTYrvyekepGlkgalkglfrreyrEVEAVDDISFTIEPgEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 63 DEPITGSQTE----IGMIFQQHN-------LVDgvsaylnaltgSLNrvsMLKSM-----LQWQSREDKLRalEALETVG 126
Cdd:COG4586 83 GYVPFKRRKEfarrIGVVFGQRSqlwwdlpAID-----------SFR---LLKAIyripdAEYKKRLDELV--ELLDLGE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 127 LLDeshQRVSQMSGGQQQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVN-IAAhFG 205
Cdd:COG4586 147 LLD---TPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDdIEA-LC 222
|
250
....*....|....
gi 493478014 206 DRFIGLRDGRKLFD 219
Cdd:COG4586 223 DRVIVIDHGRIIYD 236
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-209 |
7.29e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 75.93 E-value: 7.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 1 MSTLKVENLSKQYGDVT----ALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDpTEGSISLDDEPITGSQ----- 70
Cdd:PRK11022 1 MALLNVDKLSVHFGDESapfrAVDRISYSVKQgEVVGIVGESGSGKSVSSLAIMGLID-YPGRVMAEKLEFNGQDlqris 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 71 ---------TEIGMIFQqhnlvDGVSAYLNALTGSLNRVSMLKSMLQWQSREDKLRALEALETVGLLD-ESHQRV--SQM 138
Cdd:PRK11022 80 ekerrnlvgAEVAMIFQ-----DPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDpASRLDVypHQL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493478014 139 SGGQQQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFI 209
Cdd:PRK11022 155 SGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKII 225
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-186 |
8.90e-16 |
|
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: 73.24 E-value: 8.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYgdvtALEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQT----EIGMIF- 77
Cdd:cd03215 5 LEVRGLSVKG----AVRDVSFEVrAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPrdaiRAGIAYv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 78 ----QQHNLVDGVSAYLNALTGSLnrvsmlksmlqwqsredklralealetvglldeshqrvsqMSGGQQQRVGIARALV 153
Cdd:cd03215 81 pedrKREGLVLDLSVAENIALSSL----------------------------------------LSGGNQQKVVLARWLA 120
|
170 180 190
....*....|....*....|....*....|...
gi 493478014 154 QDPRLLLADEPVASLDPSSAETVMGYLRKAAKE 186
Cdd:cd03215 121 RDPRVLILDEPTRGVDVGAKAEIYRLIRELADA 153
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
4-219 |
1.94e-15 |
|
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: 73.34 E-value: 1.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQY----------------------GDVTALEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTDPTEGSIS 60
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrkgevGEFWALKDVSFEVpRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 61 lddepITGSQT---EIGMIFQqhnlvdgvsaylNALTGSLNrVSMLKSMLQWQSREDKLRALEALETVGLLDESHQRVSQ 137
Cdd:cd03220 81 -----VRGRVSsllGLGGGFN------------PELTGREN-IYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 138 MSGGQQQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSlHQVNIAAHFGDRFIGLRDGRKL 217
Cdd:cd03220 143 YSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVS-HDPSSIKRLCDRALVLEKGKIR 221
|
..
gi 493478014 218 FD 219
Cdd:cd03220 222 FD 223
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
19-215 |
2.78e-15 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 75.24 E-value: 2.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 19 LEDVSFQIE-DEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITG-SQTE----IGMIFQqhnlvDGV----SA 88
Cdd:COG5265 374 LKGVSFEVPaGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDvTQASlraaIGIVPQ-----DTVlfndTI 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 89 YLNALTGSLNrvsmlksmlqwQSREDKLRALEA-------------LET-VGlldeshQRVSQMSGGQQQRVGIARALVQ 154
Cdd:COG5265 449 AYNIAYGRPD-----------ASEEEVEAAARAaqihdfieslpdgYDTrVG------ERGLKLSGGEKQRVAIARTLLK 511
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493478014 155 DPRLLLADEPVASLDPSSAETVMGYLRKAAKEHdvTALVSLHQVNIAAHfGDRFIGLRDGR 215
Cdd:COG5265 512 NPPILIFDEATSALDSRTERAIQAALREVARGR--TTLVIAHRLSTIVD-ADEILVLEAGR 569
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-169 |
3.37e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 74.99 E-value: 3.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 1 MSTLKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGltdptegSISLDDEPITGSQTEIGMIFQQ 79
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDnERVCLVGRNGAGKSTLMKILNG-------EVLLDDGRIIYEQDLIVARLQQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 80 H-------NLVDGVSAYLNALTGSLNRV-------------SMLKSMLQWQSREDKL-------RALEALETVGLldESH 132
Cdd:PRK11147 74 DpprnvegTVYDFVAEGIEEQAEYLKRYhdishlvetdpseKNLNELAKLQEQLDHHnlwqlenRINEVLAQLGL--DPD 151
|
170 180 190
....*....|....*....|....*....|....*..
gi 493478014 133 QRVSQMSGGQQQRVGIARALVQDPRLLLADEPVASLD 169
Cdd:PRK11147 152 AALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-215 |
3.74e-15 |
|
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: 72.06 E-value: 3.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGD--VTALEDVSFQIEDEFAV-LLGESGAGKSTLLRCINGLTDPTEGSISLDDE-----PITGSQTEIGM 75
Cdd:cd03369 7 IEVENLSVRYAPdlPPVLKNVSFKVKAGEKIgIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIdistiPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 76 IFQQHNLVDGVsaylnaltgslnrvsmLKSMLQWQSREDKLRALEALEtvglLDESHQRVSQmsgGQQQRVGIARALVQD 155
Cdd:cd03369 87 IPQDPTLFSGT----------------IRSNLDPFDEYSDEEIYGALR----VSEGGLNLSQ---GQRQLLCLARALLKR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 156 PRLLLADEPVASLDPSSAETVMGYLRKAAKehDVTALVSLHQVNIAAHFgDRFIGLRDGR 215
Cdd:cd03369 144 PRVLVLDEATASIDYATDALIQKTIREEFT--NSTILTIAHRLRTIIDY-DKILVMDAGE 200
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
19-218 |
6.80e-15 |
|
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: 71.52 E-value: 6.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 19 LEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPT---EGSISLDDEPITGsqteigmIFQQHnlvDGVSAYLNAlt 94
Cdd:cd03233 23 LKDFSGVVKPgEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKE-------FAEKY---PGEIIYVSE-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 95 gslnrvsmlksmlqwqsrED----KLRALEALETVGLLdESHQRVSQMSGGQQQRVGIARALVQDPRLLLADEPVASLDP 170
Cdd:cd03233 91 ------------------EDvhfpTLTVRETLDFALRC-KGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDS 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 493478014 171 SSAETVMGYLRKAAKEHDVTALVSLHQVN--IAAHFgDRFIGLRDGRKLF 218
Cdd:cd03233 152 STALEILKCIRTMADVLKTTTFVSLYQASdeIYDLF-DKVLVLYEGRQIY 200
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
17-235 |
6.82e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 72.27 E-value: 6.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 17 TALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTdPTEGSISLDDEPITG-SQTEI----GMIFQQHN---LVDgVS 87
Cdd:PRK03695 10 TRLGPLSAEVRAgEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAwSAAELarhrAYLSQQQTppfAMP-VF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 88 AYLNALTGSLNRVSMLKSMLQwqsredklralEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQ-------DPRLLL 160
Cdd:PRK03695 88 QYLTLHQPDKTRTEAVASALN-----------EVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493478014 161 ADEPVASLDPSSaETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGRKLFDVGRDE-LTPELIDDLYG 235
Cdd:PRK03695 157 LDEPMNSLDVAQ-QAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEvLTPENLAQVFG 231
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
4-198 |
2.42e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 70.95 E-value: 2.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITG--------SQTEIG 74
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVpRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAmsrsrlytVRKRMS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 75 MIFQQHNLVDGVSAYLNaLTGSLNRVSMLKSMLqwqsredkLRA--LEALETVGLLDESHQRVSQMSGGQQQRVGIARAL 152
Cdd:PRK11831 88 MLFQSGALFTDMNVFDN-VAYPLREHTQLPAPL--------LHStvMMKLEAVGLRGAAKLMPSELSGGMARRAALARAI 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 493478014 153 VQDPRLLLADEPVASLDPssaeTVMGYLRKAAKEHD----VTALVSLHQV 198
Cdd:PRK11831 159 ALEPDLIMFDEPFVGQDP----ITMGVLVKLISELNsalgVTCVVVSHDV 204
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-215 |
2.46e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 72.57 E-value: 2.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 22 VSFQIED-EFAVLLGESGAGKSTLLRCINGLTdPTEGS-----ISLDDEPITGSQTEIGMIFQQHNLvdgvsaylnaLTG 95
Cdd:PRK11174 369 LNFTLPAgQRIALVGPSGAGKTSLLNALLGFL-PYQGSlkingIELRELDPESWRKHLSWVGQNPQL----------PHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 96 SL-NRVSMLKSMLQWQSREDKLRALEALETV-----GLLDESHQRVSQMSGGQQQRVGIARALVQDPRLLLADEPVASLD 169
Cdd:PRK11174 438 TLrDNVLLGNPDASDEQLQQALENAWVSEFLpllpqGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 493478014 170 PSSAETVMGYLRKAAKEHdvTALVSLHQVNIAAHFgDRFIGLRDGR 215
Cdd:PRK11174 518 AHSEQLVMQALNAASRRQ--TTLMVTHQLEDLAQW-DQIWVMQDGQ 560
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-225 |
3.06e-14 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 71.37 E-value: 3.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 1 MSTLKVENLSKQY----GDVTALEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTDP----TEGSISLDD-------- 63
Cdd:PRK15093 1 MPLLDIRNLTIEFktsdGWVKAVDRVSMTLtEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDidllrlsp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 64 ---EPITGSQteIGMIFQQ-HNLVDGVSAYLNALTGSLNRVSMLKSMLQ---WQSRedklRALEALETVGLLDES---HQ 133
Cdd:PRK15093 81 rerRKLVGHN--VSMIFQEpQSCLDPSERVGRQLMQNIPGWTYKGRWWQrfgWRKR----RAIELLHRVGIKDHKdamRS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 134 RVSQMSGGQQQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRD 213
Cdd:PRK15093 155 FPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYC 234
|
250
....*....|..
