|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-224 |
1.20e-118 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 338.17 E-value: 1.20e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 1 MK-IVKVKDLSKEY-TGKVSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDL 78
Cdd:COG1136 1 MSpLLELRNLTKSYgTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 79 AVFRRQELGFVFQSFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALI 158
Cdd:COG1136 81 ARLRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446629392 159 HAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDPVAASYCDRVIFIKDGQLYNEI 224
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVSDE 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-220 |
2.96e-107 |
|
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: 309.04 E-value: 2.96e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEY-TGKVSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAVFR 82
Cdd:cd03255 1 IELKNLSKTYgGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 83 RQELGFVFQSFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPK 162
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446629392 163 LVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDPVAASYCDRVIFIKDGQL 220
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-220 |
1.18e-76 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 231.48 E-value: 1.18e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYTGKvsHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAVFR 82
Cdd:COG2884 1 MIRFENVSKRYPGG--REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 83 RQeLGFVFQSFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPK 162
Cdd:COG2884 79 RR-IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446629392 163 LVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMlVTHDP-VAASYCDRVIFIKDGQL 220
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEINRRGTTVLI-ATHDLeLVDRMPKRVLELEDGRL 215
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
3-220 |
1.31e-72 |
|
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: 221.54 E-value: 1.31e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYT---GKVshTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLA 79
Cdd:COG4181 8 IIELRGLTKTVGtgaGEL--TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 80 VFRRQELGFVFQSFNLLHTLTVKENMVLPLVLDGMNVKRinKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIH 159
Cdd:COG4181 86 RLRARHVGFVFQSFQLLPTLTALENVMLPLELAGRRDAR--ARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFAT 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446629392 160 APKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDPVAASYCDRVIFIKDGQL 220
Cdd:COG4181 164 EPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRL 224
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-215 |
7.99e-71 |
|
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: 215.94 E-value: 7.99e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 6 VKDLSKEYTGKVshtALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAVFRRQE 85
Cdd:TIGR03608 1 LKNISKKFGDKV---ILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 86 LGFVFQSFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKLVL 165
Cdd:TIGR03608 78 LGYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLIL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446629392 166 ADEPTGNLDSKASQDVMEILTHLNKEEKaTMMLVTHDPVAASYCDRVIFI 215
Cdd:TIGR03608 158 ADEPTGSLDPKNRDEVLDLLLELNDEGK-TIIIVTHDPEVAKQADRVIEL 206
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-220 |
1.84e-69 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 214.15 E-value: 1.84e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 2 KIVKVKDLSKEYTGKVshTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAVF 81
Cdd:COG3638 1 PMLELRNLSKRYPGGT--PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 82 RRQeLGFVFQSFNLLHTLTVKENmvlplVLDGmnvkRINK-----------------RVESISKKLGISEILNKRTYEIS 144
Cdd:COG3638 79 RRR-IGMIFQQFNLVPRLSVLTN-----VLAG----RLGRtstwrsllglfppedreRALEALERVGLADKAYQRADQLS 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446629392 145 GGQAQRTAIARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDP-VAASYCDRVIFIKDGQL 220
Cdd:COG3638 149 GGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVdLARRYADRIIGLRDGRV 225
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
3-222 |
7.15e-69 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 211.83 E-value: 7.15e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEY-TGKVSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAVF 81
Cdd:TIGR02211 1 LLKCENLGKRYqEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 82 RRQELGFVFQSFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAP 161
Cdd:TIGR02211 81 RNKKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446629392 162 KLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDPVAASYCDRVIFIKDGQLYN 222
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDGQLFN 221
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-220 |
3.83e-66 |
|
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: 204.29 E-value: 3.83e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYTGKvshTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPndlavfRR 83
Cdd:cd03259 1 LELKGLSKTYGSV---RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPP------ER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 84 QELGFVFQSFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKL 163
Cdd:cd03259 72 RNIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446629392 164 VLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDPV-AASYCDRVIFIKDGQL 220
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEeALALADRIAVMNEGRI 209
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-220 |
6.86e-65 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 205.69 E-value: 6.86e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 1 MKIVKVKDLSKEYtGKVshTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDlav 80
Cdd:COG3839 1 MASLELENVSKSY-GGV--EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 81 fRRqeLGFVFQSFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHA 160
Cdd:COG3839 75 -RN--IAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVRE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446629392 161 PKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDPV-AASYCDRVIFIKDGQL 220
Cdd:COG3839 152 PKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVeAMTLADRIAVMNDGRI 212
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-220 |
7.63e-64 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 199.13 E-value: 7.63e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYTGKvshTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQlspNDLAVfrR 83
Cdd:COG1131 1 IEVRGLTKRYGDK---TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR---DPAEV--R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 84 QELGFVFQSFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKL 163
Cdd:COG1131 73 RRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPEL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446629392 164 VLADEPTGNLDSKASQDVMEILTHLNKEEKaTMMLVTHD-PVAASYCDRVIFIKDGQL 220
Cdd:COG1131 153 LILDEPTSGLDPEARRELWELLRELAAEGK-TVLLSTHYlEEAERLCDRVAIIDKGRI 209
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-213 |
2.69e-63 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 198.78 E-value: 2.69e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 1 MKIVKVKDLSKEY-TGKVSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPndla 79
Cdd:COG1116 5 APALELRGVSKRFpTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 80 vfrrqELGFVFQSFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIH 159
Cdd:COG1116 81 -----DRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446629392 160 APKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDPV-AASYCDRVI 213
Cdd:COG1116 156 DPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDeAVFLADRVV 210
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
3-220 |
4.60e-63 |
|
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: 196.78 E-value: 4.60e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEY-TGKVSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAVF 81
Cdd:TIGR02982 1 VISIRNLNHYYgHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 82 RRQeLGFVFQSFNLLHTLTVKENMVLPLVL-DGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHA 160
Cdd:TIGR02982 81 RRR-IGYIFQAHNLLGFLTARQNVQMALELqPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHH 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 161 PKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDPVAASYCDRVIFIKDGQL 220
Cdd:TIGR02982 160 PKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRILDVADRILQMEDGKL 219
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-220 |
4.15e-62 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 197.99 E-value: 4.15e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEY-TGKVSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAVF 81
Cdd:COG1135 1 MIELENLSKTFpTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 82 RRQeLGFVFQSFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAP 161
Cdd:COG1135 81 RRK-IGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 162 KLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHD-PVAASYCDRVIFIKDGQL 220
Cdd:COG1135 160 KVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEmDVVRRICDRVAVLENGRI 219
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-220 |
4.97e-62 |
|
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: 194.26 E-value: 4.97e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEY-TGKVSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAVf 81
Cdd:cd03257 1 LLEVKNLSVSFpTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKI- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 82 RRQELGFVFQ----SFNllHTLTVKENMVLPLVLDGMNVK--RINKRVESISKKLGISE-ILNKRTYEISGGQAQRTAIA 154
Cdd:cd03257 80 RRKEIQMVFQdpmsSLN--PRMTIGEQIAEPLRIHGKLSKkeARKEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446629392 155 RALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHD-PVAASYCDRVIFIKDGQL 220
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDlGVVAKIADRVAVMYAGKI 224
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-220 |
3.27e-61 |
|
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: 192.41 E-value: 3.27e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYTG-KVSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAVF 81
Cdd:cd03258 1 MIELKNVSKVFGDtGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 82 RRQeLGFVFQSFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAP 161
Cdd:cd03258 81 RRR-IGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 162 KLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHD-PVAASYCDRVIFIKDGQL 220
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEmEVVKRICDRVAVMEKGEV 219
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
3-219 |
7.75e-61 |
|
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: 190.92 E-value: 7.75e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYTGkvSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAVFR 82
Cdd:TIGR02673 1 MIEFHNVSKAYPG--GVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 83 RQeLGFVFQSFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPK 162
Cdd:TIGR02673 79 RR-IGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446629392 163 LVLADEPTGNLDSKASQDVMEILTHLNKeEKATMMLVTHDP-VAASYCDRVIFIKDGQ 219
Cdd:TIGR02673 158 LLLADEPTGNLDPDLSERILDLLKRLNK-RGTTVIVATHDLsLVDRVAHRVIILDDGR 214
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-220 |
1.11e-60 |
|
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: 199.36 E-value: 1.11e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYTGKVSH--TALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAV 80
Cdd:COG1123 260 LLEVRNLSKRYPVRGKGgvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 81 FRRQeLGFVFQ----SFNllHTLTVKENMVLPL-VLDGMNVKRINKRVESISKKLGIS-EILNKRTYEISGGQAQRTAIA 154
Cdd:COG1123 340 LRRR-VQMVFQdpysSLN--PRMTVGDIIAEPLrLHGLLSRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIA 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446629392 155 RALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHD-PVAASYCDRVIFIKDGQL 220
Cdd:COG1123 417 RALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDlAVVRYIADRVAVMYDGRI 483
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-220 |
1.71e-60 |
|
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: 190.62 E-value: 1.71e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYTGKvsHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLavfrR 83
Cdd:COG1122 1 IELENLSFSYPGG--TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLREL----R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 84 QELGFVFQ-SFNLLHTLTVKE-------NMvlplvldGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIAR 155
Cdd:COG1122 75 RKVGLVFQnPDDQLFAPTVEEdvafgpeNL-------GLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446629392 156 ALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKaTMMLVTHDP-VAASYCDRVIFIKDGQL 220
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGK-TVIIVTHDLdLVAELADRVIVLDDGRI 212
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-220 |
1.23e-59 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 192.24 E-value: 1.23e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 1 MKIVKVKDLSKEYTGkvsHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPyqlspNDLAV 80
Cdd:COG3842 3 MPALELENVSKRYGD---VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV-----TGLPP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 81 FRRQeLGFVFQSFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHA 160
Cdd:COG3842 75 EKRN-VGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446629392 161 PKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDPV-AASYCDRVIFIKDGQL 220
Cdd:COG3842 154 PRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEeALALADRIAVMNDGRI 214
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-213 |
1.53e-59 |
|
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: 187.68 E-value: 1.53e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEY-TGKVSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPndlavfr 82
Cdd:cd03293 1 LEVRNVSKTYgGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 83 rqELGFVFQSFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPK 162
Cdd:cd03293 74 --DRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446629392 163 LVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDpV--AASYCDRVI 213
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHD-IdeAVFLADRVV 203
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-219 |
4.31e-59 |
|
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: 186.13 E-value: 4.31e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 5 KVKDLSKEYtGKVSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLavfrRQ 84
Cdd:cd03225 1 ELKNLSFSY-PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKEL----RR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 85 ELGFVFQSFNL-LHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKL 163
Cdd:cd03225 76 KVGLVFQNPDDqFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446629392 164 VLADEPTGNLDSKASQDVMEILTHLNKEEKaTMMLVTHDP-VAASYCDRVIFIKDGQ 219
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKAEGK-TIIIVTHDLdLLLELADRVIVLEDGK 211
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-241 |
5.20e-59 |
|
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: 187.00 E-value: 5.20e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 5 KVKDLSKEYTGkvSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAVFRRQ 84
Cdd:cd03256 2 EVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 85 eLGFVFQSFNLLHTLTVKENMVLPL--------VLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARA 156
Cdd:cd03256 80 -IGMIFQQFNLIERLSVLENVLSGRlgrrstwrSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 157 LIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDP-VAASYCDRVIFIKDGqlynEIFYNDNRSLFYQ 235
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVdLAREYADRIVGLKDG----RIVFDGPPAELTD 234
|
....*.
gi 446629392 236 NIIDSL 241
Cdd:cd03256 235 EVLDEI 240
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-220 |
8.61e-59 |
|
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: 185.54 E-value: 8.61e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYTGKvshTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDlavfrr 83
Cdd:cd03301 1 VELENVTKRFGNV---TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 84 QELGFVFQSFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKL 163
Cdd:cd03301 72 RDIAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446629392 164 VLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDPVAA-SYCDRVIFIKDGQL 220
Cdd:cd03301 152 FLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAmTMADRIAVMNDGQI 209
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-219 |
1.30e-58 |
|
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: 183.93 E-value: 1.30e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYTGKvshTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAvfRR 83
Cdd:cd03229 1 LELKNVSKRYGQK---TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPP--LR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 84 QELGFVFQSFNLLHTLTVKENMVLPLvldgmnvkrinkrvesiskklgiseilnkrtyeiSGGQAQRTAIARALIHAPKL 163
Cdd:cd03229 76 RRIGMVFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446629392 164 VLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDP-VAASYCDRVIFIKDGQ 219
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLdEAARLADRVVVLRDGK 178
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-220 |
1.23e-57 |
|
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: 183.85 E-value: 1.23e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEY-TGKVSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKnpyQLSPNDLAVFR 82
Cdd:COG1124 2 LEVRNLSVSYgQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGR---PVTRRRRKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 83 RQeLGFVFQ----SFNLLHTL--TVKEnmvlPLVLdgMNVKRINKRVESISKKLGI-SEILNKRTYEISGGQAQRTAIAR 155
Cdd:COG1124 79 RR-VQMVFQdpyaSLHPRHTVdrILAE----PLRI--HGLPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446629392 156 ALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDPVAASY-CDRVIFIKDGQL 220
Cdd:COG1124 152 ALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRI 217
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-220 |
2.21e-56 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 179.24 E-value: 2.21e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 5 KVKDLSKEYTGKvshTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLavfrRQ 84
Cdd:COG4619 2 ELEGLSFRVGGK---PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEW----RR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 85 ELGFVFQSFNLLHTlTVKENMVLPLVLDGMNVKRinKRVESISKKLGISE-ILNKRTYEISGGQAQRTAIARALIHAPKL 163
Cdd:COG4619 75 QVAYVPQEPALWGG-TVRDNLPFPFQLRERKFDR--ERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446629392 164 VLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDP-VAASYCDRVIFIKDGQL 220
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPeQIERVADRVLTLEAGRL 209
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-241 |
1.25e-55 |
|
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: 178.65 E-value: 1.25e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYTGkvSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAVFR 82
Cdd:TIGR02315 1 MLEVENLSKVYPN--GKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 83 RQeLGFVFQSFNLLHTLTVKENMVLPLV--------LDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIA 154
Cdd:TIGR02315 79 RR-IGMIFQHYNLIERLTVLENVLHGRLgykptwrsLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 155 RALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHD-PVAASYCDRVIFIKDGqlynEIFYNDNRSLF 233
Cdd:TIGR02315 158 RALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQvDLAKKYADRIVGLKAG----EIVFDGAPSEL 233
|
....*...
gi 446629392 234 YQNIIDSL 241
Cdd:TIGR02315 234 DDEVLRHI 241
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-219 |
2.67e-55 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 177.49 E-value: 2.67e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYtGkvSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKnPYQLSPNDLAVFR 82
Cdd:COG1126 1 MIEIENLHKSF-G--DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGE-DLTDSKKDINKLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 83 RqELGFVFQSFNLLHTLTVKENMVLPLVLdgmnVKRINKR-VESISKKL----GISEILNKRTYEISGGQAQRTAIARAL 157
Cdd:COG1126 77 R-KVGMVFQQFNLFPHLTVLENVTLAPIK----VKKMSKAeAEERAMELlervGLADKADAYPAQLSGGQQQRVAIARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446629392 158 IHAPKLVLADEPTGNLDSKASQDVMEILTHLnKEEKATMMLVTHD-PVAASYCDRVIFIKDGQ 219
Cdd:COG1126 152 AMEPKVMLFDEPTSALDPELVGEVLDVMRDL-AKEGMTMVVVTHEmGFAREVADRVVFMDGGR 213
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-220 |
4.35e-55 |
|
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: 176.97 E-value: 4.35e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 5 KVKDLSKEYtGKVshTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPndlavFRRQ 84
Cdd:COG4555 3 EVENLSKKY-GKV--PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR-----EARR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 85 ELGFVFQSFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKLV 164
Cdd:COG4555 75 QIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446629392 165 LADEPTGNLDSKASQDVMEILTHLNKEEKaTMMLVTHDP-VAASYCDRVIFIKDGQL 220
Cdd:COG4555 155 LLDEPTNGLDVMARRLLREILRALKKEGK-TVLFSSHIMqEVEALCDRVVILHKGKV 210
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
8-224 |
4.52e-55 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 176.93 E-value: 4.52e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 8 DLSKEYT-GKVSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAVFRRQEL 86
Cdd:PRK11629 10 NLCKRYQeGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 87 GFVFQSFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKLVLA 166
Cdd:PRK11629 90 GFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446629392 167 DEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDPVAASYCDRVIFIKDGQLYNEI 224
Cdd:PRK11629 170 DEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAEL 227
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-220 |
5.83e-55 |
|
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: 176.54 E-value: 5.83e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYTGKvshTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAVFRR 83
Cdd:cd03261 1 IELRGLTKSFGGR---TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 84 QeLGFVFQSFNLLHTLTVKENMVLPLVLDG-MNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPK 162
Cdd:cd03261 78 R-MGMLFQSGALFDSLTVFENVAFPLREHTrLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446629392 163 LVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHD-PVAASYCDRVIFIKDGQL 220
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDlDTAFAIADRIAVLYDGKI 215
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-221 |
6.67e-55 |
|
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: 177.16 E-value: 6.67e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYTGKvshTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAvfr 82
Cdd:COG1120 1 MLEAENLSVGYGGR---PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELA--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 83 rQELGFVFQSFNLLHTLTVKEnMVL--------PLVLDGMNVKRInkrVESISKKLGISEILNKRTYEISGGQAQRTAIA 154
Cdd:COG1120 75 -RRIAYVPQEPPAPFGLTVRE-LVAlgryphlgLFGRPSAEDREA---VEEALERTGLEHLADRPVDELSGGERQRVLIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446629392 155 RALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDP-VAASYCDRVIFIKDGQLY 221
Cdd:COG1120 150 RALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLnLAARYADRLVLLKDGRIV 217
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-220 |
1.16e-54 |
|
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: 175.94 E-value: 1.16e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYTGKVshtALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAVFR 82
Cdd:COG1127 5 MIEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 83 RQeLGFVFQSFNLLHTLTVKENMVLPLV-LDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAP 161
Cdd:COG1127 82 RR-IGMLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 162 KLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHD-PVAASYCDRVIFIKDGQL 220
Cdd:COG1127 161 EILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDlDSAFAIADRVAVLADGKI 220
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-220 |
1.63e-54 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 178.84 E-value: 1.63e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEY-TGKVSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAVFR 82
Cdd:PRK11153 2 IELKNISKVFpQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 83 RQeLGFVFQSFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPK 162
Cdd:PRK11153 82 RQ-IGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446629392 163 LVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHD-PVAASYCDRVIFIKDGQL 220
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEmDVVKRICDRVAVIDAGRL 219
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-220 |
4.38e-54 |
|
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: 173.48 E-value: 4.38e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYTGkvsHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAVfrR 83
Cdd:cd03262 1 IEIKNLHKSFGD---FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINEL--R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 84 QELGFVFQSFNLLHTLTVKENMVLPLV-LDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPK 162
Cdd:cd03262 76 QKVGMVFQQFNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446629392 163 LVLADEPTGNLDSKASQDVMEILTHLnKEEKATMMLVTHD-PVAASYCDRVIFIKDGQL 220
Cdd:cd03262 156 VMLFDEPTSALDPELVGEVLDVMKDL-AEEGMTMVVVTHEmGFAREVADRVIFMDDGRI 213
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
3-220 |
2.38e-53 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 182.62 E-value: 2.38e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYT-GKVSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAVF 81
Cdd:PRK10535 4 LLELKDIRRSYPsGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 82 RRQELGFVFQSFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAP 161
Cdd:PRK10535 84 RREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446629392 162 KLVLADEPTGNLDSKASQDVMEILTHLnKEEKATMMLVTHDPVAASYCDRVIFIKDGQL 220
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-223 |
3.07e-53 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 171.89 E-value: 3.07e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 2 KIVKVKDLSKeYTGKVSH--TALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLA 79
Cdd:PRK10584 5 NIVEVHHLKK-SVGQGEHelSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 80 VFRRQELGFVFQSFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIH 159
Cdd:PRK10584 84 KLRAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446629392 160 APKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDPVAASYCDRVIFIKDGQLYNE 223
Cdd:PRK10584 164 RPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-220 |
4.40e-53 |
|
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: 169.50 E-value: 4.40e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYTGKvshTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNpyqlsPNDLAVFRR 83
Cdd:cd03230 1 IEVRNLSKRYGKK---TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKD-----IKKEPEEVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 84 QELGFVFQSFNLLHTLTVKENMVLplvldgmnvkrinkrvesiskklgiseilnkrtyeiSGGQAQRTAIARALIHAPKL 163
Cdd:cd03230 73 RRIGYLPEEPSLYENLTVRENLKL------------------------------------SGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446629392 164 VLADEPTGNLDSKASQDVMEILTHLNKEEKaTMMLVTHD-PVAASYCDRVIFIKDGQL 220
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLRELKKEGK-TILLSSHIlEEAERLCDRVAILNNGRI 173
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-220 |
9.66e-53 |
|
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: 170.88 E-value: 9.66e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYTGKVshtALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNdlavfRR 83
Cdd:cd03300 1 IELENVSKFYGGFV---ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH-----KR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 84 QeLGFVFQSFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKL 163
Cdd:cd03300 73 P-VNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446629392 164 VLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDPVAA-SYCDRVIFIKDGQL 220
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEAlTMSDRIAVMNKGKI 209
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-220 |
9.70e-53 |
|
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: 170.28 E-value: 9.70e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYTGKVshTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAVFRR 83
Cdd:cd03292 1 IEFINVTKTYPNGT--AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 84 QeLGFVFQSFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKL 163
Cdd:cd03292 79 K-IGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446629392 164 VLADEPTGNLDSKASQDVMEILTHLNKeEKATMMLVTHDP-VAASYCDRVIFIKDGQL 220
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKINK-AGTTVVVATHAKeLVDTTRHRVIALERGKL 214
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-220 |
1.44e-52 |
|
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: 177.79 E-value: 1.44e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYTGKvSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTI---DSATSGSVFINSKNPYQLSPNDla 79
Cdd:COG1123 4 LLEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRDLLELSEAL-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 80 vfRRQELGFVFQSF-NLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALI 158
Cdd:COG1123 81 --RGRRIGMVFQDPmTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446629392 159 HAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDP-VAASYCDRVIFIKDGQL 220
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLgVVAEIADRVVVMDDGRI 221
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-221 |
1.35e-51 |
|
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: 166.07 E-value: 1.35e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 5 KVKDLSKEYTGKvshTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAvfrrQ 84
Cdd:cd03214 1 EVENLSVGYGGR---TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELA----R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 85 ELGFVFQsfnllhtltvkenmvlplvldgmnvkrinkrvesISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKLV 164
Cdd:cd03214 74 KIAYVPQ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446629392 165 LADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDP-VAASYCDRVIFIKDGQLY 221
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLnLAARYADRVILLKDGRIV 177
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-220 |
2.10e-49 |
|
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: 161.96 E-value: 2.10e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYTGKvshTALSNINLTITEGEFVGIMGPSGSGKTTLLN----MISTIDSA-TSGSVFINSKNPYQLSPNDL 78
Cdd:cd03260 1 IELRDLNVYYGDK---HALKDISLDIPKGEITALIGPSGCGKSTLLRllnrLNDLIPGApDEGEVLLDGKDIYDLDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 79 AVFRRqeLGFVFQSFNLLHtLTVKENMVLPLVLDGM-NVKRINKRVESISKKLGISEILNKRT--YEISGGQAQRTAIAR 155
Cdd:cd03260 78 ELRRR--VGMVFQKPNPFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKDRLhaLGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446629392 156 ALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEekATMMLVTHDPVAASYC-DRVIFIKDGQL 220
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVaDRTAFLLNGRL 218
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-234 |
4.93e-49 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 161.80 E-value: 4.93e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 1 MKIVKVKDLSKEYTGkvsHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQlspndlav 80
Cdd:COG1121 4 MPAIELENLTVSYGG---RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 81 fRRQELGFVFQSFNLLHT--LTVKEnmvlpLVLDGMN-----VKRINK----RVESISKKLGISEILNKRTYEISGGQAQ 149
Cdd:COG1121 73 -ARRRIGYVPQRAEVDWDfpITVRD-----VVLMGRYgrrglFRRPSRadreAVDEALERVGLEDLADRPIGELSGGQQQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 150 RTAIARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKaTMMLVTHDP-VAASYCDRVIFIKDGQLY----NEI 224
Cdd:COG1121 147 RVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGK-TILVVTHDLgAVREYFDRVLLLNRGLVAhgppEEV 225
|
250
....*....|
gi 446629392 225 FYNDNRSLFY 234
Cdd:COG1121 226 LTPENLSRAY 235
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-219 |
3.20e-48 |
|
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: 157.16 E-value: 3.20e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYTGKvSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLavfrR 83
Cdd:cd03228 1 IEFKNVSFSYPGR-PKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESL----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 84 QELGFVFQSFNLLHTlTVKENmvlplvldgmnvkrinkrvesiskklgiseILnkrtyeiSGGQAQRTAIARALIHAPKL 163
Cdd:cd03228 76 KNIAYVPQDPFLFSG-TIREN------------------------------IL-------SGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446629392 164 VLADEPTGNLDSKASQDVMEILTHLNKEekATMMLVTHDPVAASYCDRVIFIKDGQ 219
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKG--KTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-220 |
6.73e-48 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 161.85 E-value: 6.73e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 1 MKIVkVKDLSKEYTgkvSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKN-PYQLSPNDLA 79
Cdd:COG1118 1 MSIE-VRNISKRFG---SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDlFTNLPPRERR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 80 VfrrqelGFVFQSFNLLHTLTVKENmvlplVLDGMNVK-----RINKRVESISKKLGISEILNKRTYEISGGQAQRTAIA 154
Cdd:COG1118 77 V------GFVFQHYALFPHMTVAEN-----IAFGLRVRppskaEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446629392 155 RALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDPV-AASYCDRVIFIKDGQL 220
Cdd:COG1118 146 RALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEeALELADRVVVMNQGRI 212
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-220 |
2.31e-47 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 157.18 E-value: 2.31e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYTgkvSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSknpyqLSPNDLAVFR 82
Cdd:PRK09493 1 MIEFKNVSKHFG---PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG-----LKVNDPKVDE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 83 ---RQELGFVFQSFNLLHTLTVKEN-MVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALI 158
Cdd:PRK09493 73 rliRQEAGMVFQQFYLFPHLTALENvMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446629392 159 HAPKLVLADEPTGNLDSKASQDVMEILTHLnKEEKATMMLVTHD-PVAASYCDRVIFIKDGQL 220
Cdd:PRK09493 153 VKPKLMLFDEPTSALDPELRHEVLKVMQDL-AEEGMTMVIVTHEiGFAEKVASRLIFIDKGRI 214
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-220 |
4.90e-47 |
|
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: 156.31 E-value: 4.90e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYTGkvSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLavfrR 83
Cdd:cd03295 1 IEFENVTKRYGG--GKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVEL----R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 84 QELGFVFQSFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISK--KLGISEILNKRTYEISGGQAQRTAIARALIHAP 161
Cdd:cd03295 75 RKIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLAlvGLDPAEFADRYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 162 KLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHD-PVAASYCDRVIFIKDGQL 220
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDiDEAFRLADRIAIMKNGEI 214
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
5-221 |
7.07e-47 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 155.68 E-value: 7.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 5 KVKDLSKEYtgkvSHTALsNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAVfrrq 84
Cdd:COG3840 3 RLDDLTYRY----GDFPL-RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPV---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 85 elGFVFQSFNLLHTLTVKENMVLPLVlDGMNVKRINK-RVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKL 163
Cdd:COG3840 74 --SMLFQENNLFPHLTVAQNIGLGLR-PGLKLTAEQRaQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPI 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446629392 164 VLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDPV-AASYCDRVIFIKDGQLY 221
Cdd:COG3840 151 LLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEdAARIADRVLLVADGRIA 209
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-206 |
2.44e-46 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 158.27 E-value: 2.44e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 1 MKIVKVKDLSKEYTGkvshTALS-NINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLA 79
Cdd:PRK11000 1 MASVTLRNVTKAYGD----VVISkDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 80 VfrrqelGFVFQSFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIH 159
Cdd:PRK11000 77 V------GMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446629392 160 APKLVLADEPTGNLDSkASQDVMEI-LTHLNKEEKATMMLVTHDPVAA 206
Cdd:PRK11000 151 EPSVFLLDEPLSNLDA-ALRVQMRIeISRLHKRLGRTMIYVTHDQVEA 197
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-220 |
2.50e-46 |
|
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: 154.06 E-value: 2.50e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYTGKVSHT-ALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSknpYQLSPNDLAVF 81
Cdd:cd03266 1 MITADALTKRFRDVKKTVqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG---FDVVKEPAEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 82 RRqeLGFVFQSFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAP 161
Cdd:cd03266 78 RR--LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 162 KLVLADEPTGNLDSKASQDVMEILTHLnKEEKATMMLVTHD-PVAASYCDRVIFIKDGQL 220
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHImQEVERLCDRVVVLHRGRV 214
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-213 |
2.90e-46 |
|
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: 156.75 E-value: 2.90e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEY-TGKVSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSA---TSGSVFINSKNPYQLSPNDL 78
Cdd:COG0444 1 LLEVRNLKVYFpTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 79 AVFRRQELGFVFQ----SFNllHTLTVKENMVLPLVL-DGMNVKRINKRVESISKKLGIS---EILNKRTYEISGGQAQR 150
Cdd:COG0444 81 RKIRGREIQMIFQdpmtSLN--PVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPdpeRRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446629392 151 TAIARALIHAPKLVLADEPTGNLDskAS-Q-DVMEILTHLNKEEKATMMLVTHD-PVAASYCDRVI 213
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALD--VTiQaQILNLLKDLQRELGLAILFITHDlGVVAEIADRVA 222
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
4-220 |
7.05e-46 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 153.42 E-value: 7.05e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYTgkvSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPndlavfRR 83
Cdd:TIGR00968 1 IEIANISKRFG---SFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHA------RD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 84 QELGFVFQSFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKL 163
Cdd:TIGR00968 72 RKIGFVFQHYALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446629392 164 VLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDPV-AASYCDRVIFIKDGQL 220
Cdd:TIGR00968 152 LLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEeAMEVADRIVVMSNGKI 209
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-216 |
1.26e-45 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 151.92 E-value: 1.26e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 5 KVKDLSKEYTGkvsHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQlspndlavfRRQ 84
Cdd:cd03235 1 EVEDLTVSYGG---HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK---------ERK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 85 ELGFVFQSFNLLHT--LTVKENMVLPLVLDGMNVKRINK----RVESISKKLGISEILNKRTYEISGGQAQRTAIARALI 158
Cdd:cd03235 69 RIGYVPQRRSIDRDfpISVRDVVLMGLYGHKGLFRRLSKadkaKVDEALERVGLSELADRQIGELSGGQQQRVLLARALV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446629392 159 HAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKaTMMLVTHDPVAAS-YCDRVIFIK 216
Cdd:cd03235 149 QDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGM-TILVVTHDLGLVLeYFDRVLLLN 206
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-221 |
9.33e-45 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 150.56 E-value: 9.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKeytgKVSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNdlavfrR 83
Cdd:cd03299 1 LKVENLSK----DWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE------K 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 84 QELGFVFQSFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKL 163
Cdd:cd03299 71 RDISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKI 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446629392 164 VLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDPV-AASYCDRVIFIKDGQLY 221
Cdd:cd03299 151 LLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEeAWALADKVAIMLNGKLI 209
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-220 |
9.81e-45 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 150.67 E-value: 9.81e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 1 MKIVKVKDLSKEYTGkvsHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSV-----FINSKNPyqLSP 75
Cdd:PRK11264 1 MSAIEVKNLVKKFHG---QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTARS--LSQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 76 NDLAVFR-RQELGFVFQSFNLLHTLTVKENMVL-PLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAI 153
Cdd:PRK11264 76 QKGLIRQlRQHVGFVFQNFNLFPHRTVLENIIEgPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446629392 154 ARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLnKEEKATMMLVTHD-PVAASYCDRVIFIKDGQL 220
Cdd:PRK11264 156 ARALAMRPEVILFDEPTSALDPELVGEVLNTIRQL-AQEKRTMVIVTHEmSFARDVADRAIFMDQGRI 222
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-219 |
4.10e-44 |
|
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: 146.24 E-value: 4.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 5 KVKDLSKEYTGKvshTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLavfrRQ 84
Cdd:cd00267 1 EIENLSFRYGGR---TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL----RR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 85 ELGFVFQsfnllhtltvkenmvlplvldgmnvkrinkrvesiskklgiseilnkrtyeISGGQAQRTAIARALIHAPKLV 164
Cdd:cd00267 74 RIGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446629392 165 LADEPTGNLDSKASQDVMEILTHLNKEEKaTMMLVTHDP-VAASYCDRVIFIKDGQ 219
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAEEGR-TVIIVTHDPeLAELAADRVIVLKDGK 157
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-221 |
5.74e-44 |
|
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: 148.04 E-value: 5.74e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYtGKVSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNpyqLSPNDLAVfrR 83
Cdd:cd03263 1 LQIRNLTKTY-KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYS---IRTDRKAA--R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 84 QELGFVFQSFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKL 163
Cdd:cd03263 75 QSLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446629392 164 VLADEPTGNLDSKASQDVMEILTHLNKeeKATMMLVTHDP-VAASYCDRVIFIKDGQLY 221
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMdEAEALCDRIAIMSDGKLR 211
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-220 |
5.84e-44 |
|
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: 149.52 E-value: 5.84e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYTGKVS--HTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAVF 81
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 82 RRQeLGFVFQsF--NLLHTLTV-KENMVLPLVLdGMNVKRINKRVESISKKLGISE-ILNKRTYEISGGQAQRTAIARAL 157
Cdd:TIGR04521 81 RKK-VGLVFQ-FpeHQLFEETVyKDIAFGPKNL-GLSEEEAEERVKEALELVGLDEeYLERSPFELSGGQMRRVAIAGVL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446629392 158 IHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHD-PVAASYCDRVIFIKDGQL 220
Cdd:TIGR04521 158 AMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSmEDVAEYADRVIVMHKGKI 221
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-220 |
9.54e-44 |
|
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: 147.87 E-value: 9.54e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYTgkvSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPndlavfRR 83
Cdd:cd03296 3 IEVRNVSKRFG---DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPV------QE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 84 QELGFVFQSFNLLHTLTVKENmvlplVLDGMNVKR---------INKRVESISKKLGISEILNKRTYEISGGQAQRTAIA 154
Cdd:cd03296 74 RNVGFVFQHYALFRHMTVFDN-----VAFGLRVKPrserppeaeIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446629392 155 RALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDPVAA-SYCDRVIFIKDGQL 220
Cdd:cd03296 149 RALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEAlEVADRVVVMNKGRI 215
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3-219 |
2.10e-43 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 150.87 E-value: 2.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYTGKvshTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNdlavfR 82
Cdd:PRK09452 14 LVELRGISKSFDGK---EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE-----N 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 83 RQeLGFVFQSFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPK 162
Cdd:PRK09452 86 RH-VNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446629392 163 LVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDPVAA-SYCDRVIFIKDGQ 219
Cdd:PRK09452 165 VLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEAlTMSDRIVVMRDGR 222
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
3-238 |
2.93e-43 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 149.84 E-value: 2.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYTGkvshTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPndlavfR 82
Cdd:NF040840 1 MIRIENLSKDWKE----FKLRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPP------E 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 83 RQELGFVFQSFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPK 162
Cdd:NF040840 71 KRGIAYVYQNYMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 163 LVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHD-PVAASYCDRVIFIKDGQLYN-----EIFYNDN-----RS 231
Cdd:NF040840 151 LLLLDEPLSALDVQTRDELIREMKRWHREFGFTAIHVTHNfEEALSLADRVGIMLNGRLSQvgdvrEVFRRPKnefvaRF 230
|
....*..
