|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
21-243 |
1.02e-123 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 350.88 E-value: 1.02e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 21 VVEAVEVKKYYKMGKFIVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAWL 100
Cdd:COG1136 4 LLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 101 RAKKIGYIFQTFNLIPVLTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDP 180
Cdd:COG1136 84 RRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502908369 181 SIILADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMVDVSDRIIWIRDGKIEKIE 243
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVSDE 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
22-239 |
4.12e-118 |
|
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: 336.38 E-value: 4.12e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 22 VEAVEVKKYYKMGKFIVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAWLR 101
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 102 AKKIGYIFQTFNLIPVLTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPS 181
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502908369 182 IILADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMVDVSDRIIWIRDGKI 239
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
21-240 |
1.18e-89 |
|
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: 264.68 E-value: 1.18e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 21 VVEAVEVKKYYKMGKFIVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAWL 100
Cdd:COG4181 8 IIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 101 RAKKIGYIFQTFNLIPVLTAVENVMLPMIFVGTPyeDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDP 180
Cdd:COG4181 88 RARHVGFVFQSFQLLPTLTALENVMLPLELAGRR--DARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 181 SIILADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMVDVSDRIIWIRDGKIE 240
Cdd:COG4181 166 AILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRLV 225
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
21-239 |
1.02e-83 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 249.20 E-value: 1.02e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 21 VVEAVEVKKYYKMGKfivKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAWL 100
Cdd:COG2884 1 MIRFENVSKRYPGGR---EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 101 RaKKIGYIFQTFNLIPVLTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDP 180
Cdd:COG2884 78 R-RRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 181 SIILADEPTGNLDLHTGLKLINLLKEINeKKGVTIVTATHDLKMVD-VSDRIIWIRDGKI 239
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEIN-RRGTTVLIATHDLELVDrMPKRVLELEDGRL 215
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
21-239 |
2.11e-75 |
|
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: 228.39 E-value: 2.11e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 21 VVEAVEVKKYYKMGKFIVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAWL 100
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 101 RAKKIGYIFQTFNLIPVLTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDP 180
Cdd:TIGR02211 81 RNKKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502908369 181 SIILADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMVDVSDRIIWIRDGKI 239
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDGQL 219
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
27-239 |
4.13e-72 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 223.80 E-value: 4.13e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 27 VKKYYKMGKFIVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAWLRaKKIG 106
Cdd:COG1135 7 LSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAR-RKIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 107 YIFQTFNLIPVLTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILAD 186
Cdd:COG1135 86 MIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502908369 187 EPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMV-DVSDRIIWIRDGKI 239
Cdd:COG1135 166 EATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVrRICDRVAVLENGRI 219
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
22-242 |
5.33e-72 |
|
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: 219.65 E-value: 5.33e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 22 VEAVEVKKYYKMGKFIVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAyelawlr 101
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 102 akKIGYIFQTFNLIPVLTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPS 181
Cdd:cd03293 74 --DRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502908369 182 IILADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDL-KMVDVSDRIIWI--RDGKIEKI 242
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIdEAVFLADRVVVLsaRPGRIVAE 215
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
21-232 |
7.60e-72 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 220.35 E-value: 7.60e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 21 VVEAVEVKKYYKMGKFIVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAyelawl 100
Cdd:COG1116 7 ALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 101 rakKIGYIFQTFNLIPVLTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDP 180
Cdd:COG1116 81 ---DRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502908369 181 SIILADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDlkmVD----VSDRII 232
Cdd:COG1116 158 EVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHD---VDeavfLADRVV 210
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
38-239 |
1.73e-70 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 216.46 E-value: 1.73e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 38 VKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAWLRAKkIGYIFQTFNLIPV 117
Cdd:COG3638 16 TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRRR-IGMIFQQFNLVPR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 118 LTAVENVM---LPMI-----FVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPT 189
Cdd:COG3638 95 LSVLTNVLagrLGRTstwrsLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARALVQEPKLILADEPV 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502908369 190 GNLDLHTGLKLINLLKEINEKKGVTIVTATHDlkmVDV----SDRIIWIRDGKI 239
Cdd:COG3638 175 ASLDPKTARQVMDLLRRIAREDGITVVVNLHQ---VDLarryADRIIGLRDGRV 225
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
21-241 |
2.98e-69 |
|
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: 212.83 E-value: 2.98e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 21 VVEAVEVKKYYKMGKFIVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAWL 100
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 101 RaKKIGYIFQTFNLIPVLTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDP 180
Cdd:cd03258 81 R-RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502908369 181 SIILADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMV-DVSDRIIWIRDGKIEK 241
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVkRICDRVAVMEKGEVVE 221
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
21-239 |
5.16e-69 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 212.55 E-value: 5.16e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 21 VVEAVEVKKYYkmGKFIVkaLDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAmLDAYELAWL 100
Cdd:COG1126 1 MIEIENLHKSF--GDLEV--LKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 101 RaKKIGYIFQTFNLIPVLTAVENVMLPMIFV-GTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALAND 179
Cdd:COG1126 76 R-RKVGMVFQQFNLFPHLTVLENVTLAPIKVkKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502908369 180 PSIILADEPTGNLD--LhTG--LKLINLLKeineKKGVTIVTATHDLKMV-DVSDRIIWIRDGKI 239
Cdd:COG1126 155 PKVMLFDEPTSALDpeL-VGevLDVMRDLA----KEGMTMVVVTHEMGFArEVADRVVFMDGGRI 214
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
21-238 |
1.67e-68 |
|
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: 210.57 E-value: 1.67e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 21 VVEAVEVKKYYKMGkfiVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAWL 100
Cdd:TIGR02673 1 MIEFHNVSKAYPGG---VAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 101 RaKKIGYIFQTFNLIPVLTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDP 180
Cdd:TIGR02673 78 R-RRIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502908369 181 SIILADEPTGNLDLHTGLKLINLLKEINeKKGVTIVTATHDLKMVD-VSDRIIWIRDGK 238
Cdd:TIGR02673 157 PLLLADEPTGNLDPDLSERILDLLKRLN-KRGTTVIVATHDLSLVDrVAHRVIILDDGR 214
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
22-240 |
6.68e-68 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 213.42 E-value: 6.68e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 22 VEAVEVKKYYkmGKFivKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYElawlR 101
Cdd:COG3842 6 LELENVSKRY--GDV--TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK----R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 102 akKIGYIFQTFNLIPVLTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPS 181
Cdd:COG3842 78 --NVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502908369 182 IILADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLK--MVdVSDRIIWIRDGKIE 240
Cdd:COG3842 156 VLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEeaLA-LADRIAVMNDGRIE 215
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
22-239 |
3.87e-67 |
|
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: 206.88 E-value: 3.87e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 22 VEAVEVKKYYKMGkfiVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAWLR 101
Cdd:cd03292 1 IEFINVTKTYPNG---TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 102 aKKIGYIFQTFNLIPVLTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPS 181
Cdd:cd03292 78 -RKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502908369 182 IILADEPTGNLDLHTGLKLINLLKEINeKKGVTIVTATHDLKMVD-VSDRIIWIRDGKI 239
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKIN-KAGTTVVVATHAKELVDtTRHRVIALERGKL 214
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
21-239 |
7.28e-67 |
|
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: 206.59 E-value: 7.28e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 21 VVEAVEVKKYYKMGKFIVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAWL 100
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 101 RaKKIGYIFQ----TFNliPVLTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLG---KFIHHKPAELSGGQQQRVAAA 173
Cdd:cd03257 81 R-KEIQMVFQdpmsSLN--PRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGlpeEVLNRYPHELSGGQRQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502908369 174 RALANDPSIILADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMV-DVSDRIIWIRDGKI 239
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVaKIADRVAVMYAGKI 224
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
19-239 |
9.97e-66 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 203.86 E-value: 9.97e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 19 EYVVEAVEVKKYYKMGKFIVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELA 98
Cdd:PRK10584 4 ENIVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 99 WLRAKKIGYIFQTFNLIPVLTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALAN 178
Cdd:PRK10584 84 KLRAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502908369 179 DPSIILADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMVDVSDRIIWIRDGKI 239
Cdd:PRK10584 164 RPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
27-239 |
1.01e-65 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 203.41 E-value: 1.01e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 27 VKKYYKMGKFIVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAWLRAKKIG 106
Cdd:NF038007 7 AEKCYITKTIKTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIILRRELIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 107 YIFQTFNLIPVLTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILAD 186
Cdd:NF038007 87 YIFQSFNLIPHLSIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLAD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502908369 187 EPTGNLDLHTGLKLINLLKEINeKKGVTIVTATHDLKMVDVSDRIIWIRDGKI 239
Cdd:NF038007 167 EPTGNLDSKNARAVLQQLKYIN-QKGTTIIMVTHSDEASTYGNRIINMKDGKL 218
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
29-240 |
1.11e-65 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 203.89 E-value: 1.11e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 29 KYYKMGKFIVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAWLRAKKIGYI 108
Cdd:PRK11629 13 KRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKLGFI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 109 FQTFNLIPVLTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEP 188
Cdd:PRK11629 93 YQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502908369 189 TGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMVDVSDRIIWIRDGKIE 240
Cdd:PRK11629 173 TGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLT 224
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
38-242 |
2.59e-65 |
|
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: 202.36 E-value: 2.59e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 38 VKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYElawlraKKIGYIFQTFNLIPV 117
Cdd:cd03259 13 VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER------RNIGMVFQDYALFPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 118 LTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLHTG 197
Cdd:cd03259 87 LTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 502908369 198 LKLINLLKEINEKKGVTIVTATHDL-KMVDVSDRIIWIRDGKIEKI 242
Cdd:cd03259 167 EELREELKELQRELGITTIYVTHDQeEALALADRIAVMNEGRIVQV 212
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
27-239 |
2.92e-65 |
|
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: 203.18 E-value: 2.92e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 27 VKKYYKMGKfivKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAWLRaKKIG 106
Cdd:cd03256 6 LSKTYPNGK---KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR-RQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 107 YIFQTFNLIPVLTAVENVMLPMI--------FVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALAN 178
Cdd:cd03256 82 MIFQQFNLIERLSVLENVLSGRLgrrstwrsLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502908369 179 DPSIILADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMV-DVSDRIIWIRDGKI 239
Cdd:cd03256 162 QPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLArEYADRIVGLKDGRI 223
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
7-239 |
1.09e-64 |
|
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: 209.76 E-value: 1.09e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 7 AKNVKLPSRRKLEYVVEAVEVKKYYKM-GKFIVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYID 85
Cdd:COG1123 246 ARGRAAPAAAAAEPLLEVRNLSKRYPVrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFD 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 86 GVDIAMLDAYELAWLRaKKIGYIFQtfN----LIPVLTAVENVMLPMIFVGT-PYEDAIVKAKKLLELVGLG-KFIHHKP 159
Cdd:COG1123 326 GKDLTKLSRRSLRELR-RRVQMVFQ--DpyssLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPpDLADRYP 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 160 AELSGGQQQRVAAARALANDPSIILADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMVD-VSDRIIWIRDGK 238
Cdd:COG1123 403 HELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRyIADRVAVMYDGR 482
|
.
gi 502908369 239 I 239
Cdd:COG1123 483 I 483
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
21-239 |
1.12e-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: 198.32 E-value: 1.12e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 21 VVEAVEVKKYYKMGKFIVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAWL 100
Cdd:TIGR02982 1 VISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 101 RaKKIGYIFQTFNLIPVLTAVENVMLPM-IFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALAND 179
Cdd:TIGR02982 81 R-RRIGYIFQAHNLLGFLTARQNVQMALeLQPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHH 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 180 PSIILADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMVDVSDRIIWIRDGKI 239
Cdd:TIGR02982 160 PKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRILDVADRILQMEDGKL 219
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
19-239 |
3.15e-63 |
|
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: 197.89 E-value: 3.15e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 19 EYVVEAVEVKKYYkmGKFIVkaLDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELA 98
Cdd:COG1127 3 EPMIEVRNLTKSF--GDRVV--LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 99 WLRaKKIGYIFQTFNLIPVLTAVENVMLPMI-FVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALA 177
Cdd:COG1127 79 ELR-RRIGMLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502908369 178 NDPSIILADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMV-DVSDRIIWIRDGKI 239
Cdd:COG1127 158 LDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAfAIADRVAVLADGKI 220
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
27-239 |
1.16e-62 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 207.27 E-value: 1.16e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 27 VKKYYKMGKFIVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAWLRAKKIG 106
Cdd:PRK10535 10 IRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRREHFG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 107 YIFQTFNLIPVLTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILAD 186
Cdd:PRK10535 90 FIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILAD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502908369 187 EPTGNLDLHTGLKLINLLKEINEkKGVTIVTATHDLKMVDVSDRIIWIRDGKI 239
Cdd:PRK10535 170 EPTGALDSHSGEEVMAILHQLRD-RGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
22-239 |
3.45e-62 |
|
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: 194.29 E-value: 3.45e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 22 VEAVEVKKYYkmGKFIVkaLDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAmLDAYELAWLR 101
Cdd:cd03262 1 IEIKNLHKSF--GDFHV--LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLT-DDKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 102 aKKIGYIFQTFNLIPVLTAVENVMLPMIFV-GTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDP 180
Cdd:cd03262 76 -QKVGMVFQQFNLFPHLTVLENITLAPIKVkGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 181 SIILADEPTGNLDLHTGLKLINLLKEInEKKGVTIVTATHDLKMV-DVSDRIIWIRDGKI 239
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDL-AEEGMTMVVVTHEMGFArEVADRVIFMDDGRI 213
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
27-239 |
2.19e-60 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 193.86 E-value: 2.19e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 27 VKKYYKMGKFIVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAWLRaKKIG 106
Cdd:PRK11153 7 ISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAR-RQIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 107 YIFQTFNLIPVLTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILAD 186
Cdd:PRK11153 86 MIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502908369 187 EPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMV-DVSDRIIWIRDGKI 239
Cdd:PRK11153 166 EATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVkRICDRVAVIDAGRL 219
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
22-248 |
3.01e-60 |
|
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: 190.14 E-value: 3.01e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 22 VEAVEVKKYYkmGKFIvkALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYElawlr 101
Cdd:cd03300 1 IELENVSKFY--GGFV--ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 102 aKKIGYIFQTFNLIPVLTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPS 181
Cdd:cd03300 72 -RPVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502908369 182 IILADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHD----LKMvdvSDRIIWIRDGKIEKIELRRDI 248
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDqeeaLTM---SDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
27-239 |
1.04e-59 |
|
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: 189.05 E-value: 1.04e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 27 VKKYYKMGKfivKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAWLRaKKIG 106
Cdd:TIGR02315 7 LSKVYPNGK---QALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLR-RRIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 107 YIFQTFNLIPVLTAVENVM---------LPMIFVGTPYEDaIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALA 177
Cdd:TIGR02315 83 MIFQHYNLIERLTVLENVLhgrlgykptWRSLLGRFSEED-KERALSALERVGLADKAYQRADQLSGGQQQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502908369 178 NDPSIILADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMV-DVSDRIIWIRDGKI 239
Cdd:TIGR02315 162 QQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAkKYADRIVGLKAGEI 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
40-242 |
1.37e-59 |
|
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: 189.39 E-value: 1.37e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 40 ALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAWLRAKKIGYIFQTFNLIPVLT 119
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 120 AVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLHTGLK 199
Cdd:cd03294 119 VLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRRE 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 502908369 200 LINLLKEINEKKGVTIVTATHDL-KMVDVSDRIIWIRDGKIEKI 242
Cdd:cd03294 199 MQDELLRLQAELQKTIVFITHDLdEALRLGDRIAIMKDGRLVQV 242
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
31-238 |
1.97e-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: 187.29 E-value: 1.97e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 31 YKMGKFIVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAwlraKKIGYIFQ 110
Cdd:cd03225 7 FSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELR----RKVGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 111 -----TFNLipvlTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILA 185
Cdd:cd03225 83 npddqFFGP----TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502908369 186 DEPTGNLDLHTGLKLINLLKEINEkKGVTIVTATHDLKMV-DVSDRIIWIRDGK 238
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKA-EGKTIIIVTHDLDLLlELADRVIVLEDGK 211
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
38-238 |
2.97e-59 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 185.47 E-value: 2.97e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 38 VKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAwlRAKKIGYIFQTFNLIPV 117
Cdd:cd03229 13 KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPP--LRRRIGMVFQDFALFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 118 LTAVENVMLPmifvgtpyedaivkakkllelvglgkfihhkpaeLSGGQQQRVAAARALANDPSIILADEPTGNLDLHTG 197
Cdd:cd03229 91 LTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITR 136
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 502908369 198 LKLINLLKEINEKKGVTIVTATHDLKMVD-VSDRIIWIRDGK 238
Cdd:cd03229 137 REVRALLKSLQAQLGITVVLVTHDLDEAArLADRVVVLRDGK 178
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
38-239 |
3.56e-59 |
|
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: 187.15 E-value: 3.56e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 38 VKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAwlraKKIGYIFQT-----F 112
Cdd:COG1122 14 TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELR----RKVGLVFQNpddqlF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 113 NLipvlTAVENVML-PMIFvGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGN 191
Cdd:COG1122 90 AP----TVEEDVAFgPENL-GLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAG 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502908369 192 LDLHTGLKLINLLKEINeKKGVTIVTATHDLKMV-DVSDRIIWIRDGKI 239
Cdd:COG1122 165 LDPRGRRELLELLKRLN-KEGKTVIIVTHDLDLVaELADRVIVLDDGRI 212
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
22-250 |
1.11e-58 |
|
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: 186.55 E-value: 1.11e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 22 VEAVEVKKYYKMGKFIVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAmldayeLAWLR 101
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVT------RRRRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 102 A--KKIGYIFQ----TFNliPVLTAVENVMLPMIFVGTPYEDAIVKakKLLELVGLGK-FIHHKPAELSGGQQQRVAAAR 174
Cdd:COG1124 76 AfrRRVQMVFQdpyaSLH--PRHTVDRILAEPLRIHGLPDREERIA--ELLEQVGLPPsFLDRYPHQLSGGQRQRVAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502908369 175 ALANDPSIILADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMVD-VSDRIIWIRDGKIEKIELRRDIEA 250
Cdd:COG1124 152 ALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAhLCDRVAVMQNGRIVEELTVADLLA 228
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
39-234 |
6.45e-58 |
|
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: 183.20 E-value: 6.45e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 39 KALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAWLRAKKIGYIFQTFNLIPVL 118
Cdd:TIGR03608 12 VILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREKLGYLFQNFALIENE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 119 TAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLHTGL 198
Cdd:TIGR03608 92 TVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDPKNRD 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 502908369 199 KLINLLKEINeKKGVTIVTATHDLKMVDVSDRIIWI 234
Cdd:TIGR03608 172 EVLDLLLELN-DEGKTIIIVTHDPEVAKQADRVIEL 206
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
22-239 |
1.45e-56 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 180.64 E-value: 1.45e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 22 VEAVEVKKYYkmGKFivKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAmldAYELAWLR 101
Cdd:COG1131 1 IEVRGLTKRY--GDK--TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA---RDPAEVRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 102 akKIGYIFQTFNLIPVLTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPS 181
Cdd:COG1131 74 --RIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502908369 182 IILADEPTGNLDLHTGLKLINLLKEINEkKGVTIVTATHDLKMVD-VSDRIIWIRDGKI 239
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELAA-EGKTVLLSTHYLEEAErLCDRVAIIDKGRI 209
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
21-232 |
1.69e-56 |
|
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: 182.95 E-value: 1.69e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 21 VVEAVEVKKYYKMGKFIVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRP---TGGKVYIDGVDIAMLDAYEL 97
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 98 AWLRAKKIGYIFQ----TFNliPVLTAVENVMLPM-IFVGTPYEDAIVKAKKLLELVGL---GKFIHHKPAELSGGQQQR 169
Cdd:COG0444 81 RKIRGREIQMIFQdpmtSLN--PVMTVGDQIAEPLrIHGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502908369 170 VAAARALANDPSIILADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMV-DVSDRII 232
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVaEIADRVA 222
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
25-240 |
1.80e-56 |
|
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: 180.39 E-value: 1.80e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 25 VEVKKYYK-MGKFIVkaLDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAWLRaK 103
Cdd:cd03261 1 IELRGLTKsFGGRTV--LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR-R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 104 KIGYIFQTFNLIPVLTAVENVMLPMifvgtpYE---------DAIVKAKklLELVGLGKFIHHKPAELSGGQQQRVAAAR 174
Cdd:cd03261 78 RMGMLFQSGALFDSLTVFENVAFPL------REhtrlseeeiREIVLEK--LEAVGLRGAEDLYPAELSGGMKKRVALAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502908369 175 ALANDPSIILADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMV-DVSDRIIWIRDGKIE 240
Cdd:cd03261 150 ALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAfAIADRIAVLYDGKIV 216
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
27-248 |
5.84e-56 |
|
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: 179.42 E-value: 5.84e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 27 VKKYYKMGKfivKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAwlraKKIG 106
Cdd:cd03295 6 VTKRYGGGK---KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELR----RKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 107 YIFQTFNLIPVLTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGL--GKFIHHKPAELSGGQQQRVAAARALANDPSIIL 184
Cdd:cd03295 79 YVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502908369 185 ADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDL-KMVDVSDRIIWIRDGKIEKIELRRDI 248
Cdd:cd03295 159 MDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
38-254 |
1.02e-55 |
|
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: 179.08 E-value: 1.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 38 VKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAwlrAKKIGYIFQTFNLIPV 117
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIA---RLGIARTFQNPRLFPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 118 LTAVENVMLPM----------IFVGTP-----YEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSI 182
Cdd:COG0411 94 LTVLENVLVAAharlgrgllaALLRLPrarreEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 183 ILADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMV-DVSDRII------WIRDGKIEkiELRRD---IEAVM 252
Cdd:COG0411 174 LLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVmGLADRIVvldfgrVIAEGTPA--EVRADprvIEAYL 251
|
..