gi 493478014 214 GRKLFDVGRDEL 225
Cdd:PRK15093 235 GQTVETAPSKEL 246
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
6-221 |
4.24e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 70.81 E-value: 4.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 6 VENLSKQYGDVT-----ALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGS---------- 69
Cdd:PRK13645 9 LDNVSYTYAKKTpfefkALNNTSLTFKKnKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANlkkikevkrl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 70 QTEIGMIFQ--QHNLVDGVSAYLNALtGSLNrvsmlksmLQWQSREDKLRALEALETVGLLDESHQRVS-QMSGGQQQRV 146
Cdd:PRK13645 89 RKEIGLVFQfpEYQLFQETIEKDIAF-GPVN--------LGENKQEAYKKVPELLKLVQLPEDYVKRSPfELSGGQKRRV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493478014 147 GIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGrKLFDVG 221
Cdd:PRK13645 160 ALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEG-KVISIG 233
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3-193 |
5.14e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 71.67 E-value: 5.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 3 TLKVENLSKQY-GDVTALEDVSFQIEDE-FAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGS-----QTEIGM 75
Cdd:PRK10790 340 RIDIDNVSFAYrDDNLVLQNINLSVPSRgFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLshsvlRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 76 IfQQHNLVDGVSAYLNALTG---SLNRVsmlksmlqWQsredklraleALETV-------GLLDESHQRVSQ----MSGG 141
Cdd:PRK10790 420 V-QQDPVVLADTFLANVTLGrdiSEEQV--------WQ----------ALETVqlaelarSLPDGLYTPLGEqgnnLSVG 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 493478014 142 QQQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRkAAKEHdvTALV 193
Cdd:PRK10790 481 QKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALA-AVREH--TTLV 529
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
33-217 |
5.36e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 70.04 E-value: 5.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 33 LLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQ-------TEIGMIFQQ------HNLVDGVSAYlnaltgSLNR 99
Cdd:PRK13638 32 LVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKrgllalrQQVATVFQDpeqqifYTDIDSDIAF------SLRN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 100 VSMLKSmlqwqsrEDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGY 179
Cdd:PRK13638 106 LGVPEA-------EITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAI 178
|
170 180 190
....*....|....*....|....*....|....*...
gi 493478014 180 LRKAAKEHDvTALVSLHQVNIAAHFGDRFIGLRDGRKL 217
Cdd:PRK13638 179 IRRIVAQGN-HVIISSHDIDLIYEISDAVYVLRQGQIL 215
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-164 |
7.83e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 70.82 E-value: 7.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQygdvTALEDVSFQI-EDE---FAVLLGesgAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTE------I 73
Cdd:COG1129 257 LEVEGLSVG----GVVRDVSFSVrAGEilgIAGLVG---AGRTELARALFGADPADSGEIRLDGKPVRIRSPRdairagI 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 74 GMI---FQQHNLVDGVSAYLNALTGSLNRVSmlKSMLQWQSREDKLrALEALETVGL-LDESHQRVSQMSGGQQQRVGIA 149
Cdd:COG1129 330 AYVpedRKGEGLVLDLSIRENITLASLDRLS--RGGLLDRRRERAL-AEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLA 406
|
170
....*....|....*
gi 493478014 150 RALVQDPRLLLADEP 164
Cdd:COG1129 407 KWLATDPKVLILDEP 421
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
4-170 |
8.29e-14 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 68.72 E-value: 8.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQIEDEFAVLL-GESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTEIGMIFQQHnl 82
Cdd:PRK13543 12 LAAHALAFSRNEEPVFGPLDFHVDAGEALLVqGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGH-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 83 vdgvsayLNALTGSLNRVSMLKSMLQWQSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDPRLLLAD 162
Cdd:PRK13543 90 -------LPGLKADLSTLENLHFLCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLD 162
|
....*...
gi 493478014 163 EPVASLDP 170
Cdd:PRK13543 163 EPYANLDL 170
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-169 |
9.50e-14 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 70.73 E-value: 9.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQIEDEFAV-LLGESGAGKSTLLRCINGLTDPTEGSISLddepitGSQTEIGMIFQQHNL 82
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVgVIGPNGAGKSTLFRMITGQEQPDSGTIEI------GETVKLAYVDQSRDA 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 83 VDGVSAYLNALTGSLNrvsmlksMLQWQSREDKLRALealetVGLLD----ESHQRVSQMSGGQQQRVGIARALVQDPRL 158
Cdd:TIGR03719 397 LDPNKTVWEEISGGLD-------IIKLGKREIPSRAY-----VGRFNfkgsDQQKKVGQLSGGERNRVHLAKTLKSGGNV 464
|
170
....*....|.
gi 493478014 159 LLADEPVASLD 169
Cdd:TIGR03719 465 LLLDEPTNDLD 475
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-219 |
1.06e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 68.95 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 1 MST-LKVENLSKQY----------------------GDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTE 56
Cdd:COG1134 1 MSSmIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERgESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 57 GSISlddepITGSQT---EIGMIFQQH-----NlvdgvsAYLNALTGSLNRVSMlksmlqwQSREDklralEALETVGLL 128
Cdd:COG1134 81 GRVE-----VNGRVSallELGAGFHPEltgreN------IYLNGRLLGLSRKEI-------DEKFD-----EIVEFAELG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 129 DESHQRVSQMSGGQQQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSlHQVNIAAHFGDRF 208
Cdd:COG1134 138 DFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVS-HSMGAVRRLCDRA 216
|
250
....*....|.
gi 493478014 209 IGLRDGRKLFD 219
Cdd:COG1134 217 IWLEKGRLVMD 227
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-174 |
1.12e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 70.31 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQIE--DEFAVLlGESGAGKSTLLRCINGLTDPTEGSISLDDepitgsQTEIGMIFQQHN 81
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEagERLAII-GENGVGKTTLLRTLVGELEPDSGTVKWSE------NANIGYYAQDHA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 82 lvdgvSAYLNALTgslnrvsMLKSMLQWQSREDKLRALEAleTVGLL----DESHQRVSQMSGGQQQRVGIARALVQDPR 157
Cdd:PRK15064 393 -----YDFENDLT-------LFDWMSQWRQEGDDEQAVRG--TLGRLlfsqDDIKKSVKVLSGGEKGRMLFGKLMMQKPN 458
|
170
....*....|....*..
gi 493478014 158 LLLADEPVASLDPSSAE 174
Cdd:PRK15064 459 VLVMDEPTNHMDMESIE 475
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-215 |
1.43e-13 |
|
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: 67.55 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTD--PTEGSISLDDEPITGSQTE------IG 74
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKgEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPEerarlgIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 75 MIFQQHNLVDGVSAylnaltgslnrvsmlksmlqwqsrEDKLRALEaletVGLldeshqrvsqmSGGQQQRVGIARALVQ 154
Cdd:cd03217 81 LAFQYPPEIPGVKN------------------------ADFLRYVN----EGF-----------SGGEKKRNEILQLLLL 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493478014 155 DPRLLLADEPVASLDPSSAETVMGYLRKAAKEhDVTALVSLHQVNIAAHF-GDRFIGLRDGR 215
Cdd:cd03217 122 EPDLAILDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITHYQRLLDYIkPDRVHVLYDGR 182
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-182 |
1.70e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 70.08 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITG------SQTEIGMI 76
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLhAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARltpakaHQLGIYLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 77 FQQHNLVDGVSAYLNALTGslnrvsmlksMLQWQSREDKLRALEALETVGLldESHQRVSQMSGGQQQRVGIARALVQDP 156
Cdd:PRK15439 92 PQEPLLFPNLSVKENILFG----------LPKRQASMQKMKQLLAALGCQL--DLDSSAGSLEVADRQIVEILRGLMRDS 159
|
170 180
....*....|....*....|....*.