gi 446629392 232 LFYQNII 238
Cdd:NF040840 231 VGFENII 237
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
24-220 |
3.35e-43 |
|
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: 145.90 E-value: 3.35e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 24 NINLTiTEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFIN------SKNPYQLSPndlavfRRQELGFVFQSFNLLH 97
Cdd:cd03297 16 KIDFD-LNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNgtvlfdSRKKINLPP------QQRKIGLVFQQYALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 98 TLTVKENMVLPLVLDGMNVKRInkRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKLVLADEPTGNLDSKA 177
Cdd:cd03297 89 HLNVRENLAFGLKRKRNREDRI--SVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446629392 178 SQDVMEILTHLNKEEKATMMLVTHDPVAASY-CDRVIFIKDGQL 220
Cdd:cd03297 167 RLQLLPELKQIKKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRL 210
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
22-170 |
3.65e-43 |
|
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: 143.56 E-value: 3.65e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 22 LSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKnpyQLSPNDLAVFRRqELGFVFQSFNLLHTLTV 101
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQ---DLTDDERKSLRK-EIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446629392 102 KENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKR----TYEISGGQAQRTAIARALIHAPKLVLADEPT 170
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-220 |
5.56e-43 |
|
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: 154.61 E-value: 5.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYTGKvSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLavfRR 83
Cdd:COG2274 474 IELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASL---RR 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 84 QeLGFVFQSFNLLHTlTVKENMVL--PLVLDgmnvkrinKRVESISKKLGISEILNKRT--YE---------ISGGQAQR 150
Cdd:COG2274 550 Q-IGVVLQDVFLFSG-TIRENITLgdPDATD--------EEIIEAARLAGLHDFIEALPmgYDtvvgeggsnLSGGQRQR 619
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 151 TAIARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKeeKATMMLVTHDPVAASYCDRVIFIKDGQL 220
Cdd:COG2274 620 LAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRLADRIIVLDKGRI 687
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-213 |
6.25e-43 |
|
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: 145.66 E-value: 6.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 5 KVKDLSKEYTGkvsHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAvfrRQ 84
Cdd:cd03219 2 EVRGLTKRFGG---LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIA---RL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 85 ELGFVFQSFNLLHTLTVKENMVLPLVLDGMN----------VKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIA 154
Cdd:cd03219 76 GIGRTFQIPRLFPELTVLENVMVAAQARTGSglllararreEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 155 RALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNkEEKATMMLVTHD-PVAASYCDRVI 213
Cdd:cd03219 156 RALATDPKLLLLDEPAAGLNPEETEELAELIRELR-ERGITVLLVEHDmDVVMSLADRVT 214
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-213 |
3.01e-42 |
|
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: 144.41 E-value: 3.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 1 MKIVKVKDLSKEYTGkvsHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNpyqLSpnDLAV 80
Cdd:COG0411 2 DPLLEVRGLTKRFGG---LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRD---IT--GLPP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 81 FRRQELGFV--FQSFNLLHTLTVKENMVLPL-------VLDGM--------NVKRINKRVESISKKLGISEILNKRTYEI 143
Cdd:COG0411 74 HRIARLGIArtFQNPRLFPELTVLENVLVAAharlgrgLLAALlrlprarrEEREARERAEELLERVGLADRADEPAGNL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446629392 144 SGGQAQRTAIARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHD-PVAASYCDRVI 213
Cdd:COG0411 154 SYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDmDLVMGLADRIV 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
21-220 |
8.42e-42 |
|
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: 143.94 E-value: 8.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 21 ALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAVFRRQELGFVFQSFNLLHTLT 100
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 101 VKENMVLPLVLDGMNVK-RINKRVESIsKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKLVLADEPTGNLDSKASQ 179
Cdd:cd03294 119 VLENVAFGLEVQGVPRAeREERAAEAL-ELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRR 197
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446629392 180 DVMEILTHLNKEEKATMMLVTHDPVAA-SYCDRVIFIKDGQL 220
Cdd:cd03294 198 EMQDELLRLQAELQKTIVFITHDLDEAlRLGDRIAIMKDGRL 239
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-202 |
7.08e-41 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 141.15 E-value: 7.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 1 MKIVKVKDLSKEYTGKV-SHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKnPYQLSPNDLA 79
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGV-PVTGPGADRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 80 VfrrqelgfVFQSFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIH 159
Cdd:COG4525 80 V--------VFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446629392 160 APKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHD 202
Cdd:COG4525 152 DPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-220 |
9.35e-41 |
|
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: 147.21 E-value: 9.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYTGkvSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLavfrR 83
Cdd:COG4988 337 IELEDVSFSYPG--GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW----R 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 84 QELGFVFQSFNLLHTlTVKENMVL--PLVLDgmnvkrinKRVESISKKLGISEILNK-----------RTYEISGGQAQR 150
Cdd:COG4988 411 RQIAWVPQNPYLFAG-TIRENLRLgrPDASD--------EELEAALEAAGLDEFVAAlpdgldtplgeGGRGLSGGQAQR 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 151 TAIARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEekATMMLVTHDPVAASYCDRVIFIKDGQL 220
Cdd:COG4988 482 LALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKG--RTVILITHRLALLAQADRILVLDDGRI 549
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-220 |
1.31e-40 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 139.76 E-value: 1.31e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 1 MKIvKVKDLSKEYTgkvSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFI-NSKNPYQLSPNDLA 79
Cdd:COG4161 1 MSI-QLKNINCFYG---SHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIaGHQFDFSQKPSEKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 80 VFR-RQELGFVFQSFNLLHTLTVKENMV-LPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARAL 157
Cdd:COG4161 77 IRLlRQKVGMVFQQYNLWPHLTVMENLIeAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446629392 158 IHAPKLVLADEPTGNLDSKASQDVMEILTHLnKEEKATMMLVTHD-PVAASYCDRVIFIKDGQL 220
Cdd:COG4161 157 MMEPQVLLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEvEFARKVASQVVYMEKGRI 219
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-219 |
1.12e-39 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 140.36 E-value: 1.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 1 MKIVKVKDLSKEYTGKVShtALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDlav 80
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKTQ--VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 81 frrQELGFVFQSFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHA 160
Cdd:PRK11650 76 ---RDIAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVRE 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446629392 161 PKLVLADEPTGNLDSKAS-QDVMEILtHLNKEEKATMMLVTHDPVAA-SYCDRVIFIKDGQ 219
Cdd:PRK11650 153 PAVFLFDEPLSNLDAKLRvQMRLEIQ-RLHRRLKTTSLYVTHDQVEAmTLADRVVVMNGGV 212
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
19-220 |
2.67e-39 |
|
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: 135.70 E-value: 2.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 19 HTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAVfrrqelGFVFQSFNLLHT 98
Cdd:cd03298 11 GEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPV------SMLFQENNLFAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 99 LTVKENMVLPLV--LDGMNVKRinKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKLVLADEPTGNLDSK 176
Cdd:cd03298 85 LTVEQNVGLGLSpgLKLTAEDR--QAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446629392 177 ASQDVMEILTHLNKEEKATMMLVTHDPV-AASYCDRVIFIKDGQL 220
Cdd:cd03298 163 LRAEMLDLVLDLHAETKMTVLMVTHQPEdAKRLAQRVVFLDNGRI 207
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
21-220 |
1.21e-38 |
|
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: 134.25 E-value: 1.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 21 ALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLavfrRQELGFVFQSFNLLHTlT 100
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL----RRNIGYVPQDVTLFYG-T 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 101 VKENMVL--PLVLDgmnvkrinKRVESISKKLGISEILNK-----------RTYEISGGQAQRTAIARALIHAPKLVLAD 167
Cdd:cd03245 94 LRDNITLgaPLADD--------ERILRAAELAGVTDFVNKhpngldlqigeRGRGLSGGQRQAVALARALLNDPPILLLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446629392 168 EPTGNLDSKASQDVMEILTHLNKEEkaTMMLVTHDPVAASYCDRVIFIKDGQL 220
Cdd:cd03245 166 EPTSAMDMNSEERLKERLRQLLGDK--TLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-220 |
1.54e-38 |
|
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: 141.06 E-value: 1.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYTGKvSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLavfrR 83
Cdd:COG4987 334 LELEDVSFRYPGA-GRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDL----R 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 84 QELGFVFQSFNLLHTlTVKEN--MVLPLVLDGmnvkrinkRVESISKKLGISEI-------LNKRTYE----ISGGQAQR 150
Cdd:COG4987 409 RRIAVVPQRPHLFDT-TLRENlrLARPDATDE--------ELWAALERVGLGDWlaalpdgLDTWLGEggrrLSGGERRR 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446629392 151 TAIARALIHAPKLVLADEPTGNLDSKASQDVME-ILTHLnkeEKATMMLVTHDPVAASYCDRVIFIKDGQL 220
Cdd:COG4987 480 LALARALLRDAPILLLDEPTEGLDAATEQALLAdLLEAL---AGRTVLLITHRLAGLERMDRILVLEDGRI 547
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
22-218 |
2.38e-38 |
|
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: 133.75 E-value: 2.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 22 LSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAVFrrqelgfvfQSFNLLHTLTV 101
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVF---------QNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 102 KENMVLPL--VLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKLVLADEPTGNLDSKASQ 179
Cdd:TIGR01184 72 RENIALAVdrVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446629392 180 DVMEILTHLNKEEKATMMLVTHDPVAASY-CDRVIFIKDG 218
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHDVDEALLlSDRVVMLTNG 191
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-220 |
2.83e-38 |
|
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: 133.26 E-value: 2.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYTGkvsHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFIN----SKNPYQLspndla 79
Cdd:cd03265 1 IEVENLVKKYGD---FEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAghdvVREPREV------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 80 vfrRQELGFVFQSFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIH 159
Cdd:cd03265 72 ---RRRIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVH 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446629392 160 APKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHD-PVAASYCDRVIFIKDGQL 220
Cdd:cd03265 149 RPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYmEEAEQLCDRVAIIDHGRI 210
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-220 |
5.95e-38 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 135.21 E-value: 5.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYT---------GKVSH---------TALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVF 64
Cdd:COG4586 1 IIEVENLSKTYRvyekepglkGALKGlfrreyrevEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 65 INSKNPYQlspndlavfRRQEL----GFVF-QSFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKR 139
Cdd:COG4586 81 VLGYVPFK---------RRKEFarriGVVFgQRSQLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 140 TYEISGGQAQRTAIARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDP--VAAsYCDRVIFIKD 217
Cdd:COG4586 152 VRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMddIEA-LCDRVIVIDH 230
|
...
gi 446629392 218 GQL 220
Cdd:COG4586 231 GRI 233
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
3-221 |
8.93e-38 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 131.92 E-value: 8.93e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYTGkvSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAVFR 82
Cdd:PRK10908 1 MIRFEHVSKAYLG--GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 83 RQeLGFVFQSFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPK 162
Cdd:PRK10908 79 RQ-IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 163 LVLADEPTGNLDSKASQDVMEILTHLNKeEKATMMLVTHD-PVAASYCDRVIFIKDGQLY 221
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDiGLISRRSYRMLTLSDGHLH 216
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-218 |
1.39e-37 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 132.06 E-value: 1.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 1 MKIvKVKDLSKEYTgkvSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFI-NSKNPYQLSPNDLA 79
Cdd:PRK11124 1 MSI-QLNGINCFYG---AHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIaGNHFDFSKTPSDKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 80 VFR-RQELGFVFQSFNLLHTLTVKENMV-LPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARAL 157
Cdd:PRK11124 77 IRElRRNVGMVFQQYNLWPHLTVQQNLIeAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446629392 158 IHAPKLVLADEPTGNLDSKASQDVMEILTHLnKEEKATMMLVTHD-PVAASYCDRVIFIKDG 218
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEvEVARKTASRVVYMENG 217
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
20-220 |
6.79e-37 |
|
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: 130.14 E-value: 6.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 20 TALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNdlavFRRQeLGFVF-QSFNLLHT 98
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKK----FLRR-IGVVFgQKTQLWWD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 99 LTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKLVLADEPTGNLDSKAS 178
Cdd:cd03267 110 LPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQ 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446629392 179 QDVMEILTHLNKEEKATMMLVTHD--PVAAsYCDRVIFIKDGQL 220
Cdd:cd03267 190 ENIRNFLKEYNRERGTTVLLTSHYmkDIEA-LARRVLVIDKGRL 232
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-220 |
1.17e-36 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 128.85 E-value: 1.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYTGKVshtALSNINLTITEGEFvGIMGPSGSGKTTLLNMISTIDSATSGSVFIN----SKNPYQLspndla 79
Cdd:cd03264 1 LQLENLTKRYGKKR---ALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDgqdvLKQPQKL------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 80 vfrRQELGFVFQSFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIH 159
Cdd:cd03264 71 ---RRRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446629392 160 APKLVLADEPTGNLDSKASQDVMEILTHLNKEekATMMLVTH--DPVAASyCDRVIFIKDGQL 220
Cdd:cd03264 148 DPSILIVDEPTAGLDPEERIRFRNLLSELGED--RIVILSTHivEDVESL-CNQVAVLNKGKL 207
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-233 |
1.69e-36 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 129.51 E-value: 1.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYTGKvshTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDS-----ATSGSVFINSKNPYqlSPND 77
Cdd:PRK14239 5 ILQVSDLSVYYNKK---KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIY--SPRT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 78 LAVFRRQELGFVFQSFNLLhTLTVKENMVLPLVLDGMNVKRI-NKRVESISKKLGISEILNKRTYE----ISGGQAQRTA 152
Cdd:PRK14239 80 DTVDLRKEIGMVFQQPNPF-PMSIYENVVYGLRLKGIKDKQVlDEAVEKSLKGASIWDEVKDRLHDsalgLSGGQQQRVC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 153 IARALIHAPKLVLADEPTGNLDSKASQDVMEILthLNKEEKATMMLVTHDPVAAS-YCDRVIFIKDGQLyneIFYNDNRS 231
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETL--LGLKDDYTMLLVTRSMQQASrISDRTGFFLDGDL---IEYNDTKQ 233
|
..
gi 446629392 232 LF 233
Cdd:PRK14239 234 MF 235
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
26-220 |
2.48e-36 |
|
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: 128.06 E-value: 2.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 26 NLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNdlavfrRQELGFVFQSFNLLHTLTVKENM 105
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPY------QRPVSMLFQENNLFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 106 VLPLVlDGMNVKRINK-RVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKLVLADEPTGNLDSKASQDVMEI 184
Cdd:TIGR01277 92 GLGLH-PGLKLNAEQQeKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLAL 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 446629392 185 LTHLNKEEKATMMLVTHDPV-AASYCDRVIFIKDGQL 220
Cdd:TIGR01277 171 VKQLCSERQRTLLMVTHHLSdARAIASQIAVVSQGKI 207
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
24-219 |
2.70e-36 |
|
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: 131.76 E-value: 2.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 24 NINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFIN------SKNPYQLSPNdlavfRRQeLGFVFQSFNLLH 97
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGgevlqdSARGIFLPPH-----RRR-IGYVFQEARLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 98 TLTVKENmvlplVLDGMnvKRINK-----RVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKLVLADEPTGN 172
Cdd:COG4148 91 HLSVRGN-----LLYGR--KRAPRaerriSFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446629392 173 LDSKASQDVMEILTHLNKEEKATMMLVTHDPV-AASYCDRVIFIKDGQ 219
Cdd:COG4148 164 LDLARKAEILPYLERLRDELDIPILYVSHSLDeVARLADHVVLLEQGR 211
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-227 |
3.07e-36 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 129.00 E-value: 3.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYTGKVshtALSNINLTITEGEFVGIMGPSGSGKTTLL---N-MISTIDSA-TSGSVFINSKNPYqlSPN- 76
Cdd:COG1117 11 KIEVRNLNVYYGDKQ---ALKDINLDIPENKVTALIGPSGCGKSTLLrclNrMNDLIPGArVEGEILLDGEDIY--DPDv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 77 DLAVFRRQeLGFVFQSFNLLhTLTVKENMVLPLVLDGMNVKR-INKRVESISKKLGI----SEILNKRTYEISGGQAQRT 151
Cdd:COG1117 86 DVVELRRR-VGMVFQKPNPF-PKSIYDNVAYGLRLHGIKSKSeLDEIVEESLRKAALwdevKDRLKKSALGLSGGQQQRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 152 AIARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEekATMMLVTHDPVAASYC-DRVIFIKDGQL--YN---EIF 225
Cdd:COG1117 164 CIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD--YTIVIVTHNMQQAARVsDYTAFFYLGELveFGpteQIF 241
|
..
gi 446629392 226 YN 227
Cdd:COG1117 242 TN 243
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
3-219 |
3.77e-36 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 127.94 E-value: 3.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYT----GKVSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPY----QLS 74
Cdd:COG4778 4 LLEVENLSKTFTlhlqGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWvdlaQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 75 PNDLAVFRRQELGFVFQsFnlLHTL-------TVKEnmvlPLVLDGMNVKRINKRVESISKKLGISEIL---NKRTYeiS 144
Cdd:COG4778 84 PREILALRRRTIGYVSQ-F--LRVIprvsaldVVAE----PLLERGVDREEARARARELLARLNLPERLwdlPPATF--S 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446629392 145 GGQAQRTAIARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLnKEEKATMMLVTHDP-VAASYCDRVIFIKDGQ 219
Cdd:COG4778 155 GGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDEeVREAVADRVVDVTPFS 229
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-237 |
3.86e-36 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 128.98 E-value: 3.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYTgkvSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSA--TSGSVFINSKNPYQLSPNDLAV 80
Cdd:PRK09984 4 IIRVEKLAKTFN---QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGdkSAGSHIELLGRTVQREGRLARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 81 FR--RQELGFVFQSFNLLHTLTVKENMVL------PL---VLDGMNVKRINKRVESISKkLGISEILNKRTYEISGGQAQ 149
Cdd:PRK09984 81 IRksRANTGYIFQQFNLVNRLSVLENVLIgalgstPFwrtCFSWFTREQKQRALQALTR-VGMVHFAHQRVSTLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 150 RTAIARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHD-PVAASYCDRVIFIKDGQLY----NEI 224
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQvDYALRYCERIVALRQGHVFydgsSQQ 239
|
250
....*....|...
gi 446629392 225 FYNDNRSLFYQNI 237
Cdd:PRK09984 240 FDNERFDHLYRSI 252
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-220 |
6.29e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 129.44 E-value: 6.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 1 MKIvKVKDLSKEYTGKVSH--TALSNINLTITEGEFVGIMGPSGSGKTTL---LNMISTIDSATSGSVFINSKNPYQLSP 75
Cdd:PRK13651 1 MQI-KVKNIVKIFNKKLPTelKALDNVSVEINQGEFIAIIGQTGSGKTTFiehLNALLLPDTGTIEWIFKDEKNKKKTKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 76 NDLAV---------FR--------RQELGFVFQ--SFNLLHTlTVKENMVLPLVLDGMNVKRINKRVESISKKLGISE-I 135
Cdd:PRK13651 80 KEKVLeklviqktrFKkikkikeiRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDEsY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 136 LNKRTYEISGGQAQRTAIARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKaTMMLVTHD-PVAASYCDRVIF 214
Cdd:PRK13651 159 LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDlDNVLEWTKRTIF 237
|
....*.