gi 502908369 253 GE 254
Cdd:COG0411 252 GE 253
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
22-242 |
1.26e-55 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 181.88 E-value: 1.26e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 22 VEAVEVKKYYkmGKFivKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAmldayelAWL- 100
Cdd:COG1118 3 IEVRNISKRF--GSF--TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF-------TNLp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 101 -RAKKIGYIFQTFNLIPVLTAVENVM--LPmifVGTPYEDAIV-KAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARAL 176
Cdd:COG1118 72 pRERRVGFVFQHYALFPHMTVAENIAfgLR---VRPPSKAEIRaRVEELLELVQLEGLADRYPSQLSGGQRQRVALARAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502908369 177 ANDPSIILADEPTGNLDLHtgLK------LINLLKEInekkGVTIVTATHDLKMV-DVSDRIIWIRDGKIEKI 242
Cdd:COG1118 149 AVEPEVLLLDEPFGALDAK--VRkelrrwLRRLHDEL----GGTTVFVTHDQEEAlELADRVVVMNQGRIEQV 215
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
41-239 |
1.25e-54 |
|
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: 176.39 E-value: 1.25e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYElawlRAKKIGYIFQTFNLIPVLTA 120
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRE----LARRIAYVPQEPPAPFGLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 121 VENVML---PMI-FVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLHT 196
Cdd:COG1120 93 RELVALgryPHLgLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAH 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 502908369 197 GLKLINLLKEINEKKGVTIVTATHDLKM-VDVSDRIIWIRDGKI 239
Cdd:COG1120 173 QLEVLELLRRLARERGRTVVMVLHDLNLaARYADRLVLLKDGRI 216
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
27-240 |
1.42e-54 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 177.59 E-value: 1.42e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 27 VKKYYKMGKfivKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAWlrakKIG 106
Cdd:COG1125 7 VTKRYPDGT---VAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVELRR----RIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 107 YIFQTFNLIPVLTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGL--GKFIHHKPAELSGGQQQRVAAARALANDPSIIL 184
Cdd:COG1125 80 YVIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 185 ADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHD----LKMvdvSDRIIWIRDGKIE 240
Cdd:COG1125 160 MDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDideaLKL---GDRIAVMREGRIV 216
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
27-240 |
1.58e-52 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 173.72 E-value: 1.58e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 27 VKKYYkmGKfiVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAmldayelaWLRAKK-- 104
Cdd:COG3839 9 VSKSY--GG--VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVT--------DLPPKDrn 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 105 IGYIFQTFNLIPVLTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIIL 184
Cdd:COG3839 77 IAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 185 ADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHD----LKMvdvSDRIIWIRDGKIE 240
Cdd:COG3839 157 LDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDqveaMTL---ADRIAVMNDGRIQ 213
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
38-232 |
1.42e-51 |
|
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: 168.00 E-value: 1.42e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 38 VKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAwlrAKKIGYIFQTFNLIPV 117
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIA---RLGIGRTFQIPRLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 118 LTAVENVMLP----------MIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADE 187
Cdd:cd03219 90 LTVLENVMVAaqartgsgllLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 502908369 188 PTGNLDLHTGLKLINLLKEINEkKGVTIVTATHDLKMV-DVSDRII 232
Cdd:cd03219 170 PAAGLNPEETEELAELIRELRE-RGITVLLVEHDMDVVmSLADRVT 214
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
22-242 |
4.58e-51 |
|
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: 165.89 E-value: 4.58e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 22 VEAVEVKKYYKMgkfiVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYElawlr 101
Cdd:cd03301 1 VELENVTKRFGN----VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 102 aKKIGYIFQTFNLIPVLTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPS 181
Cdd:cd03301 72 -RDIAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502908369 182 IILADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHD-LKMVDVSDRIIWIRDGKIEKI 242
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDqVEAMTMADRIAVMNDGQIQQI 212
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
41-239 |
6.23e-51 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 165.37 E-value: 6.23e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIamlDAYELAWLRaKKIGYIFQTfnliPVL-- 118
Cdd:COG4619 16 LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPL---SAMPPPEWR-RQVAYVPQE----PALwg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 119 -TAVENVMLPMIFVGTPYEDAivKAKKLLELVGLGKFIHHKPA-ELSGGQQQRVAAARALANDPSIILADEPTGNLDLHT 196
Cdd:COG4619 88 gTVRDNLPFPFQLRERKFDRE--RALELLERLGLPPDILDKPVeRLSGGERQRLALIRALLLQPDVLLLDEPTSALDPEN 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 502908369 197 GLKLINLLKEINEKKGVTIVTATHDLKMVD-VSDRIIWIRDGKI 239
Cdd:COG4619 166 TRRVEELLREYLAEEGRAVLWVSHDPEQIErVADRVLTLEAGRL 209
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
22-242 |
7.09e-51 |
|
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: 166.36 E-value: 7.09e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 22 VEAVEVKKYYkmGKFivKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAyelawlR 101
Cdd:cd03296 3 IEVRNVSKRF--GDF--VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPV------Q 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 102 AKKIGYIFQTFNLIPVLTAVENVM--LPMIFVGT-PYEDAI-VKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALA 177
Cdd:cd03296 73 ERNVGFVFQHYALFRHMTVFDNVAfgLRVKPRSErPPEAEIrAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502908369 178 NDPSIILADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDL-KMVDVSDRIIWIRDGKIEKI 242
Cdd:cd03296 153 VEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQeEALEVADRVVVMNKGRIEQV 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
38-239 |
2.03e-50 |
|
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: 172.40 E-value: 2.03e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 38 VKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTG---GKVYIDGVDIAMLDAyelaWLRAKKIGYIFQTF-- 112
Cdd:COG1123 19 VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSE----ALRGRRIGMVFQDPmt 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 113 NLIPVlTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNL 192
Cdd:COG1123 95 QLNPV-TVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTAL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502908369 193 DLHTGLKLINLLKEINEKKGVTIVTATHDLKMV-DVSDRIIWIRDGKI 239
Cdd:COG1123 174 DVTTQAEILDLLRELQRERGTTVLLITHDLGVVaEIADRVVVMDDGRI 221
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
25-239 |
3.85e-50 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 164.50 E-value: 3.85e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 25 VEVKKYYK-MGKFIVkaLDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIamLDAYELAWLRAK 103
Cdd:PRK09493 2 IEFKNVSKhFGPTQV--LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV--NDPKVDERLIRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 104 KIGYIFQTFNLIPVLTAVENVMLPMIFV-GTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSI 182
Cdd:PRK09493 78 EAGMVFQQFYLFPHLTALENVMFGPLRVrGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502908369 183 ILADEPTGNLD---LHTGLKLINLLKEinekKGVTIVTATHDLKMV-DVSDRIIWIRDGKI 239
Cdd:PRK09493 158 MLFDEPTSALDpelRHEVLKVMQDLAE----EGMTMVIVTHEIGFAeKVASRLIFIDKGRI 214
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
26-242 |
9.74e-50 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 166.75 E-value: 9.74e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 26 EVKKYYkmGKFivKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAyelawlRAKKI 105
Cdd:TIGR03265 9 NIRKRF--GAF--TALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPP------QKRDY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 106 GYIFQTFNLIPVLTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILA 185
Cdd:TIGR03265 79 GIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502908369 186 DEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHD----LKMvdvSDRIIWIRDGKIEKI 242
Cdd:TIGR03265 159 DEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDqeeaLSM---ADRIVVMNHGVIEQV 216
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
41-239 |
2.31e-49 |
|
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: 160.29 E-value: 2.31e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYElawlRAKKIGYIFQtfnlipvlta 120
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKE----LARKIAYVPQ---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 121 venvmlpmifvgtpyedaivkakkLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLHTGLKL 200
Cdd:cd03214 81 ------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIEL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 502908369 201 INLLKEINEKKGVTIVTATHDLKMV-DVSDRIIWIRDGKI 239
Cdd:cd03214 137 LELLRRLARERGKTVVMVLHDLNLAaRYADRVILLKDGRI 176
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
22-242 |
2.52e-49 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 162.28 E-value: 2.52e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 22 VEAVEVKKYYkmGKFivKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDayelawLR 101
Cdd:TIGR00968 1 IEIANISKRF--GSF--QALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVH------AR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 102 AKKIGYIFQTFNLIPVLTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPS 181
Cdd:TIGR00968 71 DRKIGFVFQHYALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQ 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502908369 182 IILADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDL-KMVDVSDRIIWIRDGKIEKI 242
Cdd:TIGR00968 151 VLLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQeEAMEVADRIVVMSNGKIEQI 212
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
19-232 |
3.90e-49 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 164.52 E-value: 3.90e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 19 EYVVEAVEVKKYY--KMGKFI-----VKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAM 91
Cdd:COG4608 5 EPLLEVRDLKKHFpvRGGLFGrtvgvVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 92 LDAYELAWLRaKKIGYIFQ----TFNliPVLTAVENVMLPMIFVG-TPYEDAIVKAKKLLELVGLGK-FIHHKPAELSGG 165
Cdd:COG4608 85 LSGRELRPLR-RRMQMVFQdpyaSLN--PRMTVGDIIAEPLRIHGlASKAERRERVAELLELVGLRPeHADRYPHEFSGG 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502908369 166 QQQRVAAARALANDPSIILADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMVD-VSDRII 232
Cdd:COG4608 162 QRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRhISDRVA 229
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
36-248 |
1.35e-47 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 158.77 E-value: 1.35e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 36 FIVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAWLRaKKIGYIFQ----- 110
Cdd:TIGR04521 16 FEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLR-KKVGLVFQfpehq 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 111 TFNLipvlTAVENVML-PMIFvGTPYEDAIVKAKKLLELVGLG-KFIHHKPAELSGGQQQRVAAARALANDPSIILADEP 188
Cdd:TIGR04521 95 LFEE----TVYKDIAFgPKNL-GLSEEEAEERVKEALELVGLDeEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502908369 189 TGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMV-DVSDRIIWIRDGKIEKIELRRDI 248
Cdd:TIGR04521 170 TAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVaEYADRVIVMHKGKIVLDGTPREV 230
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
41-240 |
3.13e-47 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 157.27 E-value: 3.13e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAM----------LDAYELAWLRAKkIGYIFQ 110
Cdd:COG4598 24 LKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLkpdrdgelvpADRRQLQRIRTR-LGMVFQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 111 TFNLIPVLTAVENVML-PMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPT 189
Cdd:COG4598 103 SFNLWSHMTVLENVIEaPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPT 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502908369 190 GNLD--LhTG--LKLINLLKEinekKGVTIVTATHDLKMV-DVSDRIIWIRDGKIE 240
Cdd:COG4598 183 SALDpeL-VGevLKVMRDLAE----EGRTMLVVTHEMGFArDVSSHVVFLHQGRIE 233
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
56-248 |
3.85e-47 |
|
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: 159.20 E-value: 3.85e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 56 IMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYElawlraKKIGYIFQTFNLIPVLTAVENVMLPMIFVGTPY 135
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHL------RHINMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 136 EDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLHTGLKLINLLKEINEKKGVTI 215
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITF 154
|
170 180 190
....*....|....*....|....*....|....
gi 502908369 216 VTATHDLK-MVDVSDRIIWIRDGKIEKIELRRDI 248
Cdd:TIGR01187 155 VFVTHDQEeAMTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-239 |
4.95e-47 |
|
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: 164.16 E-value: 4.95e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 4 AEEAKNVKLPSRRKLEYVVEAVEVKkyYKMGKFivkALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVY 83
Cdd:COG4988 321 AAPAGTAPLPAAGPPSIELEDVSFS--YPGGRP---ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIL 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 84 IDGVDIAMLDayeLAWLRaKKIGYIFQTfnliPVL---TAVENVMLpmifvGTPY--EDAIVKAkklLELVGLGKFIHHK 158
Cdd:COG4988 396 INGVDLSDLD---PASWR-RQIAWVPQN----PYLfagTIRENLRL-----GRPDasDEELEAA---LEAAGLDEFVAAL 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 159 P-----------AELSGGQQQRVAAARALANDPSIILADEPTGNLDLHTGLKLINLLKEIneKKGVTIVTATHDLKMVDV 227
Cdd:COG4988 460 PdgldtplgeggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL--AKGRTVILITHRLALLAQ 537
|
250
....*....|..
gi 502908369 228 SDRIIWIRDGKI 239
Cdd:COG4988 538 ADRILVLDDGRI 549
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
26-239 |
2.88e-46 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 153.88 E-value: 2.88e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 26 EVKKYYKMGKfivKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAWLRaKKI 105
Cdd:PRK10908 6 HVSKAYLGGR---QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLR-RQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 106 GYIFQTFNLIPVLTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILA 185
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502908369 186 DEPTGNLDLHTGLKLINLLKEINeKKGVTIVTATHDLKMVDVSD-RIIWIRDGKI 239
Cdd:PRK10908 162 DEPTGNLDDALSEGILRLFEEFN-RVGVTVLMATHDIGLISRRSyRMLTLSDGHL 215
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
40-239 |
3.69e-46 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 154.09 E-value: 3.69e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 40 ALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAmldayelawLRAKKIGYIFQTFNL---IP 116
Cdd:COG1121 21 VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR---------RARRRIGYVPQRAEVdwdFP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 117 VlTAVENVML----PMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNL 192
Cdd:COG1121 92 I-TVRDVVLMgrygRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGV 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502908369 193 DLHTGLKLINLLKEINeKKGVTIVTATHDLKMV-DVSDRIIWIRDGKI 239
Cdd:COG1121 171 DAATEEALYELLRELR-REGKTILVVTHDLGAVrEYFDRVLLLNRGLV 217
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
41-242 |
4.89e-46 |
|
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: 153.65 E-value: 4.89e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYElawlraKKIGYIFQTFNLIPVLTA 120
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK------RDISYVPQNYALFPHMTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 121 VENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLHTGLKL 200
Cdd:cd03299 89 YKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 502908369 201 INLLKEINEKKGVTIVTATHDLKMVDV-SDRIIWIRDGKIEKI 242
Cdd:cd03299 169 REELKKIRKEFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQV 211
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
22-239 |
5.02e-46 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 151.40 E-value: 5.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 22 VEAVEVKKYYkmGKFivKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAmldayELAWLR 101
Cdd:cd03230 1 IEVRNLSKRY--GKK--TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK-----KEPEEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 102 AKKIGYIFQTFNLIPVLTAVENVmlpmifvgtpyedaivkakkllelvglgkfihhkpaELSGGQQQRVAAARALANDPS 181
Cdd:cd03230 72 KRRIGYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502908369 182 IILADEPTGNLDLHTGLKLINLLKEINeKKGVTIVTATHDLKMV-DVSDRIIWIRDGKI 239
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELK-KEGKTILLSSHILEEAeRLCDRVAILNNGRI 173
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
40-239 |
7.28e-46 |
|
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: 162.70 E-value: 7.28e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 40 ALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDayeLAWLRaKKIGYIFQTfnliPVL- 118
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID---PASLR-RQIGVVLQD----VFLf 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 119 --TAVENVMLpmifvGTPY--EDAIVKAkklLELVGLGKFIHHKP-----------AELSGGQQQRVAAARALANDPSII 183
Cdd:COG2274 562 sgTIRENITL-----GDPDatDEEIIEA---ARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIARALLRNPRIL 633
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502908369 184 LADEPTGNLDLHTGLKLINLLKEIneKKGVTIVTATHDLKMVDVSDRIIWIRDGKI 239
Cdd:COG2274 634 ILDEATSALDAETEAIILENLRRL--LKGRTVIIIAHRLSTIRLADRIIVLDKGRI 687
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
22-239 |
1.42e-45 |
|
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: 152.33 E-value: 1.42e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 22 VEAVEVKKYYkmGKFivKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGL-----DRPTGGKVYIDGVDIAMLDaYE 96
Cdd:cd03260 1 IELRDLNVYY--GDK--HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLD-VD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 97 LAWLRaKKIGYIFQTFNLIPvLTAVENVMLPMIFVG---TPYEDAIVKakKLLELVGLGKFIHHK--PAELSGGQQQRVA 171
Cdd:cd03260 76 VLELR-RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGiklKEELDERVE--EALRKAALWDEVKDRlhALGLSGGQQQRLC 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502908369 172 AARALANDPSIILADEPTGNLDLHTGLKLINLLKEINEKkgVTIVTATHDLKMVD-VSDRIIWIRDGKI 239
Cdd:cd03260 152 LARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAArVADRTAFLLNGRL 218
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
41-189 |
1.42e-45 |
|
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: 149.72 E-value: 1.42e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIamlDAYELAWLRaKKIGYIFQTFNLIPVLTA 120
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDL---TDDERKSLR-KEIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502908369 121 VENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKF----IHHKPAELSGGQQQRVAAARALANDPSIILADEPT 189
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARAEEALEKLGLGDLadrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
39-238 |
3.68e-45 |
|
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: 148.93 E-value: 3.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 39 KALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAwlraKKIGYIFQtfnlipvl 118
Cdd:cd00267 13 TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELR----RRIGYVPQ-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 119 tavenvmlpmifvgtpyedaivkakkllelvglgkfihhkpaeLSGGQQQRVAAARALANDPSIILADEPTGNLDLHTGL 198
Cdd:cd00267 81 -------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRE 117
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 502908369 199 KLINLLKEINEkKGVTIVTATHDLKMVD-VSDRIIWIRDGK 238
Cdd:cd00267 118 RLLELLRELAE-EGRTVIIVTHDPELAElAADRVIVLKDGK 157
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
24-239 |
3.45e-44 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 149.52 E-value: 3.45e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 24 AVEVKKYYKmgKFIVKA-LDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIamlDA-----YEL 97
Cdd:PRK11264 3 AIEVKNLVK--KFHGQTvLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITI---DTarslsQQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 98 AWLRA--KKIGYIFQTFNLIPVLTAVENVML-PMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAAR 174
Cdd:PRK11264 78 GLIRQlrQHVGFVFQNFNLFPHRTVLENIIEgPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502908369 175 ALANDPSIILADEPTGNLDLHTGLKLINLLKEINEKKGvTIVTATHDLKMV-DVSDRIIWIRDGKI 239
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFArDVADRAIFMDQGRI 222
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-248 |
5.26e-44 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 152.41 E-value: 5.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 1 MQNAEEAKNVKLPsrrkleyVVEAVEVKKYYKmGKfivKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGG 80
Cdd:PRK09452 1 SKKLNKQPSSLSP-------LVELRGISKSFD-GK---EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 81 KVYIDGVDIAMLDAyelawlRAKKIGYIFQTFNLIPVLTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPA 160
Cdd:PRK09452 70 RIMLDGQDITHVPA------ENRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 161 ELSGGQQQRVAAARALANDPSIILADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHD----LKMvdvSDRIIWIRD 236
Cdd:PRK09452 144 QLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDqeeaLTM---SDRIVVMRD 220
|
250
....*....|..
gi 502908369 237 GKIEKIELRRDI 248
Cdd:PRK09452 221 GRIEQDGTPREI 232
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
38-238 |
1.24e-43 |
|
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: 145.22 E-value: 1.24e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 38 VKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDayeLAWLRaKKIGYIFQTfnlipv 117
Cdd:cd03228 15 KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLD---LESLR-KNIAYVPQD------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 118 ltavenvmlPMIFVGTpyedaivkakkLLELVglgkfihhkpaeLSGGQQQRVAAARALANDPSIILADEPTGNLDLHTG 197
Cdd:cd03228 85 ---------PFLFSGT-----------IRENI------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETE 132
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 502908369 198 LKLINLLKEIneKKGVTIVTATHDLKMVDVSDRIIWIRDGK 238
Cdd:cd03228 133 ALILEALRAL--AKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
31-239 |
1.42e-43 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 147.21 E-value: 1.42e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 31 YKMGKFIVKAldgvTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYElawlraKKIGYIFQ 110
Cdd:COG3840 9 YRYGDFPLRF----DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE------RPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 111 TFNLIPVLTAVENVMLPMifvgTP----YEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILAD 186
Cdd:COG3840 79 ENNLFPHLTVAQNIGLGL----RPglklTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502908369 187 EPTGNLDlhTGLK--LINLLKEINEKKGVTIVTATHDLK-MVDVSDRIIWIRDGKI 239
Cdd:COG3840 155 EPFSALD--PALRqeMLDLVDELCRERGLTVLMVTHDPEdAARIADRVLLVADGRI 208
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
38-242 |
2.32e-43 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 147.58 E-value: 2.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 38 VKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIamLDAYELAWLRaKKIGYIFQtfNliP- 116
Cdd:TIGR04520 15 KPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDT--LDEENLWEIR-KKVGMVFQ--N--Pd 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 117 ---VLTAV--------ENVmlpmifvGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILA 185
Cdd:TIGR04520 88 nqfVGATVeddvafglENL-------GVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502908369 186 DEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMVDVSDRIIWIRDGKIEKI 242
Cdd:TIGR04520 161 DEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAE 217
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
40-232 |
6.26e-43 |
|
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: 144.98 E-value: 6.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 40 ALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDayelawlraKKIGYIFQTFNL---IP 116
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER---------KRIGYVPQRRSIdrdFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 117 VLtaVENVML-----PMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGN 191
Cdd:cd03235 85 IS--VRDVVLmglygHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 502908369 192 LDLHTGLKLINLLKEINEkKGVTIVTATHDLKMV-DVSDRII 232
Cdd:cd03235 163 VDPKTQEDIYELLRELRR-EGMTILVVTHDLGLVlEYFDRVL 203
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
41-248 |
1.51e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 146.03 E-value: 1.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMldayELAWLRAKKIGYIFQTFNLIPVLTA 120
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTE----ENVWDIRHKIGMVFQNPDNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 121 VEN-VMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLHTGLK 199
Cdd:PRK13650 99 VEDdVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502908369 200 LINLLKEINEKKGVTIVTATHDLKMVDVSDRIIWIRDGKIEKIELRRDI 248
Cdd:PRK13650 179 LIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
22-242 |
2.13e-42 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 147.54 E-value: 2.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 22 VEAVEVKKYYkmGKfiVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAyelawlR 101
Cdd:PRK10851 3 IEIANIKKSF--GR--TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA------R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 102 AKKIGYIFQTFNLIPVLTAVENV-----MLPMifVGTPYEDAI-VKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARA 175
Cdd:PRK10851 73 DRKVGFVFQHYALFRHMTVFDNIafgltVLPR--RERPNAAAIkAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502908369 176 LANDPSIILADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLK-MVDVSDRIIWIRDGKIEKI 242
Cdd:PRK10851 151 LAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEeAMEVADRVVVMSQGNIEQA 218
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
37-242 |
2.24e-42 |
|
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: 143.59 E-value: 2.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 37 IVKALDGVTFNVK---RREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVdiAMLDAYELAWL--RAKKIGYIFQT 111
Cdd:cd03297 6 IEKRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGT--VLFDSRKKINLppQQRKIGLVFQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 112 FNLIPVLTAVENVMLPMIFVgTPYEDAIvKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGN 191
Cdd:cd03297 84 YALFPHLNVRENLAFGLKRK-RNREDRI-SVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502908369 192 LDLHTGLKLINLLKEINEKKGVTIVTATHDL-KMVDVSDRIIWIRDGKIEKI 242
Cdd:cd03297 162 LDRALRLQLLPELKQIKKNLNIPVIFVTHDLsEAEYLADRIVVMEDGRLQYI 213
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
38-239 |
2.27e-42 |
|
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: 143.88 E-value: 2.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 38 VKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELawlrAKKIGYIFQTfnliPV 117
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL----RRNIGYVPQD----VT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 118 L---TAVENVMLpmifvGTPYED--AIVKAkklLELVGLGKFIHHKP-----------AELSGGQQQRVAAARALANDPS 181
Cdd:cd03245 89 LfygTLRDNITL-----GAPLADdeRILRA---AELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502908369 182 IILADEPTGNLDLHTGLKLINLLKEINEKKgvTIVTATHDLKMVDVSDRIIWIRDGKI 239
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDK--TLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
40-221 |
5.91e-42 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 143.85 E-value: 5.91e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 40 ALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAyelawlrakKIGYIFQTFNLIPVLT 119
Cdd:COG4525 22 ALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGA---------DRGVVFQKDALLPWLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 120 AVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLHTGLK 199
Cdd:COG4525 93 VLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQ 172
|
170 180
....*....|....*....|..