gi 493478014 157 RLLLADEPVASLDPSSAETVMGYLRK 182
Cdd:PRK15439 160 RILILDEPTASLTPAETERLFSRIRE 185
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
15-171 |
2.11e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.88 E-value: 2.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 15 DVTALEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPI---TGSQTE-----IGMIFQqhnlvDG 85
Cdd:PRK10261 336 EVHAVEKVSFDLwPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlSPGKLQalrrdIQFIFQ-----DP 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 86 VSAYLNALTGSLNRVSMLKSMLQWQSREDKLRALEALETVGLLDESHQRVS-QMSGGQQQRVGIARALVQDPRLLLADEP 164
Cdd:PRK10261 411 YASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPhEFSGGQRQRICIARALALNPKVIIADEA 490
|
....*..
gi 493478014 165 VASLDPS 171
Cdd:PRK10261 491 VSALDVS 497
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
15-172 |
3.00e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 69.67 E-value: 3.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 15 DVTALEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTDPTEGSI------SLDDEPITGSQTEIGMIFQ--------- 78
Cdd:PTZ00265 397 DVEIYKDLNFTLtEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIiindshNLKDINLKWWRSKIGVVSQdpllfsnsi 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 79 QHNL---------VDGVSAYLN-----ALTGSLNRVSM-------LKSMLQWQSREDKLRALEALETV------------ 125
Cdd:PTZ00265 477 KNNIkyslyslkdLEALSNYYNedgndSQENKNKRNSCrakcagdLNDMSNTTDSNELIEMRKNYQTIkdsevvdvskkv 556
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 493478014 126 -------GLLDESHQRV----SQMSGGQQQRVGIARALVQDPRLLLADEPVASLDPSS 172
Cdd:PTZ00265 557 lihdfvsALPDKYETLVgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-196 |
3.47e-13 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 68.89 E-value: 3.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQY--GDVTALEDVSFQIEDEFAV-LLGESGAGKSTLLRCINGLTDPTEGSISLD-----DEPITGSQTEIGM 75
Cdd:PRK11176 342 IEFRNVTFTYpgKEVPALRNINFKIPAGKTVaLVGRSGSGKSTIANLLTRFYDIDEGEILLDghdlrDYTLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 76 IFQQ-HNLVDGVS---AYlnALTGSLnrvsmlksmlqwqSREDKLRALE---ALETVGLLDESHQRV-----SQMSGGQQ 143
Cdd:PRK11176 422 VSQNvHLFNDTIAnniAY--ARTEQY-------------SREQIEEAARmayAMDFINKMDNGLDTVigengVLLSGGQR 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 493478014 144 QRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKehDVTALVSLH 196
Cdd:PRK11176 487 QRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAH 537
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
33-217 |
7.01e-13 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 65.73 E-value: 7.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 33 LLGESGAGKSTLLRCINGLTDP--TEGSISLDDEPITGS-QTEIGMIFQQhnlvdgvsaylNALTGSLN-RVSMLKSMLq 108
Cdd:cd03232 38 LMGESGAGKTTLLDVLAGRKTAgvITGEILINGRPLDKNfQRSTGYVEQQ-----------DVHSPNLTvREALRFSAL- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 109 wqsredkLRALealetvglldeshqrvsqmSGGQQQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAkEHD 188
Cdd:cd03232 106 -------LRGL-------------------SVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLA-DSG 158
|
170 180 190
....*....|....*....|....*....|.
gi 493478014 189 VTALVSLHQVNIA--AHFgDRFIGLRDGRKL 217
Cdd:cd03232 159 QAILCTIHQPSASifEKF-DRLLLLKRGGKT 188
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
4-215 |
8.07e-13 |
|
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: 65.57 E-value: 8.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLS-----KQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLddepitgsQTEIGMIF 77
Cdd:cd03250 1 ISVEDASftwdsGEQETSFTLKDINLEVPKgELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV--------PGSIAYVS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 78 QQhnlvdgvsAYLnaLTGSLnrvsmlKSMLQWQSREDKLRALEALE-----------TVGLLDESHQRVSQMSGGQQQRV 146
Cdd:cd03250 73 QE--------PWI--QNGTI------RENILFGKPFDEERYEKVIKacalepdleilPDGDLTEIGEKGINLSGGQKQRI 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 147 GIARALVQDPRLLLADEPVASLDPSSAETVMGY-LRKAAKEHDVTALVSlHQVNIAAHFgDRFIGLRDGR 215
Cdd:cd03250 137 SLARAVYSDADIYLLDDPLSAVDAHVGRHIFENcILGLLLNNKTRILVT-HQLQLLPHA-DQIVVLDNGR 204
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
4-169 |
9.38e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 66.24 E-value: 9.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTD--PTEGSISLDDEPITGSQTE------IG 74
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPgEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSPDeraragIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 75 MIFQQHNLVDGVSaYLNALTGSLNRVSMLKSMLqwqsREDKLRALEALETVGLlDESH-QR---VSqMSGGQQQRVGIAR 150
Cdd:COG0396 81 LAFQYPVEIPGVS-VSNFLRTALNARRGEELSA----REFLKLLKEKMKELGL-DEDFlDRyvnEG-FSGGEKKRNEILQ 153
|
170
....*....|....*....
gi 493478014 151 ALVQDPRLLLADEPVASLD 169
Cdd:COG0396 154 MLLLEPKLAILDETDSGLD 172
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
7-230 |
1.02e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.45 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 7 ENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTE------IGMIFQQ 79
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPhSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKealengISMVHQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 80 HNLVDGVSAYLNALTGSLNRVSMLKSmlqwqsrEDKLRAlealETVGLLDE------SHQRVSQMSGGQQQRVGIARALV 153
Cdd:PRK10982 82 LNLVLQRSVMDNMWLGRYPTKGMFVD-------QDKMYR----DTKAIFDEldididPRAKVATLSVSQMQMIEIAKAFS 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493478014 154 QDPRLLLADEPVASLDPSSAETVMGYLRKaAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGRKLFDVGRDELTPELI 230
Cdd:PRK10982 151 YNAKIVIMDEPTSSLTEKEVNHLFTIIRK-LKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKI 226
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-168 |
1.68e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.95 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPIT-----GSQTE-IGMI 76
Cdd:PRK10762 5 LQLKGIDKAFPGVKALSGAALNVyPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpkSSQEAgIGII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 77 FQQHNLVDGVSAYLN-----ALTGSLNRVsmlksmlQWQ---SREDKLraleaLETVGLLDESHQRVSQMSGGQQQRVGI 148
Cdd:PRK10762 85 HQELNLIPQLTIAENiflgrEFVNRFGRI-------DWKkmyAEADKL-----LARLNLRFSSDKLVGELSIGEQQMVEI 152
|
170 180
....*....|....*....|
gi 493478014 149 ARALVQDPRLLLADEPVASL 168
Cdd:PRK10762 153 AKVLSFESKVIIMDEPTDAL 172
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
18-175 |
2.02e-12 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 66.91 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 18 ALEDVSFQIE-DEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTE-----IGMIFQQHNLVDGvSAYLN 91
Cdd:PRK13657 350 GVEDVSFEAKpGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAslrrnIAVVFQDAGLFNR-SIEDN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 92 ALTGSLN--RVSMLKSMLQWQSREDKLRALEALET-VGlldeshQRVSQMSGGQQQRVGIARALVQDPRLLLADEPVASL 168
Cdd:PRK13657 429 IRVGRPDatDEEMRAAAERAQAHDFIERKPDGYDTvVG------ERGRQLSGGERQRLAIARALLKDPPILILDEATSAL 502
|
....*..
gi 493478014 169 DpssAET 175
Cdd:PRK13657 503 D---VET 506
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
2-236 |
2.11e-12 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 65.49 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 2 STLKVENLSKQyGDVTALEDVSFQIE-DEFAVLLGESGAGKSTLLRCINGLTDP----TEGSISLDDEPITGSQ---TEI 73
Cdd:PRK10418 3 QQIELRNIALQ-AAQPLVHGVSLTLQrGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCAlrgRKI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 74 GMIFQQHNlvdgvSAYLNALTgslNRVSMLKSMLQWQSREDKLRALEALETVGLldESHQRVS-----QMSGGQQQRVGI 148
Cdd:PRK10418 82 ATIMQNPR-----SAFNPLHT---MHTHARETCLALGKPADDATLTAALEAVGL--ENAARVLklypfEMSGGMLQRMMI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 149 ARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGR--------KLFDV 220
Cdd:PRK10418 152 ALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRiveqgdveTLFNA 231
|
250
....*....|....*....