gi 446629392 215 IKDGQL 220
Cdd:PRK13651 238 FKDGKI 243
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
3-224 |
9.26e-36 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 128.00 E-value: 9.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYT-----GKVSH-TALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPN 76
Cdd:TIGR02769 2 LLEVRDVTHTYRtgglfGAKQRaPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 77 DLAVFRRqELGFVFQ----SFNllHTLTVKENMVLPLV-LDGMNVKRINKRVESISKKLGI-SEILNKRTYEISGGQAQR 150
Cdd:TIGR02769 82 QRRAFRR-DVQLVFQdspsAVN--PRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446629392 151 TAIARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHD-PVAASYCDRVIFIKDGQLYNEI 224
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDlRLVQSFCQRVAVMDKGQIVEEC 233
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
22-218 |
1.83e-35 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 129.43 E-value: 1.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 22 LSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAVfrrqelGFVFQSFNLLHTLTV 101
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKV------GFVFQHYALFRHMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 102 KENMVLPL-VL---DGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKLVLADEPTGNLDSKA 177
Cdd:PRK10851 92 FDNIAFGLtVLprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446629392 178 SQDVMEILTHLNKEEKATMMLVTHD-PVAASYCDRVIFIKDG 218
Cdd:PRK10851 172 RKELRRWLRQLHEELKFTSVFVTHDqEEAMEVADRVVVMSQG 213
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-219 |
2.03e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 127.66 E-value: 2.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYTGKVShtALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKnPYQLSPNDLAVFR 82
Cdd:PRK13636 5 ILKVEELNYNYSDGTH--ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGK-PIDYSRKGLMKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 83 rQELGFVFQS-FNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAP 161
Cdd:PRK13636 82 -ESVGMVFQDpDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446629392 162 KLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHD-PVAASYCDRVIFIKDGQ 219
Cdd:PRK13636 161 KVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDiDIVPLYCDNVFVMKEGR 219
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-219 |
4.39e-35 |
|
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: 124.85 E-value: 4.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 5 KVKDLSKEYtGKVshTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAvfrRQ 84
Cdd:cd03224 2 EVENLNAGY-GKS--QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERA---RA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 85 ELGFVFQSFNLLHTLTVKENMVLPL-VLDGMNVKRINKRVESISKKLGisEILNKRTYEISGGQAQRTAIARALIHAPKL 163
Cdd:cd03224 76 GIGYVPEGRRIFPELTVEENLLLGAyARRRAKRKARLERVYELFPRLK--ERRKQLAGTLSGGEQQMLAIARALMSRPKL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446629392 164 VLADEPTGNLDSKASQDVMEILTHLNKEEkATMMLVTHD-PVAASYCDRVIFIKDGQ 219
Cdd:cd03224 154 LLLDEPSEGLAPKIVEEIFEAIRELRDEG-VTILLVEQNaRFALEIADRAYVLERGR 209
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-219 |
4.60e-35 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 126.07 E-value: 4.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYtGkvSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFIN-------SKNPYQLSPN 76
Cdd:COG4598 9 LEVRDLHKSF-G--DLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGgeeirlkPDRDGELVPA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 77 DLA-VFR-RQELGFVFQSFNLLHTLTVKEN-MVLPL-VLdGMNVKRINKRVESISKKLGISEilnKRTY---EISGGQAQ 149
Cdd:COG4598 86 DRRqLQRiRTRLGMVFQSFNLWSHMTVLENvIEAPVhVL-GRPKAEAIERAEALLAKVGLAD---KRDAypaHLSGGQQQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446629392 150 RTAIARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLnKEEKATMMLVTHD-PVAASYCDRVIFIKDGQ 219
Cdd:COG4598 162 RAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDL-AEEGRTMLVVTHEmGFARDVSSHVVFLHQGR 231
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-219 |
6.41e-35 |
|
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: 124.32 E-value: 6.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYTgkvSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKnpyqlsPNDLAVfrR 83
Cdd:cd03269 1 LEVENVTKRFG---RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGK------PLDIAA--R 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 84 QELGFVFQSFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKL 163
Cdd:cd03269 70 NRIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPEL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446629392 164 VLADEPTGNLDSKASQDVMEILTHLnKEEKATMMLVTH--DPVAAsYCDRVIFIKDGQ 219
Cdd:cd03269 150 LILDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHqmELVEE-LCDRVLLLNKGR 205
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-220 |
6.62e-35 |
|
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: 123.91 E-value: 6.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 6 VKDLSKEYTGKVShtALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNpyqLSPNDlavfRRQE 85
Cdd:cd03226 2 IENISFSYKKGTE--ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP---IKAKE----RRKS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 86 LGFVFQSFNL-LHTLTVKENmvlpLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKLV 164
Cdd:cd03226 73 IGYVMQDVDYqLFTDSVREE----LLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446629392 165 LADEPTGNLDSKASQDVMEILTHLNKEEKAtMMLVTHDP-VAASYCDRVIFIKDGQL 220
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELIRELAAQGKA-VIVITHDYeFLAKVCDRVLLLANGAI 204
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
7-220 |
1.27e-34 |
|
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: 123.04 E-value: 1.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 7 KDLSKEYTGKVSHTA---LSNINLTITEGEFVGIMGPSGSGKTTLLNMIS--TIDSATSGSVFINSKnpyqlsPNDLAVF 81
Cdd:cd03213 7 RNLTVTVKSSPSKSGkqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGR------PLDKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 82 RRQeLGFVFQSFNLLHTLTVKENMVLPLVLDGmnvkrinkrvesiskklgiseilnkrtyeISGGQAQRTAIARALIHAP 161
Cdd:cd03213 81 RKI-IGYVPQDDILHPTLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNP 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446629392 162 KLVLADEPTGNLDSKASQDVMEILTHLNKEEKaTMMLVTHDPVAASY--CDRVIFIKDGQL 220
Cdd:cd03213 131 SLLFLDEPTSGLDSSSALQVMSLLRRLADTGR-TIICSIHQPSSEIFelFDKLLLLSQGRV 190
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-220 |
5.00e-34 |
|
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: 122.65 E-value: 5.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYTGKvshTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINsknpyQLSPNDLAVFRR 83
Cdd:cd03218 1 LRAENLSKRYGKR---KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLD-----GQDITKLPMHKR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 84 QELGFVF--QSFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAP 161
Cdd:cd03218 73 ARLGIGYlpQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446629392 162 KLVLADEPTGNLDSKASQDVMEILTHLNkeEKATMMLVTHDPV--AASYCDRVIFIKDGQL 220
Cdd:cd03218 153 KFLLLDEPFAGVDPIAVQDIQKIIKILK--DRGIGVLITDHNVreTLSITDRAYIIYEGKV 211
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-212 |
5.11e-34 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 121.82 E-value: 5.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYTGkvsHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNdlavfRR 83
Cdd:COG4133 3 LEAENLSCRRGE---RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED-----YR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 84 QELGFVFQSFNLLHTLTVKENMVLPLVLDGMNVKRInkRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKL 163
Cdd:COG4133 75 RRLAYLGHADGLKPELTVRENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446629392 164 VLADEPTGNLDSKASQDVMEIL-THLnkEEKATMMLVTHDPVAASYCDRV 212
Cdd:COG4133 153 WLLDEPFTALDAAGVALLAELIaAHL--ARGGAVLLTTHQPLELAAARVL 200
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-220 |
5.18e-34 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 127.84 E-value: 5.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYtGKVshTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKnPYQL-SPNDlAvf 81
Cdd:COG3845 5 ALELRGITKRF-GGV--VANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGK-PVRIrSPRD-A-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 82 RRQELGFVFQSFNLLHTLTVKENMVL---PLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALI 158
Cdd:COG3845 78 IALGIGMVHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALY 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446629392 159 HAPKLVLADEPTGNLDSKASQDVMEILTHLnKEEKATMMLVTH--DPVAAsYCDRVIFIKDGQL 220
Cdd:COG3845 158 RGARILILDEPTAVLTPQEADELFEILRRL-AAEGKSIIFITHklREVMA-IADRVTVLRRGKV 219
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
26-221 |
1.55e-33 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 121.23 E-value: 1.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 26 NLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNdlavfrRQELGFVFQSFNLLHTLTVKENM 105
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS------RRPVSMLFQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 106 VLplvldGMNVK-RIN----KRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKLVLADEPTGNLDSKASQD 180
Cdd:PRK10771 93 GL-----GLNPGlKLNaaqrEKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446629392 181 VMEILTHLNKEEKATMMLVTH---DpvAASYCDRVIFIKDGQLY 221
Cdd:PRK10771 168 MLTLVSQVCQERQLTLLMVSHsleD--AARIAPRSLVVADGRIA 209
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-220 |
1.58e-33 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 124.06 E-value: 1.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYtGKvsHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSpndlavFRR 83
Cdd:PRK11432 7 VVLKNITKRF-GS--NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRS------IQQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 84 QELGFVFQSFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKL 163
Cdd:PRK11432 78 RDICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446629392 164 VLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDPVAA-SYCDRVIFIKDGQL 220
Cdd:PRK11432 158 LLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAfAVSDTVIVMNKGKI 215
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-219 |
2.16e-33 |
|
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: 126.72 E-value: 2.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYTGK-------VSH-TALSNINLTITEGEFVGIMGPSGSGKTTL----LNMIstidsATSGSVFINSKNP 70
Cdd:COG4172 275 LLEARDLKVWFPIKrglfrrtVGHvKAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLI-----PSEGEIRFDGQDL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 71 YQLSPNDLAVFRRQeLGFVFQ----SFNLLHTL--TVKEnmvlPLVL--DGMNVKRINKRVESISKKLGIS-EILNKRTY 141
Cdd:COG4172 350 DGLSRRALRPLRRR-MQVVFQdpfgSLSPRMTVgqIIAE----GLRVhgPGLSAAERRARVAEALEEVGLDpAARHRYPH 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446629392 142 EISGGQAQRTAIARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHD-PVAASYCDRVIFIKDGQ 219
Cdd:COG4172 425 EFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDlAVVRALAHRVMVMKDGK 503
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
6-223 |
2.22e-33 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 121.61 E-value: 2.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 6 VKDLSKEYTgkvSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPND--LAVFR- 82
Cdd:PRK10619 8 VIDLHKRYG---EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgqLKVADk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 83 ------RQELGFVFQSFNLLHTLTVKEN-MVLPLVLDGMNVKRINKRVESISKKLGISE-ILNKRTYEISGGQAQRTAIA 154
Cdd:PRK10619 85 nqlrllRTRLTMVFQHFNLWSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIDErAQGKYPVHLSGGQQQRVSIA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 155 RALIHAPKLVLADEPTGNLDSKASQDVMEILTHLnKEEKATMMLVTHD-PVAASYCDRVIFIKDGQLYNE 223
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEmGFARHVSSHVIFLHQGKIEEE 233
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-246 |
2.54e-33 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 124.18 E-value: 2.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYTGKvshTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPndlavFR 82
Cdd:PRK11607 19 LLEIRNLTKSFDGQ---HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP-----YQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 83 RqELGFVFQSFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPK 162
Cdd:PRK11607 91 R-PINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 163 LVLADEPTGNLDSKASQ----DVMEILTHLNkeekATMMLVTHDPVAA-------SYCDRVIFIKDGQLyNEIFYNDNrS 231
Cdd:PRK11607 170 LLLLDEPMGALDKKLRDrmqlEVVDILERVG----VTCVMVTHDQEEAmtmagriAIMNRGKFVQIGEP-EEIYEHPT-T 243
|
250
....*....|....*
gi 446629392 232 LFYQNIIDSLSMLGG 246
Cdd:PRK11607 244 RYSAEFIGSVNVFEG 258
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-235 |
3.19e-33 |
|
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: 120.96 E-value: 3.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYTGKvshTALSNINLTITEGEFVGIMGPSGSGKTTLLNMIStidsatsGSVfinsknpYQLSPNDLAVF- 81
Cdd:COG1119 3 LLELRNVTVRRGGK---TILDDISWTVKPGEHWAILGPNGAGKSTLLSLIT-------GDL-------PPTYGNDVRLFg 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 82 --R--------RQELGFVfqSFNLLHTLTVKENmVLPLVLDG--------MNVKRINK-RVESISKKLGISEILNKRTYE 142
Cdd:COG1119 66 erRggedvwelRKRIGLV--SPALQLRFPRDET-VLDVVLSGffdsiglyREPTDEQReRARELLELLGLAHLADRPFGT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 143 ISGGQAQRTAIARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTH--DPVAASYcDRVIFIKDGQL 220
Cdd:COG1119 143 LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHhvEEIPPGI-THVLLLKDGRV 221
|
250 260
....*....|....*....|
gi 446629392 221 Y-----NEIFYNDNRSLFYQ 235
Cdd:COG1119 222 VaagpkEEVLTSENLSEAFG 241
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-242 |
3.78e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 120.92 E-value: 3.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 6 VKDLSKEYTGKVSHTALSNINLTITEGEFVGIMGPSGSGKTTLLN----MISTIDSA--TSGSVFINSKNPYQLSpndlA 79
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKvlnrLIEIYDSKikVDGKVLYFGKDIFQID----A 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 80 VFRRQELGFVFQSFNLLHTLTVKENMVLPLVLDGMNVKR-INKRVESISKKLG----ISEILNKRTYEISGGQAQRTAIA 154
Cdd:PRK14246 86 IKLRKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKReIKKIVEECLRKVGlwkeVYDRLNSPASQLSGGQQQRLTIA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 155 RALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEekATMMLVTHDP-VAASYCDRVIFIKDGQLY-----NEIFYND 228
Cdd:PRK14246 166 RALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPqQVARVADYVAFLYNGELVewgssNEIFTSP 243
|
250
....*....|....
gi 446629392 229 NRSLFYQNIIDSLS 242
Cdd:PRK14246 244 KNELTEKYVIGRIS 257
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
37-246 |
4.24e-33 |
|
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: 122.60 E-value: 4.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 37 IMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNdlavfrRQELGFVFQSFNLLHTLTVKENMVLPLVLDGMNV 116
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH------LRHINMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 117 KRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATM 196
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITF 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446629392 197 MLVTHDPVAA-SYCDRVIFIKDGQLYN----EIFYNDNRSLFYQNIIDSLSMLGG 246
Cdd:TIGR01187 155 VFVTHDQEEAmTMSDRIAIMRKGKIAQigtpEEIYEEPANLFVARFIGEINVFEA 209
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-220 |
4.88e-33 |
|
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: 118.09 E-value: 4.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 6 VKDLSKEYTGKvSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLavfrRQE 85
Cdd:cd03246 3 VENVSFRYPGA-EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNEL----GDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 86 LGFVFQSFNLLhTLTVKENmvlplvldgmnvkrinkrvesiskklgiseILnkrtyeiSGGQAQRTAIARALIHAPKLVL 165
Cdd:cd03246 78 VGYLPQDDELF-SGSIAEN------------------------------IL-------SGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446629392 166 ADEPTGNLDSKASQDVMEILTHLnKEEKATMMLVTHDPVAASYCDRVIFIKDGQL 220
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-220 |
5.42e-33 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 126.05 E-value: 5.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYTGkvSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLavfrR 83
Cdd:COG1132 340 IEFENVSFSYPG--DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESL----R 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 84 QELGFVFQSFNLLHTlTVKENMVLplvldGmnvkRIN---KRVESISKKLGISE-----------ILNKRTYEISGGQAQ 149
Cdd:COG1132 414 RQIGVVPQDTFLFSG-TIRENIRY-----G----RPDatdEEVEEAAKAAQAHEfiealpdgydtVVGERGVNLSGGQRQ 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446629392 150 RTAIARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEekATMMLVTHDPVAASYCDRVIFIKDGQL 220
Cdd:COG1132 484 RIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKG--RTTIVIAHRLSTIRNADRILVLDDGRI 552
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
25-220 |
5.67e-33 |
|
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: 122.91 E-value: 5.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 25 INLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFIN------SKNPYQLSPNdlavfrRQELGFVFQSFNLLHT 98
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNgrtlfdSRKGIFLPPE------KRRIGYVFQEARLFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 99 LTVKENMVLplvldGM---NVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKLVLADEPTGNLDS 175
Cdd:TIGR02142 90 LSVRGNLRY-----GMkraRPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446629392 176 KASQDVMEILTHLNKEEKATMMLVTHDPV-AASYCDRVIFIKDGQL 220
Cdd:TIGR02142 165 PRKYEILPYLERLHAEFGIPILYVSHSLQeVLRLADRVVVLEDGRV 210
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-202 |
6.30e-33 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 120.19 E-value: 6.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYTGKvshTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKnPYQlSPNdlavfr 82
Cdd:PRK11248 1 MLQISHLYADYGGK---PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK-PVE-GPG------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 83 rQELGFVFQSFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPK 162
Cdd:PRK11248 70 -AERGVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQ 148
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446629392 163 LVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHD 202
Cdd:PRK11248 149 LLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHD 188
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-223 |
7.11e-33 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 120.89 E-value: 7.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 2 KIVKVKDLSKEYTGKvSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKnpyQLSPNDLAVF 81
Cdd:PRK13635 4 EIIRVEHISFRYPDA-ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEETVWDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 82 RRQeLGFVFQS-FNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHA 160
Cdd:PRK13635 80 RRQ-VGMVFQNpDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQ 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446629392 161 PKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDPVAASYCDRVIFIKDGQLYNE 223
Cdd:PRK13635 159 PDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEE 221
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-188 |
1.25e-32 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 118.98 E-value: 1.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 1 MKIVKVKDLSKEYTGKvshTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNpyqLSpnDLAV 80
Cdd:COG1137 1 MMTLEAENLVKSYGKR---TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGED---IT--HLPM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 81 FRRQELGF--------VFQSfnllhtLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTA 152
Cdd:COG1137 73 HKRARLGIgylpqeasIFRK------LTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVE 146
|
170 180 190
....*....|....*....|....*....|....*.
gi 446629392 153 IARALIHAPKLVLADEPTGNLDSKASQDVMEILTHL 188
Cdd:COG1137 147 IARALATNPKFILLDEPFAGVDPIAVADIQKIIRHL 182
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-219 |
1.32e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 120.15 E-value: 1.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 1 MKIvKVKDLSKEYTGKV--SHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPY--QLSPN 76
Cdd:PRK13637 1 MSI-KIENLTHIYMEGTpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 77 DLavfrRQELGFVFQ--SFNLLHTlTVKENMVLPLVLDGMNVKRINKRVESISKKLGIS--EILNKRTYEISGGQAQRTA 152
Cdd:PRK13637 80 DI----RKKVGLVFQypEYQLFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446629392 153 IARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTH--DPVaASYCDRVIFIKDGQ 219
Cdd:PRK13637 155 IAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHsmEDV-AKLADRIIVMNKGK 222
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-220 |
1.53e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 119.71 E-value: 1.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 2 KIVKVKDLSKEYTGKVSHtALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFI-----NSKNPYQLspn 76
Cdd:PRK13632 6 VMIKVENVSFSYPNSENN-ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIdgitiSKENLKEI--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 77 dlavfrRQELGFVFQS-FNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIAR 155
Cdd:PRK13632 82 ------RKKIGIIFQNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIAS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446629392 156 ALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDPVAASYCDRVIFIKDGQL 220
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKL 220
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-238 |
1.99e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 119.46 E-value: 1.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSkeYTGKVSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVF-----INSKNPYQLspnd 77
Cdd:PRK13647 4 IIEVEDLH--FRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKvmgreVNAENEKWV---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 78 lavfrRQELGFVFQS-FNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARA 156
Cdd:PRK13647 78 -----RSKVGLVFQDpDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 157 LIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKaTMMLVTHD-PVAASYCDRVIFIKDGQLyneIFYNDNRSLFYQ 235
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGK-TVIVATHDvDLAAEWADQVIVLKEGRV---LAEGDKSLLTDE 228
|
...
gi 446629392 236 NII 238
Cdd:PRK13647 229 DIV 231
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
18-220 |
2.08e-32 |
|
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: 124.59 E-value: 2.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 18 SHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLavfrRQELGFVFQSFNLLH 97
Cdd:TIGR03375 477 ETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADL----RRNIGYVPQDPRLFY 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 98 TlTVKENMVL--PLVLDGMnVKRINKR--VESISKKL--GISEILNKRTYEISGGQAQRTAIARALIHAPKLVLADEPTG 171
Cdd:TIGR03375 553 G-TLRDNIALgaPYADDEE-ILRAAELagVTEFVRRHpdGLDMQIGERGRSLSGGQRQAVALARALLRDPPILLLDEPTS 630
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446629392 172 NLDSKASQDVMEILTHLNKEEkaTMMLVTHDPVAASYCDRVIFIKDGQL 220
Cdd:TIGR03375 631 AMDNRSEERFKDRLKRWLAGK--TLVLVTHRTSLLDLVDRIIVMDNGRI 677
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-220 |
3.62e-32 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 122.82 E-value: 3.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYTGkvsHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKnPYQL-SPNDlAvf 81
Cdd:COG1129 4 LLEMRGISKSFGG---VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGE-PVRFrSPRD-A-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 82 rrQELG--FVFQSFNLLHTLTVKENMVL---PLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARA 156
Cdd:COG1129 77 --QAAGiaIIHQELNLVPNLSVAENIFLgrePRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446629392 157 LIHAPKLVLADEPTGNLDSKASQDVMEILTHLnKEEKATMMLVTH--DPVAAsYCDRVIFIKDGQL 220
Cdd:COG1129 155 LSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHrlDEVFE-IADRVTVLRDGRL 218
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
16-225 |
7.32e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 118.58 E-value: 7.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 16 KVSHT----------ALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFI------NSKNPYQLSPndla 79
Cdd:PRK13634 7 KVEHRyqyktpferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNKKLKP---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 80 vfRRQELGFVFQsF--NLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISE-ILNKRTYEISGGQAQRTAIARA 156
Cdd:PRK13634 83 --LRKKVGIVFQ-FpeHQLFEETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446629392 157 LIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTH---DpvAASYCDRVIFIKDGQLY-----NEIF 225
Cdd:PRK13634 160 LAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHsmeD--AARYADQIVVMHKGTVFlqgtpREIF 234
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-220 |
9.80e-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: 115.78 E-value: 9.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYTGKvshTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNdlavfrR 83
Cdd:cd03268 1 LKTNDLTKTYGKK---RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA------L 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 84 QELGFVFQSFNLLHTLTVKENMVLPLVLDGMNvkriNKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKL 163
Cdd:cd03268 72 RRIGALIEAPGFYPNLTARENLRLLARLLGIR----KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446629392 164 VLADEPTGNLDSKASQDVMEILTHLNKEEKaTMMLVTH-----DPVAasycDRVIFIKDGQL 220
Cdd:cd03268 148 LILDEPTNGLDPDGIKELRELILSLRDQGI-TVLISSHllseiQKVA----DRIGIINKGKL 204
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-220 |
9.97e-32 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 117.09 E-value: 9.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 6 VKDLSKEYTGKvshTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSknpyqlSPNDLAvfrRQE 85
Cdd:PRK11247 15 LNAVSKRYGER---TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGT------APLAEA---RED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 86 LGFVFQSFNLLHTLTVKENMVLPLvldgmnvkRINKRVESIS--KKLGISEILNKRTYEISGGQAQRTAIARALIHAPKL 163
Cdd:PRK11247 83 TRLMFQDARLLPWKKVIDNVGLGL--------KGQWRDAALQalAAVGLADRANEWPAALSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446629392 164 VLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHD-PVAASYCDRVIFIKDGQL 220
Cdd:PRK11247 155 LLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDvSEAVAMADRVLLIEEGKI 212
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-224 |
2.49e-31 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 116.32 E-value: 2.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 1 MKIVKVKDLSKEYTG------KVSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLS 74
Cdd:PRK10419 1 MTLLNVSGLSHHYAHgglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 75 PNDLAVFRRqELGFVFQ----SFNLLHTltVKENMVLPLV-LDGMNVKRINKRVESISKKLGIS-EILNKRTYEISGGQA 148
Cdd:PRK10419 81 RAQRKAFRR-DIQMVFQdsisAVNPRKT--VREIIREPLRhLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446629392 149 QRTAIARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHD-PVAASYCDRVIFIKDGQLYNEI 224
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDlRLVERFCQRVMVMDNGQIVETQ 234
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-220 |
2.96e-31 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 115.95 E-value: 2.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYTGKvshTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAvfRR 83
Cdd:COG4604 2 IEIKNVSKRYGGK---VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELA--KR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 84 qeLGFVFQSFNLLHTLTVKEnmvlpLV-----------LDGMNVKRINkrvESISKkLGISEILNKRTYEISGGQAQRTA 152
Cdd:COG4604 77 --LAILRQENHINSRLTVRE-----LVafgrfpyskgrLTAEDREIID---EAIAY-LDLEDLADRYLDELSGGQRQRAF 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446629392 153 IARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHD-PVAASYCDRVIFIKDGQL 220
Cdd:COG4604 146 IAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDiNFASCYADHIVAMKDGRV 214
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
6-221 |
3.13e-31 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 116.02 E-value: 3.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 6 VKDLSKEYTGKvshTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAVFR--- 82
Cdd:PRK13548 5 ARNLSVRLGGR---TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRavl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 83 RQE--LGFVFqsfnllhtlTVKE--NM-VLPLVLDGMNVKRInkrVESISKKLGISEiLNKRTY-EISGGQAQRTAIARA 156
Cdd:PRK13548 82 PQHssLSFPF---------TVEEvvAMgRAPHGLSRAEDDAL---VAAALAQVDLAH-LAGRDYpQLSGGEQQRVQLARV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446629392 157 LI------HAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHD-PVAASYCDRVIFIKDGQLY 221
Cdd:PRK13548 149 LAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDlNLAARYADRIVLLHQGRLV 220
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
22-220 |
3.33e-31 |
|
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: 115.06 E-value: 3.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 22 LSNINLTITEGEFVGIMGPSGSGKTTLLNMIS---TIDSATSGSVFINSK--NPYQLspndlavfrRQELGFVFQSFNLL 96
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISgrvEGGGTTSGQILFNGQprKPDQF---------QKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 97 HTLTVKENMVLPLVLDG---MNVKRINKRVESIS-KKLGISEILNKRTYEISGGQAQRTAIARALIHAPKLVLADEPTGN 172
Cdd:cd03234 94 PGLTVRETLTYTAILRLprkSSDAIRKKRVEDVLlRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446629392 173 LDSKASQDVMEILTHLNKEEKATMMLVtHDPVAASY--CDRVIFIKDGQL 220
Cdd:cd03234 174 LDSFTALNLVSTLSQLARRNRIVILTI-HQPRSDLFrlFDRILLLSSGEI 222
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
22-213 |
3.62e-31 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 114.81 E-value: 3.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 22 LSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLavfrRQELGFVFQSFNLLHTlTV 101
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIY----RQQVSYCAQTPTLFGD-TV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 102 KENMVLPLVLDGMNVKRinKRVESISKKLGISE-ILNKRTYEISGGQAQRTAIARALIHAPKLVLADEPTGNLDSKASQD 180
Cdd:PRK10247 98 YDNLIFPWQIRNQQPDP--AIFLDDLERFALPDtILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHN 175
|
170 180 190
....*....|....*....|....*....|...
gi 446629392 181 VMEILTHLNKEEKATMMLVTHDPVAASYCDRVI 213
Cdd:PRK10247 176 VNEIIHRYVREQNIAVLWVTHDKDEINHADKVI 208
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3-223 |
4.85e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 115.95 E-value: 4.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYTGKVShtALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKnPYQLSPNDLAVFR 82
Cdd:PRK13639 1 ILETRDLKYSYPDGTE--ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGE-PIKYDKKSLLEVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 83 rQELGFVFQ-SFNLLHTLTVKENMVL-PLVLdGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHA 160
Cdd:PRK13639 78 -KTVGIVFQnPDDQLFAPTVEEDVAFgPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446629392 161 PKLVLADEPTGNLDSKASQDVMEILTHLNKeEKATMMLVTHD-PVAASYCDRVIFIKDGQLYNE 223
Cdd:PRK13639 156 PEIIVLDEPTSGLDPMGASQIMKLLYDLNK-EGITIIISTHDvDLVPVYADKVYVMSDGKIIKE 218
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
22-220 |
6.81e-31 |
|
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: 119.85 E-value: 6.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 22 LSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAvfrrQELGFVFQSFNLLHTlTV 101
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELG----RHIGYLPQDVELFDG-TI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 102 KENmvlplvldgmnVKRINK----RVESISKKLGISE-ILN-KRTYE---------ISGGQAQRTAIARALIHAPKLVLA 166
Cdd:COG4618 423 AEN-----------IARFGDadpeKVVAAAKLAGVHEmILRlPDGYDtrigeggarLSGGQRQRIGLARALYGDPRLVVL 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446629392 167 DEPTGNLDSKASQDVMEILTHLnKEEKATMMLVTHDPVAASYCDRVIFIKDGQL 220
Cdd:COG4618 492 DEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPSLLAAVDKLLVLRDGRV 544
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-220 |
8.38e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 114.94 E-value: 8.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 18 SHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTI-----DSATSGSVFINSKNPYqlSPNDLAVFRRQELGFVFQS 92
Cdd:PRK14267 16 SNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIY--SPDVDPIEVRREVGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 93 FNLLHTLTVKENMVLPLVLDGM--NVKRINKRVESISKKLG----ISEILNKRTYEISGGQAQRTAIARALIHAPKLVLA 166
Cdd:PRK14267 94 PNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAAlwdeVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLM 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446629392 167 DEPTGNLDSKASQDVMEILTHLNKEekATMMLVTHDPV-AASYCDRVIFIKDGQL 220
Cdd:PRK14267 174 DEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAqAARVSDYVAFLYLGKL 226
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
19-220 |
8.39e-31 |
|
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: 119.37 E-value: 8.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 19 HTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAVFrrqeLGFVFQSFNLLHT 98
Cdd:TIGR01842 331 KPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKH----IGYLPQDVELFPG 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 99 lTVKENmvlplvldgmnVKRINKRVES-----ISKKLGISE-ILN-KRTYE---------ISGGQAQRTAIARALIHAPK 162
Cdd:TIGR01842 407 -TVAEN-----------IARFGENADPekiieAAKLAGVHElILRlPDGYDtvigpggatLSGGQRQRIALARALYGDPK 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446629392 163 LVLADEPTGNLDSKASQDVMEILTHLnKEEKATMMLVTHDPVAASYCDRVIFIKDGQL 220
Cdd:TIGR01842 475 LVVLDEPNSNLDEEGEQALANAIKAL-KARGITVVVITHRPSLLGCVDKILVLQDGRI 531
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
3-213 |
1.07e-30 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 115.98 E-value: 1.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEY----------TGKVShtALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQ 72
Cdd:COG4608 7 LLEVRDLKKHFpvrgglfgrtVGVVK--AVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 73 LSPNDLAVFRRQeLGFVFQ----SFNLLHTL--TVKEnmvlPLVLDGM-NVKRINKRVESISKKLGIS-EILNKRTYEIS 144
Cdd:COG4608 85 LSGRELRPLRRR-MQMVFQdpyaSLNPRMTVgdIIAE----PLRIHGLaSKAERRERVAELLELVGLRpEHADRYPHEFS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446629392 145 GGQAQRTAIARALIHAPKLVLADEPTGNLD-SKASQdVMEILTHLNKEEKATMMLVTHD-PVAASYCDRVI 213
Cdd:COG4608 160 GGQRQRIGIARALALNPKLIVCDEPVSALDvSIQAQ-VLNLLEDLQDELGLTYLFISHDlSVVRHISDRVA 229
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
2-223 |
1.69e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 114.41 E-value: 1.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 2 KIVKVKDLSKEY---TGKVSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFI------NSKNPYQ 72
Cdd:PRK13633 3 EMIKCKNVSYKYesnEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVdgldtsDEENLWD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 73 LspndlavfrRQELGFVFQS-FNLLHTLTVKENMVL-PLVLdGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQR 150
Cdd:PRK13633 83 I---------RNKAGMVFQNpDNQIVATIVEEDVAFgPENL-GIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446629392 151 TAIARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDPVAASYCDRVIFIKDGQLYNE 223
Cdd:PRK13633 153 VAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVME 225
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-232 |
1.99e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 113.85 E-value: 1.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 1 MKIVKVKDLSKEYtGKVShtALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTI-----DSATSGSVFINSKNPYQLsp 75
Cdd:PRK14247 1 MNKIEIRDLKVSF-GQVE--VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKM-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 76 nDLAVFRRQeLGFVFQSFNLLHTLTVKENMVLPLVLDGM--NVKRINKRV-ESISKKLGISEI---LNKRTYEISGGQAQ 149
Cdd:PRK14247 76 -DVIELRRR-VQMVFQIPNPIPNLSIFENVALGLKLNRLvkSKKELQERVrWALEKAQLWDEVkdrLDAPAGKLSGGQQQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 150 RTAIARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEekATMMLVTHDPV-AASYCDRVIFIKDGQLYN-----E 223
Cdd:PRK14247 154 RLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQqAARISDYVAFLYKGQIVEwgptrE 231
|
....*....