gi 502908369 200 LINLLKEINEKKGVTIVTATHD 221
Cdd:COG4525 173 MQELLLDVWQRTGKGVFLITHS 194
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
22-239 |
8.04e-42 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 142.26 E-value: 8.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 22 VEAVEVKKYYKmgKFIVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIA--MLDAYelaw 99
Cdd:cd03263 1 LQIRNLTKTYK--KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRtdRKAAR---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 100 lraKKIGYIFQTFNLIPVLTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALAND 179
Cdd:cd03263 75 ---QSLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502908369 180 PSIILADEPTGNLDLHTGLKLINLLKEinEKKGVTIVTATHDLKMVDV-SDRIIWIRDGKI 239
Cdd:cd03263 152 PSVLLLDEPTSGLDPASRRAIWDLILE--VRKGRSIILTTHSMDEAEAlCDRIAIMSDGKL 210
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
39-239 |
2.39e-41 |
|
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: 150.02 E-value: 2.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 39 KALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELawlRAKkIGYIFQTfnliPVL 118
Cdd:TIGR03375 479 PALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADL---RRN-IGYVPQD----PRL 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 119 ---TAVENVMLpmifvGTPY--EDAIVKAkklLELVGLGKFIHHKP-----------AELSGGQQQRVAAARALANDPSI 182
Cdd:TIGR03375 551 fygTLRDNIAL-----GAPYadDEEILRA---AELAGVTEFVRRHPdgldmqigergRSLSGGQRQAVALARALLRDPPI 622
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502908369 183 ILADEPTGNLDLHTGLKLINLLKEINEKKgvTIVTATHDLKMVDVSDRIIWIRDGKI 239
Cdd:TIGR03375 623 LLLDEPTSAMDNRSEERFKDRLKRWLAGK--TLVLVTHRTSLLDLVDRIIVMDNGRI 677
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
27-239 |
8.01e-41 |
|
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: 139.81 E-value: 8.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 27 VKKYykmGKFivKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIaMLDAYELAwlraKKIG 106
Cdd:cd03265 7 VKKY---GDF--EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV-VREPREVR----RRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 107 YIFQTFNLIPVLTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILAD 186
Cdd:cd03265 77 IVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502908369 187 EPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMVD-VSDRIIWIRDGKI 239
Cdd:cd03265 157 EPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEqLCDRVAIIDHGRI 210
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
38-232 |
1.35e-40 |
|
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: 139.49 E-value: 1.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 38 VKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYID----GVDIAMLDAYELAWLRAKKIGYIFQTFN 113
Cdd:COG4778 24 LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQASPREILALRRRTIGYVSQFLR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 114 LIPVLTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHH-KPAELSGGQQQRVAAARALANDPSIILADEPTGNL 192
Cdd:COG4778 104 VIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLWDlPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 502908369 193 DLHTGLKLINLlkeINEKK--GVTIVTATHDLKMVD-VSDRII 232
Cdd:COG4778 184 DAANRAVVVEL---IEEAKarGTAIIGIFHDEEVREaVADRVV 223
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
41-242 |
5.92e-40 |
|
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: 137.98 E-value: 5.92e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAwlrakkigyIFQTFNLIPVLTA 120
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV---------VFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 121 VENVMLPMIFV----GTPYEDAIVKAKklLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLHT 196
Cdd:TIGR01184 72 RENIALAVDRVlpdlSKSERRAIVEEH--IALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 502908369 197 GLKLINLLKEINEKKGVTIVTATHDL-KMVDVSDRIIWIRDGKIEKI 242
Cdd:TIGR01184 150 RGNLQEELMQIWEEHRVTVLMVTHDVdEALLLSDRVVMLTNGPAANI 196
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
40-239 |
1.73e-39 |
|
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: 143.75 E-value: 1.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 40 ALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYEL----AWL--RAkkigYIFQTfn 113
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLrrriAVVpqRP----HLFDT-- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 114 lipvlTAVENVMLpmifvGTPY--EDAIVKAkklLELVGLGKFIHHKP-----------AELSGGQQQRVAAARALANDP 180
Cdd:COG4987 424 -----TLRENLRL-----ARPDatDEELWAA---LERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLALARALLRDA 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502908369 181 SIILADEPTGNLDLHTGLKLINLLKEINEKKgvTIVTATHDLKMVDVSDRIIWIRDGKI 239
Cdd:COG4987 491 PILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLAGLERMDRILVLEDGRI 547
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
40-239 |
1.49e-38 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 135.53 E-value: 1.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 40 ALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGvdiaMLDAYELAWLRAKKIGYIFQTFNLIPVLT 119
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG----MVLSEETVWDVRRQVGMVFQNPDNQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 120 AVEN-VMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLHTGL 198
Cdd:PRK13635 98 TVQDdVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRR 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 502908369 199 KLINLLKEINEKKGVTIVTATHDLKMVDVSDRIIWIRDGKI 239
Cdd:PRK13635 178 EVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEI 218
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
22-239 |
2.16e-38 |
|
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: 133.82 E-value: 2.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 22 VEAVEVKKYYKmGKFIVkalDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYElawlR 101
Cdd:cd03218 1 LRAENLSKRYG-KRKVV---NGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 102 AKK-IGYIFQTFNLIPVLTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDP 180
Cdd:cd03218 73 ARLgIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502908369 181 SIILADEPTGNLD---LHTGLKLINLLKEinekKGVTIVTATHDLK-MVDVSDRIIWIRDGKI 239
Cdd:cd03218 153 KFLLLDEPFAGVDpiaVQDIQKIIKILKD----RGIGVLITDHNVReTLSITDRAYIIYEGKV 211
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
40-239 |
7.81e-38 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 132.83 E-value: 7.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 40 ALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDI---AMLDAYELAWLRaKKIGYIFQTFNLIP 116
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIRLLR-QKVGMVFQQYNLWP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 117 VLTAVENVM-LPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLH 195
Cdd:COG4161 96 HLTVMENLIeAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 502908369 196 TGLKLINLLKEINEkKGVTIVTATHDLKMV-DVSDRIIWIRDGKI 239
Cdd:COG4161 176 ITAQVVEIIRELSQ-TGITQVIVTHEVEFArKVASQVVYMEKGRI 219
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
41-238 |
9.87e-38 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 131.45 E-value: 9.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAyelawLRAKKIGYIFQTFNLIPVLTA 120
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARE-----DYRRRLAYLGHADGLKPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 121 VENVMLPMIFVGTPYEDAIVKAkkLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLHTGLKL 200
Cdd:COG4133 93 RENLRFWAALYGLRADREAIDE--ALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALL 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 502908369 201 INLLKEiNEKKGVTIVTATHDLKMVDvSDRIIWIRDGK 238
Cdd:COG4133 171 AELIAA-HLARGGAVLLTTHQPLELA-AARVLDLGDFK 206
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
21-251 |
6.79e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 131.35 E-value: 6.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 21 VVEAVEVKKYYKMGkfiVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMlDAYELAWL 100
Cdd:PRK13639 1 ILETRDLKYSYPDG---TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKY-DKKSLLEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 101 RaKKIGYIFQTF-NLIPVLTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALAND 179
Cdd:PRK13639 77 R-KTVGIVFQNPdDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502908369 180 PSIILADEPTGNLDLHTGLKLINLLKEINeKKGVTIVTATHDLKMVDV-SDRIIWIRDGKIEK----IELRRDIEAV 251
Cdd:PRK13639 156 PEIIVLDEPTSGLDPMGASQIMKLLYDLN-KEGITIIISTHDVDLVPVyADKVYVMSDGKIIKegtpKEVFSDIETI 231
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
39-239 |
8.63e-37 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 130.52 E-value: 8.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 39 KALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGL---DRPTGGKVYIDG--VDIAMLDAYELAWLRAKKiGYIFQTFN 113
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGrtVQREGRLARDIRKSRANT-GYIFQQFN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 114 LIPVLTAVENVMLPMIFvGTPYEDAIV---------KAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIIL 184
Cdd:PRK09984 97 LVNRLSVLENVLIGALG-STPFWRTCFswftreqkqRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVIL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502908369 185 ADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLK-MVDVSDRIIWIRDGKI 239
Cdd:PRK09984 176 ADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDyALRYCERIVALRQGHV 231
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
40-254 |
1.31e-36 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 129.72 E-value: 1.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 40 ALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAwlrAKKIGYIFQTFNLIPVLT 119
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA---RMGVVRTFQHVRLFREMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 120 AVENVMLPM-------IFVG---TPY-----EDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIIL 184
Cdd:PRK11300 97 VIENLLVAQhqqlktgLFSGllkTPAfrraeSEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILM 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502908369 185 ADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMV-DVSDRIIWIRDGKIEKI----ELRRD---IEAVMGE 254
Cdd:PRK11300 177 LDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVmGISDRIYVVNQGTPLANgtpeEIRNNpdvIKAYLGE 254
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
39-241 |
1.52e-36 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 129.70 E-value: 1.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 39 KALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAML----------DAYELAWLRAKkIGYI 108
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvaDKNQLRLLRTR-LTMV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 109 FQTFNLIPVLTAVENVM-LPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHK-PAELSGGQQQRVAAARALANDPSIILAD 186
Cdd:PRK10619 98 FQHFNLWSHMTVLENVMeAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQRVSIARALAMEPEVLLFD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502908369 187 EPTGNLDLHTGLKLINLLKEINEkKGVTIVTATHDLKMV-DVSDRIIWIRDGKIEK 241
Cdd:PRK10619 178 EPTSALDPELVGEVLRIMQQLAE-EGKTMVVVTHEMGFArHVSSHVIFLHQGKIEE 232
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
19-242 |
3.21e-36 |
|
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: 134.16 E-value: 3.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 19 EYVVEAVEVKK-YYKMGKFIVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYI----DGVDiaMLD 93
Cdd:TIGR03269 277 EPIIKVRNVSKrYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVD--MTK 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 94 AYELAWLRAKK-IGYIFQTFNLIPVLTAVENvMLPMIFVGTPYEDAIVKAKKLLELVGL----GKFIHHK-PAELSGGQQ 167
Cdd:TIGR03269 355 PGPDGRGRAKRyIGILHQEYDLYPHRTVLDN-LTEAIGLELPDELARMKAVITLKMVGFdeekAEEILDKyPDELSEGER 433
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502908369 168 QRVAAARALANDPSIILADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMV-DVSDRIIWIRDGKIEKI 242
Cdd:TIGR03269 434 HRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVlDVCDRAALMRDGKIVKI 509
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
39-239 |
3.35e-36 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 128.59 E-value: 3.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 39 KALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDG--VDIAM-LDAYELAWLRaKKIGYIFQTFNLI 115
Cdd:PRK11124 16 QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhFDFSKtPSDKAIRELR-RNVGMVFQQYNLW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 116 PVLTAVENVM-LPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDL 194
Cdd:PRK11124 95 PHLTVQQNLIeAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDP 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 502908369 195 HTGLKLINLLKEINEkKGVTIVTATHDLKMV-DVSDRIIWIRDGKI 239
Cdd:PRK11124 175 EITAQIVSIIRELAE-TGITQVIVTHEVEVArKTASRVVYMENGHI 219
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
39-239 |
3.85e-36 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 134.52 E-value: 3.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 39 KALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAmldAYELAWLRaKKIGYIFQTfnliPVL 118
Cdd:COG1132 354 PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIR---DLTLESLR-RQIGVVPQD----TFL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 119 ---TAVENVMLpmifvGTPY--EDAIVKAkklLELVGLGKFIHHKP-----------AELSGGQQQRVAAARALANDPSI 182
Cdd:COG1132 426 fsgTIRENIRY-----GRPDatDEEVEEA---AKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALLKDPPI 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502908369 183 ILADEPTGNLDLHTGLKLINLLKEIneKKGVTIVTATHDLKMVDVSDRIIWIRDGKI 239
Cdd:COG1132 498 LILDEATSALDTETEALIQEALERL--MKGRTTIVIAHRLSTIRNADRILVLDDGRI 552
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-239 |
5.85e-36 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 133.66 E-value: 5.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 12 LPSRRKLEY------VVEAVEVKKYYKMGKFI-------VKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDrPT 78
Cdd:COG4172 260 EPRGDPRPVppdappLLEARDLKVWFPIKRGLfrrtvghVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PS 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 79 GGKVYIDGVDIAMLDAYELAWLRaKKIGYIFQ----TFNliPVLTAVENVMLPMI--FVGTPYEDAIVKAKKLLELVGL- 151
Cdd:COG4172 339 EGEIRFDGQDLDGLSRRALRPLR-RRMQVVFQdpfgSLS--PRMTVGQIIAEGLRvhGPGLSAAERRARVAEALEEVGLd 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 152 GKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMVD-VSDR 230
Cdd:COG4172 416 PAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRaLAHR 495
|
....*....
gi 502908369 231 IIWIRDGKI 239
Cdd:COG4172 496 VMVMKDGKV 504
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
30-239 |
7.92e-36 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 128.03 E-value: 7.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 30 YYKMGKF---IVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLD-AYelawlRAKKI 105
Cdd:COG4167 15 KYRTGLFrrqQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDyKY-----RCKHI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 106 GYIFQ----TFNliPVLTAVENVMLPMIFVgTPYEDAIVKAK--KLLELVGL-GKFIHHKPAELSGGQQQRVAAARALAN 178
Cdd:COG4167 90 RMIFQdpntSLN--PRLNIGQILEEPLRLN-TDLTAEEREERifATLRLVGLlPEHANFYPHMLSSGQKQRVALARALIL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502908369 179 DPSIILADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMVD-VSDRIIWIRDGKI 239
Cdd:COG4167 167 QPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKhISDKVLVMHQGEV 228
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
48-239 |
1.01e-35 |
|
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: 126.45 E-value: 1.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 48 VKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYElawlraKKIGYIFQTFNLIPVLTAVENVML- 126
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD------RPVSMLFQENNLFAHLTVEQNVGLg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 127 --PMIFVGTPYEDAIvkaKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLHTGLKLINLL 204
Cdd:cd03298 95 lsPGLKLTAEDRQAI---EVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190
....*....|....*....|....*....|....*...
gi 502908369 205 KEINEKKGVTIVTATH---DLKMVDvsDRIIWIRDGKI 239
Cdd:cd03298 172 LDLHAETKMTVLMVTHqpeDAKRLA--QRVVFLDNGRI 207
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
25-242 |
1.03e-35 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 129.84 E-value: 1.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 25 VEVKKYYK-MGKFIVkaLDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDayelawLRAK 103
Cdd:PRK11432 7 VVLKNITKrFGSNTV--IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRS------IQQR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 104 KIGYIFQTFNLIPVLTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSII 183
Cdd:PRK11432 79 DICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 184 LADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHD-LKMVDVSDRIIWIRDGKIEKI 242
Cdd:PRK11432 159 LFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDqSEAFAVSDTVIVMNKGKIMQI 218
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
22-239 |
2.83e-35 |
|
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: 125.56 E-value: 2.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 22 VEAVEVKKYYKMGKFIVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAwlr 101
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 102 akKIGYIFQTFNLIPVLTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPS 181
Cdd:cd03266 79 --RLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502908369 182 IILADEPTGNLDLHTGLKLINLLKEINEkKGVTIVTATHDLKMVD-VSDRIIWIRDGKI 239
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQLRA-LGKCILFSTHIMQEVErLCDRVVVLHRGRV 214
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
40-222 |
3.13e-35 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 126.35 E-value: 3.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 40 ALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYElawlrakkiGYIFQTFNLIPVLT 119
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER---------GVVFQNEGLLPWRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 120 AVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLHTGLK 199
Cdd:PRK11248 87 VQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQ 166
|
170 180
....*....|....*....|...
gi 502908369 200 LINLLKEINEKKGVTIVTATHDL 222
Cdd:PRK11248 167 MQTLLLKLWQETGKQVLLITHDI 189
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
40-239 |
4.13e-35 |
|
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: 128.29 E-value: 4.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 40 ALDgVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDiaMLDAYELAWLRAKK--IGYIFQTFNLIPV 117
Cdd:COG4148 15 TLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEV--LQDSARGIFLPPHRrrIGYVFQEARLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 118 LTAVENVMLPMIFvgTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLHTG 197
Cdd:COG4148 92 LSVRGNLLYGRKR--APRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARK 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 502908369 198 LKLINLLKEINEKKGVTIVTATHDLK-MVDVSDRIIWIRDGKI 239
Cdd:COG4148 170 AEILPYLERLRDELDIPILYVSHSLDeVARLADHVVLLEQGRV 212
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
40-242 |
6.03e-35 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 128.41 E-value: 6.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 40 ALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYElawlraKKIGYIFQTFNLIPVLT 119
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ------RPINMMFQSYALFPHMT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 120 AVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLHTGLK 199
Cdd:PRK11607 108 VEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDR 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 502908369 200 LINLLKEINEKKGVTIVTATHDL-KMVDVSDRIIWIRDGKIEKI 242
Cdd:PRK11607 188 MQLEVVDILERVGVTCVMVTHDQeEAMTMAGRIAIMNRGKFVQI 231
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
22-239 |
7.85e-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: 124.08 E-value: 7.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 22 VEAVEVkkYYkmGKFivKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAwlr 101
Cdd:cd03224 3 VENLNA--GY--GKS--QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 102 AKKIGYIFQTFNLIPVLTAVENVMLpmifVGTPYEDAIVKA--KKLLELV-GLGKFIHHKPAELSGGQQQRVAAARALAN 178
Cdd:cd03224 74 RAGIGYVPEGRRIFPELTVEENLLL----GAYARRRAKRKArlERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMS 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502908369 179 DPSIILADEPTgnldlhTGL------KLINLLKEINEkKGVTIVTATHDLKMV-DVSDRIIWIRDGKI 239
Cdd:cd03224 150 RPKLLLLDEPS------EGLapkiveEIFEAIRELRD-EGVTILLVEQNARFAlEIADRAYVLERGRV 210
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
27-241 |
8.75e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 126.35 E-value: 8.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 27 VKKYYKMGKFIVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKV---YIDGVDIAMLDAYELAW---- 99
Cdd:PRK13651 9 VKIFNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKEKEKVLeklv 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 100 --------------LRaKKIGYIFQ--TFNLIPVlTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGK-FIHHKPAEL 162
Cdd:PRK13651 89 iqktrfkkikkikeIR-RRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDEsYLQRSPFEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 163 SGGQQQRVAAARALANDPSIILADEPTGNLDLHTGLKLINLLKEINeKKGVTIVTATHDLKMV-DVSDRIIWIRDGKIEK 241
Cdd:PRK13651 167 SGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLN-KQGKTIILVTHDLDNVlEWTKRTIFFKDGKIIK 245
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
31-239 |
8.97e-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: 123.52 E-value: 8.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 31 YKMGKFIvkaLDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAmldayelAWLRAKKIGYIFQ 110
Cdd:cd03226 9 YKKGTEI---LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK-------AKERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 111 TFNLIPVLTAVENVMLPMIfvgTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTG 190
Cdd:cd03226 79 DVDYQLFTDSVREELLLGL---KELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 502908369 191 NLDLHTGLKLINLLKEInEKKGVTIVTATHDLK-MVDVSDRIIWIRDGKI 239
Cdd:cd03226 156 GLDYKNMERVGELIREL-AAQGKAVIVITHDYEfLAKVCDRVLLLANGAI 204
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
24-242 |
1.66e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 124.72 E-value: 1.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 24 AVEVKK-YYKMGKFIVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIamlDAYELAWLRa 102
Cdd:PRK13632 7 MIKVENvSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI---SKENLKEIR- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 103 KKIGYIFQTfnliPvltavENVmlpmiFVGTPYEDAI--------VKAKK-------LLELVGLGKFIHHKPAELSGGQQ 167
Cdd:PRK13632 83 KKIGIIFQN----P-----DNQ-----FIGATVEDDIafglenkkVPPKKmkdiiddLAKKVGMEDYLDKEPQNLSGGQK 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502908369 168 QRVAAARALANDPSIILADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMVDVSDRIIWIRDGKIEKI 242
Cdd:PRK13632 149 QRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQ 223
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
22-239 |
1.72e-34 |
|
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: 123.07 E-value: 1.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 22 VEAVEVKKYYKMGKfivkALDGVTFNVKRREYVsIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDI-AMLDAYElawl 100
Cdd:cd03264 1 LQLENLTKRYGKKR----ALDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVlKQPQKLR---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 101 raKKIGYIFQTFNLIPVLTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDP 180
Cdd:cd03264 72 --RRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 181 SIILADEPTGNLDLHTGLKLINLLKEINEKKgvTIVTATHDLKMV-DVSDRIIWIRDGKI 239
Cdd:cd03264 150 SILIVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVeSLCNQVAVLNKGKL 207
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
45-242 |
1.73e-34 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 127.84 E-value: 1.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 45 TFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAWLRAKKIGYIFQTFNLIPVLTAVENV 124
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 125 MLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLHTGLKLINLL 204
Cdd:PRK10070 128 AFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDEL 207
|
170 180 190
....*....|....*....|....*....|....*....
gi 502908369 205 KEINEKKGVTIVTATHDL-KMVDVSDRIIWIRDGKIEKI 242
Cdd:PRK10070 208 VKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQV 246
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
39-232 |
2.04e-34 |
|
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: 129.33 E-value: 2.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 39 KALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYelAWLRakKIGYIFQTfnliPVL 118
Cdd:TIGR02857 336 PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAD--SWRD--QIAWVPQH----PFL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 119 TA---VENVMLpmifvGTPY--EDAIVKAkklLELVGLGKFI------HHKP-----AELSGGQQQRVAAARALANDPSI 182
Cdd:TIGR02857 408 FAgtiAENIRL-----ARPDasDAEIREA---LERAGLDEFVaalpqgLDTPigeggAGLSGGQAQRLALARAFLRDAPL 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 502908369 183 ILADEPTGNLDLHTGLKLINLLKEINEkkGVTIVTATHDLKMVDVSDRII 232
Cdd:TIGR02857 480 LLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALADRIV 527
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
23-188 |
3.62e-34 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 123.22 E-value: 3.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 23 EAVEVKKYYKmGKFIVKaldGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYElawlRA 102
Cdd:COG1137 5 EAENLVKSYG-KRTVVK---DVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHK----RA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 103 KK-IGY------IFQTfnlipvLTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARA 175
Cdd:COG1137 77 RLgIGYlpqeasIFRK------LTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARA 150
|
170
....*....|...