gi 493478014 221 GRDELTPELID---DLYGS 236
Cdd:PRK10418 232 PKHAVTRSLVSahlALYGM 250
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
4-226 |
2.33e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 66.76 E-value: 2.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTaLEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLD------------DEPITgsq 70
Cdd:PRK13409 341 VEYPDLTKKLGDFS-LEVEGGEIyEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPElkisykpqyikpDYDGT--- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 71 teigmifqqhnlvdgVSAYLNALTGSLNRvSMLKSMLqwqsredklraLEALETVGLLDeshQRVSQMSGGQQQRVGIAR 150
Cdd:PRK13409 417 ---------------VEDLLRSITDDLGS-SYYKSEI-----------IKPLQLERLLD---KNVKDLSGGELQRVAIAA 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 151 ALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFI----------------GLRDG 214
Cdd:PRK13409 467 CLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMvfegepgkhghasgpmDMREG 546
|
250
....*....|....*...
gi 493478014 215 RKLF--DVG----RDELT 226
Cdd:PRK13409 547 MNRFlkELGitfrRDEET 564
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
4-197 |
7.33e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.96 E-value: 7.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQT--EIGMIFQQH 80
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLpAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCtyQKQLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 81 NlvDGVSAYLNALTGSLNRVSMLKSMLQWqsreDKLRALEALETvgLLDEShqrVSQMSGGQQQRVGIARALVQDPRLLL 160
Cdd:PRK13540 82 R--SGINPYLTLRENCLYDIHFSPGAVGI----TELCRLFSLEH--LIDYP---CGLLSSGQKRQVALLRLWMSKAKLWL 150
|
170 180 190
....*....|....*....|....*....|....*..
gi 493478014 161 ADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSlHQ 197
Cdd:PRK13540 151 LDEPLVALDELSLLTIITKIQEHRAKGGAVLLTS-HQ 186
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
15-197 |
7.54e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 62.04 E-value: 7.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 15 DVTALEDVSFQIE-DEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTE-----IGMIFQQHNLV-DGVS 87
Cdd:PRK10789 327 DHPALENVNFTLKpGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDswrsrLAVVSQTPFLFsDTVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 88 AYL-----NALTGSLNRVSMLKSMlqwqsREDKLRALEALETvglldESHQRVSQMSGGQQQRVGIARALVQDPRLLLAD 162
Cdd:PRK10789 407 NNIalgrpDATQQEIEHVARLASV-----HDDILRLPQGYDT-----EVGERGVMLSGGQKQRISIARALLLNAEILILD 476
|
170 180 190
....*....|....*....|....*....|....*
gi 493478014 163 EPVASLDPSSAETVMGYLRKAAKEHdvTALVSLHQ 197
Cdd:PRK10789 477 DALSAVDGRTEHQILHNLRQWGEGR--TVIISAHR 509
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
4-183 |
1.59e-10 |
|
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: 58.32 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTAL-EDVSFQIEDEFAVLL-GESGAGKSTLLRCINGLTDPTEGSISLddePitgSQTEIGMIFQQhn 81
Cdd:cd03223 1 IELENLSLATPDGRVLlKDLSFEIKPGDRLLItGPSGTGKSSLFRALAGLWPWGSGRIGM---P---EGEDLLFLPQR-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 82 lvdgvsAYLNALTgslnrvsmLKSML--QWQsreDKLralealetvglldeshqrvsqmSGGQQQRVGIARALVQDPRLL 159
Cdd:cd03223 73 ------PYLPLGT--------LREQLiyPWD---DVL----------------------SGGEQQRLAFARLLLHKPKFV 113
|
170 180
....*....|....*....|....
gi 493478014 160 LADEPVASLDPSSAETVMGYLRKA 183
Cdd:cd03223 114 FLDEATSALDEESEDRLYQLLKEL 137
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-230 |
2.47e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 60.57 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 5 KVENLSKQygDVTALEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTEI----GMIFQQ 79
Cdd:PRK09700 267 EVRNVTSR--DRKKVRDISFSVcRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDavkkGMAYIT 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 80 HNLVD-----GVSAYLN-ALTGSLNRVSMLKSMLQWQSREDKLRALEALETVGLLDES-HQRVSQMSGGQQQRVGIARAL 152
Cdd:PRK09700 345 ESRRDngffpNFSIAQNmAISRSLKDGGYKGAMGLFHEVDEQRTAENQRELLALKCHSvNQNITELSGGNQQKVLISKWL 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 153 VQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAhFGDRFIGLRDGR--KLFDvGRDELTPELI 230
Cdd:PRK09700 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIIT-VCDRIAVFCEGRltQILT-NRDDMSEEEI 502
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-198 |
5.12e-10 |
|
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: 59.92 E-value: 5.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQY--GDVTALEDVSFQIEDEFAV-LLGESGAGKSTLLRCINGLTDpTEGSISLDD---EPITGSQ--TEIGM 75
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVgLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGvswNSVTLQTwrKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 76 IFQQhnlvdgvsayLNALTGSLNRvsMLKSMLQWQSREdklrALEALETVGLLDESHQRVSQ-----------MSGGQQQ 144
Cdd:TIGR01271 1297 IPQK----------VFIFSGTFRK--NLDPYEQWSDEE----IWKVAEEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQ 1360
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 493478014 145 RVGIARALVQDPRLLLADEPVASLDPSSAETvmgyLRKAAKE--HDVTALVSLHQV 198
Cdd:TIGR01271 1361 LMCLARSILSKAKILLLDEPSAHLDPVTLQI----IRKTLKQsfSNCTVILSEHRV 1412
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-170 |
6.06e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 59.22 E-value: 6.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 2 STLKVENLSKQYGDVT-ALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTE-----IG 74
Cdd:PRK10522 321 QTLELRNVTFAYQDNGfSVGPINLTIKRgELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEdyrklFS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 75 MIFQQHNLVDgvsaylnALTGSLNRVSMLKSMLQWqsredklraLEALETVGLLDESHQRVS--QMSGGQQQRVGIARAL 152
Cdd:PRK10522 401 AVFTDFHLFD-------QLLGPEGKPANPALVEKW---------LERLKMAHKLELEDGRISnlKLSKGQKKRLALLLAL 464
|
170
....*....|....*...
gi 493478014 153 VQDPRLLLADEPVASLDP 170
Cdd:PRK10522 465 AEERDILLLDEWAADQDP 482
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-270 |
8.52e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 59.02 E-value: 8.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 19 LEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTDPTEGSIslddepitGSQTEIGMIFQQhnlvdgvSAYLNALTgsl 97
Cdd:PTZ00243 676 LRDVSVSVpRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV--------WAERSIAYVPQQ-------AWIMNATV--- 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 98 nRVSML------KSMLQWQSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDPRLLLADEPVASLDPS 171
Cdd:PTZ00243 738 -RGNILffdeedAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAH 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 172 SAETVM-----GYLrkAAKehdvTALVSLHQVNIAAHfGDRFIGLRDGRKLF-----DVGRDELTPELIDDLYGSVETV- 240
Cdd:PTZ00243 817 VGERVVeecflGAL--AGK----TRVLATHQVHVVPR-ADYVVALGDGRVEFsgssaDFMRTSLYATLAAELKENKDSKe 889
|
250 260 270
....*....|....*....|....*....|
gi 493478014 241 GLADQEKTVEEALDAIGDDPSEGAAEDAQR 270
Cdd:PTZ00243 890 GDADAEVAEVDAAPGGAVDHEPPVAKQEGN 919
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4-215 |
1.05e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 58.71 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLS----KQYGDVTALEDVSFQIE-DEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDD-----------EPIT 67
Cdd:PRK10261 13 LAVENLNiafmQEQQKIAAVRNLSFSLQrGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqviELSE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 68 GSQTE--------IGMIFQQHnlvdgvSAYLNALTGSLNRVSMLKSMLQWQSREDKLRALEALETVGLLDESHQRVS--- 136
Cdd:PRK10261 93 QSAAQmrhvrgadMAMIFQEP------MTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSryp 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 137 -QMSGGQQQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFIGLRDGR 215
Cdd:PRK10261 167 hQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGE 246
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
8-218 |
1.48e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 58.35 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 8 NLSKQYGDVTALEDVSFQIED--------------EFAVLLGESGAGKSTLLRCI------NGLTdpteGSISLDDEPIT 67
Cdd:PLN03211 60 NIKRILGHKPKISDETRQIQErtilngvtgmaspgEILAVLGPSGSGKSTLLNALagriqgNNFT----GTILANNRKPT 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 68 gSQT--EIGMIFQQHNLVDGVSAYLNALTGSLNRVSmlKSMlqwqSREDKLRALEA-LETVGLLDESHQRVSQ-----MS 139
Cdd:PLN03211 136 -KQIlkRTGFVTQDDILYPHLTVRETLVFCSLLRLP--KSL----TKQEKILVAESvISELGLTKCENTIIGNsfirgIS 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 140 GGQQQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDvTALVSLHQVNIAAH-FGDRFIGLRDGRKLF 218
Cdd:PLN03211 209 GGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGK-TIVTSMHQPSSRVYqMFDSVLVLSEGRCLF 287
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
33-216 |
2.00e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.20 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 33 LLGESGAGKSTLLRCINGLTdpTEGSISLDDEPITGS------QTEIGMIfQQHNLVDGVSAYLNALTGSLnRVSMLKSM 106
Cdd:TIGR00956 794 LMGASGAGKTTLLNVLAERV--TTGVITGGDRLVNGRpldssfQRSIGYV-QQQDLHLPTSTVRESLRFSA-YLRQPKSV 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 107 lqwqSREDKLRALEA------LET-----VGLLDEShqrvsqMSGGQQQRVGIARALVQDPRLLL-ADEPVASLDPSSAE 174
Cdd:TIGR00956 870 ----SKSEKMEYVEEviklleMESyadavVGVPGEG------LNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAW 939
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 493478014 175 TVMGYLRKAAKeHDVTALVSLHQ--VNIAAHFgDRFIGLRDGRK 216
Cdd:TIGR00956 940 SICKLMRKLAD-HGQAILCTIHQpsAILFEEF-DRLLLLQKGGQ 981
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
33-176 |
3.10e-09 |
|
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: 57.25 E-value: 3.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 33 LLGESGAGKSTLLRCINGLTDPTEGsislddEPITGSQTEIGMIFQQ----------HNLVDGVSAYLNALTgSLNRVSM 102
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVDKDFNG------EARPQPGIKVGYLPQEpqldptktvrENVEEGVAEIKDALD-RFNEISA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 103 L--------KSMLQWQSR-EDKL-------------RALEALEtvglLDESHQRVSQMSGGQQQRVGIARALVQDPRLLL 160
Cdd:TIGR03719 109 KyaepdadfDKLAAEQAElQEIIdaadawdldsqleIAMDALR----CPPWDADVTKLSGGERRRVALCRLLLSKPDMLL 184
|
170
....*....|....*.