gi 446629392 224 IFYNDNRSL 232
Cdd:PRK14247 232 VFTNPRHEL 240
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
21-213 |
2.44e-30 |
|
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: 118.16 E-value: 2.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 21 ALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKnpyQLSPNDLAVFRRQeLGFVFQSFNLLHTlT 100
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGV---PLADADADSWRDQ-IAWVPQHPFLFAG-T 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 101 VKENMVL--PLVLDGMnVKRINKRV---ESISK-KLGISEILNKRTYEISGGQAQRTAIARALIHAPKLVLADEPTGNLD 174
Cdd:TIGR02857 412 IAENIRLarPDASDAE-IREALERAgldEFVAAlPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLD 490
|
170 180 190
....*....|....*....|....*....|....*....
gi 446629392 175 SKASQDVMEILTHLnkEEKATMMLVTHDPVAASYCDRVI 213
Cdd:TIGR02857 491 AETEAEVLEALRAL--AQGRTVLLVTHRLALAALADRIV 527
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
18-213 |
7.03e-30 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 110.40 E-value: 7.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 18 SHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVfinsknpyqlspndlAVFRRQELGFVFQSFNLLH 97
Cdd:NF040873 4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV---------------RRAGGARVAYVPQRSEVPD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 98 TL--TVKENMVL----PLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKLVLADEPTG 171
Cdd:NF040873 69 SLplTVRDLVAMgrwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446629392 172 NLDSKASQDVMEILTHLnKEEKATMMLVTHDPVAASYCDRVI 213
Cdd:NF040873 149 GLDAESRERIIALLAEE-HARGATVVVVTHDLELVRRADPCV 189
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
21-220 |
1.06e-29 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 111.42 E-value: 1.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 21 ALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSknpYQLSPNDLAVFRRQeLGFVFQSfNLLHTLT 100
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDG---HDLALADPAWLRRQ-VGVVLQE-NVLFNRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 101 VKENMVLplVLDGMNVKRINKRV------ESISK-KLGISEILNKRTYEISGGQAQRTAIARALIHAPKLVLADEPTGNL 173
Cdd:cd03252 92 IRDNIAL--ADPGMSMERVIEAAklagahDFISElPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSAL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446629392 174 DSKASQDVMEILTHLNKEEkaTMMLVTHDPVAASYCDRVIFIKDGQL 220
Cdd:cd03252 170 DYESEHAIMRNMHDICAGR--TVIIIAHRLSTVKNADRIIVMEKGRI 214
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-219 |
2.39e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 111.74 E-value: 2.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYTgkvSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKnpyqlsPNDLAVFR 82
Cdd:COG4152 1 MLELKGLTKRFG---DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGE------PLDPEDRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 83 R-----QELGfvfqsfnLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARAL 157
Cdd:COG4152 72 RigylpEERG-------LYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAAL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446629392 158 IHAPKLVLADEPTGNLDSKASQDVMEILTHLnKEEKATMMLVTHD-PVAASYCDRVIFIKDGQ 219
Cdd:COG4152 145 LHDPELLILDEPFSGLDPVNVELLKDVIREL-AAKGTTVIFSSHQmELVEELCDRIVIINKGR 206
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-220 |
2.84e-29 |
|
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: 115.17 E-value: 2.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 1 MKIVKVKDLSKEY-TGKVSHTALSNINLTITEGEFVGIMGPSGSGKT----TLLNMISTIDSATSGSVFINSKNPYQLSP 75
Cdd:COG4172 4 MPLLSVEDLSVAFgQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 76 NDLAVFRRQELGFVFQ----SFNLLHTltVKENMVLPLVL-DGMNVKRINKRVESISKKLGISE---ILNKRTYEISGGQ 147
Cdd:COG4172 84 RELRRIRGNRIAMIFQepmtSLNPLHT--IGKQIAEVLRLhRGLSGAAARARALELLERVGIPDperRLDAYPHQLSGGQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446629392 148 AQRTAIARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHD-PVAASYCDRVIFIKDGQL 220
Cdd:COG4172 162 RQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDlGVVRRFADRVAVMRQGEI 235
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-235 |
4.43e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 111.02 E-value: 4.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 19 HTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAVFRRQELGFVFQ-SFNLLH 97
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPVRKRIGMVFQfPESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 98 TLTVKENMVLPLVLDGMNVKRINKRVESISKKLGIS-EILNKRTYEISGGQAQRTAIARALIHAPKLVLADEPTGNLDSK 176
Cdd:PRK13646 100 EDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQ 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 177 ASQDVMEILTHLNKEEKATMMLVTHD-PVAASYCDRVIFIKDGQLyneIFYNDNRSLFYQ 235
Cdd:PRK13646 180 SKRQVMRLLKSLQTDENKTIILVSHDmNEVARYADEVIVMKEGSI---VSQTSPKELFKD 236
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-220 |
5.13e-29 |
|
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: 114.51 E-value: 5.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYT----GKVShtALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYqLSPNDL 78
Cdd:TIGR03269 279 IIKVRNVSKRYIsvdrGVVK--AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEW-VDMTKP 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 79 AVFRR----QELGFVFQSFNLLHTLTVKENMV------LPLVLDGMNVKRINKRVESISKKlgISEILNKRTYEISGGQA 148
Cdd:TIGR03269 356 GPDGRgrakRYIGILHQEYDLYPHRTVLDNLTeaigleLPDELARMKAVITLKMVGFDEEK--AEEILDKYPDELSEGER 433
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446629392 149 QRTAIARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHD-PVAASYCDRVIFIKDGQL 220
Cdd:TIGR03269 434 HRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDmDFVLDVCDRAALMRDGKI 506
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-219 |
6.59e-29 |
|
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: 109.30 E-value: 6.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 1 MKIVKVKDLSKEYtGKVshTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAv 80
Cdd:COG0410 1 MPMLEVENLHAGY-GGI--HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 81 frRQELGFVFQSFNLLHTLTVKENMVLPLVLdGMNVKRINKRVESISK---KLGisEILNKRTYEISGGQAQRTAIARAL 157
Cdd:COG0410 77 --RLGIGYVPEGRRIFPSLTVEENLLLGAYA-RRDRAEVRADLERVYElfpRLK--ERRRQRAGTLSGGEQQMLAIGRAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446629392 158 IHAPKLVLADEPTGNLDSKASQDVMEILTHLNkEEKATMMLVTHD-PVAASYCDRVIFIKDGQ 219
Cdd:COG0410 152 MSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLN-REGVTILLVEQNaRFALEIADRAYVLERGR 213
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
19-220 |
1.25e-28 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 113.79 E-value: 1.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 19 HTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATsGSVFINSknpYQLSPNDLAVFRRQeLGFVFQSFNLLHT 98
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKING---IELRELDPESWRKH-LSWVGQNPQLPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 99 lTVKENMVLPlvldgmNVKRINKRVESISKKLGISEILNKRT----YEI-------SGGQAQRTAIARALIHAPKLVLAD 167
Cdd:PRK11174 438 -TLRDNVLLG------NPDASDEQLQQALENAWVSEFLPLLPqgldTPIgdqaaglSVGQAQRLALARALLQPCQLLLLD 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446629392 168 EPTGNLDSKASQDVMEILTHlNKEEKATMMlVTH--DPVAAsyCDRVIFIKDGQL 220
Cdd:PRK11174 511 EPTASLDAHSEQLVMQALNA-ASRRQTTLM-VTHqlEDLAQ--WDQIWVMQDGQI 561
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-220 |
3.52e-28 |
|
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: 105.20 E-value: 3.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYTGkvsHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDlavfrr 83
Cdd:cd03216 1 LELRGITKRFGG---VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 84 qelgfvfqsfnllhtltvkenmvlplvldgmnvkrinkrvesiSKKLGISEIlnkrtYEISGGQAQRTAIARALIHAPKL 163
Cdd:cd03216 72 -------------------------------------------ARRAGIAMV-----YQLSVGERQMVEIARALARNARL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446629392 164 VLADEPTGNLDSKASQDVMEILTHLnKEEKATMMLVTH--DPVAAsYCDRVIFIKDGQL 220
Cdd:cd03216 104 LILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHrlDEVFE-IADRVTVLRDGRV 160
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-219 |
3.78e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 107.86 E-value: 3.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKE-YTGKVS-HTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNpyqlsPNDLAV 80
Cdd:COG1101 1 MLELKNLSKTfNPGTVNeKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKD-----VTKLPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 81 FRR-QELGFVFQsfN-LLHT---LTVKENMVL--------PLVLdGMNVKRINKRVESISK-KLGISEILNKRTYEISGG 146
Cdd:COG1101 76 YKRaKYIGRVFQ--DpMMGTapsMTIEENLALayrrgkrrGLRR-GLTKKRRELFRELLATlGLGLENRLDTKVGLLSGG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446629392 147 QAQRTAIARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTH---DpvAASYCDRVIFIKDGQ 219
Cdd:COG1101 153 QRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHnmeQ--ALDYGNRLIMMHEGR 226
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-220 |
4.11e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 107.79 E-value: 4.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYTGKvshTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAvfr 82
Cdd:PRK11231 2 TLRTENLTVGYGTK---RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 83 rQELGFVFQSFNLLHTLTVKEnmvlpLV---------LDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAI 153
Cdd:PRK11231 76 -RRLALLPQHHLTPEGITVRE-----LVaygrspwlsLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446629392 154 ARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKaTMMLVTHDPVAAS-YCDRVIFIKDGQL 220
Cdd:PRK11231 150 AMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGK-TVVTVLHDLNQASrYCDHLVVLANGHV 216
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
4-219 |
5.84e-28 |
|
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: 106.85 E-value: 5.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYTGKVSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLavfrR 83
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWL----R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 84 QELGFVFQSFNLLHTlTVKENMVLplvldGMNvKRINKRVESISKKLGISEILNK-----------RTYEISGGQAQRTA 152
Cdd:cd03249 77 SQIGLVSQEPVLFDG-TIAENIRY-----GKP-DATDEEVEEAAKKANIHDFIMSlpdgydtlvgeRGSQLSGGQKQRIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446629392 153 IARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEkaTMMLVTHDPVAASYCDRVIFIKDGQ 219
Cdd:cd03249 150 IARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGR--TTIVIAHRLSTIRNADLIAVLQNGQ 214
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-220 |
6.19e-28 |
|
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: 105.21 E-value: 6.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSkeytgkvSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDlavFR 82
Cdd:cd03215 4 VLEVRGLS-------VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRD---AI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 83 RQELGFV---FQSFNLLHTLTVKENMVLPLVLdgmnvkrinkrvesiskklgiseilnkrtyeiSGGQAQRTAIARALIH 159
Cdd:cd03215 74 RAGIAYVpedRKREGLVLDLSVAENIALSSLL--------------------------------SGGNQQKVVLARWLAR 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446629392 160 APKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDPVAASYCDRVIFIKDGQL 220
Cdd:cd03215 122 DPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-223 |
6.30e-28 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 111.43 E-value: 6.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYTGKVshtALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDS--ATSGSV-----------------F 64
Cdd:TIGR03269 1 IEVKNLTKKFDGKE---VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyhvalcekcgyverpsK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 65 INSKNPY---QLSPNDL-------AVFR--RQELGFVFQ-SFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLG 131
Cdd:TIGR03269 78 VGEPCPVcggTLEPEEVdfwnlsdKLRRriRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 132 ISEILNKRTYEISGGQAQRTAIARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDP-VAASYCD 210
Cdd:TIGR03269 158 LSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPeVIEDLSD 237
|
250
....*....|...
gi 446629392 211 RVIFIKDGQLYNE 223
Cdd:TIGR03269 238 KAIWLENGEIKEE 250
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-220 |
4.74e-27 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 102.78 E-value: 4.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 6 VKDLSKEYTGKVSHtALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNdlavfRRQE 85
Cdd:cd03247 3 INNVSFSYPEQEQQ-VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-----LSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 86 LGFVFQSFNLLHTlTVKENMVLPLvldgmnvkrinkrvesiskklgiseilnkrtyeiSGGQAQRTAIARALIHAPKLVL 165
Cdd:cd03247 77 ISVLNQRPYLFDT-TLRNNLGRRF----------------------------------SGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446629392 166 ADEPTGNLDSKASQDVMEILTHLNKEEkaTMMLVTHDPVAASYCDRVIFIKDGQL 220
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDK--TLIWITHHLTGIEHMDKILFLENGKI 174
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
2-220 |
9.33e-27 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 103.62 E-value: 9.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 2 KIVKVKDLSKEY-------------------TGKVSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGS 62
Cdd:COG1134 3 SMIEVENVSKSYrlyhepsrslkelllrrrrTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 63 VFINSKNPYQLspndlavfrrqELGFVFQSfnllhTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNK--RT 140
Cdd:COG1134 83 VEVNGRVSALL-----------ELGAGFHP-----ELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQpvKT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 141 YeiSGGQAQRTAIARALIHAPKLVLADEPTGNLDS---KASQDVMEILthlnKEEKATMMLVTHDP-VAASYCDRVIFIK 216
Cdd:COG1134 147 Y--SSGMRARLAFAVATAVDPDILLVDEVLAVGDAafqKKCLARIREL----RESGRTVIFVSHSMgAVRRLCDRAIWLE 220
|
....
gi 446629392 217 DGQL 220
Cdd:COG1134 221 KGRL 224
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-235 |
1.16e-26 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 105.58 E-value: 1.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 1 MKIVKVKDLSKEYT---GKVshTALSNINLTITEGEFVGIMGPSGSGKT----TLLNMISTiDSATSGSVFINSKNPYQL 73
Cdd:PRK09473 10 DALLDVKDLRVTFStpdGDV--TAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAA-NGRIGGSATFNGREILNL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 74 SPNDLAVFRRQELGFVFQ----SFNllHTLTVKENMVLPLVLDgmnvKRINKR---VESIsKKLGISEILNKRT------ 140
Cdd:PRK09473 87 PEKELNKLRAEQISMIFQdpmtSLN--PYMRVGEQLMEVLMLH----KGMSKAeafEESV-RMLDAVKMPEARKrmkmyp 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 141 YEISGGQAQRTAIARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHD-PVAASYCDRVIFIKDGQ 219
Cdd:PRK09473 160 HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDlGVVAGICDKVLVMYAGR 239
|
250
....*....|....*.
gi 446629392 220 LYNeifYNDNRSLFYQ 235
Cdd:PRK09473 240 TME---YGNARDVFYQ 252
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-203 |
1.30e-26 |
|
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: 107.83 E-value: 1.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYTGkvSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLavfrR 83
Cdd:TIGR02868 335 LELRDLSAGYPG--APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEV----R 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 84 QELGFVFQSFNLLHTlTVKENMVL--PLVLDgmnvkrinkrvESISKKL--------------GISEILNKRTYEISGGQ 147
Cdd:TIGR02868 409 RRVSVCAQDAHLFDT-TVRENLRLarPDATD-----------EELWAALervgladwlralpdGLDTVLGEGGARLSGGE 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446629392 148 AQRTAIARALIHAPKLVLADEPTGNLDSKASQDVMEILthLNKEEKATMMLVTHDP 203
Cdd:TIGR02868 477 RQRLALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-220 |
1.41e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 104.04 E-value: 1.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 1 MKIVKVKDLSKEYTGKVSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKnpyQLSPNDLAV 80
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD---LLTEENVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 81 FRRQeLGFVFQS-FNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIH 159
Cdd:PRK13650 79 IRHK-IGMVFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446629392 160 APKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHD--PVAASycDRVIFIKDGQL 220
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDldEVALS--DRVLVMKNGQV 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-221 |
2.43e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 106.69 E-value: 2.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 6 VKDLSKEYTGKvshTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFInsknpyqlsPNDLavfrrqE 85
Cdd:COG0488 1 LENLSKSFGGR---PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI---------PKGL------R 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 86 LGFVFQSFNLLHTLTVKENmvlplVLDGMN-----VKRINK--------------------------------RVESISK 128
Cdd:COG0488 63 IGYLPQEPPLDDDLTVLDT-----VLDGDAelralEAELEEleaklaepdedlerlaelqeefealggweaeaRAEEILS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 129 KLGISEI-LNKRTYEISGGQAQRTAIARALIHAPKLVLADEPTGNLDSKAsqdvmeIL---THLnKEEKATMMLVTHD-- 202
Cdd:COG0488 138 GLGFPEEdLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES------IEwleEFL-KNYPGTVLVVSHDry 210
|
250 260
....*....|....*....|..
gi 446629392 203 ---PVaasyCDRVIFIKDGQLY 221
Cdd:COG0488 211 fldRV----ATRILELDRGKLT 228
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
3-223 |
3.31e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 102.91 E-value: 3.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYTGKVSHTaLSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKnpyQLSPNDLAVFR 82
Cdd:PRK13648 7 IIVFKNVSFQYQSDASFT-LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQ---AITDDNFEKLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 83 rQELGFVFQS-FNLLHTLTVK-------ENMVLPLvldgmnvkriNKRVESISKKLGISEILNKRTYE---ISGGQAQRT 151
Cdd:PRK13648 83 -KHIGIVFQNpDNQFVGSIVKydvafglENHAVPY----------DEMHRRVSEALKQVDMLERADYEpnaLSGGQKQRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446629392 152 AIARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDPVAASYCDRVIFIKDGQLYNE 223
Cdd:PRK13648 152 AIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKE 223
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
4-220 |
1.30e-25 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 100.38 E-value: 1.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYTGKvsHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLavfrR 83
Cdd:cd03254 3 IEFENVNFSYDEK--KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSL----R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 84 QELGFVFQSFNLLHTlTVKENmvlpLVLDGMNVKRinKRVESISKKLGISEILNKRT--YE---------ISGGQAQRTA 152
Cdd:cd03254 77 SMIGVVLQDTFLFSG-TIMEN----IRLGRPNATD--EEVIEAAKEAGAHDFIMKLPngYDtvlgenggnLSQGERQLLA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446629392 153 IARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKeeKATMMLVTHDPVAASYCDRVIFIKDGQL 220
Cdd:cd03254 150 IARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKNADKILVLDDGKI 215
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
18-213 |
1.38e-25 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 99.86 E-value: 1.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 18 SHTALSNINLTITEGEFVGIMGPSGSGKTTLLN-MISTIDSA--TSGSVFINSKnpyqlSPNDLAVFRRQeLGFVFQSfN 94
Cdd:COG4136 13 GRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSPAfsASGEVLLNGR-----RLTALPAEQRR-IGILFQD-D 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 95 LL--HtLTVKENmvLPLVLDGmNVKRINKR--VESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKLVLADEPT 170
Cdd:COG4136 86 LLfpH-LSVGEN--LAFALPP-TIGRAQRRarVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPF 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446629392 171 GNLDSKASQDVME-ILTHLnKEEKATMMLVTHDPVAASYCDRVI 213
Cdd:COG4136 162 SKLDAALRAQFREfVFEQI-RQRGIPALLVTHDEEDAPAAGRVL 204
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-220 |
1.93e-25 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 100.35 E-value: 1.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 1 MKIVKVKDLSKEYTGKvshTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAv 80
Cdd:PRK10895 1 MATLTAKNLAKAYKGR---RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 81 frRQELGFVFQSFNLLHTLTVKENMVLPL-VLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIH 159
Cdd:PRK10895 77 --RRGIGYLPQEASIFRRLSVYDNLMAVLqIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446629392 160 APKLVLADEPTGNLDSKASQDVMEILTHLnkEEKATMMLVTHDPVAASY--CDRVIFIKDGQL 220
Cdd:PRK10895 155 NPKFILLDEPFAGVDPISVIDIKRIIEHL--RDSGLGVLITDHNVRETLavCERAYIVSQGHL 215
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
22-229 |
2.07e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 101.44 E-value: 2.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 22 LSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSknpYQLSPN----DLAVFRRqELGFVFQ--SFNL 95
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAG---YHITPEtgnkNLKKLRK-KVSLVFQfpEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 96 LHTLTVKENMVLPLVLDGMNVKRINKRVESIsKKLGISE-ILNKRTYEISGGQAQRTAIARALIHAPKLVLADEPTGNLD 174
Cdd:PRK13641 99 FENTVLKDVEFGPKNFGFSEDEAKEKALKWL-KKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446629392 175 SKASQDVMEILTHLNKEEKaTMMLVTH--DPVaASYCDRVIFIKDGQLY-----NEIFYNDN 229
Cdd:PRK13641 178 PEGRKEMMQLFKDYQKAGH-TVILVTHnmDDV-AEYADDVLVLEHGKLIkhaspKEIFSDKE 237
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
3-220 |
3.06e-25 |
|
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: 99.90 E-value: 3.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYTGKVshtALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNP-----YQLSPND 77
Cdd:TIGR02323 3 LLQVSGLSKSYGGGK---GCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGaelelYQLSEAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 78 LAVFRRQELGFVFQSF--NLLHTLTVKENMVLPLVLDGmnVKRINKRVESISKKLGISEILNKRTYE----ISGGQAQRT 151
Cdd:TIGR02323 80 RRRLMRTEWGFVHQNPrdGLRMRVSAGANIGERLMAIG--ARHYGNIRATAQDWLEEVEIDPTRIDDlpraFSGGMQQRL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 152 AIARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHD-PVAASYCDRVIFIKDGQL 220
Cdd:TIGR02323 158 QIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDlGVARLLAQRLLVMQQGRV 227
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
21-227 |
3.48e-25 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 101.32 E-value: 3.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 21 ALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAVfRRQELGFVFQ----SFNll 96
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRA-VRSDIQMIFQdplaSLN-- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 97 HTLTVKENMVLPLV-----LDGMNVKrinKRVESISKKLGI-SEILNKRTYEISGGQAQRTAIARALIHAPKLVLADEPT 170
Cdd:PRK15079 113 PRMTIGEIIAEPLRtyhpkLSRQEVK---DRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPV 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446629392 171 GNLDSKASQDVMEILTHLNKEEKATMMLVTHD-PVAASYCDRVIFIKDGQ-----LYNEIFYN 227
Cdd:PRK15079 190 SALDVSIQAQVVNLLQQLQREMGLSLIFIAHDlAVVKHISDRVLVMYLGHavelgTYDEVYHN 252
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-219 |
6.18e-25 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 102.86 E-value: 6.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 19 HTALSNINLTITEGEFVGIMGPSGSGKTT----LLNMIstidsATSGSVFINSKNPYQLSPNDLAVFRRQeLGFVFQSFN 94
Cdd:PRK15134 299 NVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLLPVRHR-IQVVFQDPN 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 95 llHTLTVKENmVLPLVLDGMNV-------KRINKRVESISKKLGISEILNKRtY--EISGGQAQRTAIARALIHAPKLVL 165
Cdd:PRK15134 373 --SSLNPRLN-VLQIIEEGLRVhqptlsaAQREQQVIAVMEEVGLDPETRHR-YpaEFSGGQRQRIAIARALILKPSLII 448
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446629392 166 ADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHD-PVAASYCDRVIFIKDGQ 219
Cdd:PRK15134 449 LDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDlHVVRALCHQVIVLRQGE 503
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
5-220 |
9.09e-25 |
|
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: 98.37 E-value: 9.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 5 KVKDLSKEYTGkvSHtALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAvfrRQ 84
Cdd:TIGR03410 2 EVSNLNVYYGQ--SH-ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERA---RA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 85 ELGFVFQSFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLgiSEILNKRTYEISGGQAQRTAIARALIHAPKLV 164
Cdd:TIGR03410 76 GIAYVPQGREIFPRLTVEENLLTGLAALPRRSRKIPDEIYELFPVL--KEMLGRRGGDLSGGQQQQLAIARALVTRPKLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446629392 165 LADEPTGNLDSKASQDVMEILTHLNKEEKATMMLV-THDPVAASYCDRVIFIKDGQL 220
Cdd:TIGR03410 154 LLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVeQYLDFARELADRYYVMERGRV 210
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
18-223 |
1.09e-24 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 98.91 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 18 SHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAvfRRqeLGFVFQSFNLLH 97
Cdd:PRK10253 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA--RR--IGLLAQNATTPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 98 TLTVKEnmvlpLVLDGMNV---------KRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKLVLADE 168
Cdd:PRK10253 95 DITVQE-----LVARGRYPhqplftrwrKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446629392 169 PTGNLDSKASQDVMEILTHLNKEEKATMMLVTHD-PVAASYCDRVIFIKDGQLYNE 223
Cdd:PRK10253 170 PTTWLDISHQIDLLELLSELNREKGYTLAAVLHDlNQACRYASHLIALREGKIVAQ 225
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
21-227 |
1.58e-24 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 97.44 E-value: 1.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 21 ALSNINLTITEGEFVGIMGPSGSGKTT----LLNMISTIDSATSGSVFINSKNpyqLSPNDLavfRRQELGFVFQS---- 92
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLtclaILGLLPPGLTQTSGEILLDGRP---LLPLSI---RGRHIATIMQNprta 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 93 FNLLHTLtvKENMVLPLVLDGMNVKRINKRVESISKKLGI---SEILNKRTYEISGGQAQRTAIARALIHAPKLVLADEP 169
Cdd:TIGR02770 75 FNPLFTM--GNHAIETLRSLGKLSKQARALILEALEAVGLpdpEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446629392 170 TGNLDSKASQDVMEILTHLNKEEKATMMLVTHD-PVAASYCDRVIFIKDGQLYN-----EIFYN 227
Cdd:TIGR02770 153 TTDLDVVNQARVLKLLRELRQLFGTGILLITHDlGVVARIADEVAVMDDGRIVErgtvkEIFYN 216
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
21-227 |
2.04e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 98.54 E-value: 2.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 21 ALSNINLTITEGEFVGIMGPSGSGKTTLLNMIS-TIDSATSGSVFINSKNPYQLSPNDLAVFRRQELGFVFQ--SFNLLH 97
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNgLIISETGQTIVGDYAIPANLKKIKEVKRLRKEIGLVFQfpEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 98 TlTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRT-YEISGGQAQRTAIARALIHAPKLVLADEPTGNLDSK 176
Cdd:PRK13645 106 E-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSpFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPK 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446629392 177 ASQDVMEILTHLNKEEKATMMLVTH--DPVaASYCDRVIFIKDGQLYN-----EIFYN 227
Cdd:PRK13645 185 GEEDFINLFERLNKEYKKRIIMVTHnmDQV-LRIADEVIVMHEGKVISigspfEIFSN 241
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
7-220 |
2.14e-24 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 100.49 E-value: 2.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 7 KDLSKEYTgkVSHTALS----NINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAVFR 82