gi 502908369 176 LANDPSIILADEP 188
Cdd:COG1137 151 LATNPKFILLDEP 163
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
40-239 |
7.31e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 123.27 E-value: 7.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 40 ALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLdayELAWLRAKKIGYIFQTFNLIPVLT 119
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDE---ENLWDIRNKAGMVFQNPDNQIVAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 120 AVE-NVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLHTGL 198
Cdd:PRK13633 102 IVEeDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 502908369 199 KLINLLKEINEKKGVTIVTATHDLKMVDVSDRIIWIRDGKI 239
Cdd:PRK13633 182 EVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKV 222
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-239 |
1.43e-33 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 126.67 E-value: 1.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 19 EYVVEAVEVKKYYkmgkFIVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAML---DAy 95
Cdd:COG1129 2 EPLLEMRGISKSF----GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRsprDA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 96 elawlRAKKIGYIFQTFNLIPVLTAVENVML---PMIFVGTPYEDAIVKAKKLLELVGLgkfiHHKP----AELSGGQQQ 168
Cdd:COG1129 77 -----QAAGIAIIHQELNLVPNLSVAENIFLgrePRRGGLIDWRAMRRRARELLARLGL----DIDPdtpvGDLSVAQQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502908369 169 RVAAARALANDPSIILADEPTGNLD------LhtgLKLINLLKEinekKGVTIVTATHDLKMV-DVSDRIIWIRDGKI 239
Cdd:COG1129 148 LVEIARALSRDARVLILDEPTASLTereverL---FRIIRRLKA----QGVAIIYISHRLDEVfEIADRVTVLRDGRL 218
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
26-248 |
1.76e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 122.82 E-value: 1.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 26 EVKKYYKMGK-FIVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYI-DGVDIAMLDAYELAWLRaK 103
Cdd:PRK13634 7 KVEHRYQYKTpFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgERVITAGKKNKKLKPLR-K 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 104 KIGYIFQtfnlIPVLTAVENVML------PMIFvGTPYEDAIVKAKKLLELVGLG-KFIHHKPAELSGGQQQRVAAARAL 176
Cdd:PRK13634 86 KVGIVFQ----FPEHQLFEETVEkdicfgPMNF-GVSEEDAKQKAREMIELVGLPeELLARSPFELSGGQMRRVAIAGVL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502908369 177 ANDPSIILADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHdlKMVDV---SDRIIWIRDGKIEKIELRRDI 248
Cdd:PRK13634 161 AMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTH--SMEDAaryADQIVVMHKGTVFLQGTPREI 233
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
21-239 |
1.89e-33 |
|
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: 121.84 E-value: 1.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 21 VVEAVEVKKYYKMGKFIVK-----ALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAY 95
Cdd:TIGR02769 2 LLEVRDVTHTYRTGGLFGAkqrapVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 96 ELAWLRaKKIGYIFQ----TFNliPVLTAVENVMLPMIFVGTPYEDA-IVKAKKLLELVGLGKFIHHK-PAELSGGQQQR 169
Cdd:TIGR02769 82 QRRAFR-RDVQLVFQdspsAVN--PRMTVRQIIGEPLRHLTSLDESEqKARIAELLDMVGLRSEDADKlPRQLSGGQLQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502908369 170 VAAARALANDPSIILADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMVD-VSDRIIWIRDGKI 239
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQsFCQRVAVMDKGQI 229
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
38-248 |
2.21e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 121.56 E-value: 2.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 38 VKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGL-----DRPTGGKVYIDGVDIAMLDAYELAwlraKKIGYIFQTF 112
Cdd:PRK14247 16 VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIELR----RRVQMVFQIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 113 NLIPVLTAVENVMLpmifvgTPYEDAIVKAKK--------LLELVGLGKFIHHK---PA-ELSGGQQQRVAAARALANDP 180
Cdd:PRK14247 92 NPIPNLSIFENVAL------GLKLNRLVKSKKelqervrwALEKAQLWDEVKDRldaPAgKLSGGQQQRLCIARALAFQP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502908369 181 SIILADEPTGNLDLHTGLKLINLLKEIneKKGVTIVTATH-DLKMVDVSDRIIWIRDGKIEKIELRRDI 248
Cdd:PRK14247 166 EVLLADEPTANLDPENTAKIESLFLEL--KKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
40-239 |
2.60e-33 |
|
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: 120.41 E-value: 2.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 40 ALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIamlDAYELAWLRaKKIGYIFQTFNLIPVlT 119
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDI---RDISRKSLR-SMIGVVLQDTFLFSG-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 120 AVENVMLpmifvGTPY--EDAIVKAKKlleLVGLGKFIHHKP-----------AELSGGQQQRVAAARALANDPSIILAD 186
Cdd:cd03254 93 IMENIRL-----GRPNatDEEVIEAAK---EAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKILILD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502908369 187 EPTGNLDLHTGLKLINLLKEINEKKgVTIVTAtHDLKMVDVSDRIIWIRDGKI 239
Cdd:cd03254 165 EATSNIDTETEKLIQEALEKLMKGR-TSIIIA-HRLSTIKNADKILVLDDGKI 215
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
41-239 |
2.72e-33 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 121.72 E-value: 2.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAWLRaKKIGYIFQ----TFNliP 116
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFR-RDIQMVFQdsisAVN--P 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 117 VLTAVENVMLPMIFVGTPYE-DAIVKAKKLLELVGLGKFIHHK-PAELSGGQQQRVAAARALANDPSIILADEPTGNLDL 194
Cdd:PRK10419 105 RKTVREIIREPLRHLLSLDKaERLARASEMLRAVDLDDSVLDKrPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 502908369 195 HTGLKLINLLKEINEKKGVTIVTATHDLKMVD-VSDRIIWIRDGKI 239
Cdd:PRK10419 185 VLQAGVIRLLKKLQQQFGTACLFITHDLRLVErFCQRVMVMDNGQI 230
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
39-239 |
3.98e-33 |
|
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of this protein family are the ATP-binding subunit of an ABC transporter system that is associated with PQQ biosynthesis and PQQ-dependent alcohol dehydrogenases. While this family shows homology to several efflux ABC transporter subunits, the presence of a periplasmic substrate-binding protein and association with systems for catabolism of alcohols suggests a role in import rather than detoxification. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 274822 [Multi-domain] Cd Length: 236 Bit Score: 120.47 E-value: 3.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 39 KALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDiamLDAYELAWLRakKIGYIFQTFNLIPVL 118
Cdd:TIGR03864 15 RALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVAGHD---LRRAPRAALA--RLGVVFQQPTLDLDL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 119 TAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLHTGL 198
Cdd:TIGR03864 90 SVRQNLRYHAALHGLSRAEARARIAELLARLGLAERADDKVRELNGGHRRRVEIARALLHRPALLLLDEPTVGLDPASRA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 502908369 199 KLINLLKEINEKKGVTIVTATHDLKMVDVSDRIIWIRDGKI 239
Cdd:TIGR03864 170 AITAHVRALARDQGLSVLWATHLVDEIEASDRLVVLHRGRV 210
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
42-225 |
3.98e-33 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 121.03 E-value: 3.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 42 DGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAWLRaKKIGYIFQTFNLIPVLTAV 121
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVR-KRMSMLFQSGALFTDMNVF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 122 ENVMLPMiFVGTPYEDAIVKAKKL--LELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLHTGLK 199
Cdd:PRK11831 103 DNVAYPL-REHTQLPAPLLHSTVMmkLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGV 181
|
170 180
....*....|....*....|....*.
gi 502908369 200 LINLLKEINEKKGVTIVTATHDLKMV 225
Cdd:PRK11831 182 LVKLISELNSALGVTCVVVSHDVPEV 207
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
40-242 |
6.05e-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: 122.53 E-value: 6.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 40 ALDgVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAmlDAYELAWLRAKK--IGYIFQTFNLIPV 117
Cdd:TIGR02142 13 SLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLF--DSRKGIFLPPEKrrIGYVFQEARLFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 118 LTAVENVMLPMIFVGTPYEDaiVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLHTG 197
Cdd:TIGR02142 90 LSVRGNLRYGMKRARPSERR--ISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRK 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 502908369 198 LKLINLLKEINEKKGVTIVTATHDL-KMVDVSDRIIWIRDGKIEKI 242
Cdd:TIGR02142 168 YEILPYLERLHAEFGIPILYVSHSLqEVLRLADRVVVLEDGRVAAA 213
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
31-239 |
8.44e-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: 124.80 E-value: 8.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 31 YKMGKFIVKALDGVTFNVKRREYVSIMGPSGSGKT-TLFNMIGGLDRP---TGGKVYIDGVDIAMLDAYELAWLRAKKIG 106
Cdd:COG4172 16 FGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPaahPSGSILFDGQDLLGLSERELRRIRGNRIA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 107 YIFQ---TfNLIPVLTaVENVMLPMIFV--GTPYEDAIVKAKKLLELVG-------LGKFIHhkpaELSGGQQQRVAAAR 174
Cdd:COG4172 96 MIFQepmT-SLNPLHT-IGKQIAEVLRLhrGLSGAAARARALELLERVGipdperrLDAYPH----QLSGGQRQRVMIAM 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502908369 175 ALANDPSIILADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMV-DVSDRIIWIRDGKI 239
Cdd:COG4172 170 ALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVrRFADRVAVMRQGEI 235
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
21-239 |
9.71e-33 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 119.71 E-value: 9.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 21 VVEAVEVKKYYkmGKFivKALDGVTFNVKRREYVSIMGPSGSGKTTL---FNMIGGL--DRPTGGKVYIDGVDI--AMLD 93
Cdd:TIGR00972 1 AIEIENLNLFY--GEK--EALKNINLDIPKNQVTALIGPSGCGKSTLlrsLNRMNDLvpGVRIEGKVLFDGQDIydKKID 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 94 AYELAwlraKKIGYIFQTFNLIPvLTAVENVMLPMIFVGTPYE---DAIVKakKLLELVGLGKFI----HHKPAELSGGQ 166
Cdd:TIGR00972 77 VVELR----RRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIKDKkelDEIVE--ESLKKAALWDEVkdrlHDSALGLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502908369 167 QQRVAAARALANDPSIILADEPTGNLDLHTGLKLINLLKEIneKKGVTIVTATHDLKM-VDVSDRIIWIRDGKI 239
Cdd:TIGR00972 150 QQRLCIARALAVEPEVLLLDEPTSALDPIATGKIEELIQEL--KKKYTIVIVTHNMQQaARISDRTAFFYDGEL 221
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
41-193 |
1.10e-32 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 118.35 E-value: 1.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFN-MIGGLDRP--TGGKVYIDGVDIAMLDAYelawlrAKKIGYIFQTFNLIPV 117
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSPAfsASGEVLLNGRRLTALPAE------QRRIGILFQDDLLFPH 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502908369 118 LTAVENVM--LPmifVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLD 193
Cdd:COG4136 91 LSVGENLAfaLP---PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
38-242 |
1.46e-32 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 124.14 E-value: 1.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 38 VKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLD--RPTGGKV-----------YID------------------- 85
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIiyhvalcekcgYVErpskvgepcpvcggtlepe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 86 GVDIAMLDAYELAWLRaKKIGYIFQ-TFNLIPVLTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSG 164
Cdd:TIGR03269 93 EVDFWNLSDKLRRRIR-KRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRITHIARDLSG 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502908369 165 GQQQRVAAARALANDPSIILADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLK-MVDVSDRIIWIRDGKIEKI 242
Cdd:TIGR03269 172 GEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEvIEDLSDKAIWLENGEIKEE 250
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
41-239 |
1.75e-32 |
|
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: 119.03 E-value: 1.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPT-GGKVYIDGVDiamLDAYELAWLRaKKIGYIFQTF-NLIPVL 118
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTyGNDVRLFGER---RGGEDVWELR-KRIGLVSPALqLRFPRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 119 TAVENVML----PMIFVGTPYEDA-IVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLD 193
Cdd:COG1119 95 ETVLDVVLsgffDSIGLYREPTDEqRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 502908369 194 LHTGLKLINLLKEINEKKGVTIVTATHDLK-MVDVSDRIIWIRDGKI 239
Cdd:COG1119 175 LGARELLLALLDKLAAEGAPTLVLVTHHVEeIPPGITHVLLLKDGRV 221
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
30-240 |
1.97e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 119.77 E-value: 1.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 30 YYKMGKFIVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAyELAWLRaKKIGYIF 109
Cdd:PRK13637 12 YMEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKV-KLSDIR-KKVGLVF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 110 Q--TFNLIPVlTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLG--KFIHHKPAELSGGQQQRVAAARALANDPSIILA 185
Cdd:PRK13637 90 QypEYQLFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILIL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502908369 186 DEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDlkMVDVS---DRIIWIRDGKIE 240
Cdd:PRK13637 169 DEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHS--MEDVAklaDRIIVMNKGKCE 224
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
47-239 |
2.52e-32 |
|
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: 117.65 E-value: 2.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 47 NVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYElawlraKKIGYIFQTFNLIPVLTAVENVML 126
Cdd:TIGR01277 20 NVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQ------RPVSMLFQENNLFAHLTVRQNIGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 127 ---PMIFVGTPYEDAIVKAKKLlelVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLHTGLKLINL 203
Cdd:TIGR01277 94 glhPGLKLNAEQQEKVVDAAQQ---VGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLAL 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 502908369 204 LKEINEKKGVTIVTATHDLK-MVDVSDRIIWIRDGKI 239
Cdd:TIGR01277 171 VKQLCSERQRTLLMVTHHLSdARAIASQIAVVSQGKI 207
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
15-239 |
3.14e-32 |
|
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: 117.82 E-value: 3.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 15 RRKLEYVVEAVevKKYYKMGKFIVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGvdiamLDA 94
Cdd:cd03267 13 YSKEPGLIGSL--KSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-----LVP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 95 YELAWLRAKKIGYIF-QTFNLIPVLTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAA 173
Cdd:cd03267 86 WKRRKKFLRRIGVVFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502908369 174 RALANDPSIILADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMVD-VSDRIIWIRDGKI 239
Cdd:cd03267 166 AALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEaLARRVLVIDKGRL 232
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
22-239 |
3.47e-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: 116.93 E-value: 3.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 22 VEAVEVKKYYKMGKfivkALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDiaMLDAYELawlr 101
Cdd:cd03268 1 LKTNDLTKTYGKKR----VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKS--YQKNIEA---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 102 AKKIGYIFQTFNLIPVLTAVENVMLPMIFVGTPYEDaivkAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPS 181
Cdd:cd03268 71 LRRIGALIEAPGFYPNLTARENLRLLARLLGIRKKR----IDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502908369 182 IILADEPTGNLDLHTGLKLINLLKEINeKKGVTIVTATHDLKMVD-VSDRIIWIRDGKI 239
Cdd:cd03268 147 LLILDEPTNGLDPDGIKELRELILSLR-DQGITVLISSHLLSEIQkVADRIGIINKGKL 204
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
41-239 |
4.22e-32 |
|
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: 115.78 E-value: 4.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAwlraKKIGYIFQtfnlipvlta 120
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELG----DHVGYLPQ---------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 121 veNVMLpmiFVGTpYEDAIvkakkllelvglgkfihhkpaeLSGGQQQRVAAARALANDPSIILADEPTGNLDLHTGLKL 200
Cdd:cd03246 84 --DDEL---FSGS-IAENI----------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERAL 135
|
170 180 190
....*....|....*....|....*....|....*....
gi 502908369 201 INLLKEINeKKGVTIVTATHDLKMVDVSDRIIWIRDGKI 239
Cdd:cd03246 136 NQAIAALK-AAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
19-225 |
5.49e-32 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 119.68 E-value: 5.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 19 EYVVEAVEVKKYY--KMGKF----IVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAML 92
Cdd:PRK11308 3 QPLLQAIDLKKHYpvKRGLFkperLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 93 DAYELAWLRaKKIGYIFQ----TFNlipvltavenvmlPMIFVGTPYEDAIV------------KAKKLLELVGLgKFIH 156
Cdd:PRK11308 83 DPEAQKLLR-QKIQIVFQnpygSLN-------------PRKKVGQILEEPLLintslsaaerreKALAMMAKVGL-RPEH 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502908369 157 HK--PAELSGGQQQRVAAARALANDPSIILADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMV 225
Cdd:PRK11308 148 YDryPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVV 218
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
13-222 |
6.29e-32 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 117.83 E-value: 6.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 13 PSRRKLEYVVEAVEVKKYYkmGKFivKALDGVTFNVKRREYVSIMGPSGSGKTTL---FN----MIGGLdRpTGGKVYID 85
Cdd:COG1117 3 APASTLEPKIEVRNLNVYY--GDK--QALKDINLDIPENKVTALIGPSGCGKSTLlrcLNrmndLIPGA-R-VEGEILLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 86 GVDIamLDA-YELAWLRaKKIGYIFQTFNLIPvLTAVENVMLPMIFVG--TPYE-DAIVKakKLLELVGLG---KFIHHK 158
Cdd:COG1117 77 GEDI--YDPdVDVVELR-RRVGMVFQKPNPFP-KSIYDNVAYGLRLHGikSKSElDEIVE--ESLRKAALWdevKDRLKK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502908369 159 PA-ELSGGQQQRVAAARALANDPSIILADEPTGNLDLHTGLKLINLLKEIneKKGVTIVTATHDL 222
Cdd:COG1117 151 SAlGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILEL--KKDYTIVIVTHNM 213
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
22-239 |
1.21e-31 |
|
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: 116.23 E-value: 1.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 22 VEAVEVkkYYkmGKfiVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAwlr 101
Cdd:COG0410 6 VENLHA--GY--GG--IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIA--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 102 AKKIGYIFQTFNLIPVLTAVENVMLpmifvGTPYEDAIVKAKKLLELVG-----LGKFIHHKPAELSGGQQQRVAAARAL 176
Cdd:COG0410 77 RLGIGYVPEGRRIFPSLTVEENLLL-----GAYARRDRAEVRADLERVYelfprLKERRRQRAGTLSGGEQQMLAIGRAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 177 ANDPSIILADEPTgnldlhTGL------KLINLLKEINEkKGVTIVTATHDLKMV-DVSDRIIWIRDGKI 239
Cdd:COG0410 152 MSRPKLLLLDEPS------LGLapliveEIFEIIRRLNR-EGVTILLVEQNARFAlEIADRAYVLERGRI 214
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
40-239 |
1.39e-31 |
|
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: 116.43 E-value: 1.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 40 ALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDayeLAWLRAkKIGYIFQTfNLIPVLT 119
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALAD---PAWLRR-QVGVVLQE-NVLFNRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 120 AVENVMLPMifVGTPYEDAIVKAKklleLVGLGKFIHHKP-----------AELSGGQQQRVAAARALANDPSIILADEP 188
Cdd:cd03252 92 IRDNIALAD--PGMSMERVIEAAK----LAGAHDFISELPegydtivgeqgAGLSGGQRQRIAIARALIHNPRILIFDEA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502908369 189 TGNLDLHTGLKLINLLKEINekKGVTIVTATHDLKMVDVSDRIIWIRDGKI 239
Cdd:cd03252 166 TSALDYESEHAIMRNMHDIC--AGRTVIIIAHRLSTVKNADRIIVMEKGRI 214
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
40-239 |
2.55e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 116.63 E-value: 2.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 40 ALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAmlDAYELAWLRaKKIGYIFQTFNLIPVLT 119
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTG--DFSKLQGIR-KLVGIVFQNPETQFVGR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 120 AVE--------NVMLPMIFVGTPYEDAIVKakkllelVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGN 191
Cdd:PRK13644 94 TVEedlafgpeNLCLPPIEIRKRVDRALAE-------IGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSM 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502908369 192 LDLHTGLKLINLLKEINEkKGVTIVTATHDLKMVDVSDRIIWIRDGKI 239
Cdd:PRK13644 167 LDPDSGIAVLERIKKLHE-KGKTIVYITHNLEELHDADRIIVMDRGKI 213
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
38-241 |
7.03e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 115.58 E-value: 7.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 38 VKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMldayELAWLRAKKIGYIFQTFNLIPV 117
Cdd:PRK13642 20 VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTA----ENVWNLRRKIGMVFQNPDNQFV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 118 LTAVEN-VMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLHT 196
Cdd:PRK13642 96 GATVEDdVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 502908369 197 GLKLINLLKEINEKKGVTIVTATHDLKMVDVSDRIIWIRDGKIEK 241
Cdd:PRK13642 176 RQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIK 220
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
22-239 |
9.50e-31 |
|
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: 111.75 E-value: 9.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 22 VEAVEVKKYYKMgkfiVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYElAwlR 101
Cdd:cd03216 1 LELRGITKRFGG----VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD-A--R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 102 AKKIGYIFQtfnlipvltavenvmlpmifvgtpyedaivkakkllelvglgkfihhkpaeLSGGQQQRVAAARALANDPS 181
Cdd:cd03216 74 RAGIAMVYQ---------------------------------------------------LSVGERQMVEIARALARNAR 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502908369 182 IILADEPTGNLDLHTGLKLINLLKEInEKKGVTIVTATHDLKMV-DVSDRIIWIRDGKI 239
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVfEIADRVTVLRDGRV 160
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
40-248 |
1.23e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 114.85 E-value: 1.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 40 ALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIamlDAYELAWLRaKKIGYIFQ--------T 111
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAI---TDDNFEKLR-KHIGIVFQnpdnqfvgS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 112 FNLIPVLTAVENVMLPmifvgtpYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGN 191
Cdd:PRK13648 100 IVKYDVAFGLENHAVP-------YDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSM 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502908369 192 LDLHTGLKLINLLKEINEKKGVTIVTATHDLKMVDVSDRIIWIRDGKIEKIELRRDI 248
Cdd:PRK13648 173 LDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
19-238 |
1.54e-30 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 118.21 E-value: 1.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 19 EYVVEAVEVKKYYkmGKfiVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAM---LDAy 95
Cdd:COG3845 3 PPALELRGITKRF--GG--VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIrspRDA- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 96 elawlRAKKIGYIFQTFNLIPVLTAVENVML---PMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAA 172
Cdd:COG3845 78 -----IALGIGMVHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502908369 173 ARALANDPSIILADEPTGNLDLHTGLKLINLLKEINEkKGVTIVTATHDLKMV-DVSDRIIWIRDGK 238
Cdd:COG3845 153 LKALYRGARILILDEPTAVLTPQEADELFEILRRLAA-EGKSIIFITHKLREVmAIADRVTVLRRGK 218
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
41-239 |
1.81e-30 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 114.00 E-value: 1.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAmlDAYElawlrakKIGYIFQTFNLIPVLTA 120
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLA--EARE-------DTRLMFQDARLLPWKKV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 121 VENVMLPMifvGTPYEDAivkAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLHTGLKL 200
Cdd:PRK11247 99 IDNVGLGL---KGQWRDA---ALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEM 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 502908369 201 INLLKEINEKKGVTIVTATHDL-KMVDVSDRIIWIRDGKI 239
Cdd:PRK11247 173 QDLIESLWQQHGFTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
39-240 |
1.94e-30 |
|
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: 111.64 E-value: 1.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 39 KALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAyelawLRAKKIGYIFQTfnlipvl 118
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK-----ALSSLISVLNQR------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 119 tavenvmlPMIFVGTPYEDaivkakkllelvgLGKfihhkpaELSGGQQQRVAAARALANDPSIILADEPTGNLDLHTGL 198
Cdd:cd03247 84 --------PYLFDTTLRNN-------------LGR-------RFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITER 135
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 502908369 199 KLINLLKEINEKKgvTIVTATHDLKMVDVSDRIIWIRDGKIE 240
Cdd:cd03247 136 QLLSLIFEVLKDK--TLIWITHHLTGIEHMDKILFLENGKII 175
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
41-248 |
3.36e-30 |
|
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: 117.83 E-value: 3.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAwlraKKIGYIFQTFNLIPVlTA 120
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFG----KHIGYLPQDVELFPG-TV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 121 VENVMLpmiFVGTPYEDAIVKAKKLL---ELV-----GLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNL 192
Cdd:TIGR01842 409 AENIAR---FGENADPEKIIEAAKLAgvhELIlrlpdGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNL 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502908369 193 DLHTGLKLINLLKEInEKKGVTIVTATHDLKMVDVSDRIIWIRDGKIEKIELRRDI 248
Cdd:TIGR01842 486 DEEGEQALANAIKAL-KARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEV 540
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
41-240 |
5.46e-30 |
|
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: 117.16 E-value: 5.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELawlrAKKIGYIFQTFNLIPVlTA 120
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREEL----GRHIGYLPQDVELFDG-TI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 121 VENV--MlpmifvGTPYEDAIVKAKKlleLVGLGKFIHHKP-----------AELSGGQQQRVAAARALANDPSIILADE 187
Cdd:COG4618 423 AENIarF------GDADPEKVVAAAK---LAGVHEMILRLPdgydtrigeggARLSGGQRQRIGLARALYGDPRLVVLDE 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502908369 188 PTGNLDlHTG----LKLINLLKEinekKGVTIVTATHDLKMVDVSDRIIWIRDGKIE 240
Cdd:COG4618 494 PNSNLD-DEGeaalAAAIRALKA----RGATVVVITHRPSLLAAVDKLLVLRDGRVQ 545
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
27-242 |
8.86e-30 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 114.17 E-value: 8.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 27 VKKYYKMGkfiVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDG--V--------DIAMldaye 96
Cdd:PRK11650 9 VRKSYDGK---TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGrvVnelepadrDIAM----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 97 lawlrakkigyIFQTFNLIPVLTAVENVMLPMIFVGTPYEDA---IVKAKKLLELvglGKFIHHKPAELSGGQQQRVAAA 173