gi 493478014 161 ADEPVASLDpssAETV 176
Cdd:TIGR03719 185 LDEPTNHLD---AESV 197
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-215 |
3.41e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.98 E-value: 3.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQygdvtALEDVSFQIE-DEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQT----EIGMIF- 77
Cdd:PRK15439 269 LTVEDLTGE-----GFRNISLEVRaGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTaqrlARGLVYl 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 78 ----QQHNLVDGVSAYLNALTGSLNRVSMlksmlqWQSREDKLRALEAL-ETVGL-LDESHQRVSQMSGGQQQRVGIARA 151
Cdd:PRK15439 344 pedrQSSGLYLDAPLAWNVCALTHNRRGF------WIKPARENAVLERYrRALNIkFNHAEQAARTLSGGNQQKVLIAKC 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493478014 152 LVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVS--LHQVniaAHFGDRFIGLRDGR 215
Cdd:PRK15439 418 LEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISsdLEEI---EQMADRVLVMHQGE 480
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-198 |
6.34e-09 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 55.63 E-value: 6.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQY--GDVTALEDVSFQIEDEFAV-LLGESGAGKSTLLRCINGLTDpTEGSISLD-----DEPITGSQTEIGM 75
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVgLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDgvswnSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 76 IFQQhnlvdgvsayLNALTGSLNRvsMLKSMLQWQSREdklrALEALETVGLLDESHQRVSQ-----------MSGGQQQ 144
Cdd:cd03289 82 IPQK----------VFIFSGTFRK--NLDPYGKWSDEE----IWKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQ 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 493478014 145 RVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKehDVTALVSLHQV 198
Cdd:cd03289 146 LMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFA--DCTVILSEHRI 197
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-169 |
7.70e-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: 56.46 E-value: 7.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 19 LEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTEI---GMIfqQHNLVDGVSaYLNALT 94
Cdd:TIGR01271 442 LKNISFKLEKgQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWimpGTI--KDNIIFGLS-YDEYRY 518
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493478014 95 GSLNRVSMLKSMLQWQSREDKLRALEALETvglldeshqrvsqMSGGQQQRVGIARALVQDPRLLLADEPVASLD 169
Cdd:TIGR01271 519 TSVIKACQLEEDIALFPEKDKTVLGEGGIT-------------LSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
8-193 |
9.76e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 55.56 E-value: 9.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 8 NLSKQYGDVTaLEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLD------------DEPITgsqteig 74
Cdd:COG1245 346 DLTKSYGGFS-LEVEGGEIrEGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDlkisykpqyispDYDGT------- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 75 mifqqhnlvdgVSAYL-NALTGSLNrVSMLKSMLqwqsredklraLEALETVGLLDeshQRVSQMSGGQQQRVGIARALV 153
Cdd:COG1245 418 -----------VEEFLrSANTDDFG-SSYYKTEI-----------IKPLGLEKLLD---KNVKDLSGGELQRVAIAACLS 471
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 493478014 154 QDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALV 193
Cdd:COG1245 472 RDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMV 511
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
29-218 |
1.13e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.89 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 29 EFAVLLGESGAGKSTLLRCINGLTD----PTEGSISLD------------DEPITGSQTEI--GMIFQQHNLVdgvsaYL 90
Cdd:TIGR00956 88 ELTVVLGRPGSGCSTLLKTIASNTDgfhiGVEGVITYDgitpeeikkhyrGDVVYNAETDVhfPHLTVGETLD-----FA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 91 NALTGSLNRVSMLksmlqwqSRED---KLRALeALETVGLldeSHQR--------VSQMSGGQQQRVGIARALVQDPRLL 159
Cdd:TIGR00956 163 ARCKTPQNRPDGV-------SREEyakHIADV-YMATYGL---SHTRntkvgndfVRGVSGGERKRVSIAEASLGGAKIQ 231
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493478014 160 LADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQV--NIAAHFgDRFIGLRDGRKLF 218
Cdd:TIGR00956 232 CWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCsqDAYELF-DKVIVLYEGYQIY 291
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
7-268 |
1.30e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.52 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 7 ENLSKQYGDVTALEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTE----IGMIFQ--- 78
Cdd:NF033858 270 RGLTMRFGDFTAVDHVSFRIRRgEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIAtrrrVGYMSQafs 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 79 -------QHNLVdgVSAYLNALTGSlnrvsmlksmlQWQSREDklralEALETVGLLDESHQRVSQMSGGQQQRVGIARA 151
Cdd:NF033858 350 lygeltvRQNLE--LHARLFHLPAA-----------EIAARVA-----EMLERFDLADVADALPDSLPLGIRQRLSLAVA 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 152 LVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFgDRfIGLRDGRKLFDVGrdelTPELId 231
Cdd:NF033858 412 VIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAERC-DR-ISLMHAGRVLASD----TPAAL- 484
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 493478014 232 dlygsVETVGLAdqekTVEEAL-----DAIGDDPSEGAAEDA 268
Cdd:NF033858 485 -----VAARGAA----TLEEAFiayleEAAGAAAAPAAAAAP 517
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-169 |
1.52e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.18 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQIEDEFAV-LLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGsqteigmIFQQHNL 82
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIgLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLG-------YFAQHQL 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 83 vdgvsAYLNALTGSLNRVSMLKSmlqwQSREDKLRalEALETVGLL-DESHQRVSQMSGGQQQRVGIARALVQDPRLLLA 161
Cdd:PRK10636 386 -----EFLRADESPLQHLARLAP----QELEQKLR--DYLGGFGFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLL 454
|
....*...
gi 493478014 162 DEPVASLD 169
Cdd:PRK10636 455 DEPTNHLD 462
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-169 |
1.62e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.01 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKqygdvTALEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPIT------GSQTEIGMI 76
Cdd:PRK10762 258 LKVDNLSG-----PGVNDVSFTLrKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVtrspqdGLANGIVYI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 77 FQQHN---LVDGVSAYLNALTGSLNRVSmlKSMLQWQSREDKLRALEALETVGLLDES-HQRVSQMSGGQQQRVGIARAL 152
Cdd:PRK10762 333 SEDRKrdgLVLGMSVKENMSLTALRYFS--RAGGSLKHADEQQAVSDFIRLFNIKTPSmEQAIGLLSGGNQQKVAIARGL 410
|
170
....*....|....*..