Cdd:PRK10070 27 QGLSKEQI--LEKTGLSlgvkDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 83 RQELGFVFQSFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPK 162
Cdd:PRK10070 105 RKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPD 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446629392 163 LVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHD-PVAASYCDRVIFIKDGQL 220
Cdd:PRK10070 185 ILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDlDEAMRIGDRIAIMQNGEV 243
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
21-220 |
2.74e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 98.28 E-value: 2.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 21 ALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAVFRRQELGFVFQ-SFNLLHTL 99
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQfPESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 100 TVKENMVLPLVLDGMNVKRINKRVESISKKLGISEIL-NKRTYEISGGQAQRTAIARALIHAPKLVLADEPTGNLDSKAS 178
Cdd:PRK13649 102 TVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446629392 179 QDVMEILTHLNkEEKATMMLVTH--DPVaASYCDRVIFIKDGQL 220
Cdd:PRK13649 182 KELMTLFKKLH-QSGMTIVLVTHlmDDV-ANYADFVYVLEKGKL 223
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
9-221 |
3.98e-24 |
|
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: 96.45 E-value: 3.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 9 LSKEYTGKVSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLspndlavfrrqELGF 88
Cdd:cd03220 25 ILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLL-----------GLGG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 89 VFQSfnllhTLTVKENMVLPLVLDGMNVKRINKRVESIskkLGISEI---LNK--RTYeiSGGQAQRTAIARALIHAPKL 163
Cdd:cd03220 94 GFNP-----ELTGRENIYLNGRLLGLSRKEIDEKIDEI---IEFSELgdfIDLpvKTY--SSGMKARLAFAIATALEPDI 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446629392 164 VLADEPTGNLDSKASQDVMEILTHLnKEEKATMMLVTHDPVA-ASYCDRVIFIKDGQLY 221
Cdd:cd03220 164 LLIDEVLAVGDAAFQEKCQRRLREL-LKQGKTVILVSHDPSSiKRLCDRALVLEKGKIR 221
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3-219 |
6.56e-24 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 96.53 E-value: 6.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYTGKVshtALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNP-----YQLSPND 77
Cdd:PRK11701 6 LLSVRGLTKLYGPRK---GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGqlrdlYALSEAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 78 LAVFRRQELGFVFQsfN----LLHTLTVKENMVLPLVLDGM-NVKRINkrvESISKKLGISEILNKR------TYeiSGG 146
Cdd:PRK11701 83 RRRLLRTEWGFVHQ--HprdgLRMQVSAGGNIGERLMAVGArHYGDIR---ATAGDWLERVEIDAARiddlptTF--SGG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446629392 147 QAQRTAIARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHD-PVAASYCDRVIFIKDGQ 219
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDlAVARLLAHRLLVMKQGR 229
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
22-219 |
7.31e-24 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 100.12 E-value: 7.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 22 LSNINLTITEGEFVGIMGPSGSGKTTLLNMI---STIDSATSGSVFINSKnpyqlsPNDLAVFRRQElGFVFQSFNLLHT 98
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALafrSPKGVKGSGSVLLNGM------PIDAKEMRAIS-AYVQQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 99 LTVKENMVLplvldgMNVKRINKRVESISKKLGISEILNK---------------RTYEISGGQAQRTAIARALIHAPKL 163
Cdd:TIGR00955 114 LTVREHLMF------QAHLRMPRRVTKKEKRERVDEVLQAlglrkcantrigvpgRVKGLSGGERKRLAFASELLTDPPL 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446629392 164 VLADEPTGNLDSKASQDVMEILTHLNKEEKaTMMLVTHDPVAASYC--DRVIFIKDGQ 219
Cdd:TIGR00955 188 LFCDEPTSGLDSFMAYSVVQVLKGLAQKGK-TIICTIHQPSSELFElfDKIILMAEGR 244
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-218 |
1.27e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 97.59 E-value: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYTGKVSHTALSninLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSV-FINSKNPYQlspndlAVFR 82
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLS---FTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItVLGVPVPAR------ARLA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 83 RQELGFVFQSFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPK 162
Cdd:PRK13536 113 RARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQ 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446629392 163 LVLADEPTGNLDSKASQDVMEILTHLNKEEKaTMMLVTH-DPVAASYCDRVIFIKDG 218
Cdd:PRK13536 193 LLILDEPTTGLDPHARHLIWERLRSLLARGK-TILLTTHfMEEAERLCDRLCVLEAG 248
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-202 |
2.01e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 95.64 E-value: 2.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 1 MKIVKVKDLSKEYTGKVShtALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKnpyQLSPNDLAV 80
Cdd:PRK13652 1 MHLIETRDLCYSYSGSKE--ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGE---PITKENIRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 81 FRRQeLGFVFQ-SFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIH 159
Cdd:PRK13652 76 VRKF-VGLVFQnPDDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAM 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446629392 160 APKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHD 202
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQ 197
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
4-219 |
2.61e-23 |
|
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: 93.69 E-value: 2.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYTGKVSHTA--LSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKnpyqlspndlavf 81
Cdd:cd03250 1 ISVEDASFTWDSGEQETSftLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 82 rrqeLGFVFQSFNLLHTlTVKENMVLPLVLDGmnvKRINKRVESISKKLGIsEILNK--RTyEI-------SGGQAQRTA 152
Cdd:cd03250 68 ----IAYVSQEPWIQNG-TIRENILFGKPFDE---ERYEKVIKACALEPDL-EILPDgdLT-EIgekginlSGGQKQRIS 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446629392 153 IARALIHAPKLVLADEPTGNLDSKASQDVME--ILTHLNKeeKATMMLVTHDPVAASYCDRVIFIKDGQ 219
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLN--NKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-219 |
2.82e-23 |
|
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: 94.22 E-value: 2.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYTGKVShTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLavfrR 83
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASL----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 84 QELGFVFQSFNLLHTlTVKENMVLPlvLDGMNVKRINKRVES-------ISKKLGISEILNKRTYEISGGQAQRTAIARA 156
Cdd:cd03251 76 RQIGLVSQDVFLFND-TVAENIAYG--RPGATREEVEEAARAanahefiMELPEGYDTVIGERGVKLSGGQRQRIAIARA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446629392 157 LIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEkaTMMLVTHDPVAASYCDRVIFIKDGQ 219
Cdd:cd03251 153 LLKDPPILILDEATSALDTESERLVQAALERLMKNR--TTFVIAHRLSTIENADRIVVLEDGK 213
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
2-223 |
9.08e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 94.00 E-value: 9.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 2 KIVKVKDLSKEYTGKVSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKnpyQLSPNDLAVF 81
Cdd:PRK13642 3 KILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE---LLTAENVWNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 82 RRQeLGFVFQS-FNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHA 160
Cdd:PRK13642 80 RRK-IGMVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446629392 161 PKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDPVAASYCDRVIFIKDGQLYNE 223
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKE 221
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-220 |
1.12e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 96.43 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 6 VKDLSKEYTGKvSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLavfrRQE 85
Cdd:PRK11160 341 LNNVSFTYPDQ-PQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAL----RQA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 86 LGFVFQSFNLLHTlTVKENMVL--PLVLDGmNVKRINKRVEsISKKLGISEILNKRTYE----ISGGQAQRTAIARALIH 159
Cdd:PRK11160 416 ISVVSQRVHLFSA-TLRDNLLLaaPNASDE-ALIEVLQQVG-LEKLLEDDKGLNAWLGEggrqLSGGEQRRLGIARALLH 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446629392 160 -APkLVLADEPTGNLDSKASQDVMEILTHLNKEEkaTMMLVTHDPVAASYCDRVIFIKDGQL 220
Cdd:PRK11160 493 dAP-LLLLDEPTEGLDAETERQILELLAEHAQNK--TVLMITHRLTGLEQFDRICVMDNGQI 551
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
22-220 |
1.49e-22 |
|
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: 92.29 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 22 LSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNpyqLSPNDLAVFRRQeLGFVFQSFNLLHTlTV 101
Cdd:cd03253 17 LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQD---IREVTLDSLRRA-IGVVPQDTVLFND-TI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 102 KENmvlplVLDGmNVKRINKRVESISKKLGISEILNK-----------RTYEISGGQAQRTAIARALIHAPKLVLADEPT 170
Cdd:cd03253 92 GYN-----IRYG-RPDATDEEVIEAAKAAQIHDKIMRfpdgydtivgeRGLKLSGGEKQRVAIARAILKNPPILLLDEAT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446629392 171 GNLDSKASQDVMEILTHLNKeeKATMMLVTHDPVAASYCDRVIFIKDGQL 220
Cdd:cd03253 166 SALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVNADKIIVLKDGRI 213
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-218 |
1.76e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 95.62 E-value: 1.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 2 KIVKVKDLSKEYTGKvshTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAvf 81
Cdd:PRK09700 4 PYISMAGIGKSFGPV---HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 82 rRQELGFVFQSFNLLHTLTVKENMVLPLVLD----GMNV---KRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIA 154
Cdd:PRK09700 79 -QLGIGIIYQELSVIDELTVLENLYIGRHLTkkvcGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446629392 155 RALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDPVAASYCDRVIFIKDG 218
Cdd:PRK09700 158 KTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-234 |
7.79e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 91.25 E-value: 7.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEY-TGKVshtaLSNINLTITEGEFVGIMGPSGSGKTTL---LNMISTIDSAT--SGSVFINSKNPYQLSPNd 77
Cdd:PRK14258 8 IKVNNLSFYYdTQKI----LEGVSMEIYQSKVTAIIGPSGCGKSTFlkcLNRMNELESEVrvEGRVEFFNQNIYERRVN- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 78 LAVFRRQeLGFVFQSFNLLhTLTVKENMVLPLVLDGMNVK-RINKRVESISKKLG----ISEILNKRTYEISGGQAQRTA 152
Cdd:PRK14258 83 LNRLRRQ-VSMVHPKPNLF-PMSVYDNVAYGVKIVGWRPKlEIDDIVESALKDADlwdeIKHKIHKSALDLSGGQQQRLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 153 IARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHD-PVAASYCDRVIFIKDGQ----------LY 221
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNlHQVSRLSDFTAFFKGNEnrigqlvefgLT 240
|
250
....*....|....*
gi 446629392 222 NEIFYN--DNRSLFY 234
Cdd:PRK14258 241 KKIFNSphDSRTREY 255
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-220 |
1.51e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 93.16 E-value: 1.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSkeytgkvSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKnPYQL-SPNDlAVf 81
Cdd:COG1129 256 VLEVEGLS-------VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGK-PVRIrSPRD-AI- 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 82 rrqELGFVF-----QSFNLLHTLTVKENMVLPlVLDG------MNVKRINKRVESISKKLGI---SeiLNKRTYEISGGQ 147
Cdd:COG1129 326 ---RAGIAYvpedrKGEGLVLDLSIRENITLA-SLDRlsrgglLDRRRERALAEEYIKRLRIktpS--PEQPVGNLSGGN 399
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446629392 148 AQRTAIARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDPVAASYCDRVIFIKDGQL 220
Cdd:COG1129 400 QQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-219 |
1.54e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 91.02 E-value: 1.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYTgkvSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPndlavFR 82
Cdd:PRK13537 7 PIDFRNVEKRYG---DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRAR-----HA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 83 RQELGFVFQSFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPK 162
Cdd:PRK13537 79 RQRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446629392 163 LVLADEPTGNLDSKASQDVMEILTHLNKEEKaTMMLVTH-DPVAASYCDRVIFIKDGQ 219
Cdd:PRK13537 159 VLVLDEPTTGLDPQARHLMWERLRSLLARGK-TILLTTHfMEEAERLCDRLCVIEEGR 215
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-218 |
2.02e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 92.21 E-value: 2.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 1 MKIVKVKDLSKEYTGKvshTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAv 80
Cdd:PRK09536 1 MPMIDVSDLSVEFGDT---TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAS- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 81 frrQELGFVFQSFNLLHTLTVKENMVL---PLV--LDGMNvKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIAR 155
Cdd:PRK09536 77 ---RRVASVPQDTSLSFEFDVRQVVEMgrtPHRsrFDTWT-ETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446629392 156 ALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVtHD-PVAASYCDRVIFIKDG 218
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAI-HDlDLAARYCDELVLLADG 215
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-220 |
2.26e-21 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 91.12 E-value: 2.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 1 MKIVKVKDLSKEYT---GKVShtALSNINLTITEGEFVGIMGPSGSGKT----TLLNMISTIDSATSGSVFINSKNPYQL 73
Cdd:COG4170 1 MPLLDIRNLTIEIDtpqGRVK--AVDRVSLTLNEGEIRGLVGESGSGKSliakAICGITKDNWHVTADRFRWNGIDLLKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 74 SPNDLAVFRRQELGFVFQ--SFNLLHTLTVKENM--VLP-LVLDGMNVKRIN---KRVESISKKLGI---SEILNKRTYE 142
Cdd:COG4170 79 SPRERRKIIGREIAMIFQepSSCLDPSAKIGDQLieAIPsWTFKGKWWQRFKwrkKRAIELLHRVGIkdhKDIMNSYPHE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446629392 143 ISGGQAQRTAIARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDPVA-ASYCDRVIFIKDGQL 220
Cdd:COG4170 159 LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESiSQWADTITVLYCGQT 237
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
22-218 |
2.39e-21 |
|
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: 88.93 E-value: 2.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 22 LSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAVFRRQELGFVFQSFNLLHTlTV 101
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLLNA-TV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 102 KENMVLPlvlDGMNVKRINKRVESISKKLGISEI-------LNKRTYEISGGQAQRTAIARALIHAPKLVLADEPTGNLD 174
Cdd:cd03290 96 EENITFG---SPFNKQRYKAVTDACSLQPDIDLLpfgdqteIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446629392 175 SKASQDVME--ILTHLnKEEKATMMLVTHDPVAASYCDRVIFIKDG 218
Cdd:cd03290 173 IHLSDHLMQegILKFL-QDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-221 |
6.91e-21 |
|
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: 91.61 E-value: 6.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSK--EYTGKvshTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNpyqLSPNDLAVf 81
Cdd:TIGR01257 929 VCVKNLVKifEPSGR---PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKD---IETNLDAV- 1001
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 82 rRQELGFVFQSFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAP 161
Cdd:TIGR01257 1002 -RQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDA 1080
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446629392 162 KLVLADEPTGNLDSKASQDVMEILthLNKEEKATMMLVTHDPVAASYC-DRVIFIKDGQLY 221
Cdd:TIGR01257 1081 KVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLgDRIAIISQGRLY 1139
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
23-220 |
8.92e-21 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 88.28 E-value: 8.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 23 SNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAVFRRQeLGFVFQSFNLLHTLTVK 102
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKR-MSMLFQSGALFTDMNVF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 103 ENMVLPLvldgmnvkRINKRV------ESISKKL---GISEILNKRTYEISGGQAQRTAIARALIHAPKLVLADEPTGNL 173
Cdd:PRK11831 103 DNVAYPL--------REHTQLpapllhSTVMMKLeavGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446629392 174 DSKASQDVMEILTHLNKEEKATMMLVTHD-PVAASYCDRVIFIKDGQL 220
Cdd:PRK11831 175 DPITMGVLVKLISELNSALGVTCVVVSHDvPEVLSIADHAYIVADKKI 222
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-212 |
1.06e-20 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 90.95 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 20 TALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKnpyQLSPNDLAVfrRQELGFVFQSFNLLHTL 99
Cdd:NF033858 280 TAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQ---PVDAGDIAT--RRRVGYMSQAFSLYGEL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 100 TVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKLVLADEPTGNLDSKASQ 179
Cdd:NF033858 355 TVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARD 434
|
170 180 190
....*....|....*....|....*....|...
gi 446629392 180 DVMEILTHLNKEEKATMMLVTHDPVAASYCDRV 212
Cdd:NF033858 435 MFWRLLIELSREDGVTIFISTHFMNEAERCDRI 467
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-220 |
1.22e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 88.32 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYTGKvSHTALSNINLTITEGEFVGIMGPSGSGKTT---LLNMISTIDSATSGSVFINSKNPYQLSPNDLa 79
Cdd:PRK13640 5 IVEFKHVSFTYPDS-KKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTAKTVWDI- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 80 vfrRQELGFVFQS-FNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALI 158
Cdd:PRK13640 83 ---REKVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446629392 159 HAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDPVAASYCDRVIFIKDGQL 220
Cdd:PRK13640 160 VEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKL 221
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-227 |
2.48e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 87.98 E-value: 2.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYTGKVSH--TALSNINLTITEGEFVGIMGPSGSGKTTLLN-----MISTIDSATSGSVFINSKNPYQLSP 75
Cdd:PRK13631 21 ILRVKNLYCVFDEKQENelVALNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglIKSKYGTIQVGDIYIGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 76 NDLAVFR-------RQELGFVFQ--SFNLLHTLTVKENMVLPLVLdGMNVKRINKRVESISKKLGISE-ILNKRTYEISG 145
Cdd:PRK13631 101 TNPYSKKiknfkelRRRVSMVFQfpEYQLFKDTIEKDIMFGPVAL-GVKKSEAKKLAKFYLNKMGLDDsYLERSPFGLSG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 146 GQAQRTAIARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKaTMMLVTHD-----PVAasycDRVIFIKDGQL 220
Cdd:PRK13631 180 GQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNK-TVFVITHTmehvlEVA----DEVIVMDKGKI 254
|
250
....*....|..
gi 446629392 221 YN-----EIFYN 227
Cdd:PRK13631 255 LKtgtpyEIFTD 266
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
2-218 |
2.78e-20 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 86.97 E-value: 2.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 2 KIVKVKDLSKEYTGKVshtALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAvf 81
Cdd:PRK11300 4 PLLSVSGLMMRFGGLL---AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 82 rRQELGFVFQSFNLLHTLTVKENMVLPL-------VLDGMNVKRINKRVESIS--------KKLGISEILNKRTYEISGG 146
Cdd:PRK11300 79 -RMGVVRTFQHVRLFREMTVIENLLVAQhqqlktgLFSGLLKTPAFRRAESEAldraatwlERVGLLEHANRQAGNLAYG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446629392 147 QAQRTAIARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHD-PVAASYCDRVIFIKDG 218
Cdd:PRK11300 158 QQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDmKLVMGISDRIYVVNQG 230
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-225 |
3.28e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 87.87 E-value: 3.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 1 MKIVKVKDLSKEY-TGKVSHTALSNINLTITEGEFVGIMGPSGSGKT-TLLNMISTID---SATSGSVFINSKNPYQLSP 75
Cdd:PRK11022 1 MALLNVDKLSVHFgDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDypgRVMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 76 NDlavfRRQ----ELGFVFQ----SFNLLHTLTVkENMVLPLVLDGMNVKRINKRVESISKKLGI---SEILNKRTYEIS 144
Cdd:PRK11022 81 KE----RRNlvgaEVAMIFQdpmtSLNPCYTVGF-QIMEAIKVHQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 145 GGQAQRTAIARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHD-PVAASYCDRVIFIKDGQLY-- 221
Cdd:PRK11022 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDlALVAEAAHKIIVMYAGQVVet 235
|
....*..
gi 446629392 222 ---NEIF 225
Cdd:PRK11022 236 gkaHDIF 242
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
3-202 |
3.82e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 87.71 E-value: 3.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYT-------GKVSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSP 75
Cdd:PRK11308 5 LLQAIDLKKHYPvkrglfkPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 76 NDLAVfRRQELGFVFQ----SFNLLHTL--TVKEnmvlPLVLD-GMNVKRINKRVESISKKLGI-SEILNKRTYEISGGQ 147
Cdd:PRK11308 85 EAQKL-LRQKIQIVFQnpygSLNPRKKVgqILEE----PLLINtSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446629392 148 AQRTAIARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHD 202
Cdd:PRK11308 160 RQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHD 214
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-220 |
3.89e-20 |
|
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: 89.01 E-value: 3.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYTGKvSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSpndLAVFRR 83
Cdd:TIGR02203 331 VEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT---LASLRR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 84 QeLGFVFQSFNLLHTlTVKENmVLPLVLDGMNVKRINKRVESISKK-------LGISEILNKRTYEISGGQAQRTAIARA 156
Cdd:TIGR02203 407 Q-VALVSQDVVLFND-TIANN-IAYGRTEQADRAEIERALAAAYAQdfvdklpLGLDTPIGENGVLLSGGQRQRLAIARA 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446629392 157 LI-HAPKLVLaDEPTGNLDSKASQDVMEILTHLNKEEkaTMMLVTHDPVAASYCDRVIFIKDGQL 220
Cdd:TIGR02203 484 LLkDAPILIL-DEATSALDNESERLVQAALERLMQGR--TTLVIAHRLSTIEKADRIVVMDDGRI 545
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
21-223 |
4.19e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 86.58 E-value: 4.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 21 ALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNpyQLSPNDLAVFRRQeLGFVFQSFNLLHT-L 99
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGID--TGDFSKLQGIRKL-VGIVFQNPETQFVgR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 100 TVK-------ENMVLPLVldgmnvkRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKLVLADEPTGN 172
Cdd:PRK13644 94 TVEedlafgpENLCLPPI-------EIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSM 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446629392 173 LDSKASQDVMEILTHLNKEEKaTMMLVTHDPVAASYCDRVIFIKDGQLYNE 223
Cdd:PRK13644 167 LDPDSGIAVLERIKKLHEKGK-TIVYITHNLEELHDADRIIVMDRGKIVLE 216
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
21-238 |
4.82e-20 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 89.03 E-value: 4.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 21 ALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLavfrRQELGFVFQS---F---- 93
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTL----RQFINYLPQEpyiFsgsi 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 94 --NLLhtLTVKENMVLPLVLDGMNVKRINKRVESISkkLGISEILNKRTYEISGGQAQRTAIARALIHAPKLVLADEPTG 171
Cdd:TIGR01193 565 leNLL--LGAKENVSQDEIWAACEIAEIKDDIENMP--LGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTS 640
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446629392 172 NLDSKASQDVMEILTHLNKEekaTMMLVTHDPVAASYCDRVIFIKDGQLYNEIFYND--NRSLFYQNII 238
Cdd:TIGR01193 641 NLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDEllDRNGFYASLI 706
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
5-219 |
6.76e-20 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 85.50 E-value: 6.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 5 KVKDLSKEYTGKvshTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDS--ATSGSVFINSKNPYQLSPNDLAvfr 82
Cdd:COG0396 2 EIKNLHVSVEGK---EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSPDERA--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 83 RQELGFVFQS---------FNLLHTLTvkeNMVLplvLDGMNVKRINKRVESISKKLGISEILNKRtyEI----SGGQAQ 149
Cdd:COG0396 76 RAGIFLAFQYpveipgvsvSNFLRTAL---NARR---GEELSAREFLKLLKEKMKELGLDEDFLDR--YVnegfSGGEKK 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446629392 150 RTAIARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKAtMMLVTH-----DPVAAsycDRVIFIKDGQ 219
Cdd:COG0396 148 RNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRG-ILIITHyqrilDYIKP---DFVHVLVDGR 218
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
24-201 |
1.12e-19 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 86.47 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 24 NINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFIN------SKNPYQLSPNDlavfRRqeLGFVFQSFNLLH 97
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNgrvlfdAEKGICLPPEK----RR--IGYVFQDARLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 98 TLTVKENMvlplvLDGMNvKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKLVLADEPTGNLDSKA 177
Cdd:PRK11144 90 HYKVRGNL-----RYGMA-KSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPR 163
|
170 180
....*....|....*....|....
gi 446629392 178 SQDVMEILTHLNKEEKATMMLVTH 201
Cdd:PRK11144 164 KRELLPYLERLAREINIPILYVSH 187
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
21-220 |
1.87e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 85.17 E-value: 1.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 21 ALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAVFRRQELGFVFQ--SFNLLHT 98
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQfpESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 99 LTVKENMVLPLVLdGMNVKRINKRVESISKKLGIS-EILNKRTYEISGGQAQRTAIARALIHAPKLVLADEPTGNLDSKA 177
Cdd:PRK13643 101 TVLKDVAFGPQNF-GIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446629392 178 SQDVMEILTHLNKEEKaTMMLVTH--DPVaASYCDRVIFIKDGQL 220
Cdd:PRK13643 180 RIEMMQLFESIHQSGQ-TVVLVTHlmDDV-ADYADYVYLLEKGHI 222
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
4-220 |
1.94e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 87.08 E-value: 1.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYTGKVSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSpndlAVFRR 83
Cdd:TIGR00958 479 IEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYD----HHYLH 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 84 QELGFVFQSfNLLHTLTVKENMVLPLVLDGMNvkrinkRVESISKKLG----ISEILNKRTYEI-------SGGQAQRTA 152
Cdd:TIGR00958 555 RQVALVGQE-PVLFSGSVRENIAYGLTDTPDE------EIMAAAKAANahdfIMEFPNGYDTEVgekgsqlSGGQKQRIA 627
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446629392 153 IARALIHAPKLVLADEPTGNLDSKASQDVMEilthLNKEEKATMMLVTHDPVAASYCDRVIFIKDGQL 220
Cdd:TIGR00958 628 IARALVRKPRVLILDEATSALDAECEQLLQE----SRSRASRTVLLIAHRLSTVERADQILVLKKGSV 691
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-233 |
2.05e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 87.07 E-value: 2.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 1 MKIVKVKDLSKEYT-GKVSHTALSNINLTITEGEFVGIMGPSGSGKT-TLLNMISTIDSA----TSGSVFINSKNPYQLS 74
Cdd:PRK15134 3 QPLLAIENLSVAFRqQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 75 PNDLAVFRRQELGFVFQ----SFNLLHTLTVKENMVLPLvLDGMnvKRINKRVESIS--KKLGISEI---LNKRTYEISG 145
Cdd:PRK15134 83 EQTLRGVRGNKIAMIFQepmvSLNPLHTLEKQLYEVLSL-HRGM--RREAARGEILNclDRVGIRQAakrLTDYPHQLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 146 GQAQRTAIARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHD-PVAASYCDRVIFIKDGQLYNEi 224
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNlSIVRKLADRVAVMQNGRCVEQ- 238
|
....*....