Cdd:PRK11650 81 -----------VFQNYALYPHMSVRENMAYGLKIRGMPKAEIeerVAEAARILEL---EPLLDRKPRELSGGQRQRVAMG 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502908369 174 RALANDPSIILADEPTGNLDlhtgLKL-INLLKEIneKK-----GVTIVTATHD-LKMVDVSDRIIWIRDGKIEKI 242
Cdd:PRK11650 147 RAIVREPAVFLFDEPLSNLD----AKLrVQMRLEI--QRlhrrlKTTSLYVTHDqVEAMTLADRVVVMNGGVAEQI 216
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
41-239 |
9.77e-30 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 112.13 E-value: 9.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAWLRAkkigyifqtfnlipVL-- 118
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRA--------------VLpq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 119 --------TAVENVML---PMIFVGTPYEDAIVKAkklLELVGLGKFIHHKPAELSGGQQQRVAAARALA-------NDP 180
Cdd:COG4559 83 hsslafpfTVEEVVALgraPHGSSAAQDRQIVREA---LALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 181 SIILADEPTGNLDLHTGLKLINLLKEINEkKGVTIVTATHDLKMV-DVSDRIIWIRDGKI 239
Cdd:COG4559 160 RWLFLDEPTSALDLAHQHAVLRLARQLAR-RGGGVVAVLHDLNLAaQYADRILLLHQGRL 218
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
18-239 |
2.39e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 111.37 E-value: 2.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 18 LEYVVEAVEVKKYYKMGkfiVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYel 97
Cdd:PRK13647 1 MDNIIEVEDLHFRYKDG---TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEK-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 98 aWLRaKKIGYIFQT-FNLIPVLTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARAL 176
Cdd:PRK13647 76 -WVR-SKVGLVFQDpDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502908369 177 ANDPSIILADEPTGNLDLHTGLKLINLLKEINeKKGVTIVTATHDLKM-VDVSDRIIWIRDGKI 239
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLH-NQGKTVIVATHDVDLaAEWADQVIVLKEGRV 216
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
40-239 |
4.74e-29 |
|
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: 109.38 E-value: 4.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 40 ALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGL----DRPTGGKVYIDGVDIAMLDayelawLRAKKIGYIFQT---- 111
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLlppgLTQTSGEILLDGRPLLPLS------IRGRHIATIMQNprta 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 112 FNliPVLTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGL--GKFIHHK-PAELSGGQQQRVAAARALANDPSIILADEP 188
Cdd:TIGR02770 75 FN--PLFTMGNHAIETLRSLGKLSKQARALILEALEAVGLpdPEEVLKKyPFQLSGGMLQRVMIALALLLEPPFLIADEP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502908369 189 TGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMV-DVSDRIIWIRDGKI 239
Cdd:TIGR02770 153 TTDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVaRIADEVAVMDDGRI 204
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
37-240 |
4.95e-29 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 109.16 E-value: 4.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 37 IVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDayelawlrakkIGYIFQtfnliP 116
Cdd:cd03220 34 EFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLG-----------LGGGFN-----P 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 117 VLTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLHT 196
Cdd:cd03220 98 ELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAF 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 502908369 197 GLKLINLLKEINeKKGVTIVTATHDLKMV-DVSDRIIWIRDGKIE 240
Cdd:cd03220 178 QEKCQRRLRELL-KQGKTVILVSHDPSSIkRLCDRALVLEKGKIR 221
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
38-239 |
9.89e-29 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 112.24 E-value: 9.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 38 VKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAwlraKKIGYIFQ----TFN 113
Cdd:PRK09536 16 TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAS----RRVASVPQdtslSFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 114 LiPVLTAVENVMLPMI--FVG-TPYEDAIVKakKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTG 190
Cdd:PRK09536 92 F-DVRQVVEMGRTPHRsrFDTwTETDRAAVE--RAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 502908369 191 NLDLHTGLKLINLLKEINEkKGVTIVTATHDLKM-VDVSDRIIWIRDGKI 239
Cdd:PRK09536 169 SLDINHQVRTLELVRRLVD-DGKTAVAAIHDLDLaARYCDELVLLADGRV 217
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
21-239 |
1.87e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 109.12 E-value: 1.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 21 VVEAVEVKKYYKMGKfiVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGL---DRPTGGKVYIDGVDIAMldayEL 97
Cdd:PRK13640 5 IVEFKHVSFTYPDSK--KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTA----KT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 98 AWLRAKKIGYIFQT-FNLIPVLTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARAL 176
Cdd:PRK13640 79 VWDIREKVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGIL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502908369 177 ANDPSIILADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMVDVSDRIIWIRDGKI 239
Cdd:PRK13640 159 AVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKL 221
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
38-239 |
2.01e-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: 108.01 E-value: 2.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 38 VKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDayeLAWLRaKKIGYIFQTfnliPV 117
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLN---LRWLR-SQIGLVSQE----PV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 118 L---TAVENVMLpmifvGTPYEDA--IVKAKKLlelVGLGKFIHHKP-----------AELSGGQQQRVAAARALANDPS 181
Cdd:cd03249 88 LfdgTIAENIRY-----GKPDATDeeVEEAAKK---ANIHDFIMSLPdgydtlvgergSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502908369 182 IILADEPTGNLDLHTGlklinllKEINEK-----KGVTIVTATHDLKMVDVSDRIIWIRDGKI 239
Cdd:cd03249 160 ILLLDEATSALDAESE-------KLVQEAldramKGRTTIVIAHRLSTIRNADLIAVLQNGQV 215
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
40-232 |
2.49e-28 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 106.55 E-value: 2.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 40 ALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGvdiamldayelawlrAKKIGYIFQTFNLIPVL- 118
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG---------------GARVAYVPQRSEVPDSLp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 119 -TAVENVML----PMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLD 193
Cdd:NF040873 72 lTVRDLVAMgrwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 502908369 194 LHTGLKLINLLKEINEkKGVTIVTATHDLKMVDVSDRII 232
Cdd:NF040873 152 AESRERIIALLAEEHA-RGATVVVVTHDLELVRRADPCV 189
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
41-239 |
5.25e-28 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 107.09 E-value: 5.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAwlraKKIGYIFQTFNLIPVLTA 120
Cdd:COG4604 17 LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELA----KRLAILRQENHINSRLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 121 VENVMlpmiFVGTPY-------ED--AIVKAKKLLELVGL-GKFIHhkpaELSGGQQQRVAAARALANDPSIILADEPTG 190
Cdd:COG4604 93 RELVA----FGRFPYskgrltaEDreIIDEAIAYLDLEDLaDRYLD----ELSGGQRQRAFIAMVLAQDTDYVLLDEPLN 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 502908369 191 NLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMVDV-SDRIIWIRDGKI 239
Cdd:COG4604 165 NLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCyADHIVAMKDGRV 214
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
45-239 |
8.69e-28 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 106.20 E-value: 8.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 45 TFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVD----------IAMLdayelawlrakkigyiFQTFNL 114
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDhtttppsrrpVSML----------------FQENNL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 115 IPVLTAVENVML---PMIFVgTPYEDAivKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGN 191
Cdd:PRK10771 83 FSHLTVAQNIGLglnPGLKL-NAAQRE--KLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502908369 192 LDLHTGLKLINLLKEINEKKGVTIVTATHDLK-MVDVSDRIIWIRDGKI 239
Cdd:PRK10771 160 LDPALRQEMLTLVSQVCQERQLTLLMVSHSLEdAARIAPRSLVVADGRI 208
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
40-239 |
1.08e-27 |
|
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: 105.65 E-value: 1.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 40 ALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDayeLAWLRaKKIGYIFQtfnlIPVLt 119
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG---LHDLR-SRISIIPQ----DPVL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 120 avenvmlpmiFVGT------PY----EDAIVKAkklLELVGLGKFIHHKP-----------AELSGGQQQRVAAARALAN 178
Cdd:cd03244 90 ----------FSGTirsnldPFgeysDEELWQA---LERVGLKEFVESLPggldtvveeggENLSVGQRQLLCLARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502908369 179 DPSIILADEPTGNLDLHTGLKLINLLKEinEKKGVTIVTATHDLKMVDVSDRIIWIRDGKI 239
Cdd:cd03244 157 KSKILVLDEATASVDPETDALIQKTIRE--AFKDCTVLTIAHRLDTIIDSDRILVLDKGRV 215
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
41-239 |
1.48e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 106.39 E-value: 1.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAWLRAkkigyifqtfnlipVL-- 118
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRA--------------VLpq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 119 --------TAVENV-MLPMIFVGTPYEDAIVKAKKLlELVGLGKFIHHKPAELSGGQQQRVAAARALA------NDPSII 183
Cdd:PRK13548 84 hsslsfpfTVEEVVaMGRAPHGLSRAEDDALVAAAL-AQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502908369 184 LADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKM-VDVSDRIIWIRDGKI 239
Cdd:PRK13548 163 LLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLaARYADRIVLLHQGRL 219
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
39-239 |
1.57e-27 |
|
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: 105.39 E-value: 1.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 39 KALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAmldAYELAWLRaKKIGYIFQT---FNLi 115
Cdd:cd03251 16 PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVR---DYTLASLR-RQIGLVSQDvflFND- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 116 pvlTAVENVMLpmifvGTP--YEDAIVKAkklLELVGLGKFIHHKP-----------AELSGGQQQRVAAARALANDPSI 182
Cdd:cd03251 91 ---TVAENIAY-----GRPgaTREEVEEA---ARAANAHEFIMELPegydtvigergVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502908369 183 ILADEPTGNLDLHTGLKLINLLKEINEKKgVTIVTAtHDLKMVDVSDRIIWIRDGKI 239
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNR-TTFVIA-HRLSTIENADRIVVLEDGKI 214
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
17-239 |
2.37e-27 |
|
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: 104.17 E-value: 2.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 17 KLEYVVEAVEVKKYYKMGKFIVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTG--GKVYIDGVDIamlda 94
Cdd:cd03213 1 GVTLSFRNLTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPL----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 95 yELAWLRaKKIGYIFQTFNLIPVLTAVENVMLPmifvgtpyedaivkakklLELVGlgkfihhkpaeLSGGQQQRVAAAR 174
Cdd:cd03213 76 -DKRSFR-KIIGYVPQDDILHPTLTVRETLMFA------------------AKLRG-----------LSGGERKRVSIAL 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502908369 175 ALANDPSIILADEPTGNLDLHTGLKLINLLKEInEKKGVTIVTATHDL--KMVDVSDRIIWIRDGKI 239
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRL-ADTGRTIICSIHQPssEIFELFDKLLLLSQGRV 190
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
31-239 |
2.87e-27 |
|
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: 105.00 E-value: 2.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 31 YKMGKFIvkaLDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIamlDAYELAWLRaKKIGYIFQ 110
Cdd:cd03253 10 YDPGRPV---LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI---REVTLDSLR-RAIGVVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 111 T---FNLipvlTAVENvmlpmIFVGTP--YEDAIVKAKKLLElvglgkfIHHKPAE---------------LSGGQQQRV 170
Cdd:cd03253 83 DtvlFND----TIGYN-----IRYGRPdaTDEEVIEAAKAAQ-------IHDKIMRfpdgydtivgerglkLSGGEKQRV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502908369 171 AAARALANDPSIILADEPTGNLDLHTGLKLINLLKEIneKKGVTIVTATHDLKMVDVSDRIIWIRDGKI 239
Cdd:cd03253 147 AIARAILKNPPILLLDEATSALDTHTEREIQAALRDV--SKGRTTIVIAHRLSTIVNADKIIVLKDGRI 213
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
37-239 |
3.15e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 106.71 E-value: 3.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 37 IVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIamldayelaWLR----AKKIGYIF-QT 111
Cdd:COG4586 34 EVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVP---------FKRrkefARRIGVVFgQR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 112 FNLIPVLTAVEN-VMLPMIFvGTPYEDAIVKAKKLLELVGLGKFIHhKPA-ELSGGQQQRVAAARALANDPSIILADEPT 189
Cdd:COG4586 105 SQLWWDLPAIDSfRLLKAIY-RIPDAEYKKRLDELVELLDLGELLD-TPVrQLSLGQRMRCELAAALLHRPKILFLDEPT 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502908369 190 GNLDLHTGLKLINLLKEINEKKGVTIVTATHDlkMVDV---SDRIIWIRDGKI 239
Cdd:COG4586 183 IGLDVVSKEAIREFLKEYNRERGTTILLTSHD--MDDIealCDRVIVIDHGRI 233
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
22-239 |
3.84e-27 |
|
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: 103.90 E-value: 3.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 22 VEAVEVKKYYKMgkfiVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDayelawlr 101
Cdd:cd03269 1 LEVENVTKRFGR----VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 102 AKKIGYIFQTFNLIPVLTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPS 181
Cdd:cd03269 69 RNRIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502908369 182 IILADEPTgnldlhTGLKLIN---LLKEINE--KKGVTIVTATHDLKMV-DVSDRIIWIRDGKI 239
Cdd:cd03269 149 LLILDEPF------SGLDPVNvelLKDVIRElaRAGKTVILSTHQMELVeELCDRVLLLNKGRA 206
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
39-239 |
4.58e-27 |
|
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: 102.90 E-value: 4.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 39 KALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELawlRAKKIGYI---FQTFNLI 115
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDA---IRAGIAYVpedRKREGLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 116 PVLTAVENVMLPMIfvgtpyedaivkakkllelvglgkfihhkpaeLSGGQQQRVAAARALANDPSIILADEPTGNLDLH 195
Cdd:cd03215 91 LDLSVAENIALSSL--------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 502908369 196 TGLKLINLLKEINEkKGVTIVTATHDL-KMVDVSDRIIWIRDGKI 239
Cdd:cd03215 139 AKAEIYRLIRELAD-AGKAVLLISSELdELLGLCDRILVMYEGRI 182
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
19-217 |
1.29e-26 |
|
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: 103.12 E-value: 1.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 19 EYVVEAVEVKKYYKMGKFIVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRP---TGGKVYIDGVDiamLDAY 95
Cdd:cd03234 1 QRVLPWWDVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQP---RKPD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 96 ElaWLraKKIGYIFQTFNLIPVLTAVENVMLPMIFVGTPYEDAIVKAKK----LLELVGLGKFIHHKPAELSGGQQQRVA 171
Cdd:cd03234 78 Q--FQ--KCVAYVRQDDILLPGLTVRETLTYTAILRLPRKSSDAIRKKRvedvLLRDLALTRIGGNLVKGISGGERRRVS 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 502908369 172 AARALANDPSIILADEPTGNLDLHTGLKLINLLKEINEKKGVTIVT 217
Cdd:cd03234 154 IAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILT 199
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
40-222 |
1.46e-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: 107.45 E-value: 1.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 40 ALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAwlraKKIGYIFQTFNLIPVlT 119
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVR----RRVSVCAQDAHLFDT-T 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 120 AVENVMLPMifvGTPYEDAIVKAkklLELVGLGKFIHHKP-----------AELSGGQQQRVAAARALANDPSIILADEP 188
Cdd:TIGR02868 425 VRENLRLAR---PDATDEELWAA---LERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDEP 498
|
170 180 190
....*....|....*....|....*....|....
gi 502908369 189 TGNLDLHTGLKLINLLKEINEkkGVTIVTATHDL 222
Cdd:TIGR02868 499 TEHLDAETADELLEDLLAALS--GRTVVLITHHL 530
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
39-229 |
1.77e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 104.14 E-value: 1.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 39 KALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDI-AMLDAYELAWLRaKKIGYIFQtFNLIPV 117
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItPETGNKNLKKLR-KKVSLVFQ-FPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 118 L--TAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGK-FIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDL 194
Cdd:PRK13641 99 FenTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178
|
170 180 190
....*....|....*....|....*....|....*
gi 502908369 195 HTGLKLINLLKEInEKKGVTIVTATHDlkMVDVSD 229
Cdd:PRK13641 179 EGRKEMMQLFKDY-QKAGHTVILVTHN--MDDVAE 210
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
39-232 |
2.59e-26 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 104.40 E-value: 2.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 39 KALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDiaMLDAYELAWLRAKK-IGYIFQT--FNLI 115
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKD--LLGMKDDEWRAVRSdIQMIFQDplASLN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 116 PVLTAVENVMLPMI--FVGTPYEDAIVKAKKLLELVGL-GKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNL 192
Cdd:PRK15079 113 PRMTIGEIIAEPLRtyHPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 192
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 502908369 193 DLHTGLKLINLLKEINEKKGVTIVTATHDLKMVD-VSDRII 232
Cdd:PRK15079 193 DVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKhISDRVL 233
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
31-239 |
3.22e-26 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 102.95 E-value: 3.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 31 YKMGKF---IVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLD-AYelawlRAKKIG 106
Cdd:PRK15112 16 YRTGWFrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDySY-----RSQRIR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 107 YIFQ--TFNLIPVLTAVENVMLPMIF----VGTPYEDAIVKAkklLELVGL-GKFIHHKPAELSGGQQQRVAAARALAND 179
Cdd:PRK15112 91 MIFQdpSTSLNPRQRISQILDFPLRLntdlEPEQREKQIIET---LRQVGLlPDHASYYPHMLAPGQKQRLGLARALILR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502908369 180 PSIILADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMVD-VSDRIIWIRDGKI 239
Cdd:PRK15112 168 PKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKhISDQVLVMHQGEV 228
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
40-239 |
4.11e-26 |
|
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: 101.83 E-value: 4.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 40 ALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYElawlRAKK-IGYIFQTFNLIPVL 118
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHE----RARAgIAYVPQGREIFPRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 119 TAVENVMlpMIFVGTPYEDAIVKAKkLLEL--VgLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTgnldlhT 196
Cdd:TIGR03410 91 TVEENLL--TGLAALPRRSRKIPDE-IYELfpV-LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPT------E 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 502908369 197 GL-----KLI-NLLKEINEKKGVTIVTATHDLKMV-DVSDRIIWIRDGKI 239
Cdd:TIGR03410 161 GIqpsiiKDIgRVIRRLRAEGGMAILLVEQYLDFArELADRYYVMERGRV 210
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
41-239 |
1.04e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 104.76 E-value: 1.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDgvdiamldayelawlRAKKIGYIFQTFNLIPVLTA 120
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP---------------KGLRIGYLPQEPPLDDDLTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 121 VENVM---LPMIFVGTPYEDAIVK-----------------------------AKKLLELVGLGKFIHHKP-AELSGGQQ 167
Cdd:COG0488 79 LDTVLdgdAELRALEAELEELEAKlaepdedlerlaelqeefealggweaearAEEILSGLGFPEEDLDRPvSELSGGWR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502908369 168 QRVAAARALANDPSIILADEPTGNLDLHTGLKLINLLKeiNEKKGVTIVtaTHDLKMVD-VSDRIIWIRDGKI 239
Cdd:COG0488 159 RRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLK--NYPGTVLVV--SHDRYFLDrVATRILELDRGKL 227
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
38-252 |
1.17e-25 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 100.93 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 38 VKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGvdiamldayELAWLRAkkIGYIFQtfnliPV 117
Cdd:COG1134 39 FWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG---------RVSALLE--LGAGFH-----PE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 118 LTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLHTG 197
Cdd:COG1134 103 LTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQ 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502908369 198 LKLINLLKEINEkKGVTIVTATHDLKMV-DVSDRIIWIRDGKIEKIElrrDIEAVM 252
Cdd:COG1134 183 KKCLARIRELRE-SGRTVIFVSHSMGAVrRLCDRAIWLEKGRLVMDG---DPEEVI 234
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
30-239 |
1.21e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 101.78 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 30 YYKMGKFIVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDI-AMLDAYELAWLRaKKIGYI 108
Cdd:PRK13646 12 YQKGTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITItHKTKDKYIRPVR-KRIGMV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 109 FQtfnlIPVLTAVE-NVMLPMIF----VGTPYEDAIVKAKKLLELVGLGKFIHHK-PAELSGGQQQRVAAARALANDPSI 182
Cdd:PRK13646 91 FQ----FPESQLFEdTVEREIIFgpknFKMNLDEVKNYAHRLLMDLGFSRDVMSQsPFQMSGGQMRKIAIVSILAMNPDI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 183 ILADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDlkMVDV---SDRIIWIRDGKI 239
Cdd:PRK13646 167 IVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHD--MNEVaryADEVIVMKEGSI 224
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
39-232 |
1.64e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 100.17 E-value: 1.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 39 KALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAML--DAYElawlraKKIGYIFQTfnliP 116
Cdd:PRK10247 21 KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLkpEIYR------QQVSYCAQT----P 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 117 VL---TAVENVMLP-MIFVGTPYEDAIVKAkklLELVGLGKFIHHKP-AELSGGQQQRVAAARALANDPSIILADEPTGN 191
Cdd:PRK10247 91 TLfgdTVYDNLIFPwQIRNQQPDPAIFLDD---LERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEITSA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 502908369 192 LDLHTGLKLINLLKEINEKKGVTIVTATHDLKMVDVSDRII 232
Cdd:PRK10247 168 LDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVI 208
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
26-229 |
2.18e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 100.97 E-value: 2.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 26 EVKKYYKMGK-FIVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDI-AMLDAYELAWLRaK 103
Cdd:PRK13649 7 NVSYTYQAGTpFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItSTSKNKDIKQIR-K 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 104 KIGYIFQtFNLIPVL--TAVENVML-PMIFvGTPYEDAIVKAKKLLELVGLGKFIHHK-PAELSGGQQQRVAAARALAND 179
Cdd:PRK13649 86 KVGLVFQ-FPESQLFeeTVLKDVAFgPQNF-GVSQEEAEALAREKLALVGISESLFEKnPFELSGGQMRRVAIAGILAME 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 502908369 180 PSIILADEPTGNLDLHTGLKLINLLKEINEkKGVTIVTATHdlKMVDVSD 229
Cdd:PRK13649 164 PKILVLDEPTAGLDPKGRKELMTLFKKLHQ-SGMTIVLVTH--LMDDVAN 210
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
30-239 |
2.71e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 100.96 E-value: 2.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 30 YYKMGKFIVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYI-DGVDIAMLDAYELAWLRaKKIGYI 108
Cdd:PRK13643 11 YQPNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgDIVVSSTSKQKEIKPVR-KKVGVV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 109 FQtfnlIPVLTAVENVML------PMIFvGTPYEDAIVKAKKLLELVGLGK-FIHHKPAELSGGQQQRVAAARALANDPS 181
Cdd:PRK13643 90 FQ----FPESQLFEETVLkdvafgPQNF-GIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502908369 182 IILADEPTGNLDLHTGLKLINLLKEINEkKGVTIVTATHDLKMV-DVSDRIIWIRDGKI 239
Cdd:PRK13643 165 VLVLDEPTAGLDPKARIEMMQLFESIHQ-SGQTVVLVTHLMDDVaDYADYVYLLEKGHI 222
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
38-248 |
3.30e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 100.65 E-value: 3.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 38 VKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAwlraKKIGYIFQTFNLIPV 117
Cdd:PRK13652 17 KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVR----KFVGLVFQNPDDQIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 118 LTAVE-NVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLHT 196
Cdd:PRK13652 93 SPTVEqDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502908369 197 GLKLINLLKEINEKKGVTIVTATHDLKMVDVSDRIIWIRD-------GKIEKIELRRDI 248
Cdd:PRK13652 173 VKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDkgrivayGTVEEIFLQPDL 231
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-239 |
3.52e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 100.57 E-value: 3.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 21 VVEAVEVKKYYkmGKFivKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAyelawl 100
Cdd:COG4152 1 MLELKGLTKRF--GDK--TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDR------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 101 raKKIGYIFQTFNLIPVLTAVENvmlpMIFV----GTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARAL 176
Cdd:COG4152 71 --RRIGYLPEERGLYPKMKVGEQ----LVYLarlkGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAAL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502908369 177 ANDPSIILADEPTGNLD-LHTGLkLINLLKEINEkKGVTIVTATHDLKMVD-VSDRIIWIRDGKI 239
Cdd:COG4152 145 LHDPELLILDEPFSGLDpVNVEL-LKDVIRELAA-KGTTVIFSSHQMELVEeLCDRIVIINKGRK 207
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
38-241 |
4.44e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 101.08 E-value: 4.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 38 VKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAWL--------RAKK----I 105
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELITnpyskkikNFKElrrrV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 106 GYIFQTFNLIPVLTAVE-NVMLPMIFVGTPYEDAIVKAKKLLELVGLGK-FIHHKPAELSGGQQQRVAAARALANDPSII 183
Cdd:PRK13631 119 SMVFQFPEYQLFKDTIEkDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDsYLERSPFGLSGGQKRRVAIAGILAIQPEIL 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502908369 184 LADEPTGNLDLHTGLKLINLLKEiNEKKGVTIVTATHDLKMV-DVSDRIIWIRDGKIEK 241
Cdd:PRK13631 199 IFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVlEVADEVIVMDKGKILK 256
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
52-242 |
5.14e-25 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 101.64 E-value: 5.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 52 EYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDgvDIAMLDAYElawlrAKK-IGYIFQTFNLIPVLTAVENVMLPMIF 130
Cdd:PRK11000 30 EFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIG--EKRMNDVPP-----AERgVGMVFQSYALYPHLSVAENMSFGLKL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 131 VGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLHTGLKLINLLKEINEK 210
Cdd:PRK11000 103 AGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKR 182
|
170 180 190
....*....|....*....|....*....|...