gi 493478014 153 VQDPRLLLADEPVASLD 169
Cdd:PRK10762 411 MTRPKVLILDEPTRGVD 427
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
15-214 |
5.37e-08 |
|
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: 52.33 E-value: 5.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 15 DVTALEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTEIGMIFQQHNLvdgvsAYLNAL 93
Cdd:cd03290 13 GLATLSNINIRIpTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSV-----AYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 94 TGSLNrvSMLKSMLQWQSREDKLRALEALETVGL---LD--------ESHQRVSQMSGGQQQRVGIARALVQDPRLLLAD 162
Cdd:cd03290 88 PWLLN--ATVEENITFGSPFNKQRYKAVTDACSLqpdIDllpfgdqtEIGERGINLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 493478014 163 EPVASLDPSSAETVM--GYLRKAAKEHDVTALVSlHQVNIAAHfGDRFIGLRDG 214
Cdd:cd03290 166 DPFSALDIHLSDHLMqeGILKFLQDDKRTLVLVT-HKLQYLPH-ADWIIAMKDG 217
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
138-198 |
5.56e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.88 E-value: 5.56e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493478014 138 MSGGQQQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQV 198
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI 1419
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-169 |
6.63e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.20 E-value: 6.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQIEDEFAV-LLGESGAGKSTLLRCINGLTDPTEGSISLddepitGSQTEIGMIFQQHNL 82
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVgIIGPNGAGKSTLFKMITGQEQPDSGTIKI------GETVKLAYVDQSRDA 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 83 VDGVSAYLNALTGSLNrvsmlksMLQWQSREDKLRALealetVGLLD----ESHQRVSQMSGGQQQRVGIARALVQDPRL 158
Cdd:PRK11819 399 LDPNKTVWEEISGGLD-------IIKVGNREIPSRAY-----VGRFNfkggDQQKKVGVLSGGERNRLHLAKTLKQGGNV 466
|
170
....*....|.
gi 493478014 159 LLADEPVASLD 169
Cdd:PRK11819 467 LLLDEPTNDLD 477
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
5-209 |
7.55e-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: 51.03 E-value: 7.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 5 KVENLSKQYGDVTALEDVSFQIEDEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDdepitgsqteigmifqqhnlvd 84
Cdd:cd03222 2 LYPDCVKRYGVFFLLVELGVVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWD---------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 85 gvsaylnaltgsLNRVSMlksmlqwqsredklralealetvglldeSHQRVSqMSGGQQQRVGIARALVQDPRLLLADEP 164
Cdd:cd03222 60 ------------GITPVY----------------------------KPQYID-LSGGELQRVAIAAALLRNATFYLFDEP 98
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 493478014 165 VASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAHFGDRFI 209
Cdd:cd03222 99 SAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIH 143
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
12-170 |
7.84e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.71 E-value: 7.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 12 QYGDVTALEDVSFQIE-DEFAVLLGESGAGKSTLLRCING-----------LTDPTEGSisldDEPITGSQTEIGMIFQQ 79
Cdd:PRK10938 269 SYNDRPILHNLSWQVNpGEHWQIVGPNGAGKSTLLSLITGdhpqgysndltLFGRRRGS----GETIWDIKKHIGYVSSS 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 80 HNLVDGVSAYLNA--LTGSLNRVSMlksmlqWQSREDKLRAL--EALETVGLLDE-SHQRVSQMSGGQQQRVGIARALVQ 154
Cdd:PRK10938 345 LHLDYRVSTSVRNviLSGFFDSIGI------YQAVSDRQQKLaqQWLDILGIDKRtADAPFHSLSWGQQRLALIVRALVK 418
|
170
....*....|....*.
gi 493478014 155 DPRLLLADEPVASLDP 170
Cdd:PRK10938 419 HPTLLILDEPLQGLDP 434
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
102-249 |
8.25e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 52.43 E-value: 8.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 102 MLKSMLQWQSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLR 181
Cdd:NF000106 109 MIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVR 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 182 KAAKEhDVTALVSLHQVNIAAHFGDRFIGLRDGRKLFDVGRDELTPEL--------------IDDLYGSVETVGL----- 242
Cdd:NF000106 189 SMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVggrtlqirpahaaeLDRMVGAIAQAGLdgiag 267
|
....*....
gi 493478014 243 --ADQEKTV 249
Cdd:NF000106 268 atADHEDGV 276
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
4-184 |
1.01e-07 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 51.16 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLsKQYGDVTALEdvsfqIEDEFAVLLGESGAGKSTLLRCIN-GLTDPTEGSISLDDEPIT--GSQTEIGMIFQQH 80
Cdd:COG0419 5 LRLENF-RSYRDTETID-----FDDGLNLIVGPNGAGKSTILEAIRyALYGKARSRSKLRSDLINvgSEEASVELEFEHG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 81 NLV------DGVSAYLNALTGSlNRVSMLKSMLQ---WQSREDKLRALEA-----LETVGLLDESHQR----------VS 136
Cdd:COG0419 79 GKRyrierrQGEFAEFLEAKPS-ERKEALKRLLGleiYEELKERLKELEEalesaLEELAELQKLKQEilaqlsgldpIE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 493478014 137 QMSGGQQQRVGIARALvqdpRLLLaDepVASLDPSSAETVMGYLRKAA 184
Cdd:COG0419 158 TLSGGERLRLALADLL----SLIL-D--FGSLDEERLERLLDALEELA 198
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
33-176 |
1.04e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.43 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 33 LLGESGAGKSTLLRCINGLTDPTEGSISLDDEpITgsqteIGMIFQQ----------HNLVDGVSAYLNALTgSLNRVSM 102
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEARPAPG-IK-----VGYLPQEpqldpektvrENVEEGVAEVKAALD-RFNEIYA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 103 LKS--------MLQWQSR-EDKL-------------RALEALEtvglLDESHQRVSQMSGGQQQRVGIARALVQDPRLLL 160
Cdd:PRK11819 111 AYAepdadfdaLAAEQGElQEIIdaadawdldsqleIAMDALR----CPPWDAKVTKLSGGERRRVALCRLLLEKPDMLL 186
|
170
....*....|....*.
gi 493478014 161 ADEPVASLDpssAETV 176
Cdd:PRK11819 187 LDEPTNHLD---AESV 199
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
14-177 |
1.49e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.17 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 14 GDVTALEDVSFQIE-DEFAVLLGESGAGKSTLLRCINGLTDPTEGSIslddepITGSQTEIGmIFQQHNlVDGVSAYLNA 92
Cdd:PLN03073 520 GGPLLFKNLNFGIDlDSRIAMVGPNGIGKSTILKLISGELQPSSGTV------FRSAKVRMA-VFSQHH-VDGLDLSSNP 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 93 LtgslnrVSMLKSMLQwqSREDKLRA-LEALETVGLLdeSHQRVSQMSGGQQQRVGIARALVQDPRLLLADEPVASLDPS 171
Cdd:PLN03073 592 L------LYMMRCFPG--VPEQKLRAhLGSFGVTGNL--ALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLD 661
|
....*.
gi 493478014 172 SAETVM 177
Cdd:PLN03073 662 AVEALI 667
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
19-169 |
2.28e-07 |
|
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: 51.01 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 19 LEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQTEI---GMIfqQHNLVDGVSaylnalT 94
Cdd:cd03291 53 LKNINLKIEKgEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWimpGTI--KENIIFGVS------Y 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493478014 95 GSLNRVSMLKSMlqwQSREDKLRALEALETVglLDESHqrvSQMSGGQQQRVGIARALVQDPRLLLADEPVASLD 169
Cdd:cd03291 125 DEYRYKSVVKAC---QLEEDITKFPEKDNTV--LGEGG---ITLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
33-182 |
3.32e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 51.55 E-value: 3.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 33 LLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITgsqTEIGMIFQQHNLVDGVSAYLNALTGSlNRVSMLKSMLQWQSR 112
Cdd:TIGR01257 1970 LLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL---TNISDVHQNMGYCPQFDAIDDLLTGR-EHLYLYARLRGVPAE 2045
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493478014 113 EDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDPRLLLADEPVASLDPSSAE----TVMGYLRK 182
Cdd:TIGR01257 2046 EIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRmlwnTIVSIIRE 2119
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-199 |
7.41e-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: 50.33 E-value: 7.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 19 LEDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITgsqtEIGMifqqHNLVDGVSA-------YL 90
Cdd:TIGR00957 1302 LRHINVTIHGgEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIA----KIGL----HDLRFKITIipqdpvlFS 1373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 91 NALTGSLNRVSMLKSMLQWQSRE-DKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDPRLLLADEPVASLD 169
Cdd:TIGR00957 1374 GSLRMNLDPFSQYSDEEVWWALElAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1453
|
170 180 190
....*....|....*....|....*....|
gi 493478014 170 PSSAETVMGYLRkaAKEHDVTALVSLHQVN 199
Cdd:TIGR00957 1454 LETDNLIQSTIR--TQFEDCTVLTIAHRLN 1481
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
18-163 |
8.95e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 49.50 E-value: 8.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 18 ALEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTDPTEGSISlddepITGSQTEIgmifqqhnlvdGVSAYLNALTGS 96
Cdd:PRK13545 39 ALNNISFEVpEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVD-----IKGSAALI-----------AISSGLNGQLTG 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493478014 97 LNRVSMLKSMLQWQSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDPRLLLADE 163
Cdd:PRK13545 103 IENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE 169
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
14-169 |
1.54e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 49.17 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 14 GDVTALEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTDPTEGSISlddepITGSQTEIgmifQQHNLVDGVSAYLNA 92
Cdd:TIGR00957 649 DLPPTLNGITFSIpEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVH-----MKGSVAYV----PQQAWIQNDSLRENI 719
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493478014 93 LTGSLNRVSMLKSMLQWQSRedkLRALEALETvGLLDESHQRVSQMSGGQQQRVGIARALVQDPRLLLADEPVASLD 169
Cdd:TIGR00957 720 LFGKALNEKYYQQVLEACAL---LPDLEILPS-GDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
4-169 |
1.90e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 47.71 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGDVTALEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGltDP----TEGSIS------LDDEPITGSQTE 72
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSInKGEIHAIMGPNGSGKSTLSKVIAG--HPaykiLEGDILfkgesiLDLEPEERAHLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 73 IGMIFQQHNLVDGVSaylNA--LTGSLNrvSMLKSmlQWQSREDKLRALE----ALETVGlLDES--HQRVSQ-MSGGQQ 143
Cdd:CHL00131 86 IFLAFQYPIEIPGVS---NAdfLRLAYN--SKRKF--QGLPELDPLEFLEiineKLKLVG-MDPSflSRNVNEgFSGGEK 157
|
170 180
....*....|....*....|....*.