gi 446629392 225 fyNDNRSLF 233
Cdd:PRK15134 239 --NRAATLF 245
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-223 |
8.23e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 82.62 E-value: 8.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 1 MKIVKVKDLSKEYtGKVShtALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPndlAV 80
Cdd:PRK11614 3 KVMLSFDKVSAHY-GKIQ--ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQT---AK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 81 FRRQELGFVFQSFNLLHTLTVKENmvlpLVLDGMNVKRIN-----KRVESISKKLgiSEILNKRTYEISGGQAQRTAIAR 155
Cdd:PRK11614 77 IMREAVAIVPEGRRVFSRMTVEEN----LAMGGFFAERDQfqeriKWVYELFPRL--HERRIQRAGTMSGGEQQMLAIGR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446629392 156 ALIHAPKLVLADEPTGNLDSKASQDVMEILTHLnKEEKATMMLVTHDP-VAASYCDRVIFIKDGQLYNE 223
Cdd:PRK11614 151 ALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNAnQALKLADRGYVLENGHVVLE 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-220 |
9.51e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 85.12 E-value: 9.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 2 KIVKVKDLSKEYTGKvshTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKnpyqlspndlaVf 81
Cdd:COG0488 314 KVLELEGLSKSYGDK---TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGET-----------V- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 82 rrqELGFVFQSFNLLH-TLTVKENMVlplvlDGMNvkriNKRVESISKKLG----ISEILNKRTYEISGGQAQRTAIARA 156
Cdd:COG0488 379 ---KIGYFDQHQEELDpDKTVLDELR-----DGAP----GGTEQEVRGYLGrflfSGDDAFKPVGVLSGGEKARLALAKL 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446629392 157 LIHAPKLVLADEPTGNLDSkasqDVMEILTHLNKEEKATMMLVTHDPvaasY-----CDRVIFIKDGQL 220
Cdd:COG0488 447 LLSPPNVLLLDEPTNHLDI----ETLEALEEALDDFPGTVLLVSHDR----YfldrvATRILEFEDGGV 507
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-207 |
1.31e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 82.52 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYTgkvSHTALSNINLTITEGEFVGIMGPSGSGKTTLLN----MISTIDSA-TSGSVFINSKNPYQLSPND 77
Cdd:PRK14243 10 VLRTENLNVYYG---SFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrLNDLIPGFrVEGKVTFHGKNLYAPDVDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 78 LAVFRRqeLGFVFQSFNLLHTlTVKENMVLPLVLDGMNVKrINKRVESISKKLG----ISEILNKRTYEISGGQAQRTAI 153
Cdd:PRK14243 87 VEVRRR--IGMVFQKPNPFPK-SIYDNIAYGARINGYKGD-MDELVERSLRQAAlwdeVKDKLKQSGLSLSGGQQQRLCI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446629392 154 ARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLnkEEKATMMLVTHDPVAAS 207
Cdd:PRK14243 163 ARAIAVQPEVILMDEPCSALDPISTLRIEELMHEL--KEQYTIIIVTHNMQQAA 214
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
22-219 |
1.40e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 84.47 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 22 LSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKN--------PY--------QLS-PNDLAVFRRQ 84
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGArvlflpqrPYlplgtlreALLyPATAEAFSDA 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 85 ELGFVFQSFNLLHtltvkenmvlpLV--LDgmnvkrinkRVESISKKLgiseilnkrtyeiSGGQAQRTAIARALIHAPK 162
Cdd:COG4178 459 ELREALEAVGLGH-----------LAerLD---------EEADWDQVL-------------SLGEQQRLAFARLLLHKPD 505
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446629392 163 LVLADEPTGNLDSKASQDVMEILTHLNKEekATMMLVTHDPVAASYCDRVIFIKDGQ 219
Cdd:COG4178 506 WLFLDEATSALDEENEAALYQLLREELPG--TTVISVGHRSTLAAFHDRVLELTGDG 560
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
20-219 |
1.79e-18 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 84.55 E-value: 1.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 20 TALSNINLTITEGEFVGIMGPSGSGKTTLLNMIS--TIDSATSGSVFINSKNPYQlspndlAVFRRqeLGFVFQSFNLLH 97
Cdd:PLN03211 82 TILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgrIQGNNFTGTILANNRKPTK------QILKR--TGFVTQDDILYP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 98 TLTVKENMVLP--LVLDGMNVKRINKRV-ESISKKLGISE-----ILNKRTYEISGGQAQRTAIARALIHAPKLVLADEP 169
Cdd:PLN03211 154 HLTVRETLVFCslLRLPKSLTKQEKILVaESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEP 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446629392 170 TGNLDSKASQDVMEILTHLNKEEKaTMMLVTHDPVAASY--CDRVIFIKDGQ 219
Cdd:PLN03211 234 TSGLDATAAYRLVLTLGSLAQKGK-TIVTSMHQPSSRVYqmFDSVLVLSEGR 284
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-220 |
2.37e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 83.92 E-value: 2.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSkeYTGKVSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNdlavfR 82
Cdd:COG3845 257 VLEVENLS--VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPR-----E 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 83 RQELGFVF-----QSFNLLHTLTVKENMVL------PLVLDG-MNVKRINKRVESISKKLGIseilnkRTYEI------- 143
Cdd:COG3845 330 RRRLGVAYipedrLGRGLVPDMSVAENLILgryrrpPFSRGGfLDRKAIRAFAEELIEEFDV------RTPGPdtparsl 403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446629392 144 SGGQAQRTAIARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATmMLVTHD-PVAASYCDRVIFIKDGQL 220
Cdd:COG3845 404 SGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAV-LLISEDlDEILALSDRIAVMYEGRI 480
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
3-220 |
3.20e-18 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 80.59 E-value: 3.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYTGKVSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKnPYQLSPNDlavFR 82
Cdd:cd03248 11 IVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGK-PISQYEHK---YL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 83 RQELGFVFQSfNLLHTLTVKENMVLplvldGMNVKRINKRVESISK----------KLGISEILNKRTYEISGGQAQRTA 152
Cdd:cd03248 87 HSKVSLVGQE-PVLFARSLQDNIAY-----GLQSCSFECVKEAAQKahahsfiselASGYDTEVGEKGSQLSGGQKQRVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446629392 153 IARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNkeEKATMMLVTHDPVAASYCDRVIFIKDGQL 220
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAESEQQVQQALYDWP--ERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-219 |
3.61e-18 |
|
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: 80.92 E-value: 3.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 28 TITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVfinsknpyqLSPNDLAVFRRQELGFVFQSfnllhtlTVKEnmVL 107
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI---------EIELDTVSYKPQYIKADYEG-------TVRD--LL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 108 PLVLDGMNVKRINKrvESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKLVLADEPTGNLDSKASQDVMEILTH 187
Cdd:cd03237 83 SSITKDFYTHPYFK--TEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRR 160
|
170 180 190
....*....|....*....|....*....|...
gi 446629392 188 LNKEEKATMMLVTHDPVAASY-CDRVIfIKDGQ 219
Cdd:cd03237 161 FAENNEKTAFVVEHDIIMIDYlADRLI-VFEGE 192
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-219 |
5.73e-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: 77.87 E-value: 5.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYTGKVShtaLSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNpyqlspndlavfrr 83
Cdd:cd03221 1 IELENLSKTYGGKLL---LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV-------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 84 qELGFVFQsfnllhtltvkenmvlplvldgmnvkrinkrvesiskklgiseilnkrtyeISGGQAQRTAIARALIHAPKL 163
Cdd:cd03221 64 -KIGYFEQ---------------------------------------------------LSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446629392 164 VLADEPTGNLDSKASQDVMEILthlnKEEKATMMLVTHDP-----VaasyCDRVIFIKDGQ 219
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEAL----KEYPGTVILVSHDRyfldqV----ATKIIELEDGK 144
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-227 |
9.06e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 82.14 E-value: 9.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYTGKVShtalsNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPND----- 77
Cdd:PRK09700 265 VFEVRNVTSRDRKKVR-----DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDavkkg 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 78 --LAVFRRQELGFvfqsfnlLHTLTVKENM-VLPLVLDG--------MNVKRINKRVESISKKLGIS-EILNKRTYEISG 145
Cdd:PRK09700 340 maYITESRRDNGF-------FPNFSIAQNMaISRSLKDGgykgamglFHEVDEQRTAENQRELLALKcHSVNQNITELSG 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 146 GQAQRTAIARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDPVAASYCDRVIFIKDGQLyNEIF 225
Cdd:PRK09700 413 GNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL-TQIL 491
|
..
gi 446629392 226 YN 227
Cdd:PRK09700 492 TN 493
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
20-220 |
1.52e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 79.45 E-value: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 20 TALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKnpyQLSPNDLAVFRRqELGFVFQSFNLLHTL 99
Cdd:PRK10575 25 TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQ---PLESWSSKAFAR-KVAYLPQQLPAAEGM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 100 TVKEnmvlpLVLDGM-----NVKRIN----KRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKLVLADEPT 170
Cdd:PRK10575 101 TVRE-----LVAIGRypwhgALGRFGaadrEKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPT 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446629392 171 GNLDSKASQDVMEILTHLNKEEKATMMLVTHD-PVAASYCDRVIFIKDGQL 220
Cdd:PRK10575 176 SALDIAHQVDVLALVHRLSQERGLTVIAVLHDiNMAARYCDYLVALRGGEM 226
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-218 |
2.85e-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: 81.21 E-value: 2.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYTGKvSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQlSPNDLavfr 82
Cdd:TIGR01257 1937 ILRLNELTKVYSGT-SSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDV---- 2010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 83 RQELGFVFQSFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPK 162
Cdd:TIGR01257 2011 HQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPP 2090
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446629392 163 LVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDPVAASYCDRVIFIKDG 218
Cdd:TIGR01257 2091 LVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-220 |
2.99e-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: 77.92 E-value: 2.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYtGKVSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLavfrR 83
Cdd:cd03244 3 IEFKNVSLRY-RPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDL----R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 84 QELGFVFQSfNLLHTLTVKENMVlPL----------VLDGMNVKrinKRVESISKKLGISEILNKRTyeISGGQAQRTAI 153
Cdd:cd03244 78 SRISIIPQD-PVLFSGTIRSNLD-PFgeysdeelwqALERVGLK---EFVESLPGGLDTVVEEGGEN--LSVGQRQLLCL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446629392 154 ARALIHAPKLVLADEPTGNLDSKASQDVMEILthlnKEE--KATMMLVTH--DPVAAsyCDRVIFIKDGQL 220
Cdd:cd03244 151 ARALLRKSKILVLDEATASVDPETDALIQKTI----REAfkDCTVLTIAHrlDTIID--SDRILVLDKGRV 215
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
5-218 |
3.40e-17 |
|
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: 77.18 E-value: 3.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 5 KVKDLSKEYTGKvshTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDS--ATSGSVFINSKNPYQLSPNDLAvfr 82
Cdd:cd03217 2 EIKDLHVSVGGK---EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPEERA--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 83 RQELGFVFQSFNLLHTLTVKEnmvlplVLDGMNVKrinkrvesiskklgiseilnkrtyeISGGQAQRTAIARALIHAPK 162
Cdd:cd03217 76 RLGIFLAFQYPPEIPGVKNAD------FLRYVNEG-------------------------FSGGEKKRNEILQLLLLEPD 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446629392 163 LVLADEPTGNLDSKASQDVMEILTHLnKEEKATMMLVTHDPVAASYC--DRVIFIKDG 218
Cdd:cd03217 125 LAILDEPDSGLDIDALRLVAEVINKL-REEGKSVLIITHYQRLLDYIkpDRVHVLYDG 181
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
10-220 |
5.40e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 79.96 E-value: 5.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 10 SKEYTGkVShtALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKnPYQLsPNDLAVFrRQELGFV 89
Cdd:PRK11288 11 GKTFPG-VK--ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ-EMRF-ASTTAAL-AAGVAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 90 FQSFNLLHTLTVKENMVL---PLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKLVLA 166
Cdd:PRK11288 85 YQELHLVPEMTVAENLYLgqlPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAF 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446629392 167 DEPTGNLDSKASQDVMEILTHLNKEEKAtMMLVTH--DPVAAsYCDRVIFIKDGQL 220
Cdd:PRK11288 165 DEPTSSLSAREIEQLFRVIRELRAEGRV-ILYVSHrmEEIFA-LCDAITVFKDGRY 218
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
21-220 |
7.38e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 79.51 E-value: 7.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 21 ALSNINLTITEGEFVGIMGPSGSGKTT----LLNMISTidsaTSGSVFINSKNPYQLSPNDLAVFRRqELGFVFQS--FN 94
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTtgraLLRLVES----QGGEIIFNGQRIDTLSPGKLQALRR-DIQFIFQDpyAS 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 95 LLHTLTVKENMVLPLVLDGM-NVKRINKRVESISKKLGI-SEILNKRTYEISGGQAQRTAIARALIHAPKLVLADEPTGN 172
Cdd:PRK10261 414 LDPRQTVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSA 493
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446629392 173 LDSKASQDVMEILTHLNKEEKATMMLVTHD-PVAASYCDRVIFIKDGQL 220
Cdd:PRK10261 494 LDVSIRGQIINLLLDLQRDFGIAYLFISHDmAVVERISHRVAVMYLGQI 542
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-223 |
8.16e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 77.83 E-value: 8.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 8 DLSKEYTGKvshTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSG-----SVFINSKNPYQLspNDLAVFR 82
Cdd:PRK14271 26 NLTLGFAGK---TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNY--RDVLEFR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 83 RQeLGFVFQSFNLLhTLTVKENmvlplVLDGMNVKRI----------NKRVESISKKLGISEILNKRTYEISGGQAQRTA 152
Cdd:PRK14271 101 RR-VGMLFQRPNPF-PMSIMDN-----VLAGVRAHKLvprkefrgvaQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLC 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446629392 153 IARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLnkEEKATMMLVTHD-PVAASYCDRVIFIKDGQLYNE 223
Cdd:PRK14271 174 LARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSL--ADRLTVIIVTHNlAQAARISDRAALFFDGRLVEE 243
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-219 |
1.30e-16 |
|
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: 78.71 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 20 TALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTI--DSATSGSVFINSKnpyQLSPNDLAVFRRQELGFVFQSFNLLH 97
Cdd:TIGR02633 15 KALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGS---PLKASNIRDTERAGIVIIHQELTLVP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 98 TLTVKENMVL--PLVLDG--MNVKRINKRVESISKKLGISEILNKRTY-EISGGQAQRTAIARALIHAPKLVLADEPTGN 172
Cdd:TIGR02633 92 ELSVAENIFLgnEITLPGgrMAYNAMYLRAKNLLRELQLDADNVTRPVgDYGGGQQQLVEIAKALNKQARLLILDEPSSS 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446629392 173 LDSKASQDVMEILTHLnKEEKATMMLVTH--DPVAAsYCDRVIFIKDGQ 219
Cdd:TIGR02633 172 LTEKETEILLDIIRDL-KAHGVACVYISHklNEVKA-VCDTICVIRDGQ 218
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
2-220 |
1.59e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 76.75 E-value: 1.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 2 KIVKVKDLSKEY---TGKVSH---TALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSknpYQLSP 75
Cdd:PRK15112 3 TLLEVRNLSKTFryrTGWFRRqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDD---HPLHF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 76 NDLAvFRRQELGFVFQ--SFNLLHTLTVKENMVLPLVLD-GMNVKRINKRVESISKKLGI-SEILNKRTYEISGGQAQRT 151
Cdd:PRK15112 80 GDYS-YRSQRIRMIFQdpSTSLNPRQRISQILDFPLRLNtDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 152 AIARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVT-HDPVAASYCDRVIFIKDGQL 220
Cdd:PRK15112 159 GLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTqHLGMMKHISDQVLVMHQGEV 228
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-219 |
3.00e-16 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 76.76 E-value: 3.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 1 MKIVKVKDLSKEY-TGKVSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTID----SATSGSVFINSKNPYQLSP 75
Cdd:PRK15093 1 MPLLDIRNLTIEFkTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTkdnwRVTADRMRFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 76 NDlavfRRQELG----FVFQSFNllHTLTVKENMVLPLV--LDGMNVK-----RIN---KRVESISKKLGISE---ILNK 138
Cdd:PRK15093 81 RE----RRKLVGhnvsMIFQEPQ--SCLDPSERVGRQLMqnIPGWTYKgrwwqRFGwrkRRAIELLHRVGIKDhkdAMRS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 139 RTYEISGGQAQRTAIARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHD-PVAASYCDRVIFIKD 217
Cdd:PRK15093 155 FPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDlQMLSQWADKINVLYC 234
|
..
gi 446629392 218 GQ 219
Cdd:PRK15093 235 GQ 236
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-220 |
6.33e-16 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 76.60 E-value: 6.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYTGKvSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKN--PYQLSpnDLavf 81
Cdd:PRK11176 342 IEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDlrDYTLA--SL--- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 82 rRQELGFVFQSFNLLHTlTVKENMVLPlVLDGMNVKRINKR------VESISK-KLGISEILNKRTYEISGGQAQRTAIA 154
Cdd:PRK11176 416 -RNQVALVSQNVHLFND-TIANNIAYA-RTEQYSREQIEEAarmayaMDFINKmDNGLDTVIGENGVLLSGGQRQRIAIA 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446629392 155 RALIH-APKLVLaDEPTGNLDSKASQDVMEILTHLNKEEkaTMMLVTHDPVAASYCDRVIFIKDGQL 220
Cdd:PRK11176 493 RALLRdSPILIL-DEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEKADEILVVEDGEI 556
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
3-202 |
9.23e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 76.39 E-value: 9.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYTG---KVSHTalsninlTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFIN---SKNPYQLSPN 76
Cdd:PRK13409 340 LVEYPDLTKKLGDfslEVEGG-------EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPElkiSYKPQYIKPD 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 77 dlavfrrqelgfvfqsfnllHTLTVKENMvlplvldgmnvKRINKRVES------ISKKLGISEILNKRTYEISGGQAQR 150
Cdd:PRK13409 413 --------------------YDGTVEDLL-----------RSITDDLGSsyykseIIKPLQLERLLDKNVKDLSGGELQR 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446629392 151 TAIARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHD 202
Cdd:PRK13409 462 VAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHD 513
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
22-202 |
1.91e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.61 E-value: 1.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 22 LSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVfinsKNPYQLspndlavfrrqELGFVFQSFNLLHT--L 99
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI----KRNGKL-----------RIGYVPQKLYLDTTlpL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 100 TVKENMVLPLVLDGMNVKRINKRVESiskklgiSEILNKRTYEISGGQAQRTAIARALIHAPKLVLADEPTGNLDSKASQ 179
Cdd:PRK09544 85 TVNRFLRLRPGTKKEDILPALKRVQA-------GHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQV 157
|
170 180
....*....|....*....|...
gi 446629392 180 DVMEILTHLNKEEKATMMLVTHD 202
Cdd:PRK09544 158 ALYDLIDQLRRELDCAVLMVSHD 180
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
18-217 |
3.56e-15 |
|
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: 71.03 E-value: 3.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 18 SHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMIS--------TIDSATSGSVFINSKNPYqlspndlavfrrqelgfv 89
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAglwpwgsgRIGMPEGEDLLFLPQRPY------------------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 90 fqsfnlLHTLTVKENMVLPLvldgmnvkrinkrvesiskklgiSEILnkrtyeiSGGQAQRTAIARALIHAPKLVLADEP 169
Cdd:cd03223 75 ------LPLGTLREQLIYPW-----------------------DDVL-------SGGEQQRLAFARLLLHKPKFVFLDEA 118
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446629392 170 TGNLDSKASQDVMEILthlnKEEKATMMLVTHDPVAASYCDRVIFIKD 217
Cdd:cd03223 119 TSALDEESEDRLYQLL----KELGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
4-220 |
4.58e-15 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 74.23 E-value: 4.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYTGkvSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLavfrR 83
Cdd:PRK13657 335 VEFDDVSFSYDN--SRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASL----R 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 84 QELGFVFQSfNLLHTLTVKENMVL--PLVLDGmNVKRINKRVES---ISKK-LGISEILNKRTYEISGGQAQRTAIARAL 157
Cdd:PRK13657 409 RNIAVVFQD-AGLFNRSIEDNIRVgrPDATDE-EMRAAAERAQAhdfIERKpDGYDTVVGERGRQLSGGERQRLAIARAL 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446629392 158 I-HAPKLVLaDEPTGNLDSKASQDVMEILTHLNKEEkaTMMLVTHDPVAASYCDRVIFIKDGQL 220
Cdd:PRK13657 487 LkDPPILIL-DEATSALDVETEAKVKAALDELMKGR--TTFIIAHRLSTVRNADRILVFDNGRV 547
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-219 |
7.23e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 73.42 E-value: 7.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYTGKvshTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTI--DSATSGSVFINSKnpyQLSPNDLAV 80
Cdd:PRK13549 5 LLEMKNITKTFGGV---KALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGE---ELQASNIRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 81 FRRQELGFVFQSFNLLHTLTVKENMVL--PLVLDG-MNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARAL 157
Cdd:PRK13549 79 TERAGIAIIHQELALVKELSVLENIFLgnEITPGGiMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKAL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446629392 158 IHAPKLVLADEPTGNLDSKASQDVMEILTHLnKEEKATMMLVTH--DPVAAsYCDRVIFIKDGQ 219
Cdd:PRK13549 159 NKQARLLILDEPTASLTESETAVLLDIIRDL-KAHGIACIYISHklNEVKA-ISDTICVIRDGR 220
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-202 |
7.85e-15 |
|
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: 73.67 E-value: 7.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 28 TITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQ---LSPNdlavfrrqelgfvfqsfnllHTLTVKEn 104
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYKpqyISPD--------------------YDGTVEE- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 105 mvlplVLDGMNVKRINK---RVEsISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKLVLADEPTGNLDSKASQDV 181
Cdd:COG1245 421 -----FLRSANTDDFGSsyyKTE-IIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAV 494
|
170 180
....*....|....*....|.
gi 446629392 182 MEILTHLNKEEKATMMLVTHD 202
Cdd:COG1245 495 AKAIRRFAENRGKTAMVVDHD 515
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
23-220 |
9.64e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 71.65 E-value: 9.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 23 SNINLTITEGEFVGIMGPSGSGKT----TLLNMISTIDSATSGSVFINSKnpyQLSPNDLavfRRQELGFVFQ----SFN 94
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGK---PVAPCAL---RGRKIATIMQnprsAFN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 95 LLHTLT--VKENmvlplvLDGMNVKRINKRVESISKKLGISE---ILNKRTYEISGGQAQRTAIARALIHAPKLVLADEP 169
Cdd:PRK10418 94 PLHTMHthARET------CLALGKPADDATLTAALEAVGLENaarVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446629392 170 TGNLDSKASQDVMEILTHLNKEEKATMMLVTHD-PVAASYCDRVIFIKDGQL 220
Cdd:PRK10418 168 TTDLDVVAQARILDLLESIVQKRALGMLLVTHDmGVVARLADDVAVMSHGRI 219
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
4-235 |
1.17e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 73.23 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYTGKVSHTALSNINLTITEGEFVGIMGPSGSGKTTLLN-MISTIDSATSGSVFINSKNPY--QLSpndlav 80
Cdd:PLN03130 615 ISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGTVAYvpQVS------ 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 81 frrqelgFVFQSfnllhtlTVKENMVLPLVLDGmnvKRINK--RVESISKKLGI------SEIlNKRTYEISGGQAQRTA 152
Cdd:PLN03130 689 -------WIFNA-------TVRDNILFGSPFDP---ERYERaiDVTALQHDLDLlpggdlTEI-GERGVNISGGQKQRVS 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 153 IARALIHAPKLVLADEPTGNLDSKASQDVMEilTHLNKE-EKATMMLVTHDPVAASYCDRVIFIKDGQLYNEIFYND--- 228
Cdd:PLN03130 751 MARAVYSNSDVYIFDDPLSALDAHVGRQVFD--KCIKDElRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEElsn 828
|
....*..
gi 446629392 229 NRSLFYQ 235
Cdd:PLN03130 829 NGPLFQK 835
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
22-218 |
1.24e-14 |
|
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: 69.96 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 22 LSNINLTITEGEFVGIMGPSGSGKTTLLNMIS--TIDSATSGSVFINSKnpyqlsPNDLAvFRRqELGFVFQSFNLLHTL 99
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAgrKTAGVITGEILINGR------PLDKN-FQR-STGYVEQQDVHSPNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 100 TVKENMVLPLVLDGMNVKrinkrvesiskklgiseilnkrtyeisggQAQRTAIARALIHAPKLVLADEPTGNLDSKASQ 179
Cdd:cd03232 95 TVREALRFSALLRGLSVE-----------------------------QRKRLTIGVELAAKPSILFLDEPTSGLDSQAAY 145
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446629392 180 DVMEILTHLNKEEKAtmMLVT-HDPVAA--SYCDRVIFIKDG 218
Cdd:cd03232 146 NIVRFLKKLADSGQA--ILCTiHQPSASifEKFDRLLLLKRG 185
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
21-219 |
1.30e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 72.97 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 21 ALSNINLTITEGEFVGIMGPSGSGKT-TLLNMISTIDSA----TSGSVFINSKNPY-----QLSPNDLAVFRRQELGFVF 90
Cdd:PRK10261 31 AVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQAgglvQCDKMLLRRRSRQvielsEQSAAQMRHVRGADMAMIF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 91 Q----SFNLLHTL--TVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKLV 164
Cdd:PRK10261 111 QepmtSLNPVFTVgeQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVL 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446629392 165 LADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHD-PVAASYCDRVIFIKDGQ 219
Cdd:PRK10261 191 IADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDmGVVAEIADRVLVMYQGE 246
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-202 |
1.48e-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: 72.66 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYTGKvsHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFinsknpyqLSPNdlavfr 82
Cdd:TIGR03719 4 IYTMNRVSKVVPPK--KEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEAR--------PQPG------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 83 rQELGFVFQSFNLLHTLTVKENmvlplVLDGM-NVKRINKRVESISKKLG---------------ISEILN-------KR 139
Cdd:TIGR03719 68 -IKVGYLPQEPQLDPTKTVREN-----VEEGVaEIKDALDRFNEISAKYAepdadfdklaaeqaeLQEIIDaadawdlDS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 140 TYEI-----------------SGGQAQRTAIARALIHAPKLVLADEPTGNLDSKaSQDVMEilTHLnKEEKATMMLVTHD 202
Cdd:TIGR03719 142 QLEIamdalrcppwdadvtklSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAE-SVAWLE--RHL-QEYPGTVVAVTHD 217
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
17-214 |
2.15e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.99 E-value: 2.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 17 VSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMI--STIDSATSGSVFINSKNPYQLSPNDLAVFRRQELGfvfQSFN 94
Cdd:COG2401 41 VERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLagALKGTPVAGCVDVPDNQFGREASLIDAIGRKGDFK---DAVE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 95 LLHTltvkenmvlplvldgmnvkrinkrvesiskkLGISE-ILNKRTY-EISGGQAQRTAIARALIHAPKLVLADEPTGN 172
Cdd:COG2401 118 LLNA-------------------------------VGLSDaVLWLRRFkELSTGQKFRFRLALLLAERPKLLVIDEFCSH 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446629392 173 LDSKASQDVMEILTHLNKEEKATMMLVTHDP--VAASYCDRVIF 214
Cdd:COG2401 167 LDRQTAKRVARNLQKLARRAGITLVVATHHYdvIDDLQPDLLIF 210
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
14-216 |
6.28e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 69.53 E-value: 6.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 14 TGKVSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFInsknpYQLSPNDlaVFRRQELGFVFQSF 93
Cdd:PRK15056 15 TWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISI-----LGQPTRQ--ALQKNLVAYVPQSE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 94 NLLHTLTV-KENMVLPLVLDGMNVKRINK-----RVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKLVLAD 167
Cdd:PRK15056 88 EVDWSFPVlVEDVVMMGRYGHMGWLRRAKkrdrqIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446629392 168 EPTGNLDSKASQDVMEILTHLnKEEKATMMLVTHDPVAAS-YCDRVIFIK 216
Cdd:PRK15056 168 EPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTeFCDYTVMVK 216
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
20-221 |
6.55e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.19 E-value: 6.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 20 TALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSAtSGSVFINSKNPYQLSPNDLAVFRrqelGFVFQS----FNL 95
Cdd:PRK03695 10 TRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAAELARHR----AYLSQQqtppFAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 96 --LHTLTvkenMVLPlvlDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARAL--IH-----APKLVLA 166
Cdd:PRK03695 85 pvFQYLT----LHQP---DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqVWpdinpAGQLLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446629392 167 DEPTGNLDSkASQDVMEILTHLNKEEKATMMLVTHD-PVAASYCDRVIFIKDGQLY 221
Cdd:PRK03695 158 DEPMNSLDV-AQQAALDRLLSELCQQGIAVVMSSHDlNHTLRHADRVWLLKQGKLL 212
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-220 |
9.31e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 70.46 E-value: 9.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEytgkvshtALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDlavfr 82
Cdd:PRK15439 268 VLTVEDLTGE--------GFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ----- 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 83 RQELGFVF-----QSFNL---------LHTLTVKEnmvLPLVLDGmnvKRINKRVESISKKLGIS-EILNKRTYEISGGQ 147
Cdd:PRK15439 335 RLARGLVYlpedrQSSGLyldaplawnVCALTHNR---RGFWIKP---ARENAVLERYRRALNIKfNHAEQAARTLSGGN 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446629392 148 AQRTAIARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDPVAASYCDRVIFIKDGQL 220
Cdd:PRK15439 409 QQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
15-226 |
1.97e-13 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 66.90 E-value: 1.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 15 GKVSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNmisTIDSATSGSVFINSKNPYQ-LSPNDLAVFRRQELGFVFQSF 93
Cdd:cd03233 16 GRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLK---ALANRTEGNVSVEGDIHYNgIPYKEFAEKYPGEIIYVSEED 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 94 NLLHTLTVKENMVLPLVLDGMNVKRinkrvesiskklgiseilnkrtyEISGGQAQRTAIARALIHAPKLVLADEPTGNL 173
Cdd:cd03233 93 VHFPTLTVRETLDFALRCKGNEFVR-----------------------GISGGERKRVSIAEALVSRASVLCWDNSTRGL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446629392 174 DSKASQDVMEILTHLNKEEKATMMLVTHDPVAASY--CDRVIFIKDGQlynEIFY 226
Cdd:cd03233 150 DSSTALEILKCIRTMADVLKTTTFVSLYQASDEIYdlFDKVLVLYEGR---QIYY 201
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-201 |
2.38e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 69.36 E-value: 2.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYTGkvSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLavfrR 83
Cdd:PRK10790 341 IDIDNVSFAYRD--DNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL----R 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 84 QELGFVFQ-----SFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKklGISEILNKRTYEISGGQAQRTAIARALI 158
Cdd:PRK10790 415 QGVAMVQQdpvvlADTFLANVTLGRDISEEQVWQALETVQLAELARSLPD--GLYTPLGEQGNNLSVGQKQLLALARVLV 492
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446629392 159 HAPKLVLADEPTGNLDSKASQDVMEILTHLnkEEKATMMLVTH 201
Cdd:PRK10790 493 QTPQILILDEATANIDSGTEQAIQQALAAV--REHTTLVVIAH 533
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
5-223 |
3.99e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.49 E-value: 3.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 5 KVKDLSKEytgkvshtALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPND-LAVfrr 83
Cdd:PRK10762 259 KVDNLSGP--------GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDgLAN--- 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 84 qelGFVFQSFN-----LLHTLTVKENMVLPlVLDGMNVK--RINKRVESISKKLGIsEILNKRT-------YEISGGQAQ 149
Cdd:PRK10762 328 ---GIVYISEDrkrdgLVLGMSVKENMSLT-ALRYFSRAggSLKHADEQQAVSDFI-RLFNIKTpsmeqaiGLLSGGNQQ 402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446629392 150 RTAIARALIHAPKLVLADEPTGNLDSKASQdvmEILTHLN--KEEKATMMLVTHD-PVAASYCDRVIFIKDGQLYNE 223
Cdd:PRK10762 403 KVAIARGLMTRPKVLILDEPTRGVDVGAKK---EIYQLINqfKAEGLSIILVSSEmPEVLGMSDRILVMHEGRISGE 476
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-220 |
4.41e-13 |
|
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: 66.28 E-value: 4.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYTGKVShTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLavfrR 83
Cdd:cd03369 7 IEVENLSVRYAPDLP-PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL----R 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 84 QELGFVFQSfnllhtltvkenmvlPLVLDG---MNVKRINKRV-ESISKKLGISEI-LNkrtyeISGGQAQRTAIARALI 158
Cdd:cd03369 82 SSLTIIPQD---------------PTLFSGtirSNLDPFDEYSdEEIYGALRVSEGgLN-----LSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446629392 159 HAPKLVLADEPTGNLDSKASQDVMEILthlnKEE--KATMMLVTHDPVAASYCDRVIFIKDGQL 220
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTI----REEftNSTILTIAHRLRTIIDYDKILVMDAGEV 201
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
20-204 |
7.75e-13 |
|
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: 65.46 E-value: 7.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 20 TALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNdlavfRRQELGFVFQSFNLLHTL 99
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE-----PHENILYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 100 TVKENMVLPLVLDGMNVKRINKRVEsiskKLGISEILNKRTYEISGGQAQRTAIARALIHAPKLVLADEPTGNLDSKASQ 179
Cdd:TIGR01189 89 SALENLHFWAAIHGGAQRTIEDALA----AVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVA 164
|
170 180
....*....|....*....|....*.