gi 502908369 211 KGVTIVTATHD-LKMVDVSDRIIWIRDGKIEKI 242
Cdd:PRK11000 183 LGRTMIYVTHDqVEAMTLADKIVVLDAGRVAQV 215
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
34-239 |
7.64e-25 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 99.29 E-value: 7.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 34 GKFIVKalDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAwlraKKIGYIFQ--- 110
Cdd:PRK10253 18 GKYTVA--ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA----RRIGLLAQnat 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 111 TFNLIPVLTAVENVMLPMIFVGTPY----EDAIVKAkklLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILAD 186
Cdd:PRK10253 92 TPGDITVQELVARGRYPHQPLFTRWrkedEEAVTKA---MQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502908369 187 EPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDL-KMVDVSDRIIWIRDGKI 239
Cdd:PRK10253 169 EPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLnQACRYASHLIALREGKI 222
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
38-238 |
8.20e-25 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 102.31 E-value: 8.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 38 VKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLdRPTG---GKVYIDGvdiAMLDAYELAWLRAKKIGYIFQTFNL 114
Cdd:PRK13549 18 VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHGtyeGEIIFEG---EELQASNIRDTERAGIAIIHQELAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 115 IPVLTAVENvmlpmIFVG---TP-----YEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILAD 186
Cdd:PRK13549 94 VKELSVLEN-----IFLGneiTPggimdYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502908369 187 EPTGNLDLHTGLKLINLLKEInEKKGVTIVTATHDLKMV-DVSDRIIWIRDGK 238
Cdd:PRK13549 169 EPTASLTESETAVLLDIIRDL-KAHGIACIYISHKLNEVkAISDTICVIRDGR 220
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
30-239 |
1.36e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 99.31 E-value: 1.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 30 YYKMGKFIVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDI--AMLDAYELAWLRaKKIGY 107
Cdd:PRK13645 16 YAKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpaNLKKIKEVKRLR-KEIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 108 IFQ--TFNLIPVlTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGK-FIHHKPAELSGGQQQRVAAARALANDPSIIL 184
Cdd:PRK13645 95 VFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEdYVKRSPFELSGGQKRRVALAGIIAMDGNTLV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502908369 185 ADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMV-DVSDRIIWIRDGKI 239
Cdd:PRK13645 174 LDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVlRIADEVIVMHEGKV 229
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
13-238 |
1.68e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 99.91 E-value: 1.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 13 PSRRKLEYVVEAVEVKKYYKmGKFIVkalDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAml 92
Cdd:PRK13536 33 IPGSMSTVAIDLAGVSKSYG-DKAVV---NGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP-- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 93 dayELAWLRAKKIGYIFQTFNLIPVLTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAA 172
Cdd:PRK13536 107 ---ARARLARARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502908369 173 ARALANDPSIILADEPTGNLDLHTGLKLINLLKEInEKKGVTIVTATHDLKMVD-VSDRIIWIRDGK 238
Cdd:PRK13536 184 ARALINDPQLLILDEPTTGLDPHARHLIWERLRSL-LARGKTILLTTHFMEEAErLCDRLCVLEAGR 249
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
40-222 |
3.65e-24 |
|
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: 95.89 E-value: 3.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 40 ALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAmldayELAWLRAKKIGYIFQTFNLIPVLT 119
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLA-----EQRDEPHENILYLGHLPGLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 120 AVENVMlpmiFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLhTGLK 199
Cdd:TIGR01189 90 ALENLH----FWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK-AGVA 164
|
170 180
....*....|....*....|....
gi 502908369 200 LIN-LLKEINEKKGVTIVTATHDL 222
Cdd:TIGR01189 165 LLAgLLRAHLARGGIVLLTTHQDL 188
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
38-241 |
4.08e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 100.95 E-value: 4.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 38 VKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAmldAYELAWLRaKKIGYIFQTfnliPV 117
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLV---QYDHHYLH-RQVALVGQE----PV 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 118 L---TAVENVMLPMIFvgTPYEDAIVKAKKLLELVGLGKF-------IHHKPAELSGGQQQRVAAARALANDPSIILADE 187
Cdd:TIGR00958 566 LfsgSVRENIAYGLTD--TPDEEIMAAAKAANAHDFIMEFpngydteVGEKGSQLSGGQKQRIAIARALVRKPRVLILDE 643
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502908369 188 PTGNLDLHTGlkliNLLKEINEKKGVTIVTATHDLKMVDVSDRIIWIRDGKIEK 241
Cdd:TIGR00958 644 ATSALDAECE----QLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVE 693
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
41-239 |
6.64e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 96.65 E-value: 6.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGV------DIAMLDAYELAwlraKKIGYIFQTFNL 114
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLR----KEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 115 IPVLTAVENVMLPMIFVGTPYEDAIVK-AKKLLELVGLGKFIHHK---PA-ELSGGQQQRVAAARALANDPSIILADEPT 189
Cdd:PRK14246 102 FPHLSIYDNIAYPLKSHGIKEKREIKKiVEECLRKVGLWKEVYDRlnsPAsQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502908369 190 GNLDLHTGLKLINLLKEIneKKGVTIVTATHDLKMV-DVSDRIIWIRDGKI 239
Cdd:PRK14246 182 SMIDIVNSQAIEKLITEL--KNEIAIVIVSHNPQQVaRVADYVAFLYNGEL 230
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
42-233 |
8.69e-24 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 94.87 E-value: 8.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 42 DGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLD---AYELAWLrakkiGYIfqtfNLI-PV 117
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRdeyHQDLLYL-----GHQ----PGIkTE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 118 LTAVENVMLPMIFVGTPYEDAIVKAkklLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLHTG 197
Cdd:PRK13538 89 LTALENLRFYQRLHGPGDDEALWEA---LAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGV 165
|
170 180 190
....*....|....*....|....*....|....*.
gi 502908369 198 LKLINLLKEINEKKGVTIVTATHDLKMVDVSDRIIW 233
Cdd:PRK13538 166 ARLEALLAQHAEQGGMVILTTHQDLPVASDKVRKLR 201
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
19-239 |
8.88e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 96.84 E-value: 8.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 19 EYVVEAVEVKKYYKMGkfiVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMlDAYELA 98
Cdd:PRK13636 3 DYILKVEELNYNYSDG---THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDY-SRKGLM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 99 WLRaKKIGYIFQT-FNLIPVLTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKfIHHKPAE-LSGGQQQRVAAARAL 176
Cdd:PRK13636 79 KLR-ESVGMVFQDpDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEH-LKDKPTHcLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502908369 177 ANDPSIILADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMVDV-SDRIIWIRDGKI 239
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLyCDNVFVMKEGRV 220
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
22-238 |
9.24e-24 |
|
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: 93.28 E-value: 9.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 22 VEAVEVKKYYKmGKFIvkaLDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVyidgvdiamldayelAWLR 101
Cdd:cd03221 1 IELENLSKTYG-GKLL---LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV---------------TWGS 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 102 AKKIGYIFQtfnlipvltavenvmlpmifvgtpyedaivkakkllelvglgkfihhkpaeLSGGQQQRVAAARALANDPS 181
Cdd:cd03221 62 TVKIGYFEQ---------------------------------------------------LSGGEKMRLALAKLLLENPN 90
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502908369 182 IILADEPTGNLDLHTGLKLINLLKeinEKKGvTIVTATHDLKMVD-VSDRIIWIRDGK 238
Cdd:cd03221 91 LLLLDEPTNHLDLESIEALEEALK---EYPG-TVILVSHDRYFLDqVATKIIELEDGK 144
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
38-246 |
1.20e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 99.54 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 38 VKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAWLRaKKIGYIFQT--FNLI 115
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALR-RDIQFIFQDpyASLD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 116 PVLTAVENVMLPMIFVGT-PYEDAIVKAKKLLELVGLgKFIH--HKPAELSGGQQQRVAAARALANDPSIILADEPTGNL 192
Cdd:PRK10261 416 PRQTVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGL-LPEHawRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502908369 193 DLHTGLKLINLLKEINEKKGVTIVTATHDLKMVD-VSDRIIWIRDGKIEKIELRR 246
Cdd:PRK10261 495 DVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVErISHRVAVMYLGQIVEIGPRR 549
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-242 |
2.22e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 94.91 E-value: 2.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 18 LEYVVEAVEVKKYYKMGKFIvkalDGVTFNVKRREYVSIMGPSGSGKTTL---FNMIGGL--DRPTGGKVYIDGVDIAM- 91
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNHVI----KGVDLKIPQNGVFALMGPSGCGKSTLlrtFNRLLELneEARVEGEVRLFGRNIYSp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 92 -LDAYELAwlraKKIGYIFQTFNLIPVLTAVENVMLpmifvGTPYEDAIVKAKKLLELV--GLGKF---------IHHKP 159
Cdd:PRK14267 77 dVDPIEVR----REVGMVFQYPNPFPHLTIYDNVAI-----GVKLNGLVKSKKELDERVewALKKAalwdevkdrLNDYP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 160 AELSGGQQQRVAAARALANDPSIILADEPTGNLDLHTGLKLINLLKEIneKKGVTIVTATHD-LKMVDVSDRIIWIRDGK 238
Cdd:PRK14267 148 SNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFEL--KKEYTIVLVTHSpAQAARVSDYVAFLYLGK 225
|
....
gi 502908369 239 IEKI 242
Cdd:PRK14267 226 LIEV 229
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
41-239 |
2.46e-23 |
|
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: 94.46 E-value: 2.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMldaYELAWLRaKKIGYIFQTfnliPVLTA 120
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQ---YEHKYLH-SKVSLVGQE----PVLFA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 121 ---VENVMLPMifVGTPYEDAIVKAKKllelVGLGKFIH-----------HKPAELSGGQQQRVAAARALANDPSIILAD 186
Cdd:cd03248 102 rslQDNIAYGL--QSCSFECVKEAAQK----AHAHSFISelasgydtevgEKGSQLSGGQKQRVAIARALIRNPQVLILD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502908369 187 EPTGNLDLHTGLKLINLLKEINEKKGVTIVtaTHDLKMVDVSDRIIWIRDGKI 239
Cdd:cd03248 176 EATSALDAESEQQVQQALYDWPERRTVLVI--AHRLSTVERADQILVLDGGRI 226
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
31-239 |
3.56e-23 |
|
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: 98.27 E-value: 3.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 31 YKMGkFIVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAWLrakkIGYIFQ 110
Cdd:TIGR01193 481 YSYG-YGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQF----INYLPQ 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 111 TfnlipvltavenvmlPMIFVGTPYEDAIVKAK---------KLLELVGLGKFIHHKP-----------AELSGGQQQRV 170
Cdd:TIGR01193 556 E---------------PYIFSGSILENLLLGAKenvsqdeiwAACEIAEIKDDIENMPlgyqtelseegSSISGGQKQRI 620
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502908369 171 AAARALANDPSIILADEPTGNLDLHTGLKLINLLKEINEKkgvTIVTATHDLKMVDVSDRIIWIRDGKI 239
Cdd:TIGR01193 621 ALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQSDKIIVLDHGKI 686
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
56-239 |
4.42e-23 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 96.10 E-value: 4.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 56 IMGPSGSGKTTLFNMIGGLDRPTGGKVYIDgvDIAMLDAYELAWLRAKK--IGYIFQTFNLIPVLTAVENVMLPMIFVGT 133
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLN--GRVLFDAEKGICLPPEKrrIGYVFQDARLFPHYKVRGNLRYGMAKSMV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 134 PYEDAIVkakkllELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLHTGLKLINLLKEINEKKGV 213
Cdd:PRK11144 107 AQFDKIV------ALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINI 180
|
170 180
....*....|....*....|....*..
gi 502908369 214 TIVTATHDL-KMVDVSDRIIWIRDGKI 239
Cdd:PRK11144 181 PILYVSHSLdEILRLADRVVVLEQGKV 207
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
37-225 |
5.27e-23 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 95.56 E-value: 5.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 37 IVKALDGVTFNVKRREYVSIMGPSGSGKT-TLFNMIGGLDRP--TGGKVYIDGVDIAMLDAYELAWLRAKKIGYIFQ--T 111
Cdd:PRK09473 28 DVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREILNLPEKELNKLRAEQISMIFQdpM 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 112 FNLIPVLTAVENVM-LPMIFVGTPYEDAIVKAKKLLELVGLG---KFIHHKPAELSGGQQQRVAAARALANDPSIILADE 187
Cdd:PRK09473 108 TSLNPYMRVGEQLMeVLMLHKGMSKAEAFEESVRMLDAVKMPearKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADE 187
|
170 180 190
....*....|....*....|....*....|....*...
gi 502908369 188 PTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMV 225
Cdd:PRK09473 188 PTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVV 225
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
39-239 |
1.37e-22 |
|
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: 91.70 E-value: 1.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 39 KALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDayeLAWLRaKKIGYIFQTfnlipvl 118
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIP---LEDLR-SSLTIIPQD------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 119 tavenvmlPMIFVGT------PY----EDAIVKAKKLLElVGLgkfihhkpaELSGGQQQRVAAARALANDPSIILADEP 188
Cdd:cd03369 91 --------PTLFSGTirsnldPFdeysDEEIYGALRVSE-GGL---------NLSQGQRQLLCLARALLKRPRVLVLDEA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502908369 189 TGNLDLHTGLKLINLLKEinEKKGVTIVTATHDLKMVDVSDRIIWIRDGKI 239
Cdd:cd03369 153 TASIDYATDALIQKTIRE--EFTNSTILTIAHRLRTIIDYDKILVMDAGEV 201
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
39-239 |
2.71e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 92.15 E-value: 2.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 39 KALDGVTFNVKRREYVSIMGPSGSGKTTLF---NMIGGL--DRPTGGKVYIDGVDI--AMLDAYELAwlraKKIGYIFQT 111
Cdd:PRK14239 19 KALNSVSLDFYPNEITALIGPSGSGKSTLLrsiNRMNDLnpEVTITGSIVYNGHNIysPRTDTVDLR----KEIGMVFQQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 112 FNLIPvLTAVENVMLPMIFVGtpyedaiVKAKKLLE------LVGLGKF------IHHKPAELSGGQQQRVAAARALAND 179
Cdd:PRK14239 95 PNPFP-MSIYENVVYGLRLKG-------IKDKQVLDeaveksLKGASIWdevkdrLHDSALGLSGGQQQRVCIARVLATS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502908369 180 PSIILADEPTGNLDLHTGLKLINLLkeINEKKGVTIVTATHDLKMVD-VSDRIIWIRDGKI 239
Cdd:PRK14239 167 PKIILLDEPTSALDPISAGKIEETL--LGLKDDYTMLLVTRSMQQASrISDRTGFFLDGDL 225
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
40-239 |
3.66e-22 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 95.03 E-value: 3.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 40 ALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDayeLAWLRaKKIGYIFQT---FNlip 116
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT---RASLR-RNIAVVFQDaglFN--- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 117 vLTAVENvmlpmIFVGTPyeDA----IVKAKKL---LELV-----GLGKFIHHKPAELSGGQQQRVAAARALANDPSIIL 184
Cdd:PRK13657 423 -RSIEDN-----IRVGRP--DAtdeeMRAAAERaqaHDFIerkpdGYDTVVGERGRQLSGGERQRLAIARALLKDPPILI 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502908369 185 ADEPTGNLDLHTGLKLINLLKEIneKKGVTIVTATHDLKMVDVSDRIIWIRDGKI 239
Cdd:PRK13657 495 LDEATSALDVETEAKVKAALDEL--MKGRTTFIIAHRLSTVRNADRILVFDNGRV 547
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
39-239 |
4.51e-22 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 91.53 E-value: 4.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 39 KALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELA-----WLRAKKIGYIFQtfN 113
Cdd:PRK11701 20 KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSeaerrRLLRTEWGFVHQ--H 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 114 ----LIPVLTAVENVMLPMIFVGTP-YEDAIVKAKKLLELVGLG-KFIHHKPAELSGGQQQRVAAARALANDPSIILADE 187
Cdd:PRK11701 98 prdgLRMQVSAGGNIGERLMAVGARhYGDIRATAGDWLERVEIDaARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502908369 188 PTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMVDV-SDRIIWIRDGKI 239
Cdd:PRK11701 178 PTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLlAHRLLVMKQGRV 230
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
41-220 |
5.46e-22 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 90.32 E-value: 5.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELawlrakkIGYIFQTFNLIPVLTA 120
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA-------CHYLGHRNAMKPALTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 121 VENVMLPMIFVGTPyEDAIVKAkklLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLHTGLKL 200
Cdd:PRK13539 91 AENLEFWAAFLGGE-ELDIAAA---LEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALF 166
|
170 180
....*....|....*....|
gi 502908369 201 INLLKEINEKKGvTIVTATH 220
Cdd:PRK13539 167 AELIRAHLAQGG-IVIAATH 185
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
42-239 |
6.84e-22 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 90.91 E-value: 6.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 42 DGVTFNVKRREYVSIMGPSGSGKTtlFNMIGGLD------RPTGGKVYIDGVDIAmldayeLAWLRAKKIGYIFQT---- 111
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGilpagvRQTAGRVLLDGKPVA------PCALRGRKIATIMQNprsa 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 112 FNliPVLTAVENVMLPMIFVGTPYEDAIVKAkkLLELVGLG---KFIHHKPAELSGGQQQRVAAARALANDPSIILADEP 188
Cdd:PRK10418 92 FN--PLHTMHTHARETCLALGKPADDATLTA--ALEAVGLEnaaRVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502908369 189 TGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMV-DVSDRIIWIRDGKI 239
Cdd:PRK10418 168 TTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVaRLADDVAVMSHGRI 219
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
40-225 |
7.68e-22 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 91.48 E-value: 7.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 40 ALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLdayelawLRAKKIGYIFQTFNL---IP 116
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQA-------LQKNLVAYVPQSEEVdwsFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 117 VLtaVENVML-------PMIFVGTPYEDAIVKAKklLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPT 189
Cdd:PRK15056 95 VL--VEDVVMmgryghmGWLRRAKKRDRQIVTAA--LARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPF 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 502908369 190 GNLDLHTGLKLINLLKEINEkKGVTIVTATHDLKMV 225
Cdd:PRK15056 171 TGVDVKTEARIISLLRELRD-EGKTMLVSTHNLGSV 205
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
34-220 |
1.57e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 92.95 E-value: 1.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 34 GKFIVKALDgvtFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKvyidgvdIAMLDAYELAWL--RAkkigYIfqt 111
Cdd:COG4178 375 GRPLLEDLS---LSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGR-------IARPAGARVLFLpqRP----YL--- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 112 fnliPVLTAVENVMLPmiFVGTPYEDAIVKAkkLLELVGLGKFIHHKPAE------LSGGQQQRVAAARALANDPSIILA 185
Cdd:COG4178 438 ----PLGTLREALLYP--ATAEAFSDAELRE--ALEAVGLGHLAERLDEEadwdqvLSLGEQQRLAFARLLLHKPDWLFL 509
|
170 180 190
....*....|....*....|....*....|....*
gi 502908369 186 DEPTGNLDLHTGLKLINLLKEinEKKGVTIVTATH 220
Cdd:COG4178 510 DEATSALDEENEAALYQLLRE--ELPGTTVISVGH 542
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
21-240 |
1.64e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.82 E-value: 1.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 21 VVEAVEVKKYYKmGKFIvkaLDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIdGVDIamldayelawl 100
Cdd:COG0488 315 VLELEGLSKSYG-DKTL---LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 101 rakKIGYIFQTF-NLIPVLTAVENVMlpmifvgtpyedAIVKAKKLLELVG-LGKFI-----HHKPAE-LSGGQQQRVAA 172
Cdd:COG0488 379 ---KIGYFDQHQeELDPDKTVLDELR------------DGAPGGTEQEVRGyLGRFLfsgddAFKPVGvLSGGEKARLAL 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 173 ARALANDPSIILADEPTGNLDLHTglklINLLKE-INEKKGvTIVTATHDLKMVD-VSDRIIWIRDGKIE 240
Cdd:COG0488 444 AKLLLSPPNVLLLDEPTNHLDIET----LEALEEaLDDFPG-TVLLVSHDRYFLDrVATRILEFEDGGVR 508
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
38-255 |
1.81e-21 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 92.67 E-value: 1.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 38 VKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAwlrAKKIGYIFQTFNLIPV 117
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAAL---AAGVAIIYQELHLVPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 118 LTAVENVMLPMIfvgtPYEDAIVKAKKL-----LELVGLGKFI--HHKPAELSGGQQQRVAAARALANDPSIILADEPTG 190
Cdd:PRK11288 94 MTVAENLYLGQL----PHKGGIVNRRLLnyearEQLEHLGVDIdpDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502908369 191 NLDLHTGLKLINLLKEInEKKGVTIVTATHDLKMVD-VSDRIIWIRDGKieKIELRRDIEAVMGEQ 255
Cdd:PRK11288 170 SLSAREIEQLFRVIREL-RAEGRVILYVSHRMEEIFaLCDAITVFKDGR--YVATFDDMAQVDRDQ 232
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
38-238 |
2.24e-21 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 92.61 E-value: 2.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 38 VKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDG----------VDIAMLDAYELAWLRAKKIGY 107
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQSAAQMRHVRGADMAM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 108 IFQ--TFNLIPVLTAVENVMLPM-IFVGTPYEDAIVKAKKLLELVGLGK---FIHHKPAELSGGQQQRVAAARALANDPS 181
Cdd:PRK10261 109 IFQepMTSLNPVFTVGEQIAESIrLHQGASREEAMVEAKRMLDQVRIPEaqtILSRYPHQLSGGMRQRVMIAMALSCRPA 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502908369 182 IILADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMV-DVSDRIIWIRDGK 238
Cdd:PRK10261 189 VLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVaEIADRVLVMYQGE 246
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
41-232 |
2.34e-21 |
|
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: 88.32 E-value: 2.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGvdiAMLDAYELAWLRAkkIGYIFQTFNLIPVLTA 120
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG---GPLDFQRDSIARG--LLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 121 VENVMLPMIFVGTpyeDAIVKAkklLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLHTGLKL 200
Cdd:cd03231 91 LENLRFWHADHSD---EQVEEA---LARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF 164
|
170 180 190
....*....|....*....|....*....|..