gi 493478014 144 QRVGIARALVQDPRLLLADEPVASLD 169
Cdd:CHL00131 158 KRNEILQMALLDSELAILDETDSGLD 183
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
18-228 |
2.85e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 47.50 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 18 ALEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDepitgsqtEIGMIfqqhnlvdGVSAYLNA-LTG 95
Cdd:PRK13546 39 ALDDISLKAyEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG--------EVSVI--------AISAGLSGqLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 96 SLN-RVSMLksMLQWQSREDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIARALVQDPRLLLADEPVASLDPSSAE 174
Cdd:PRK13546 103 IENiEFKML--CMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQ 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 493478014 175 TVMGYLRKaAKEHDVTALVSLHQVNIAAHFGDRfIGLRDGRKLFDVGR-DELTPE 228
Cdd:PRK13546 181 KCLDKIYE-FKEQNKTIFFVSHNLGQVRQFCTK-IAWIEGGKLKDYGElDDVLPK 233
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
33-169 |
7.95e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.81 E-value: 7.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 33 LLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITG--SQTEIGmiFQQHNLVDGV---SAYLNALTGSLNRVSMLKSMl 107
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGklRQDQFA--FEEFTVLDTVimgHTELWEVKQERDRIYALPEM- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 108 qwqSREDKLRALEaLET--------------------VGLLDESHQ-RVSQMSGGQQQRVGIARALVQDPRLLLADEPVA 166
Cdd:PRK15064 109 ---SEEDGMKVAD-LEVkfaemdgytaearagelllgVGIPEEQHYgLMSEVAPGWKLRVLLAQALFSNPDILLLDEPTN 184
|
...
gi 493478014 167 SLD 169
Cdd:PRK15064 185 NLD 187
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-230 |
1.63e-05 |
|
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: 45.59 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 4 LKVENLSKQYGD---VTALEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTDPT-EGSISLDDEPIT------GSQTE 72
Cdd:TIGR02633 258 LEARNLTCWDVInphRKRVDDVSFSLrRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDirnpaqAIRAG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 73 IGMI---FQQHNLVDGVSAYLNALTGSLNRVSmlksmlqwqsredKLRALEALETVGLLDESHQRVS-----------QM 138
Cdd:TIGR02633 338 IAMVpedRKRHGIVPILGVGKNITLSVLKSFC-------------FKMRIDAAAELQIIGSAIQRLKvktaspflpigRL 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 139 SGGQQQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSLHQVNIAAhFGDRFIGLRDGRKLF 218
Cdd:TIGR02633 405 SGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLG-LSDRVLVIGEGKLKG 483
|
250
....*....|..
gi 493478014 219 DVGRDELTPELI 230
Cdd:TIGR02633 484 DFVNHALTQEQV 495
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-192 |
2.22e-05 |
|
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: 44.66 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 33 LLGESGAGKSTLLRCINGLTDPTEGSisLDDEPitgSQTEIGMIFQQHNLVDgvsaYLNALTGSLNRVSMLK-------- 104
Cdd:cd03236 31 LVGPNGIGKSTALKILAGKLKPNLGK--FDDPP---DWDEILDEFRGSELQN----YFTKLLEGDVKVIVKPqyvdlipk 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 105 ----SMLQWQSREDKLRALE----ALETVGLLDeshQRVSQMSGGQQQRVGIARALVQDPRLLLADEPVASLDPSSAETV 176
Cdd:cd03236 102 avkgKVGELLKKKDERGKLDelvdQLELRHVLD---RNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNA 178
|
170 180
....*....|....*....|....
gi 493478014 177 MGYLRKAAK--------EHDVTAL 192
Cdd:cd03236 179 ARLIRELAEddnyvlvvEHDLAVL 202
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-198 |
2.49e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 45.54 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 19 LEDVSFQIEDEFAV-LLGESGAGKSTLLRCINGLTDPTEGSISLDDEPItGS------QTEIGMIFQQHNLVDGvsayln 91
Cdd:PTZ00243 1326 LRGVSFRIAPREKVgIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREI-GAyglrelRRQFSMIPQDPVLFDG------ 1398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 92 alTGSLNrvsmLKSMLQWQSREdklrALEALETVGLLD----ESH---QRV----SQMSGGQQQRVGIARALVQ-DPRLL 159
Cdd:PTZ00243 1399 --TVRQN----VDPFLEASSAE----VWAALELVGLRErvasESEgidSRVleggSNYSVGQRQLMCMARALLKkGSGFI 1468
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 493478014 160 LADEPVASLDPSSAETVMGYLRKAAKEHDV-TALVSLHQV 198
Cdd:PTZ00243 1469 LMDEATANIDPALDRQIQATVMSAFSAYTViTIAHRLHTV 1508
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-172 |
7.26e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.96 E-value: 7.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 6 VENLSKQYGDVTALEDVSFQIEDEFAV-LLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGS------QTEIGMIFQ 78
Cdd:NF033858 4 LEGVSHRYGKTVALDDVSLDIPAGCMVgLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADArhrravCPRIAYMPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 79 --QHNLVDGVSAYLNA-----LTGslnrvsmlksmlqwQSR-EDKLRALEALETVGLLDESHQRVSQMSGGQQQRVGIAR 150
Cdd:NF033858 84 glGKNLYPTLSVFENLdffgrLFG--------------QDAaERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCC 149
|
170 180
....*....|....*....|..
gi 493478014 151 ALVQDPRLLLADEPVASLDPSS 172
Cdd:NF033858 150 ALIHDPDLLILDEPTTGVDPLS 171
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
3-169 |
7.36e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.56 E-value: 7.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 3 TLKVENLSKQygDVTALEDVSFQI-EDEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPI--------------- 66
Cdd:PRK10982 250 ILEVRNLTSL--RQPSIRDVSFDLhKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKInnhnaneainhgfal 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 67 -------TGSQTEIGMIFqqHNLVDGVSAYLNAlTGSLNRVSMlKSMLQWqsredklraleALETVGLLDESHQ-RVSQM 138
Cdd:PRK10982 328 vteerrsTGIYAYLDIGF--NSLISNIRNYKNK-VGLLDNSRM-KSDTQW-----------VIDSMRVKTPGHRtQIGSL 392
|
170 180 190
....*....|....*....|....*....|.