gi 446629392 180 DVMEILT-HLNKeeKATMMLVTHDPV 204
Cdd:TIGR01189 165 LLAGLLRaHLAR--GGIVLLTTHQDL 188
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-202 |
1.78e-12 |
|
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: 66.73 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 28 TITEGEFVGIMGPSGSGKTTLLNMIStidsatsGsvfinsknpyQLSPN----------D--LAVFRRQELgfvFQSFNL 95
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILS-------G----------ELKPNlgdydeepswDevLKRFRGTEL---QDYFKK 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 96 LH--TLTV--KENMV--LPLVLDGmNVKRINKRV------ESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKL 163
Cdd:COG1245 155 LAngEIKVahKPQYVdlIPKVFKG-TVRELLEKVdergklDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADF 233
|
170 180 190
....*....|....*....|....*....|....*....
gi 446629392 164 VLADEPTGNLDSKASQDVMEILTHLNKEEKAtMMLVTHD 202
Cdd:COG1245 234 YFFDEPSSYLDIYQRLNVARLIRELAEEGKY-VLVVEHD 271
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1-215 |
2.60e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.59 E-value: 2.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 1 MKIVKVKDLSKEYTGKVSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFIN-------------- 66
Cdd:PTZ00265 380 IKKIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdshnlkdinlkwwr 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 67 ------SKNP------------YQL-SPNDLAVFRRQ--ELGFVFQS-FNLLHTLTVKENMVLPLVLDGMNVKRI----- 119
Cdd:PTZ00265 460 skigvvSQDPllfsnsiknnikYSLySLKDLEALSNYynEDGNDSQEnKNKRNSCRAKCAGDLNDMSNTTDSNELiemrk 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 120 ------NKRVESISKKLGISE-----------ILNKRTYEISGGQAQRTAIARALIHAPKLVLADEPTGNLDSKASQDVM 182
Cdd:PTZ00265 540 nyqtikDSEVVDVSKKVLIHDfvsalpdkyetLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
|
250 260 270
....*....|....*....|....*....|...
gi 446629392 183 EILTHLNKEEKATMMLVTHDPVAASYCDrVIFI 215
Cdd:PTZ00265 620 KTINNLKGNENRITIIIAHRLSTIRYAN-TIFV 651
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-223 |
3.54e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.41 E-value: 3.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYTGKvshTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDlavfr 82
Cdd:PRK10762 4 LLQLKGIDKAFPGV---KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKS----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 83 RQE--LGFVFQSFNLLHTLTVKENMVL----PLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARA 156
Cdd:PRK10762 76 SQEagIGIIHQELNLIPQLTIAENIFLgrefVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446629392 157 LIHAPKLVLADEPTGNLDSKASQDVMEILTHLnKEEKATMMLVTHD-PVAASYCDRVIFIKDGQLYNE 223
Cdd:PRK10762 156 LSFESKVIIMDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRlKEIFEICDDVTVFRDGQFIAE 222
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
20-203 |
3.88e-12 |
|
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: 63.28 E-value: 3.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 20 TALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNdlavfRRQELGFVFQSFNLLHTL 99
Cdd:cd03231 14 ALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDS-----IARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 100 TVKENMVLplvldgmnVKRINKR--VESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKLVLADEPTGNLDsKA 177
Cdd:cd03231 89 SVLENLRF--------WHADHSDeqVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD-KA 159
|
170 180
....*....|....*....|....*.
gi 446629392 178 SQDVMEILTHLNKEEKATMMLVTHDP 203
Cdd:cd03231 160 GVARFAEAMAGHCARGGMVVLTTHQD 185
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-174 |
4.11e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 65.34 E-value: 4.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 2 KIVKVKDLSKEYTGKVshtALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSknpyqlspndlAVf 81
Cdd:TIGR03719 321 KVIEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGE-----------TV- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 82 rrqELGFVFQSFNllhTLTVKENmVLPLVLDGMNVKRINKRvesiskklgisEIlNKRTY----------------EISG 145
Cdd:TIGR03719 386 ---KLAYVDQSRD---ALDPNKT-VWEEISGGLDIIKLGKR-----------EI-PSRAYvgrfnfkgsdqqkkvgQLSG 446
|
170 180
....*....|....*....|....*....
gi 446629392 146 GQAQRTAIARALIHAPKLVLADEPTGNLD 174
Cdd:TIGR03719 447 GERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
18-220 |
4.82e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 64.08 E-value: 4.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 18 SHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMIS--------TIDSATSGSVFINSKNPYQLSPNDLAVFR-----RQ 84
Cdd:PRK13547 13 HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgdltgggaPRGARVTGDVTLNGEPLAAIDAPRLARLRavlpqAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 85 ELGFVFqsfnllhtlTVKENMVL---PLVLDGMNVKRINKRVESISKKLGISEILNKR-TYEISGGQAQRTAIARAL--- 157
Cdd:PRK13547 93 QPAFAF---------SAREIVLLgryPHARRAGALTHRDGEIAWQALALAGATALVGRdVTTLSGGELARVQFARVLaql 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 158 ------IHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDP-VAASYCDRVIFIKDGQL 220
Cdd:PRK13547 164 wpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPnLAARHADRIAMLADGAI 233
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
22-202 |
5.12e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 65.36 E-value: 5.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 22 LSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINsknpyqlspNDLAVFR------RQELGFVF----- 90
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE---------QDLIVARlqqdppRNVEGTVYdfvae 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 91 ----------QSFNLLHTL-------TVKENMVLPLVLDGMNVKRINKRVESISKKLGISEilNKRTYEISGGQAQRTAI 153
Cdd:PRK11147 90 gieeqaeylkRYHDISHLVetdpsekNLNELAKLQEQLDHHNLWQLENRINEVLAQLGLDP--DAALSSLSGGWLRKAAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446629392 154 ARALIHAPKLVLADEPTGNLDSkasqDVMEILTHLNKEEKATMMLVTHD 202
Cdd:PRK11147 168 GRALVSNPDVLLLDEPTNHLDI----ETIEWLEGFLKTFQGSIIFISHD 212
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
7-219 |
6.29e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 64.75 E-value: 6.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 7 KDLSKEYTGKvshTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKnPYQLSPNDLAVfrRQEL 86
Cdd:PRK10982 2 SNISKSFPGV---KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGK-EIDFKSSKEAL--ENGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 87 GFVFQSFNLLHTLTVKENMVL---PlvLDGMNV--KRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAP 161
Cdd:PRK10982 76 SMVHQELNLVLQRSVMDNMWLgryP--TKGMFVdqDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446629392 162 KLVLADEPTGNLDSKASQDVMEILTHLnKEEKATMMLVTHD-PVAASYCDRVIFIKDGQ 219
Cdd:PRK10982 154 KIVIMDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKmEEIFQLCDEITILRDGQ 211
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
6-190 |
7.24e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 62.58 E-value: 7.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 6 VKDLSKEYTGKVshtALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAVFrrqe 85
Cdd:PRK13539 5 GEDLACVRGGRV---LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHY---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 86 LGfvfqsfnllH------TLTVKENMVLPLVLDGMNVKRINKRVESIskklGISEILNKRTYEISGGQAQRTAIARALI- 158
Cdd:PRK13539 78 LG---------HrnamkpALTVAENLEFWAAFLGGEELDIAAALEAV----GLAPLAHLPFGYLSAGQKRRVALARLLVs 144
|
170 180 190
....*....|....*....|....*....|....
gi 446629392 159 HAPKLVLaDEPTGNLDSkASQDVME--ILTHLNK 190
Cdd:PRK13539 145 NRPIWIL-DEPTAALDA-AAVALFAelIRAHLAQ 176
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
16-220 |
9.87e-12 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 64.35 E-value: 9.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 16 KVSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLavfrRQELGFVFQSfNL 95
Cdd:PRK10789 325 QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSW----RSRLAVVSQT-PF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 96 LHTLTVKENMVL--PlvldgmnvKRINKRVESISKKLGISE-ILN----------KRTYEISGGQAQRTAIARALIHAPK 162
Cdd:PRK10789 400 LFSDTVANNIALgrP--------DATQQEIEHVARLASVHDdILRlpqgydtevgERGVMLSGGQKQRISIARALLLNAE 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446629392 163 LVLADEPTGNLDSKASQdvmEILTHLNK-EEKATMMLVTHDPVAASYCDRVIFIKDGQL 220
Cdd:PRK10789 472 ILILDDALSAVDGRTEH---QILHNLRQwGEGRTVIISAHRLSALTEASEILVMQHGHI 527
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-237 |
1.40e-11 |
|
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: 62.95 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYTgKVSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSaTSGSVFINSknpyqLSPNDLAVFR- 82
Cdd:cd03289 3 MTVKDLTAKYT-EGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDG-----VSWNSVPLQKw 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 83 RQELGFVFQSFnLLHTLTVKENmvlplvLD---GMNVKRINKRVESISKKLGISE-------ILNKRTYEISGGQAQRTA 152
Cdd:cd03289 76 RKAFGVIPQKV-FIFSGTFRKN------LDpygKWSDEEIWKVAEEVGLKSVIEQfpgqldfVLVDGGCVLSHGHKQLMC 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 153 IARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEekATMMLVTHDPVAASYCDRVIFIKDGQL--YNEI--FYND 228
Cdd:cd03289 149 LARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFAD--CTVILSEHRIEAMLECQRFLVIEENKVrqYDSIqkLLNE 226
|
....*....
gi 446629392 229 nRSLFYQNI 237
Cdd:cd03289 227 -KSHFKQAI 234
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
29-219 |
1.72e-11 |
|
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: 61.05 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 29 ITEGEFVGIMGPSGSGKTTLLNMISTidsatsgsvfinsknpyQLSPNDlavfrrqelgfvfqsfnllhtltvkENMVLP 108
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAG-----------------QLIPNG-------------------------DNDEWD 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 109 LVldgmnvkRINKRVESISkklgiseilnkrtyeISGGQAQRTAIARALIHAPKLVLADEPTGNLDSKASQDVMEILTHL 188
Cdd:cd03222 60 GI-------TPVYKPQYID---------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
|
170 180 190
....*....|....*....|....*....|.
gi 446629392 189 NKEEKATMMLVTHDPVAASYCDRVIFIKDGQ 219
Cdd:cd03222 118 SEEGKKTALVVEHDLAVLDYLSDRIHVFEGE 148
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-202 |
2.12e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 63.29 E-value: 2.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 28 TITEGEFVGIMGPSGSGKTTLLNMIStidsatsGsvfinsknpyQLSPN----------D--LAVFRRQELgfvFQSFNL 95
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILS-------G----------ELIPNlgdyeeepswDevLKRFRGTEL---QNYFKK 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 96 LH----TLTVKENMV--LPLVLDGmNVKRINKRV------ESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKL 163
Cdd:PRK13409 155 LYngeiKVVHKPQYVdlIPKVFKG-KVRELLKKVdergklDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADF 233
|
170 180 190
....*....|....*....|....*....|....*....
gi 446629392 164 VLADEPTGNLDSKASQDVMEILTHLNkeEKATMMLVTHD 202
Cdd:PRK13409 234 YFFDEPTSYLDIRQRLNVARLIRELA--EGKYVLVVEHD 270
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-201 |
2.68e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 61.97 E-value: 2.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 2 KIVKVKDLskeYTGKVSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDS--ATSGSVFINSKNPYQLSPNDla 79
Cdd:CHL00131 6 PILEIKNL---HASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAykILEGDILFKGESILDLEPEE-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 80 vfrRQELGfVFQSFNLLHTLTVKENM-VLPLVLdgmNVKRINKRV---------ESISKKLGI----SEILNKRTYE-IS 144
Cdd:CHL00131 81 ---RAHLG-IFLAFQYPIEIPGVSNAdFLRLAY---NSKRKFQGLpeldpleflEIINEKLKLvgmdPSFLSRNVNEgFS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446629392 145 GGQAQRTAIARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKAtMMLVTH 201
Cdd:CHL00131 154 GGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENS-IILITH 209
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-173 |
3.34e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 62.76 E-value: 3.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYTGKVshtALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNdlavfR 82
Cdd:PRK15439 11 LLCARSISKQYSGVE---VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-----K 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 83 RQELG--FVFQSFNLLHTLTVKENMVLPLVldgmNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHA 160
Cdd:PRK15439 83 AHQLGiyLVPQEPLLFPNLSVKENILFGLP----KRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRD 158
|
170
....*....|...
gi 446629392 161 PKLVLADEPTGNL 173
Cdd:PRK15439 159 SRILILDEPTASL 171
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
24-229 |
5.90e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 62.15 E-value: 5.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 24 NINLTITEGEFVGIMGPSGSGKTTLLNMI-STIDSATSGSVFINSK-----NPYQ-------LSPNDlavfrRQELGFVF 90
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKpvdirNPAQairagiaMVPED-----RKRHGIVP 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 91 QsfnllhtLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEiLNKRTYE-------ISGGQAQRTAIARALIHAPKL 163
Cdd:TIGR02633 353 I-------LGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQR-LKVKTASpflpigrLSGGNQQKAVLAKMLLTNPRV 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446629392 164 VLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDPVAASYCDRVIFIKDGQLYNEiFYNDN 229
Cdd:TIGR02633 425 LILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGD-FVNHA 489
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
4-223 |
8.28e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.92 E-value: 8.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYTGKVSHTALSNINLTITEGEFVGIMGPSGSGKTTLLN-MISTIDSATSGSVFINSKNPYqlSPndlavfr 82
Cdd:PLN03232 615 ISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGSVAY--VP------- 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 83 rqELGFVFQSfnllhtlTVKENMvlpLVLDGMNVKRINKRVESISKKLGI--------SEIlNKRTYEISGGQAQRTAIA 154
Cdd:PLN03232 686 --QVSWIFNA-------TVRENI---LFGSDFESERYWRAIDVTALQHDLdllpgrdlTEI-GERGVNISGGQKQRVSMA 752
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446629392 155 RALIHAPKLVLADEPTGNLDSKASQDVMEILThlnKEE--KATMMLVTHDPVAASYCDRVIFIKDGQLYNE 223
Cdd:PLN03232 753 RAVYSNSDIYIFDDPLSALDAHVAHQVFDSCM---KDElkGKTRVLVTNQLHFLPLMDRIILVSEGMIKEE 820
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
5-220 |
8.92e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 61.44 E-value: 8.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 5 KVKDLSKEYTGKVSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSknpyqlSPNDLAVfrrq 84
Cdd:PRK13545 23 KLKDLFFRSKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG------SAALIAI---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 85 elgfvfqSFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKLV 164
Cdd:PRK13545 93 -------SSGLNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDIL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446629392 165 LADEPTGNLDSKASQDVMEILTHLnKEEKATMMLVTHD-PVAASYCDRVIFIKDGQL 220
Cdd:PRK13545 166 VIDEALSVGDQTFTKKCLDKMNEF-KEQGKTIFFISHSlSQVKSFCTKALWLHYGQV 221
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-170 |
1.01e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 61.29 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYtGKVshTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFInsknpyqLSpNDLA--V 80
Cdd:NF033858 1 VARLEGVSHRY-GKT--VALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEV-------LG-GDMAdaR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 81 FRR----------QELGfvfqsFNLLHTLTVKENmvlplvLD------GMNVKRINKRVESISKKLGISEILNKRTYEIS 144
Cdd:NF033858 70 HRRavcpriaympQGLG-----KNLYPTLSVFEN------LDffgrlfGQDAAERRRRIDELLRATGLAPFADRPAGKLS 138
|
170 180
....*....|....*....|....*.
gi 446629392 145 GGQAQRTAIARALIHAPKLVLADEPT 170
Cdd:NF033858 139 GGMKQKLGLCCALIHDPDLLILDEPT 164
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
22-218 |
1.11e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 61.66 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 22 LSNINLTITEGEFVGIMGPSGSGKTTLLNMIS---TIDSATSGSVFINSKnpyqlsPNDlAVFRRQeLGFVFQSFNLLHT 98
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLAervTTGVITGGDRLVNGR------PLD-SSFQRS-IGYVQQQDLHLPT 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 99 LTVKENMVLPLVLdgmnvkRINKRVeSISKKL----GISEILNKRTYE----------ISGGQAQRTAIARALIHAPKLV 164
Cdd:TIGR00956 851 STVRESLRFSAYL------RQPKSV-SKSEKMeyveEVIKLLEMESYAdavvgvpgegLNVEQRKRLTIGVELVAKPKLL 923
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446629392 165 L-ADEPTGNLDSKASQDVMEILTHLNKEEKAtmMLVT-HDPVAASYC--DRVIFIKDG 218
Cdd:TIGR00956 924 LfLDEPTSGLDSQTAWSICKLMRKLADHGQA--ILCTiHQPSAILFEefDRLLLLQKG 979
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
22-233 |
1.39e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 60.95 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 22 LSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSV---------FINSKNPYQLSPNDLAV------FRRQEL 86
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYtfpgnwqlaWVNQETPALPQPALEYVidgdreYRQLEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 87 gfvfqsfNLLHTLTVKENMVLPLV---LDGMNVKRINKRVESISKKLGIS-EILNKRTYEISGGQAQRTAIARALIHAPK 162
Cdd:PRK10636 97 -------QLHDANERNDGHAIATIhgkLDAIDAWTIRSRAASLLHGLGFSnEQLERPVSDFSGGWRMRLNLAQALICRSD 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446629392 163 LVLADEPTGNLDskasQDVMEILTHLNKEEKATMMLVTH-----DPVAasycDRVIFIKDGQLYNeifYNDNRSLF 233
Cdd:PRK10636 170 LLLLDEPTNHLD----LDAVIWLEKWLKSYQGTLILISHdrdflDPIV----DKIIHIEQQSLFE---YTGNYSSF 234
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
26-199 |
1.54e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.80 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 26 NLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLAVFRRQElgfvFQSFNllhtltvkENM 105
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDE----WQRNN--------TDM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 106 VLPLVLD-GMNVKRI-------NKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKLVLADEPTGNLDSKA 177
Cdd:PRK10938 91 LSPGEDDtGRTTAEIiqdevkdPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVAS 170
|
170 180
....*....|....*....|..
gi 446629392 178 SQDVMEILTHLNKeEKATMMLV 199
Cdd:PRK10938 171 RQQLAELLASLHQ-SGITLVLV 191
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-202 |
1.74e-10 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 59.69 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 31 EGEFVGIMGPSGSGKTTLLNMIStidsatsGSVFINSKNpYQLSPN---DLAVFRRQELGFVFQSfnLLH---TLTVKEN 104
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILA-------GKLKPNLGK-FDDPPDwdeILDEFRGSELQNYFTK--LLEgdvKVIVKPQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 105 MV--LPLVLDG---MNVKRINKR--VESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKLVLADEPTGNLDSKA 177
Cdd:cd03236 95 YVdlIPKAVKGkvgELLKKKDERgkLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQ 174
|
170 180
....*....|....*....|....*
gi 446629392 178 SQDVMEILTHLNKEEKAtMMLVTHD 202
Cdd:cd03236 175 RLNAARLIRELAEDDNY-VLVVEHD 198
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
22-221 |
2.56e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.03 E-value: 2.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 22 LSNINLTITEGEFVGIMGPSGSGKTTLLNMIsTIDSATSGSvfinsknpyqlspNDLAVFRRQ------------ELGFV 89
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI-TGDHPQGYS-------------NDLTLFGRRrgsgetiwdikkHIGYV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 90 FQSFNLLH--TLTVKeNMVLPLVLDGMNV-----KRINKRVESISKKLGISEILNKRTYE-ISGGQaQRTA-IARALIHA 160
Cdd:PRK10938 342 SSSLHLDYrvSTSVR-NVILSGFFDSIGIyqavsDRQQKLAQQWLDILGIDKRTADAPFHsLSWGQ-QRLAlIVRALVKH 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446629392 161 PKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDPVAASYC--DRVIFIKDGQLY 221
Cdd:PRK10938 420 PTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDAPACitHRLEFVPDGDIY 482
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
22-253 |
2.65e-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: 60.31 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 22 LSNINLTITEGEFVGIMGPSGSGKTTLLNMISTidsatsgsvfinsknpyQLSPNDLAVFRRQELGFVFQsFNLLHTLTV 101
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMG-----------------ELEPSEGKIKHSGRISFSPQ-TSWIMPGTI 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 102 KENMVLPLVLDGMNVKRINKRV---ESISKKLGISEI-LNKRTYEISGGQAQRTAIARALIHAPKLVLADEPTGNLDSKA 177
Cdd:TIGR01271 504 KDNIIFGLSYDEYRYTSVIKACqleEDIALFPEKDKTvLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446629392 178 SQDVME-ILTHL--NKeekaTMMLVTHDPVAASYCDRVIFIKDGQLYneiFYNdnrslfyqniidSLSMLGGNKNDFST 253
Cdd:TIGR01271 584 EKEIFEsCLCKLmsNK----TRILVTSKLEHLKKADKILLLHEGVCY---FYG------------TFSELQAKRPDFSS 643
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
22-210 |
3.09e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.04 E-value: 3.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 22 LSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNpyqlSPNDLAVFRRQeLGFVFQSFNLLHTLTV 101
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQS----IKKDLCTYQKQ-LCFVGHRSGINPYLTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 102 KENMVLPLVLDGMNVKrinkrVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKLVLADEPTGNLDSKASQDV 181
Cdd:PRK13540 92 RENCLYDIHFSPGAVG-----ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTI 166
|
170 180 190
....*....|....*....|....*....|
gi 446629392 182 M-EILTHlnKEEKATMMLVTHDPVAASYCD 210
Cdd:PRK13540 167 ItKIQEH--RAKGGAVLLTSHQDLPLNKAD 194
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
22-185 |
4.81e-10 |
|
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: 59.45 E-value: 4.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 22 LSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLavfrRQELGFVFQS---FNLlht 98
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASL----RAAIGIVPQDtvlFND--- 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 99 lTVKEN--------------------------MVLPlvlDGMNVkrinkRV-EsiskklgiseilnkRTYEISGGQAQRT 151
Cdd:COG5265 447 -TIAYNiaygrpdaseeeveaaaraaqihdfiESLP---DGYDT-----RVgE--------------RGLKLSGGEKQRV 503
|
170 180 190
....*....|....*....|....*....|....
gi 446629392 152 AIARALIHAPKLVLADEPTGNLDSKASQDVMEIL 185
Cdd:COG5265 504 AIARTLLKNPPILIFDEATSALDSRTERAIQAAL 537
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-174 |
1.17e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.21 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 2 KIVKVKDLSKEYTGKVshtALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSknpyqlspndlAVf 81
Cdd:PRK11819 323 KVIEAENLSKSFGDRL---LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGE-----------TV- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 82 rrqELGFVFQSfnllhtltvKENmvlplvLDGmnvkriNKRV-ESISK-----KLGISEIlNKRTY-------------- 141
Cdd:PRK11819 388 ---KLAYVDQS---------RDA------LDP------NKTVwEEISGgldiiKVGNREI-PSRAYvgrfnfkggdqqkk 442
|
170 180 190
....*....|....*....|....*....|....*
gi 446629392 142 --EISGGQAQRTAIARALIHAPKLVLADEPTGNLD 174
Cdd:PRK11819 443 vgVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
23-206 |
1.25e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 56.35 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 23 SNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKnpyqlspndlavfRRQELGFVFQSfNLL---HT- 98
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGE-------------PIRRQRDEYHQ-DLLylgHQp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 99 -----LTVKENMvlplvldgmnvkRINKRVESISKKLGISEILNK---RTYE------ISGGQAQRTAIARALIHAPKLV 164
Cdd:PRK13538 84 gikteLTALENL------------RFYQRLHGPGDDEALWEALAQvglAGFEdvpvrqLSAGQQRRVALARLWLTRAPLW 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446629392 165 LADEPTGNLDSKASQDVMEILT-HLnkEEKATMMLVTHDPVAA 206
Cdd:PRK13538 152 ILDEPFTAIDKQGVARLEALLAqHA--EQGGMVILTTHQDLPV 192
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
3-219 |
1.87e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 57.49 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYTGkVshTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATS--GSVFINSKnpyqlspndLAV 80
Cdd:NF040905 1 ILEMRGITKTFPG-V--KALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGE---------VCR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 81 FRR----QELGFVF--QSFNLLHTLTVKENMVLplvldG--------MNVKRINKRVESISKKLGISEILNKRTYEISGG 146
Cdd:NF040905 69 FKDirdsEALGIVIihQELALIPYLSIAENIFL-----GnerakrgvIDWNETNRRARELLAKVGLDESPDTLVTDIGVG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446629392 147 QAQRTAIARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLnKEEKATMMLVTH-----DPVAasycDRVIFIKDGQ 219
Cdd:NF040905 144 KQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHklneiRRVA----DSITVLRDGR 216
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
3-202 |
2.27e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 57.56 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYTGkvSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNpyqlspnDLAVFR 82
Cdd:PLN03073 508 IISFSDASFGYPG--GPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKV-------RMAVFS 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 83 RQEL-GFVFQSFNLLHTLTVkenmvLPLVLDgmnvkrinKRVESISKKLGISEILN-KRTYEISGGQAQRTAIARALIHA 160
Cdd:PLN03073 579 QHHVdGLDLSSNPLLYMMRC-----FPGVPE--------QKLRAHLGSFGVTGNLAlQPMYTLSGGQKSRVAFAKITFKK 645
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446629392 161 PKLVLADEPTGNLDSKASQDVMEILTHLnkeeKATMMLVTHD 202
Cdd:PLN03073 646 PHILLLDEPSNHLDLDAVEALIQGLVLF----QGGVLMVSHD 683
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-202 |
4.02e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.67 E-value: 4.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 7 KDLSKEYTGKvsHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFinsknpyqLSPNdlavfrrQEL 86
Cdd:PRK11819 10 NRVSKVVPPK--KQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEAR--------PAPG-------IKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 87 GFVFQSFNLLHTLTVKENmvlplVLDGM-NVKRINKRVESISKKLG---------------ISEILN-------KRTYEI 143
Cdd:PRK11819 73 GYLPQEPQLDPEKTVREN-----VEEGVaEVKAALDRFNEIYAAYAepdadfdalaaeqgeLQEIIDaadawdlDSQLEI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446629392 144 -----------------SGGQAQRTAIARALIHAPKLVLADEPTGNLDSKaSQDVMEilTHLnKEEKATMMLVTHD 202
Cdd:PRK11819 148 amdalrcppwdakvtklSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE-SVAWLE--QFL-HDYPGTVVAVTHD 219
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
6-237 |
4.81e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 56.46 E-value: 4.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 6 VKDLSKEYTgKVSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSaTSGSVFINSknpyqLSPNDLAVFR-RQ 84
Cdd:TIGR01271 1220 VQGLTAKYT-EAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDG-----VSWNSVTLQTwRK 1292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 85 ELGFVFQSFNLLhTLTVKENM---------VLPLVLDGMNVKRInkrVESISKKLGIseILNKRTYEISGGQAQRTAIAR 155
Cdd:TIGR01271 1293 AFGVIPQKVFIF-SGTFRKNLdpyeqwsdeEIWKVAEEVGLKSV---IEQFPDKLDF--VLVDGGYVLSNGHKQLMCLAR 1366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 156 ALIHAPKLVLADEPTGNLDSKASQDVMEILTHlnKEEKATMMLVTHDPVAASYCDRVIFIKDGQL--YNEI--FYNDnRS 231
Cdd:TIGR01271 1367 SILSKAKILLLDEPSAHLDPVTLQIIRKTLKQ--SFSNCTVILSEHRVEALLECQQFLVIEGSSVkqYDSIqkLLNE-TS 1443
|
....*.