gi 502908369 201 INLLKEINEKKGVTIVTATHDLKMVDVSDRII 232
Cdd:cd03231 165 AEAMAGHCARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
41-222 |
2.39e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 89.69 E-value: 2.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAwlrakkigyifQTFNLIP-VLT 119
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA-----------RRLALLPqHHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 120 AVENVML-PMIFVG-TPY---------ED-AIVKakKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADE 187
Cdd:PRK11231 87 TPEGITVrELVAYGrSPWlslwgrlsaEDnARVN--QAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDE 164
|
170 180 190
....*....|....*....|....*....|....*
gi 502908369 188 PTGNLDLHTGLKLINLLKEINEkKGVTIVTATHDL 222
Cdd:PRK11231 165 PTTYLDINHQVELMRLMRELNT-QGKTVVTVLHDL 198
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
38-239 |
3.03e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 92.01 E-value: 3.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 38 VKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYElawLRAKKIGYI---FQTFNL 114
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRE---RRRLGVAYIpedRLGRGL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 115 IPVLTAVENVMLpmifvGTPYEDAIVK------------AKKLLElvglgKF------IHHKPAELSGGQQQRVAAARAL 176
Cdd:COG3845 348 VPDMSVAENLIL-----GRYRRPPFSRggfldrkairafAEELIE-----EFdvrtpgPDTPARSLSGGNQQKVILAREL 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502908369 177 ANDPSIILADEPTGNLDL------HTglkliNLLKEINEKKGVTIVTAthDLkmvD----VSDRIIWIRDGKI 239
Cdd:COG3845 418 SRDPKLLIAAQPTRGLDVgaiefiHQ-----RLLELRDAGAAVLLISE--DL---DeilaLSDRIAVMYEGRI 480
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
36-239 |
3.32e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 92.22 E-value: 3.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 36 FIVKALDG------VTFNVKRREYVSIMGPSGSGKTTLFNMIGGLdRPTGGKVYIDGVDIAMLDayELAWLRakKIGYIF 109
Cdd:PRK11174 355 LEILSPDGktlagpLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELD--PESWRK--HLSWVG 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 110 QTFNLiPVLTAVENVMLpmifvGTP-YEDAIVKAkkLLELVGLGKFIHHKP-----------AELSGGQQQRVAAARALA 177
Cdd:PRK11174 430 QNPQL-PHGTLRDNVLL-----GNPdASDEQLQQ--ALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALL 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502908369 178 NDPSIILADEPTGNLDLHTGLKLINLLKEINEKKgvTIVTATHDLKMVDVSDRIIWIRDGKI 239
Cdd:PRK11174 502 QPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQ--TTLMVTHQLEDLAQWDQIWVMQDGQI 561
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
21-238 |
3.53e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 90.25 E-value: 3.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 21 VVEAVEVKKYYkmGKFIVkaLDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAmldayELAWL 100
Cdd:PRK13537 7 PIDFRNVEKRY--GDKLV--VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVP-----SRARH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 101 RAKKIGYIFQTFNLIPVLTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDP 180
Cdd:PRK13537 78 ARQRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502908369 181 SIILADEPTGNLDLHTGLKLINLLKEInEKKGVTIVTATHDLKMVD-VSDRIIWIRDGK 238
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLRSL-LARGKTILLTTHFMEEAErLCDRLCVIEEGR 215
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
39-229 |
3.60e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 89.33 E-value: 3.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 39 KALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRpTGGKVYIDG-VDIAMLDAYE----LAWLRaKKIGYIFQTFN 113
Cdd:PRK14258 21 KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGrVEFFNQNIYErrvnLNRLR-RQVSMVHPKPN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 114 LIPvLTAVENVMLPMIFVG----TPYEDAIVKAKKLLELVGLGKFIHHKPA-ELSGGQQQRVAAARALANDPSIILADEP 188
Cdd:PRK14258 99 LFP-MSVYDNVAYGVKIVGwrpkLEIDDIVESALKDADLWDEIKHKIHKSAlDLSGGQQQRLCIARALAVKPKVLLMDEP 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 502908369 189 TGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMVD-VSD 229
Cdd:PRK14258 178 CFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSrLSD 219
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
40-239 |
1.21e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 90.53 E-value: 1.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 40 ALDGVTFNVKRREYVSIMGPSGSGKTT----LFNMIggldrPTGGKVYIDGVDIAMLDAYELAWLRaKKIGYIFQTFN-- 113
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLLPVR-HRIQVVFQDPNss 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 114 LIPVLTaVENVMLPMIFVGTPY------EDAIVKAkklLELVGLGKFIHHK-PAELSGGQQQRVAAARALANDPSIILAD 186
Cdd:PRK15134 375 LNPRLN-VLQIIEEGLRVHQPTlsaaqrEQQVIAV---MEEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILD 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502908369 187 EPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMV-DVSDRIIWIRDGKI 239
Cdd:PRK15134 451 EPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVrALCHQVIVLRQGEV 504
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
39-239 |
2.01e-20 |
|
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: 87.19 E-value: 2.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 39 KALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAWLRAKKI-----GYIFQTF- 112
Cdd:TIGR02323 17 KGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLSEAERRRLmrtewGFVHQNPr 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 113 -NLIPVLTAVENVMLPMIFVGTP-YEDAIVKAKKLLELVGLGKF-IHHKPAELSGGQQQRVAAARALANDPSIILADEPT 189
Cdd:TIGR02323 97 dGLRMRVSAGANIGERLMAIGARhYGNIRATAQDWLEEVEIDPTrIDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDEPT 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502908369 190 GNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMVD-VSDRIIWIRDGKI 239
Cdd:TIGR02323 177 GGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARlLAQRLLVMQQGRV 227
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
38-247 |
2.02e-20 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 89.85 E-value: 2.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 38 VKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLdRPTG---GKVYIDGvdiamldayELAWLR------AKKIGYI 108
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHGsyeGEILFDG---------EVCRFKdirdseALGIVII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 109 FQTFNLIPVLTAVENvmlpmIFVGTP--------YEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDP 180
Cdd:NF040905 84 HQELALIPYLSIAEN-----IFLGNErakrgvidWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502908369 181 SIILADEPTGNLDLHTGLKLINLLKEInEKKGVTIVTATHDLKMV-DVSDRIIWIRDGK-IEKIELRRD 247
Cdd:NF040905 159 KLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIrRVADSITVLRDGRtIETLDCRAD 226
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
40-238 |
2.05e-20 |
|
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: 85.98 E-value: 2.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 40 ALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGvdiamldayelawlrakKIGYIFQTfnliPVL- 118
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-----------------SIAYVSQE----PWIq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 119 --TAVENVmlpmIFvGTPYE----DAIVKA---KKLLELVGLG--KFIHHKPAELSGGQQQRVAAARALANDPSIILADE 187
Cdd:cd03250 79 ngTIRENI----LF-GKPFDeeryEKVIKAcalEPDLEILPDGdlTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502908369 188 PTGNLDLHTGLKLIN--LLKEINEKKgvTIVTATHDLKMVDVSDRIIWIRDGK 238
Cdd:cd03250 154 PLSAVDAHVGRHIFEncILGLLLNNK--TRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
39-239 |
2.11e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 86.87 E-value: 2.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 39 KALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYElawlRAKK-IGYIFQTFNLIPV 117
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA----RARRgIGYLPQEASIFRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 118 LTAVENVMLPM-IFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLHT 196
Cdd:PRK10895 93 LSVYDNLMAVLqIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPIS 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 502908369 197 GLKLINLLKEINEkKGVTIVTATHDLK-MVDVSDRIIWIRDGKI 239
Cdd:PRK10895 173 VIDIKRIIEHLRD-SGLGVLITDHNVReTLAVCERAYIVSQGHL 215
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
41-222 |
3.60e-20 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 86.43 E-value: 3.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLdRPTGGKVYIDGVDIAMLDAYELAWLRAkkigYIFQTFNLIPVLTA 120
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAELARHRA----YLSQQQSPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 121 VENVMLPMIFVGTPYEDAIVKAKkLLELVGLGKFIHHKPAELSGGQQQRVAAARAL-----ANDPS--IILADEPTGNLD 193
Cdd:COG4138 87 FQYLALHQPAGASSEAVEQLLAQ-LAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPEgqLLLLDEPMNSLD 165
|
170 180
....*....|....*....|....*....
gi 502908369 194 LHTGLKLINLLKEINEkKGVTIVTATHDL 222
Cdd:COG4138 166 VAQQAALDRLLRELCQ-QGITVVMSSHDL 193
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
16-239 |
3.89e-20 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 89.69 E-value: 3.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 16 RKLEYVVEAVEVKKYYKM----GKfivKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAM 91
Cdd:TIGR01257 920 RELPGLVPGVCVKNLVKIfepsGR---PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET 996
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 92 -LDAYElawlraKKIGYIFQTFNLIPVLTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLgkfiHHKPAE----LSGGQ 166
Cdd:TIGR01257 997 nLDAVR------QSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGL----HHKRNEeaqdLSGGM 1066
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502908369 167 QQRVAAARALANDPSIILADEPTGNLDLHTGLKLINLLkeINEKKGVTIVTATHDLKMVDV-SDRIIWIRDGKI 239
Cdd:TIGR01257 1067 QRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLlGDRIAIISQGRL 1138
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
38-238 |
4.41e-20 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 88.73 E-value: 4.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 38 VKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLdRPTG---GKVYIDGvdiAMLDAYELAWLRAKKIGYIFQTFNL 114
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHGtwdGEIYWSG---SPLKASNIRDTERAGIVIIHQELTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 115 IPVLTAVENvmlpmIFVG---------TPYEDAIVKAKKLLELVGLGKFIHHKP-AELSGGQQQRVAAARALANDPSIIL 184
Cdd:TIGR02633 90 VPELSVAEN-----IFLGneitlpggrMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQARLLI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502908369 185 ADEPTGNLDLHTGLKLINLLKEInEKKGVTIVTATHDLKMVD-VSDRIIWIRDGK 238
Cdd:TIGR02633 165 LDEPSSSLTEKETEILLDIIRDL-KAHGVACVYISHKLNEVKaVCDTICVIRDGQ 218
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
39-239 |
6.67e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 87.10 E-value: 6.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 39 KALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGL-DRPtgGKVY-----IDGVDIAMLDAYELAWLRAKKIGYIFQ-- 110
Cdd:PRK11022 21 RAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLiDYP--GRVMaekleFNGQDLQRISEKERRNLVGAEVAMIFQdp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 111 TFNLIPVLTAVENVMLPM-IFVGTPYEDAIVKAKKLLELVGL---GKFIHHKPAELSGGQQQRVAAARALANDPSIILAD 186
Cdd:PRK11022 99 MTSLNPCYTVGFQIMEAIkVHQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIAD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502908369 187 EPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMV-DVSDRIIWIRDGKI 239
Cdd:PRK11022 179 EPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVaEAAHKIIVMYAGQV 232
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
27-237 |
7.20e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 88.30 E-value: 7.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 27 VKKYYKMGKF-----IVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLD---AYELA 98
Cdd:PRK09700 2 ATPYISMAGIgksfgPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDhklAAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 99 wlrakkIGYIFQTFNLIPVLTAVENV----MLPMIFVGTP---YEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVA 171
Cdd:PRK09700 82 ------IGIIYQELSVIDELTVLENLyigrHLTKKVCGVNiidWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502908369 172 AARALANDPSIILADEPTGNLDLHTGLKLINLLKEInEKKGVTIVTATHDLKMV-DVSDRIIWIRDG 237
Cdd:PRK09700 156 IAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQL-RKEGTAIVYISHKLAEIrRICDRYTVMKDG 221
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
39-239 |
2.62e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 86.80 E-value: 2.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 39 KALDGVTFNVKRREYVSIMGPSGSGKTTLFNMiggLDR---PTGGKVYIDGVDIAmldAYELAWLRAkkigyifqtfnLI 115
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQL---LTRawdPQQGEILLNGQPIA---DYSEAALRQ-----------AI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 116 PVLTavenvMLPMIFVGTPYED-AIVKAK----KL---LELVGLGKFIHHKPA----------ELSGGQQQRVAAARALA 177
Cdd:PRK11160 417 SVVS-----QRVHLFSATLRDNlLLAAPNasdeALievLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGIARALL 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502908369 178 NDPSIILADEPTGNLDLHTGLKLINLLKEINEKKgvTIVTATHDLKMVDVSDRIIWIRDGKI 239
Cdd:PRK11160 492 HDAPLLLLDEPTEGLDAETERQILELLAEHAQNK--TVLMITHRLTGLEQFDRICVMDNGQI 551
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
18-229 |
2.80e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 84.06 E-value: 2.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 18 LEYVVEAVEVKKYYkmGKFIvkALDGVTFNVKRREYVSIMGPSGSGKTTL---FNMIGGL--DRPTGGKVYIDGVDI--A 90
Cdd:PRK14243 7 TETVLRTENLNVYY--GSFL--AVKNVWLDIPKNQITAFIGPSGCGKSTIlrcFNRLNDLipGFRVEGKVTFHGKNLyaP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 91 MLDAYELAwlraKKIGYIFQTFNLIPVlTAVENVML-PMI---------FVGTPYEDAIV--KAKKLLELVGLGkfihhk 158
Cdd:PRK14243 83 DVDPVEVR----RRIGMVFQKPNPFPK-SIYDNIAYgARIngykgdmdeLVERSLRQAALwdEVKDKLKQSGLS------ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502908369 159 paeLSGGQQQRVAAARALANDPSIILADEPTGNLDLHTGLKLINLLKEINEKkgVTIVTATHDLKMVD-VSD 229
Cdd:PRK14243 152 ---LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAArVSD 218
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
38-238 |
3.90e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 86.21 E-value: 3.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 38 VKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGldrptggkvyidgvdIAMLDAYELAWL------------RAKKI 105
Cdd:PRK10762 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTG---------------IYTRDAGSILYLgkevtfngpkssQEAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 106 GYIFQTFNLIPVLTAVENVMLPMIFVGT----PYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPS 181
Cdd:PRK10762 82 GIIHQELNLIPQLTIAENIFLGREFVNRfgriDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESK 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 182 IILADEPTGNLdlhTGLKLINLLKEINEKK--GVTIVTATHDLKMV-DVSDRIIWIRDGK 238
Cdd:PRK10762 162 VIIMDEPTDAL---TDTETESLFRVIRELKsqGRGIVYISHRLKEIfEICDDVTVFRDGQ 218
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
39-252 |
5.99e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 85.46 E-value: 5.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 39 KALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYElAwlRAKKIGYI---FQTFNLI 115
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRD-A--IRAGIAYVpedRKGEGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 116 PVLTAVENVMLPMI-------FVGTPYEDAIvkAKKLLELVGLgKF--IHHKPAELSGGQQQRVAAARALANDPSIILAD 186
Cdd:COG1129 343 LDLSIRENITLASLdrlsrggLLDRRRERAL--AEEYIKRLRI-KTpsPEQPVGNLSGGNQQKVVLAKWLATDPKVLILD 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502908369 187 EPTGNLD------LHtglKLINLLKEinekKGVTIVTATHDLK-MVDVSDRIIWIRDGKIEKiELRRD---IEAVM 252
Cdd:COG1129 420 EPTRGIDvgakaeIY---RLIRELAA----EGKAVIVISSELPeLLGLSDRILVMREGRIVG-ELDREeatEEAIM 487
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
39-225 |
6.47e-19 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 82.85 E-value: 6.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 39 KALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGvdiamldayelawlrAKKIGYIFQTFNLIPVL 118
Cdd:PRK09544 18 RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG---------------KLRIGYVPQKLYLDTTL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 119 T-AVENVMlpMIFVGTPYEDaIVKAkklLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLHTG 197
Cdd:PRK09544 83 PlTVNRFL--RLRPGTKKED-ILPA---LKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQ 156
|
170 180
....*....|....*....|....*...