gi 493478014 139 SGGQQQRVGIARALVQDPRLLLADEPVASLD 169
Cdd:PRK10982 393 SGGNQQKVIIGRWLLTQPEILMLDEPTRGID 423
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
33-206 |
1.10e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.31 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 33 LLGESGAGKSTLLR-----CINGLtdPTEGSISLDDEPITGSQT------------------EIGMIFQQHNLVDGVSAY 89
Cdd:PLN03073 208 LVGRNGTGKTTFLRymamhAIDGI--PKNCQILHVEQEVVGDDTtalqcvlntdiertqlleEEAQLVAQQRELEFETET 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 90 LN---ALTGSLNRVSMLKSMLQWQSREDKLRALEALETVGLL--------DESHQRVSQMSGGQQQRVGIARALVQDPRL 158
Cdd:PLN03073 286 GKgkgANKDGVDKDAVSQRLEEIYKRLELIDAYTAEARAASIlaglsftpEMQVKATKTFSGGWRMRIALARALFIEPDL 365
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 159 LLADEPVASLDPSSAETVMGYLRKAAK-----EHD-------VTALVSLHQVNIAAHFGD 206
Cdd:PLN03073 366 LLLDEPTNHLDLHAVLWLETYLLKWPKtfivvSHAreflntvVTDILHLHGQKLVTYKGD 425
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-230 |
2.48e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 42.21 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 20 EDVSFQIED-EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPI----TGSQTEIGM-----------IFQQHNLV 83
Cdd:PRK11288 270 EPISFSVRAgEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIdirsPRDAIRAGImlcpedrkaegIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 84 D--GVSAYLNALTGS--LNRvsmlksmlQWQSRE-DKLRALEALETVGlldeSHQRVSQMSGGQQQRVGIARALVQDPRL 158
Cdd:PRK11288 350 DniNISARRHHLRAGclINN--------RWEAENaDRFIRSLNIKTPS----REQLIMNLSGGNQQKAILGRWLSEDMKV 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493478014 159 LLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVS--LHQV-NIAahfgDRFIGLRDGRKLFDVGRDELTPELI 230
Cdd:PRK11288 418 ILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSsdLPEVlGVA----DRIVVMREGRIAGELAREQATERQA 488
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
33-192 |
2.57e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 42.08 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 33 LLGESGAGKSTLLRCINGLTDPTEGSIslDDEPitgSQTEI-----GMIFQQhnlvdgvsaYLNALT-GSLnRVSMLKSM 106
Cdd:COG1245 104 ILGPNGIGKSTALKILSGELKPNLGDY--DEEP---SWDEVlkrfrGTELQD---------YFKKLAnGEI-KVAHKPQY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 107 LQWQSREDKLRALEALETV---GLLDE-------SH---QRVSQMSGGQQQRVGIARALVQDPRLLLADEPVASLDPSSA 173
Cdd:COG1245 169 VDLIPKVFKGTVRELLEKVderGKLDElaeklglENildRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQR 248
|
170 180
....*....|....*....|....*..
gi 493478014 174 ETVMGYLRKAAK--------EHDVTAL 192
Cdd:COG1245 249 LNVARLIRELAEegkyvlvvEHDLAIL 275
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
126-214 |
2.95e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 42.03 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 126 GLLDESHQRVSQMSGGQQQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRKAAKEHDVTALVSlHQVNIAAHFg 205
Cdd:PLN03130 729 GDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVT-NQLHFLSQV- 806
|
....*....
gi 493478014 206 DRFIGLRDG 214
Cdd:PLN03130 807 DRIILVHEG 815
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
31-169 |
2.96e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 41.01 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 31 AVLLGESGAGKSTLLRCINGLTDPTEGSISLDDEPITGSQ----TEIGmifqqHNLvdgvsaylnaltGSLNRVSMLKSM 106
Cdd:PRK13541 29 TYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAkpycTYIG-----HNL------------GLKLEMTVFENL 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493478014 107 LQW----QSREDKLRALEALETVGLLDEshqRVSQMSGGQQQRVGIARALVQDPRLLLADEPVASLD 169
Cdd:PRK13541 92 KFWseiyNSAETLYAAIHYFKLHDLLDE---KCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-169 |
3.28e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 41.86 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 6 VENLSKQYGDVTALEDVSFQIE--DEFAvLLGESGAGKSTLLRCINGLTDPTEGSISlddepiTGSQTEIGMiFQQH--- 80
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQrgDKIA-LIGPNGCGKTTLLKLMLGQLQADSGRIH------CGTKLEVAY-FDQHrae 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 81 ---------NLVDGvsaylnaltgslnrvsmlKS--MLQWQSR------EDKL----RALealetvglldeshQRVSQMS 139
Cdd:PRK11147 394 ldpektvmdNLAEG------------------KQevMVNGRPRhvlgylQDFLfhpkRAM-------------TPVKALS 442
|
170 180 190
....*....|....*....|....*....|
gi 493478014 140 GGQQQRVGIARALVQDPRLLLADEPVASLD 169
Cdd:PRK11147 443 GGERNRLLLARLFLKPSNLLILDEPTNDLD 472
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
132-169 |
4.40e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 41.45 E-value: 4.40e-04
10 20 30
....*....|....*....|....*....|....*...
gi 493478014 132 HQRVSQMSGGQQQRVGIARALVQDPRLLLADEPVASLD 169
Cdd:PRK13549 400 ELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-176 |
5.72e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 41.11 E-value: 5.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 19 LEDVSFQIE-DEFAVLLGESGAGKSTLLRCINGLTDPTEGSiSLDDEPITGSQTEIGMIFQ---QHNLVDGvSAYLNALT 94
Cdd:PLN03232 633 LSDINLEIPvGSLVAIVGGTGEGKTSLISAMLGELSHAETS-SVVIRGSVAYVPQVSWIFNatvRENILFG-SDFESERY 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 95 GSLNRVSMLKSMLQWQSREDklralealetvglLDESHQRVSQMSGGQQQRVGIARALVQDPRLLLADEPVASLDPSSAE 174
Cdd:PLN03232 711 WRAIDVTALQHDLDLLPGRD-------------LTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAH 777
|
..
gi 493478014 175 TV 176
Cdd:PLN03232 778 QV 779
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
33-192 |
7.70e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 40.56 E-value: 7.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 33 LLGESGAGKSTLLRCINGLTDPTEGSisLDDEP--------ITGsqTEIGMIFQQhnLVDG----------VSAYLNALT 94
Cdd:PRK13409 104 ILGPNGIGKTTAVKILSGELIPNLGD--YEEEPswdevlkrFRG--TELQNYFKK--LYNGeikvvhkpqyVDLIPKVFK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 95 GSLNRVsmLKsmlqwqsREDKLRAL----EALETVGLLDeshQRVSQMSGGQQQRVGIARALVQDPRLLLADEPVASLDP 170
Cdd:PRK13409 178 GKVREL--LK-------KVDERGKLdevvERLGLENILD---RDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDI 245
|
170 180
....*....|....*....|....*....
gi 493478014 171 SSAETVMGYLRKAAK-------EHDVTAL 192
Cdd:PRK13409 246 RQRLNVARLIRELAEgkyvlvvEHDLAVL 274
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
130-182 |
1.00e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 37.60 E-value: 1.00e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493478014 130 ESHQRVSQMSGGQQQ-------------RVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLRK 182
Cdd:pfam13558 25 ETYRRSGGLSGGEKQllaylplaaalaaQYGSAEGRPPAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-218 |
3.51e-03 |
|
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: 36.97 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 29 EFAVLLGESGAGKSTLLRCINGLTDPTEGSISLddepITGSQTEIGMIFQQHNLVDGVSAYLNaltgslnrvsmlksmlq 108
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGPPGGGVIY----IDGEDILEEVLDQLLLIIVGGKKASG----------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 109 wqsredklralealetvglldeshqrvsqmSGGQQQRVGIARALVQDPRLLLADEPVASLDPSSAETVMGYLR-----KA 183
Cdd:smart00382 62 ------------------------------SGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlllLL 111
|
170 180 190
....*....|....*....|....*....|....*
gi 493478014 184 AKEHDVTALVSlhqVNIAAHFGDRFIGLRDGRKLF 218
Cdd:smart00382 112 KSEKNLTVILT---TNDEKDLGPALLRRRFDRRIV 143
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
18-48 |
4.52e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 37.84 E-value: 4.52e-03
10 20 30
....*....|....*....|....*....|...
gi 493478014 18 ALEDVSFQIEDE--FAVLLGESGAGKSTLLRCI 48
Cdd:COG3267 31 ALARLEYALAQGggFVVLTGEVGTGKTTLLRRL 63
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
16-182 |
4.61e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 36.92 E-value: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 16 VTALEDVSFQIEDEFAVLL-GESGAGKSTLlrCINGLTdpTEGSISLDDEPITGSQTEIGMIFQQHNLVDGVSAYLnalt 94
Cdd:cd03238 8 VHNLQNLDVSIPLNVLVVVtGVSGSGKSTL--VNEGLY--ASGKARLISFLPKFSRNKLIFIDQLQFLIDVGLGYL---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493478014 95 gSLNrvsmlksmlqwqsredklralealetvglldeshQRVSQMSGGQQQRVGIARALVQDPR--LLLADEPVASLDPSS 172
Cdd:cd03238 80 -TLG----------------------------------QKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQD 124
|
170
....*....|
gi 493478014 173 AETVMGYLRK 182
Cdd:cd03238 125 INQLLEVIKG 134
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
5-63 |
6.42e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 36.75 E-value: 6.42e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 493478014 5 KVENLSKQYGDvtALEDVSFQIEDEFAVLLGESGAGKSTLLRCINGLTDPTEGSISLDD 63
Cdd:pfam03193 85 PVLFVSAKTGE--GIEALKELLKGKTTVLAGQSGVGKSTLLNALLPELDLRTGEISEKL 141
|
|
| |