gi 446629392 232 LFYQNI 237
Cdd:TIGR01271 1444 LFKQAM 1449
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
29-206 |
5.55e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.85 E-value: 5.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 29 ITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKnpyqlsPNDLAVfRRQELGFVFQSFNLLHTLTVKENMVLP 108
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK------TATRGD-RSRFMAYLGHLPGLKADLSTLENLHFL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 109 LVLDGMNVKRINKRVESIskkLGISEILNKRTYEISGGQAQRTAIARALIHAPKLVLADEPTGNLDSKASQDVMEILT-H 187
Cdd:PRK13543 107 CGLHGRRAKQMPGSALAI---VGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISaH 183
|
170
....*....|....*....
gi 446629392 188 LNKEEKAtmMLVTHDPVAA 206
Cdd:PRK13543 184 LRGGGAA--LVTTHGAYAA 200
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
22-253 |
6.03e-09 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 55.25 E-value: 6.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 22 LSNINLTITEGEFVGIMGPSGSGKTTLLNMISTidsatsgsvfinsknpyQLSPNDLAVFRRQELGFVFQsFNLLHTLTV 101
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILG-----------------ELEPSEGKIKHSGRISFSSQ-FSWIMPGTI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 102 KENMVLPLVLDGMNVKRINKRV---ESISKklgISE----ILNKRTYEISGGQAQRTAIARALIHAPKLVLADEPTGNLD 174
Cdd:cd03291 115 KENIIFGVSYDEYRYKSVVKACqleEDITK---FPEkdntVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 175 SKASQDVME-ILTHL--NKeekaTMMLVTHDPVAASYCDRVIFIKDGQLYneiFYNdnrslfyqniidSLSMLGGNKNDF 251
Cdd:cd03291 192 VFTEKEIFEsCVCKLmaNK----TRILVTSKMEHLKKADKILILHEGSSY---FYG------------TFSELQSLRPDF 252
|
..
gi 446629392 252 ST 253
Cdd:cd03291 253 SS 254
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
22-226 |
6.70e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 56.27 E-value: 6.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 22 LSNINLTITEGEFVGIMGPSGSGKTTLLnmiSTIDSATSGS-VFINSKNPYQ-LSPNDLAVFRRQELGFVFQSFNLLHTL 99
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLL---KTIASNTDGFhIGVEGVITYDgITPEEIKKHYRGDVVYNAETDVHFPHL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 100 TVKENMVLPLVLDG-----MNVKR---INKRVESISKKLGISEILNKRTYE-----ISGGQAQRTAIARALIHAPKLVLA 166
Cdd:TIGR00956 154 TVGETLDFAARCKTpqnrpDGVSReeyAKHIADVYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKIQCW 233
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446629392 167 DEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDPVAASY--CDRVIFIKDGQlynEIFY 226
Cdd:TIGR00956 234 DNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSQDAYelFDKVIVLYEGY---QIYF 292
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
22-202 |
1.02e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 54.63 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 22 LSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKnPYQLSPNDLAVFRrQELGFVFQSFN--LLHTl 99
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGK-PLDYSKRGLLALR-QQVATVFQDPEqqIFYT- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 100 TVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKLVLADEPTGNLDSKASQ 179
Cdd:PRK13638 94 DIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRT 173
|
170 180
....*....|....*....|...
gi 446629392 180 DVMEILTHLNKEEKaTMMLVTHD 202
Cdd:PRK13638 174 QMIAIIRRIVAQGN-HVIISSHD 195
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
24-229 |
1.06e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 55.32 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 24 NINLTITEGEFVGIMGPSGSGKTTLLNMI-STIDSATSGSVFINSK-----NPYQ-------LSPNDlavfrRQELGFVF 90
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLfGAYPGRWEGEIFIDGKpvkirNPQQaiaqgiaMVPED-----RKRDGIVP 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 91 QsfnllhtLTVKENMVLPLVLDGMNVKRINK--------------RVESISKKLGISEIlnkrtyeiSGGQAQRTAIARA 156
Cdd:PRK13549 355 V-------MGVGKNITLAALDRFTGGSRIDDaaelktilesiqrlKVKTASPELAIARL--------SGGNQQKAVLAKC 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446629392 157 LIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDPVAASYCDRVIFIKDGQLYNEiFYNDN 229
Cdd:PRK13549 420 LLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLKGD-LINHN 491
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
13-219 |
1.18e-08 |
|
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: 53.10 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 13 YTGKVSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMIStidsATSGSVFINSknpyqlspnDLAVFRRQELGFVFQs 92
Cdd:cd03238 2 TVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL----YASGKARLIS---------FLPKFSRNKLIFIDQ- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 93 fnlLHTLTvkenmvlplvldgmnvkrinkrvesiskKLGISEI-LNKRTYEISGGQAQRTAIARALIHAPK--LVLADEP 169
Cdd:cd03238 68 ---LQFLI----------------------------DVGLGYLtLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446629392 170 TGNLDSKASQDVMEILTHLnKEEKATMMLVTHDPVAASYCDRVIFIKDGQ 219
Cdd:cd03238 117 STGLHQQDINQLLEVIKGL-IDLGNTVILIEHNLDVLSSADWIIDFGPGS 165
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
2-202 |
1.70e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.57 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 2 KIV-KVKDLSKEYTGKvshTALSNINLTITEGEFVGIMGPSGSGKTTLLN-MISTIdSATSGSVFINSKnpyqLspnDLA 79
Cdd:PRK11147 317 KIVfEMENVNYQIDGK---QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKlMLGQL-QADSGRIHCGTK----L---EVA 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 80 VF--RRQELGfvfqsfnllHTLTVKENmvlplVLDGMNVKRINKRVESIskkLG-ISEIL--NKRTYE----ISGGQAQR 150
Cdd:PRK11147 386 YFdqHRAELD---------PEKTVMDN-----LAEGKQEVMVNGRPRHV---LGyLQDFLfhPKRAMTpvkaLSGGERNR 448
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446629392 151 TAIARALIHAPKLVLADEPTGNLDSkasqDVMEILTHLNKEEKATMMLVTHD 202
Cdd:PRK11147 449 LLLARLFLKPSNLLILDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHD 496
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
21-221 |
2.04e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 54.21 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 21 ALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKnpyQLSPNDLAVFRRQeLGFVFQSFNLLHTLT 100
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK---PVTAEQPEDYRKL-FSAVFTDFHLFDQLL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 101 VKENMVLPlvldgmnvkriNKRVESISKKLGISEILNKRTYEI-----SGGQAQRTAIARALIHAPKLVLADEPTGNLDS 175
Cdd:PRK10522 414 GPEGKPAN-----------PALVEKWLERLKMAHKLELEDGRIsnlklSKGQKKRLALLLALAEERDILLLDEWAADQDP 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446629392 176 KASQDVMEILTHLNKEEKATMMLVTHDPVAASYCDRVIFIKDGQLY 221
Cdd:PRK10522 483 HFRREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLS 528
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-222 |
3.24e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.74 E-value: 3.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYTGKvshTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVfinsknpyQLSPNdlavfrr 83
Cdd:PRK15064 320 LEVENLTKGFDNG---PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV--------KWSEN------- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 84 QELGFVFQSfnllHTLTVKENMVLplvLDGMNVKRINKRVE-SISKKLG----ISEILNKRTYEISGGQAQRTAIARALI 158
Cdd:PRK15064 382 ANIGYYAQD----HAYDFENDLTL---FDWMSQWRQEGDDEqAVRGTLGrllfSQDDIKKSVKVLSGGEKGRMLFGKLMM 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446629392 159 HAPKLVLADEPTGNLDskasqdvMEILTHLN---KEEKATMMLVTHD-PVAASYCDRVIFIKDGQLYN 222
Cdd:PRK15064 455 QKPNVLVMDEPTNHMD-------MESIESLNmalEKYEGTLIFVSHDrEFVSSLATRIIEITPDGVVD 515
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
143-213 |
3.63e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.88 E-value: 3.63e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446629392 143 ISGGQAQRTAIARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDPVAASYCDRVI 213
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIV 1429
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
17-203 |
6.17e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 51.41 E-value: 6.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 17 VSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNpyqlsPNDLAvfrRQELGFVFQSFNLL 96
Cdd:PRK13541 11 IEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCN-----INNIA---KPYCTYIGHNLGLK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 97 HTLTVKENMVLplvldgmnVKRINKRVESISKKL---GISEILNKRTYEISGGQAQRTAIARALIHAPKLVLADEPTGNL 173
Cdd:PRK13541 83 LEMTVFENLKF--------WSEIYNSAETLYAAIhyfKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNL 154
|
170 180 190
....*....|....*....|....*....|
gi 446629392 174 dSKASQDVMEILTHLNKEEKATMMLVTHDP 203
Cdd:PRK13541 155 -SKENRDLLNNLIVMKANSGGIVLLSSHLE 183
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
112-201 |
1.09e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.17 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 112 DGMNVKRINKRVESISKKL-----------------GIS---EILNKRTYEISGGQAQRTAIARALIHAPKLVLADEPTG 171
Cdd:PLN03073 294 DGVDKDAVSQRLEEIYKRLelidaytaearaasilaGLSftpEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTN 373
|
90 100 110
....*....|....*....|....*....|
gi 446629392 172 NLDSKAsqdVMEILTHLNKEEKaTMMLVTH 201
Cdd:PLN03073 374 HLDLHA---VLWLETYLLKWPK-TFIVVSH 399
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
21-220 |
1.86e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 50.97 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 21 ALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSvfinsknpyqlspndlaVFRRQELGFVFQSFNLLHTLT 100
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGK-----------------VDRNGEVSVIAISAGLSGQLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 101 VKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIHAPKLVLADEPTGNLDSKASQD 180
Cdd:PRK13546 102 GIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446629392 181 VMEILTHLnKEEKATMMLVTHD-PVAASYCDRVIFIKDGQL 220
Cdd:PRK13546 182 CLDKIYEF-KEQNKTIFFVSHNlGQVRQFCTKIAWIEGGKL 221
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
3-201 |
1.87e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 50.56 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKEYTGKvshTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTID--SATSGSVFINSKNPYQLSPND--- 77
Cdd:PRK09580 1 MLSIKDLHVSVEDK---AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDrag 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 78 ----LAVFRRQELGFVFQSFNLLHTLTVKENMVLPLVLDGMNVKRInkrVESISKKLGISEILNKRTYEI--SGGQAQRT 151
Cdd:PRK09580 78 egifMAFQYPVEIPGVSNQFFLQTALNAVRSYRGQEPLDRFDFQDL---MEEKIALLKMPEDLLTRSVNVgfSGGEKKRN 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446629392 152 AIARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLnKEEKATMMLVTH 201
Cdd:PRK09580 155 DILQMAVLEPELCILDESDSGLDIDALKIVADGVNSL-RDGKRSFIIVTH 203
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
25-224 |
2.22e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 51.07 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 25 INLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSK-----NPYQ-------LSPNDlavfrRQELGFVfqs 92
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKpidirSPRDairagimLCPED-----RKAEGII--- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 93 fnllHTLTVKENMvlplvldGMNVKR--------INKRVESISKKLGISEiLNKRT-------YEISGGQAQRTAIARAL 157
Cdd:PRK11288 344 ----PVHSVADNI-------NISARRhhlragclINNRWEAENADRFIRS-LNIKTpsreqliMNLSGGNQQKAILGRWL 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446629392 158 IHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDPVAASYCDRVIFIKDGQLYNEI 224
Cdd:PRK11288 412 SEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGEL 478
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
3-220 |
2.47e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.88 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 3 IVKVKDLSKeytgkVSHTALSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPND----- 77
Cdd:PRK10982 250 ILEVRNLTS-----LRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEainhg 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 78 --LAVFRRQELGFV------FQS-----------FNLLHTLTVKENMvlPLVLDGMNVKrinkrveSISKKLGISEIlnk 138
Cdd:PRK10982 325 faLVTEERRSTGIYayldigFNSlisnirnyknkVGLLDNSRMKSDT--QWVIDSMRVK-------TPGHRTQIGSL--- 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 139 rtyeiSGGQAQRTAIARALIHAPKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDPVAASYCDRVIFIKDG 218
Cdd:PRK10982 393 -----SGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG 467
|
..
gi 446629392 219 QL 220
Cdd:PRK10982 468 LV 469
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
25-220 |
2.63e-07 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 50.95 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 25 INLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKnpyQLSPNDLAVFRRQelgF--VFQSFNLLHTLTVK 102
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQ---PVTADNREAYRQL---FsaVFSDFHLFDRLLGL 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 103 ENMVLPlvldgmnvkrinKRVESISKKLGISEIL---NKR--TYEISGGQAQRTaiarALIHA-----PKLVLaDEPTgn 172
Cdd:COG4615 425 DGEADP------------ARARELLERLELDHKVsveDGRfsTTDLSQGQRKRL----ALLVAlledrPILVF-DEWA-- 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446629392 173 ldskASQD-------VMEILTHLNKEEKaTMMLVTHDPVAASYCDRVIFIKDGQL 220
Cdd:COG4615 486 ----ADQDpefrrvfYTELLPELKARGK-TVIAISHDDRYFDLADRVLKMDYGKL 535
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-218 |
5.70e-07 |
|
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: 47.75 E-value: 5.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 32 GEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFInsknpyqLSPNDLAVFRRQELGFVfqsfnllhtltvkenmvlplvl 111
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY-------IDGEDILEEVLDQLLLI---------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 112 dgmnvkrinkrvesiskklgiseILNKRTYEISGGQAQRTAIARALIHAPKLVLADEPTGNLDSKASQDVMEI-----LT 186
Cdd:smart00382 53 -----------------------IVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLL 109
|
170 180 190
....*....|....*....|....*....|....*...
gi 446629392 187 HLNKEEKATMMLVTHDP------VAASYCDRVIFIKDG 218
Cdd:smart00382 110 LLKSEKNLTVILTTNDEkdlgpaLLRRRFDRRIVLLLI 147
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-220 |
1.09e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 49.35 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 22 LSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLavfrRQELGFVFQSfNLLHTLTV 101
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDL----RKVLGIIPQA-PVLFSGTV 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 102 KENmvlplvLDGMNVKRINKRVESISK----------KLGISEILNKRTYEISGGQAQRTAIARALIHAPKLVLADEPTG 171
Cdd:PLN03130 1330 RFN------LDPFNEHNDADLWESLERahlkdvirrnSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATA 1403
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446629392 172 NLDSKAsqDVMeILTHLNKEEKA-TMMLVTHDPVAASYCDRVIFIKDGQL 220
Cdd:PLN03130 1404 AVDVRT--DAL-IQKTIREEFKScTMLIIAHRLNTIIDCDRILVLDAGRV 1450
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-220 |
1.85e-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: 48.79 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 22 LSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFInsknpyqlspndlavfrRQELGFVFQSfNLLHTLTV 101
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM-----------------KGSVAYVPQQ-AWIQNDSL 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 102 KENMVLPLVLdgmNVKRINKRVESISKkLGISEIL--------NKRTYEISGGQAQRTAIARALIHAPKLVLADEPTGNL 173
Cdd:TIGR00957 716 RENILFGKAL---NEKYYQQVLEACAL-LPDLEILpsgdrteiGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAV 791
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446629392 174 DSKASQDVME-ILTHLNKEEKATMMLVTHDPVAASYCDRVIFIKDGQL 220
Cdd:TIGR00957 792 DAHVGKHIFEhVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKI 839
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
22-213 |
2.26e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 47.25 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 22 LSNINLTITEGEFVGIMGPSGSGKTTLlnMISTIdSATSGSVFINSKNPYQ-----------------LSP------NDL 78
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSL--AFDTI-YAEGQRRYVESLSAYArqflgqmdkpdvdsiegLSPaiaidqKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 79 AVFRRQELGFVFQSFNLLHTLTVKENmvlplvldgmnvkrINKRVESIsKKLGISEI-LNKRTYEISGGQAQRTAIARAL 157
Cdd:cd03270 88 SRNPRSTVGTVTEIYDYLRLLFARVG--------------IRERLGFL-VDVGLGYLtLSRSAPTLSGGEAQRIRLATQI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 158 ihAPKLV----LADEPTGNLDSKASQDVMEILTHLnKEEKATMMLVTHDPVAASYCDRVI 213
Cdd:cd03270 153 --GSGLTgvlyVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDTIRAADHVI 209
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-174 |
4.56e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 47.63 E-value: 4.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 22 LSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKNPYQLSPNDLavfrRQELGFVFQSfNLLHTLTV 101
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDL----RFKITIIPQD-PVLFSGSL 1376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 102 KENMVlPL-------VLDGMNVKRINKRVESISKKlgiseiLNKRTYE----ISGGQAQRTAIARALIHAPKLVLADEPT 170
Cdd:TIGR00957 1377 RMNLD-PFsqysdeeVWWALELAHLKTFVSALPDK------LDHECAEggenLSVGQRQLVCLARALLRKTKILVLDEAT 1449
|
....
gi 446629392 171 GNLD 174
Cdd:TIGR00957 1450 AAVD 1453
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
22-220 |
4.82e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.47 E-value: 4.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 22 LSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFInsknpyqlspndlavfrRQELGFVFQSFNLLHTlTV 101
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWA-----------------ERSIAYVPQQAWIMNA-TV 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 102 KENMvlpLVLDGMNVKRINK--RVESISKKL-----GISEILNKRTYEISGGQAQRTAIARALIHAPKLVLADEPTGNLD 174
Cdd:PTZ00243 738 RGNI---LFFDEEDAARLADavRVSQLEADLaqlggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446629392 175 SKASQDVME--ILTHLNKEekaTMMLVTHDPVAASYCDRVIFIKDGQL 220
Cdd:PTZ00243 815 AHVGERVVEecFLGALAGK---TRVLATHQVHVVPRADYVVALGDGRV 859
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
110-218 |
1.25e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.36 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 110 VLDGMNvKRInkrveSISKKLGISEILNKRTYE-ISGGQAQRTAIARAL---IHAPKLVLaDEPTGNLDSKASQDVMEIL 185
Cdd:PRK00635 449 VLQGLK-SRL-----SILIDLGLPYLTPERALAtLSGGEQERTALAKHLgaeLIGITYIL-DEPSIGLHPQDTHKLINVI 521
|
90 100 110
....*....|....*....|....*....|...
gi 446629392 186 THLnKEEKATMMLVTHDPVAASYCDRVIFIKDG 218
Cdd:PRK00635 522 KKL-RDQGNTVLLVEHDEQMISLADRIIDIGPG 553
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
22-203 |
2.84e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 43.12 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 22 LSNINLTITEGEFVGIMGPSGSGKTTLLNMISTIdsatsgsVFINSKNPYQLSPNDLAVFR-RQELGFVFqsfnLLHTLt 100
Cdd:cd03227 11 FVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLA-------LGGAQSATRRRSGVKAGCIVaAVSAELIF----TRLQL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 101 vkenmvlplvldgmnvkrinkrvesiskklgiseilnkrtyeiSGGQAQRTAIARALIHAPK----LVLADEPTGNLDSK 176
Cdd:cd03227 79 -------------------------------------------SGGEKELSALALILALASLkprpLYILDEIDRGLDPR 115
|
170 180
....*....|....*....|....*..
gi 446629392 177 ASQDVMEILTHLNKeEKATMMLVTHDP 203
Cdd:cd03227 116 DGQALAEAILEHLV-KGAQVIVITHLP 141
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
4-201 |
2.94e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 44.73 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYtGKVShtALSNINLTITEGEFVGIMGPSGSG--KTTLLNMISTIDSAtsgsvfinsKNPYQLSP--NDLA 79
Cdd:NF000106 14 VEVRGLVKHF-GEVK--AVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAG---------RRPWRF*TwcANRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 80 VFRRQELGFVFQSFNLLHTLTVKENMVLPLVLDGMNVKRINKRVESISKKLGISEILNKRTYEISGGQAQRTAIARALIH 159
Cdd:NF000106 82 ALRRTIG*HRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446629392 160 APKLVLADEPTGNLDSKASQDVMEILTHLNKeEKATMMLVTH 201
Cdd:NF000106 162 RPAVLYLDEPTTGLDPRTRNEVWDEVRSMVR-DGATVLLTTQ 202
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
27-53 |
6.15e-05 |
|
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.
Pssm-ID: 410880 [Multi-domain] Cd Length: 265 Bit Score: 43.32 E-value: 6.15e-05
10 20
....*....|....*....|....*..
gi 446629392 27 LTITEGEFVGIMGPSGSGKTTLLNMIS 53
Cdd:cd01136 62 LTCGEGQRIGIFAGSGVGKSTLLGMIA 88
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
4-220 |
9.41e-05 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 42.59 E-value: 9.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 4 VKVKDLSKEYTGKVShTALSNINLTITEGEFVGIMGPSGSGKTTL----LNMISTIDsatsGSVFIN----SKNPYQLSP 75
Cdd:cd03288 20 IKIHDLCVRYENNLK-PVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDgidiSKLPLHTLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 76 NDLAVFRRQELGFVFQ-SFNLLHTLTVKENMvlplVLDGMNVKRINKRVESISKklGISEILNKRTYEISGGQAQRTAIA 154
Cdd:cd03288 95 SRLSIILQDPILFSGSiRFNLDPECKCTDDR----LWEALEIAQLKNMVKSLPG--GLDAVVTEGGENFSVGQRQLFCLA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446629392 155 RALIHAPKLVLADEPTGNLDsKASQDVME--ILTHLNKEEKATMMLVTHDPVAAsycDRVIFIKDGQL 220
Cdd:cd03288 169 RAFVRKSSILIMDEATASID-MATENILQkvVMTAFADRTVVTIAHRVSTILDA---DLVLVLSRGIL 232
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
24-224 |
1.07e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.85 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 24 NINLTITEGEFVGIMGPSGSGKTTLlnMIS----TIDSATSGSVFINSKnPYQLSPNDLAVFR--------RQELGfvfq 91
Cdd:NF040905 278 DVSLNVRRGEIVGIAGLMGAGRTEL--AMSvfgrSYGRNISGTVFKDGK-EVDVSTVSDAIDAglayvtedRKGYG---- 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 92 sFNLLHtlTVKENMVLPlvldgmNVKRINKR-----------VESISKKLGI-SEILNKRTYEISGGQAQRTAIARALIH 159
Cdd:NF040905 351 -LNLID--DIKRNITLA------NLGKVSRRgvideneeikvAEEYRKKMNIkTPSVFQKVGNLSGGNQQKVVLSKWLFT 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446629392 160 APKLVLADEPTGNLDSKASQDVMEILTHLNKEEKATMMLVTHDPVAASYCDRVIFIKDGQLYNEI 224
Cdd:NF040905 422 DPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRITGEL 486
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
25-203 |
1.16e-04 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 43.20 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 25 INLTITEGEFVGIMGPSGSGKTTLLNMISTIDSATSGSVFINSKN--------PY--------QL----SPNDLAV--FR 82
Cdd:TIGR00954 471 LSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGklfyvpqrPYmtlgtlrdQIiypdSSEDMKRrgLS 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 83 RQELGFVFQSFNLLHTLtvKENMVLPLVLDGMNVkrinkrvesiskklgiseilnkrtyeISGGQAQRTAIARALIHAPK 162
Cdd:TIGR00954 551 DKDLEQILDNVQLTHIL--EREGGWSAVQDWMDV--------------------------LSGGEKQRIAMARLFYHKPQ 602
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446629392 163 LVLADEPTgnldSKASQDVMEILTHLNKEEKATMMLVTHDP 203
Cdd:TIGR00954 603 FAILDECT----SAVSVDVEGYMYRLCREFGITLFSVSHRK 639
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
22-52 |
1.17e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 43.14 E-value: 1.17e-04
10 20 30
....*....|....*....|....*....|.
gi 446629392 22 LSNINLTITEGEFVGIMGPSGSGKTTLLNMI 52
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLINET 655
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
22-52 |
1.80e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 42.69 E-value: 1.80e-04
10 20 30
....*....|....*....|....*....|.
gi 446629392 22 LSNINLTITEGEFVGIMGPSGSGKTTLLNMI 52
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLINDT 654
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
22-50 |
3.58e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 41.06 E-value: 3.58e-04
10 20
....*....|....*....|....*....
gi 446629392 22 LSNINLTITEGEFVGIMGPSGSGKTTLLN 50
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIN 39
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
25-52 |
9.25e-04 |
|
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440771 [Multi-domain] Cd Length: 433 Bit Score: 40.01 E-value: 9.25e-04
10 20 30
....*....|....*....|....*....|
gi 446629392 25 IN--LTITEGEFVGIMGPSGSGKTTLLNMI 52
Cdd:COG1157 148 IDglLTVGRGQRIGIFAGSGVGKSTLLGMI 177
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
37-216 |
1.15e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 39.13 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 37 IMGPSGSGKTTLLNMISTidsATSGSVFINSKnpyqLSPNDLAVFRRQE-LGFVFQSFnllhTLTVKENMVLplvldgmn 115
Cdd:cd03240 27 IVGQNGAGKTTIIEALKY---ALTGELPPNSK----GGAHDPKLIREGEvRAQVKLAF----ENANGKKYTI-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 116 VKRINKRVESI------SKKLgiseILNKRTYeISGGQ------AQRTAIARAL-IHAPKLVLaDEPTGNLDS-KASQDV 181
Cdd:cd03240 88 TRSLAILENVIfchqgeSNWP----LLDMRGR-CSGGEkvlaslIIRLALAETFgSNCGILAL-DEPTTNLDEeNIEESL 161
|
170 180 190
....*....|....*....|....*....|....*
gi 446629392 182 MEILTHLNKEEKATMMLVTHDPVAASYCDRVIFIK 216
Cdd:cd03240 162 AEIIEERKSQKNFQLIVITHDEELVDAADHIYRVE 196
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
27-53 |
2.00e-03 |
|
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho.
Pssm-ID: 425417 [Multi-domain] Cd Length: 212 Bit Score: 38.49 E-value: 2.00e-03
10 20
....*....|....*....|....*..
gi 446629392 27 LTITEGEFVGIMGPSGSGKTTLLNMIS 53
Cdd:pfam00006 9 LPIGRGQRIGIFGGSGVGKTVLAGMIA 35
|
|
| UMPK_like |
cd02028 |
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the ... |
34-77 |
2.39e-03 |
|
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or uridine-cytidine kinase (UCK).
Pssm-ID: 238986 [Multi-domain] Cd Length: 179 Bit Score: 37.67 E-value: 2.39e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 446629392 34 FVGIMGPSGSGKTTLLNMISTIdsatsgsVFINSKNPYQLSPND 77
Cdd:cd02028 1 VVGIAGPSGSGKTTFAKKLSNQ-------LRVNGIGPVVISLDD 37
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
136-218 |
3.23e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.46 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446629392 136 LNKRTYEISGGQAQRTAIARALIHAPKLVL--ADEPTGNLDSKASQDVMEILTHLnKEEKATMMLVTHDPVAASYCDRVI 213
Cdd:TIGR00630 482 LSRAAGTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHDEDTIRAADYVI 560
|
....*
gi 446629392 214 FIKDG 218
Cdd:TIGR00630 561 DIGPG 565
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
22-48 |
3.76e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.47 E-value: 3.76e-03
10 20
....*....|....*....|....*..
gi 446629392 22 LSNINLTITEGEFVGIMGPSGSGKTTL 48
Cdd:COG0178 16 LKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
22-52 |
6.14e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 37.70 E-value: 6.14e-03
10 20 30
....*....|....*....|....*....|.
gi 446629392 22 LSNINLTITEGEFVGIMGPSGSGKTTLLNMI 52
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKSTLVNDI 651
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
21-87 |
6.36e-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: 37.07 E-value: 6.36e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446629392 21 ALSNINLTITEGE-FVGIMGPSGSGKTTLLNM-ISTIDSATSGSVFINSknpyQLSPNDL--AVFrrQELG 87
Cdd:COG3267 31 ALARLEYALAQGGgFVVLTGEVGTGKTTLLRRlLERLPDDVKVAYIPNP----QLSPAELlrAIA--DELG 95
|
|
| |