gi 502908369 198 LKLINLLKEINEKKGVTIVTATHDLKMV 225
Cdd:PRK09544 157 VALYDLIDQLRRELDCAVLMVSHDLHLV 184
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
41-250 |
6.99e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 82.81 E-value: 6.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLD--RPTGGKVYIDGVDIAMLDAYElawlRAKK-IGYIFQ------- 110
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDE----RARAgIFLAFQypveipg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 111 --TFNLIpvLTAVENVMLPMIfvgtPYEDAIVKAKKLLELVGLGKFIHHKP--AELSGGQQQRVAAARALANDPSIILAD 186
Cdd:COG0396 92 vsVSNFL--RTALNARRGEEL----SAREFLKLLKEKMKELGLDEDFLDRYvnEGFSGGEKKRNEILQMLLLEPKLAILD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502908369 187 EPTGNLDLhTGLKL----INLLKeiNEKKGVTIVtaTHDLKMVD--VSDRIIWIRDGKIEK---IELRRDIEA 250
Cdd:COG0396 166 ETDSGLDI-DALRIvaegVNKLR--SPDRGILII--THYQRILDyiKPDFVHVLVDGRIVKsggKELALELEE 233
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
41-239 |
7.99e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 85.48 E-value: 7.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRP---TGGKVYIDGVDIAmldayelAWLRAKKIGYIFQTFNLIPV 117
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPID-------AKEMRAISAYVQQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 118 LTAVENVMLPMIF---VGTPYEDAIVKAKKLLELVGLGKFIH--------HKpaELSGGQQQRVAAARALANDPSIILAD 186
Cdd:TIGR00955 114 LTVREHLMFQAHLrmpRRVTKKEKRERVDEVLQALGLRKCANtrigvpgrVK--GLSGGERKRLAFASELLTDPPLLFCD 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502908369 187 EPTGNLDLHTGLKLINLLKEINEkKGVTIVTATHD--LKMVDVSDRIIWIRDGKI 239
Cdd:TIGR00955 192 EPTSGLDSFMAYSVVQVLKGLAQ-KGKTIICTIHQpsSELFELFDKIILMAEGRV 245
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
41-250 |
1.22e-18 |
|
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: 81.03 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLD--RPTGGKVYIDGVDIAMLDAYElawlRAKK-IGYIFQtfnlipv 117
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEE----RARLgIFLAFQ------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 118 ltavenvmlpmifvgTPYEDAIVKAKKLLELVGLGkfihhkpaeLSGGQQQRVAAARALANDPSIILADEPTGNLDLhTG 197
Cdd:cd03217 85 ---------------YPPEIPGVKNADFLRYVNEG---------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI-DA 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502908369 198 LKLI-NLLKEI-NEKKGVTIVTATHDLKMVDVSDRIIWIRDGKIEKI---ELRRDIEA 250
Cdd:cd03217 140 LRLVaEVINKLrEEGKSVLIITHYQRLLDYIKPDRVHVLYDGRIVKSgdkELALEIEK 197
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
41-239 |
1.78e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 82.45 E-value: 1.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDI---AMLDAYELAWLRaKKIGYIFQTFNLIPv 117
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLggrSIFNYRDVLEFR-RRVGMLFQRPNPFP- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 118 LTAVENVMLPM-IFVGTPYEDAIVKAKKLLELVGLGKFIHHK----PAELSGGQQQRVAAARALANDPSIILADEPTGNL 192
Cdd:PRK14271 115 MSIMDNVLAGVrAHKLVPRKEFRGVAQARLTEVGLWDAVKDRlsdsPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSAL 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502908369 193 DLHTGLKLINLLKEINEKkgVTIVTATHDL-KMVDVSDRIIWIRDGKI 239
Cdd:PRK14271 195 DPTTTEKIEEFIRSLADR--LTVIIVTHNLaQAARISDRAALFFDGRL 240
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
36-238 |
3.33e-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: 3.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 36 FIVKALDGVTFNV-----KRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAmldaYELAWLRAKKIGYIFQ 110
Cdd:cd03237 5 TMKKTLGEFTLEVeggsiSESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS----YKPQYIKADYEGTVRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 111 tfnlipVLTAVENVMLPMIFvgtpYEDAIVKAKKLLELvglgkfIHHKPAELSGGQQQRVAAARALANDPSIILADEPTG 190
Cdd:cd03237 81 ------LLSSITKDFYTHPY----FKTEIAKPLQIEQI------LDREVPELSGGELQRVAIAACLSKDADIYLLDEPSA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502908369 191 NLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMVD-VSDRIIwIRDGK 238
Cdd:cd03237 145 YLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDyLADRLI-VFEGE 192
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
40-239 |
3.66e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 81.37 E-value: 3.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 40 ALDGVTFNVKRR-------------EYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAwlraKKIG 106
Cdd:PRK10575 13 ALRNVSFRVPGRtllhplsltfpagKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFA----RKVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 107 YIFQTFNLIPVLTAVEnvmlpMIFVGT-PYEDAI--------VKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALA 177
Cdd:PRK10575 89 YLPQQLPAAEGMTVRE-----LVAIGRyPWHGALgrfgaadrEKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502908369 178 NDPSIILADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKM-VDVSDRIIWIRDGKI 239
Cdd:PRK10575 164 QDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMaARYCDYLVALRGGEM 226
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
44-238 |
7.88e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 79.98 E-value: 7.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 44 VTFNVKRREYVSIMGPSGSGKTTLFNMIGGLdRPTGGKVYIDGVDIAMLDAYELAWLRAkkigYIFQ----TFNLiPV-- 117
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHRA----YLSQqqtpPFAM-PVfq 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 118 -LTavenVMLPmifVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVA-AARALANDPSI------ILADEPT 189
Cdd:PRK03695 89 yLT----LHQP---DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRlAAVVLQVWPDInpagqlLLLDEPM 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 502908369 190 GNLDLHTGLKLINLLKEINEkKGVTIVTATHDLKMV-DVSDRIIWIRDGK 238
Cdd:PRK03695 162 NSLDVAQQAALDRLLSELCQ-QGIAVVMSSHDLNHTlRHADRVWLLKQGK 210
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
41-239 |
2.57e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 78.90 E-value: 2.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAwLRaKKIGYIFQTFNLIPVLTA 120
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLA-LR-QQVATVFQDPEQQIFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 121 VE-NVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLHTGLK 199
Cdd:PRK13638 95 IDsDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 502908369 200 LINLLKEInEKKGVTIVTATHDLKMV-DVSDRIIWIRDGKI 239
Cdd:PRK13638 175 MIAIIRRI-VAQGNHVIISSHDIDLIyEISDAVYVLRQGQI 214
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
41-239 |
3.62e-17 |
|
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: 80.25 E-value: 3.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAmldAYELAWLRAKkIGYIFQTfnliPVL-- 118
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIR---DVTQASLRAA-IGIVPQD----TVLfn 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 119 -TAVENvmlpmIFVGTP--YEDAIVKAKKLLELvglGKFIHHKPA-----------ELSGGQQQRVAAARALANDPSIIL 184
Cdd:COG5265 446 dTIAYN-----IAYGRPdaSEEEVEAAARAAQI---HDFIESLPDgydtrvgerglKLSGGEKQRVAIARTLLKNPPILI 517
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502908369 185 ADEPTGNLDLHTGLKLINLLKEINEKKgVTIVTAtHDLKMVDVSDRIIWIRDGKI 239
Cdd:COG5265 518 FDEATSALDSRTERAIQAALREVARGR-TTLVIA-HRLSTIVDADEILVLEAGRI 570
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
38-225 |
4.32e-17 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 79.18 E-value: 4.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 38 VKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRP----TGGKVYIDGVDIAMLDAYELAWLRAKKIGYIFQ--T 111
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPRERRKIIGREIAMIFQepS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 112 FNLIPVLTAVENVM--LPMIFVGTPY----EDAIVKAKKLLELVGLGKfihHK------PAELSGGQQQRVAAARALAND 179
Cdd:COG4170 100 SCLDPSAKIGDQLIeaIPSWTFKGKWwqrfKWRKKRAIELLHRVGIKD---HKdimnsyPHELTEGECQKVMIAMAIANQ 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 502908369 180 PSIILADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMV 225
Cdd:COG4170 177 PRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESI 222
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
42-238 |
6.75e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 79.75 E-value: 6.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 42 DGVTFNVKRREYVSIMGPSGSGKT-TLFNMIGGLdrPTGGKVYIDGvDI-----AMLDAYE--LAWLRAKKIGYIFQ--T 111
Cdd:PRK15134 26 NDVSLQIEAGETLALVGESGSGKSvTALSILRLL--PSPPVVYPSG-DIrfhgeSLLHASEqtLRGVRGNKIAMIFQepM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 112 FNLIPvLTAVENVMLPMIFV--GTPYEDAIVKAKKLLELVGL---GKFIHHKPAELSGGQQQRVAAARALANDPSIILAD 186
Cdd:PRK15134 103 VSLNP-LHTLEKQLYEVLSLhrGMRREAARGEILNCLDRVGIrqaAKRLTDYPHQLSGGERQRVMIAMALLTRPELLIAD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502908369 187 EPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMV-DVSDRIIWIRDGK 238
Cdd:PRK15134 182 EPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVrKLADRVAVMQNGR 234
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
38-231 |
1.63e-16 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 77.54 E-value: 1.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 38 VKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLD----RPTGGKVYIDGVDIAMLDAYELAWLRAKKIGYIFQTfn 113
Cdd:PRK15093 20 VKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTkdnwRVTADRMRFDDIDLLRLSPRERRKLVGHNVSMIFQE-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 114 liPvltavENVMLPMIFVGTPYEDAI-----------------VKAKKLLELVGLG---KFIHHKPAELSGGQQQRVAAA 173
Cdd:PRK15093 98 --P-----QSCLDPSERVGRQLMQNIpgwtykgrwwqrfgwrkRRAIELLHRVGIKdhkDAMRSFPYELTEGECQKVMIA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502908369 174 RALANDPSIILADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMVD-VSDRI 231
Cdd:PRK15093 171 IALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSqWADKI 229
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
31-239 |
1.99e-16 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 78.09 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 31 YKMGKFIVKALDgvtFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDG--VDIAMLDAYElawlraKKIGYI 108
Cdd:PRK10522 332 YQDNGFSVGPIN---LTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGkpVTAEQPEDYR------KLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 109 FQTFNLIPVLTAVEnvmlpmifvGTPYEDAIVkaKKLLELVGLGKFIHHKPAE-----LSGGQQQRVAAARALANDPSII 183
Cdd:PRK10522 403 FTDFHLFDQLLGPE---------GKPANPALV--EKWLERLKMAHKLELEDGRisnlkLSKGQKKRLALLLALAEERDIL 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 184 LADEPTGNLDLHTG----LKLINLLKEinekKGVTIVTATHDLKMVDVSDRIIWIRDGKI 239
Cdd:PRK10522 472 LLDEWAADQDPHFRrefyQVLLPLLQE----MGKTIFAISHDDHYFIHADRLLEMRNGQL 527
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
40-239 |
2.22e-16 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 78.14 E-value: 2.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 40 ALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDiamLDAYELAWLRaKKIGYIFQT---FNLip 116
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHD---LRDYTLASLR-NQVALVSQNvhlFND-- 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 117 vlTAVENVMLPmifVGTPYEDA-IVKAKKL---LELV-----GLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADE 187
Cdd:PRK11176 432 --TIANNIAYA---RTEQYSREqIEEAARMayaMDFInkmdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDE 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502908369 188 PTGNLDLHTGLKLINLLKEIneKKGVTIVTATHDLKMVDVSDRIIWIRDGKI 239
Cdd:PRK11176 507 ATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEKADEILVVEDGEI 556
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
37-232 |
1.05e-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: 75.98 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 37 IVKALDGVTFNV-----KRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDgVDIAmldaYelawlrakKIGYIFQT 111
Cdd:COG1245 347 LTKSYGGFSLEVeggeiREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-LKIS----Y--------KPQYISPD 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 112 FNlIPVLTAVENVmLPMIFVGTPYEDAIVKakKLlelvGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGN 191
Cdd:COG1245 414 YD-GTVEEFLRSA-NTDDFGSSYYKTEIIK--PL----GLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAH 485
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 502908369 192 LDLHTGLKLINLLKEINEKKGVTIVTATHDLKMVD-VSDRII 232
Cdd:COG1245 486 LDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDyISDRLM 527
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
38-239 |
1.52e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.47 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 38 VKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAyelawLRAKKIG-YIF-QTFNLI 115
Cdd:PRK15439 24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTP-----AKAHQLGiYLVpQEPLLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 116 PVLTAVENvmlpmIFVGTP-YEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLdl 194
Cdd:PRK15439 99 PNLSVKEN-----ILFGLPkRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASL-- 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502908369 195 hTGLKLINLLKEINE--KKGVTIVTATHDLKMV-DVSDRIIWIRDGKI 239
Cdd:PRK15439 172 -TPAETERLFSRIREllAQGVGIVFISHKLPEIrQLADRISVMRDGTI 218
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
41-220 |
4.81e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 74.15 E-value: 4.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTG--GKVYIDGVDIAMLdayelawlRAKKIGYIFQTFNLIPVL 118
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQ--------ILKRTGFVTQDDILYPHL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 119 TAVENvmlpMIFVGT-------PYEDAIVKAKKLLELVGLGK---------FIHHkpaeLSGGQQQRVAAARALANDPSI 182
Cdd:PLN03211 156 TVRET----LVFCSLlrlpkslTKQEKILVAESVISELGLTKcentiignsFIRG----ISGGERKRVSIAHEMLINPSL 227
|
170 180 190
....*....|....*....|....*....|....*...
gi 502908369 183 ILADEPTGNLDLHTGLKLINLLKEInEKKGVTIVTATH 220
Cdd:PLN03211 228 LILDEPTSGLDATAAYRLVLTLGSL-AQKGKTIVTSMH 264
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
34-220 |
6.74e-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: 70.26 E-value: 6.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 34 GKFIVKALDgvtFNVKRREYVSIMGPSGSGKTTLFNMIGGL--------DRPTGGKVYidgvdiamldayelawlrakki 105
Cdd:cd03223 13 GRVLLKDLS---FEIKPGDRLLITGPSGTGKSSLFRALAGLwpwgsgriGMPEGEDLL---------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 106 gYIFQTfnlipvltavenvmlPMIFVGTpyedaivkakkLLELVglgkfIHHKPAELSGGQQQRVAAARALANDPSIILA 185
Cdd:cd03223 68 -FLPQR---------------PYLPLGT-----------LREQL-----IYPWDDVLSGGEQQRLAFARLLLHKPKFVFL 115
|
170 180 190
....*....|....*....|....*....|....*
gi 502908369 186 DEPTGNLDLHTGLKLINLLKEinekKGVTIVTATH 220
Cdd:cd03223 116 DEATSALDEESEDRLYQLLKE----LGITVISVGH 146
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
38-226 |
7.48e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 71.45 E-value: 7.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 38 VKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAmldAYELAWLRAKKIGYIFQTFNLIPV 117
Cdd:PRK11614 18 IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDIT---DWQTAKIMREAVAIVPEGRRVFSR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 118 LTAVENVMLPMIFVG-TPYEDAIVKAKKLLELvgLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLHT 196
Cdd:PRK11614 95 MTVEENLAMGGFFAErDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPII 172
|
170 180 190
....*....|....*....|....*....|....
gi 502908369 197 GLKLINLLKEINEkKGVTIV----TATHDLKMVD 226
Cdd:PRK11614 173 IQQIFDTIEQLRE-QGMTIFlveqNANQALKLAD 205
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
41-220 |
1.33e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 70.76 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGG--LDRPTGGKVYIDGVDIAmldayelawlrakkigyifqtfnliPVL 118
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVPDNQFG-------------------------REA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 119 TAVENVmlpmifvgtPYEDAIVKAKKLLELVGLGK--FIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLHT 196
Cdd:COG2401 101 SLIDAI---------GRKGDFKDAVELLNAVGLSDavLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
170 180
....*....|....*....|....
gi 502908369 197 GLKLINLLKEINEKKGVTIVTATH 220
Cdd:COG2401 172 AKRVARNLQKLARRAGITLVVATH 195
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
37-232 |
1.60e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 72.53 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 37 IVKALDGVTFNV-----KRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDgVDIAmldaYELAWLRAKKIGYIFQT 111
Cdd:PRK13409 346 LTKKLGDFSLEVeggeiYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKIS----YKPQYIKPDYDGTVEDL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 112 FNLIPVltavenvmlpmIFVGTPYEDAIVKakKLlelvGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGN 191
Cdd:PRK13409 421 LRSITD-----------DLGSSYYKSEIIK--PL----QLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAH 483
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 502908369 192 LDLHTGLKLINLLKEINEKKGVTIVTATHDLKMVD-VSDRII 232
Cdd:PRK13409 484 LDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDyISDRLM 525
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
38-237 |
8.26e-14 |
|
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: 68.51 E-value: 8.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 38 VKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAWLRAKKIGYIFQTFNLIPV 117
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLLNA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 118 lTAVENVMLPMIFVGTPYEdAIVKAKKLLELVGLGKF-----IHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNL 192
Cdd:cd03290 94 -TVEENITFGSPFNKQRYK-AVTDACSLQPDIDLLPFgdqteIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSAL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 502908369 193 DLHTGLKLIN--LLKEINEKKGvTIVTATHDLKMVDVSDRIIWIRDG 237
Cdd:cd03290 172 DIHLSDHLMQegILKFLQDDKR-TLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
41-224 |
1.04e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 67.67 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAM-LDAYElawlraKKIGYIFQTFNLIPVLT 119
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKdLCTYQ------KQLCFVGHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 120 AVENVMLPMIFVGTPYEdaivkAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLHTGLK 199
Cdd:PRK13540 91 LRENCLYDIHFSPGAVG-----ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLT 165
|
170 180
....*....|....*....|....*
gi 502908369 200 LINLLKEINEKKGVTIVTATHDLKM 224
Cdd:PRK13540 166 IITKIQEHRAKGGAVLLTSHQDLPL 190
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
55-232 |
1.12e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 70.44 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 55 SIMGPSGSGK-TTLFNmiggldrpTGGKVYIDGVDIAmldAYELAWLRakkigyifqtfNLIPVLTAVenvmlPMIFVGT 133
Cdd:PTZ00265 1259 SLTKEGGSGEdSTVFK--------NSGKILLDGVDIC---DYNLKDLR-----------NLFSIVSQE-----PMLFNMS 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 134 PYE-------DAIVK-AKKLLELVGLGKFIHHKPAE-----------LSGGQQQRVAAARALANDPSIILADEPTGNLDL 194
Cdd:PTZ00265 1312 IYEnikfgkeDATREdVKRACKFAAIDEFIESLPNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDS 1391
|
170 180 190
....*....|....*....|....*....|....*...
gi 502908369 195 HTGLKLINLLKEINEKKGVTIVTATHDLKMVDVSDRII 232
Cdd:PTZ00265 1392 NSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIV 1429
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
46-220 |
1.14e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 67.95 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 46 FNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDayelawlRAKKIGYIFQTFNLIPVLTAVENVM 125
Cdd:PRK13543 32 FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD-------RSRFMAYLGHLPGLKADLSTLENLH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 126 LPMIFVGTpyedaivKAKKL----LELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLHtGLKLI 201
Cdd:PRK13543 105 FLCGLHGR-------RAKQMpgsaLAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE-GITLV 176
|
170 180
....*....|....*....|
gi 502908369 202 N-LLKEINEKKGVTIVTaTH 220
Cdd:PRK13543 177 NrMISAHLRGGGAALVT-TH 195
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
18-241 |
1.16e-13 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 69.92 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 18 LEYVVEAVEVKKYYKM-GKFIVK---------------ALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGK 81
Cdd:PRK13545 1 MNYKVKFEHVTKKYKMyNKPFDKlkdlffrskdgeyhyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 82 VYIDGVdiamldayelAWLRAKKIGYIFQtfnlipvLTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAE 161
Cdd:PRK13545 81 VDIKGS----------AALIAISSGLNGQ-------LTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 162 LSGGQQQRVAAARALANDPSIILADEPTGNLDLHTGLKLINLLKEINEkKGVTIVTATHDLKMVD-VSDRIIWIRDGKIE 240
Cdd:PRK13545 144 YSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKE-QGKTIFFISHSLSQVKsFCTKALWLHYGQVK 222
|
.
gi 502908369 241 K 241
Cdd:PRK13545 223 E 223
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
39-247 |
1.65e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 69.43 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 39 KALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAwlrAKKIGYIFQT---FNLI 115
Cdd:PRK09700 277 KKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAV---KKGMAYITESrrdNGFF 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 116 PVLTAVENVmlpmifvgtpyedAIVKAKKLLELVGLGKFIHHKP-----------------------AELSGGQQQRVAA 172
Cdd:PRK09700 354 PNFSIAQNM-------------AISRSLKDGGYKGAMGLFHEVDeqrtaenqrellalkchsvnqniTELSGGNQQKVLI 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502908369 173 ARALANDPSIILADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKMVDVSDRIIWIRDGKIEKIELRRD 247
Cdd:PRK09700 421 SKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRD 495
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
41-242 |
1.69e-13 |
|
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: 69.97 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFN-MIGGLDRpTGGKVYIDGvDIAMLDayELAWLRAKkigyifqtfnlipvlT 119
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDK-VEGHVHMKG-SVAYVP--QQAWIQND---------------S 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 120 AVENVMLPMIfVGTPYEDAIVKAKKLL---ELVGLGKF--IHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDL 194
Cdd:TIGR00957 715 LRENILFGKA-LNEKYYQQVLEACALLpdlEILPSGDRteIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDA 793
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502908369 195 HTGLKLI-NLLKEINEKKGVTIVTATHDLKMVDVSDRIIWIRDGKIEKI 242
Cdd:TIGR00957 794 HVGKHIFeHVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEM 842
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
41-239 |
1.74e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 69.77 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFN-MIGGLDRPTGGKVYIDGVDiamldAYelawlrAKKIGYIFQTfnlipvlT 119
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGTV-----AY------VPQVSWIFNA-------T 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 120 AVENVMLPMIFVGTPYEDAI-VKA-KKLLELVGLGKF--IHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLH 195
Cdd:PLN03130 695 VRDNILFGSPFDPERYERAIdVTAlQHDLDLLPGGDLteIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAH 774
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 502908369 196 TGLKLIN-LLKEinEKKGVTIVTATHDLKMVDVSDRIIWIRDGKI 239
Cdd:PLN03130 775 VGRQVFDkCIKD--ELRGKTRVLVTNQLHFLSQVDRIILVHEGMI 817
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
41-193 |
1.85e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 69.27 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGlDRPTG--------GKVYIDGvdiamldayELAWLRAKKIGYIFQTF 112
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQGysndltlfGRRRGSG---------ETIWDIKKHIGYVSSSL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 113 NL-IPVLTAVENVMLPMIFvgtpyeDAI-----------VKAKKLLELVGLGKFIHHKP-AELSGGQQQRVAAARALAND 179
Cdd:PRK10938 346 HLdYRVSTSVRNVILSGFF------DSIgiyqavsdrqqKLAQQWLDILGIDKRTADAPfHSLSWGQQRLALIVRALVKH 419
|
170
....*....|....
gi 502908369 180 PSIILADEPTGNLD 193
Cdd:PRK10938 420 PTLLILDEPLQGLD 433
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
38-239 |
3.63e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.40 E-value: 3.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 38 VKALDG------VTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAM---LDAyelawLRA------ 102
Cdd:PRK11288 260 LDGLKGpglrepISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIrspRDA-----IRAgimlcp 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 103 ---KKIGyifqtfnLIPVLTAVENV-------MLPMIFvgtpyedaIVKAKKLLELVGlgKFI----------HHKPAEL 162
Cdd:PRK11288 335 edrKAEG-------IIPVHSVADNInisarrhHLRAGC--------LINNRWEAENAD--RFIrslniktpsrEQLIMNL 397
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502908369 163 SGGQQQRVAAARALANDPSIILADEPTGNLDLHTGLKLINLLKEINEkKGVTIVTATHDLKMV-DVSDRIIWIRDGKI 239
Cdd:PRK11288 398 SGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAA-QGVAVLFVSSDLPEVlGVADRIVVMREGRI 474
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
16-220 |
5.60e-13 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 65.73 E-value: 5.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 16 RKLEYVVEAVEVKKyykmgkfivKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGldRPTGGkvYIDGvDIaMLDAY 95
Cdd:cd03232 7 KNLNYTVPVKGGKR---------QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAG--VITG-EI-LINGR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 96 ELAWLRAKKIGYIFQTFNLIPVLTAVENVMLpmifvgtpyedaivkakkllelvglgkfiHHKPAELSGGQQQRVAAARA 175
Cdd:cd03232 72 PLDKNFQRSTGYVEQQDVHSPNLTVREALRF-----------------------------SALLRGLSVEQRKRLTIGVE 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 502908369 176 LANDPSIILADEPTGNLDLHTGLKLINLLKEINEkKGVTIVTATH 220
Cdd:cd03232 123 LAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLAD-SGQAILCTIH 166
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
41-239 |
1.15e-12 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 67.05 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAyelAWLRaKKIGYIFQTfnliPVLTA 120
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSH---SVLR-QGVAMVQQD----PVVLA 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 121 veNVMLPMIFVGTPY-EDAIVKAkklLELVGLGKFIHHKPA-----------ELSGGQQQRVAAARALANDPSIILADEP 188
Cdd:PRK10790 429 --DTFLANVTLGRDIsEEQVWQA---LETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALARVLVQTPQILILDEA 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502908369 189 TGNLDLHTGLKLINLLKEINEKkgVTIVTATHDLKMVDVSDRIIWIRDGKI 239
Cdd:PRK10790 504 TANIDSGTEQAIQQALAAVREH--TTLVVIAHRLSTIVEADTILVLHRGQA 552
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
36-243 |
1.71e-12 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 66.36 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 36 FIVKALDgvtFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIamlDAYELAWLRAkKIGYIFQTFNLI 115
Cdd:COG4615 346 FTLGPID---LTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV---TADNREAYRQ-LFSAVFSDFHLF 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 116 PVLTAVENVMLPmifvgtpyedaiVKAKKLLELVGLgkfiHHKPA---------ELSGGQQQRVAAARALANDPSIILAD 186
Cdd:COG4615 419 DRLLGLDGEADP------------ARARELLERLEL----DHKVSvedgrfsttDLSQGQRKRLALLVALLEDRPILVFD 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502908369 187 E------PTgnldlhtgLK------LINLLKeineKKGVTIVTATHDLKMVDVSDRIIWIRDGKIEKIE 243
Cdd:COG4615 483 EwaadqdPE--------FRrvfyteLLPELK----ARGKTVIAISHDDRYFDLADRVLKMDYGKLVELT 539
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
40-241 |
2.10e-12 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 65.22 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 40 ALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDG-VDIAMLDAyelawlrakkigyifqtfNLIPVL 118
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGeVSVIAISA------------------GLSGQL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 119 TAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLHTGL 198
Cdd:PRK13546 101 TGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQ 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 502908369 199 KLINLLKEINEKKGvTIVTATHDLKMV-DVSDRIIWIRDGKIEK 241
Cdd:PRK13546 181 KCLDKIYEFKEQNK-TIFFVSHNLGQVrQFCTKIAWIEGGKLKD 223
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
38-238 |
3.81e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.52 E-value: 3.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 38 VKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAwlrAKKIGYIFQTFNLIPV 117
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEAL---ENGISMVHQELNLVLQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 118 LTAVENVML---PM--IFV--GTPYEDaivkAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTG 190
Cdd:PRK10982 88 RSVMDNMWLgryPTkgMFVdqDKMYRD----TKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502908369 191 NL---DLHTGLKLINLLKEinekKGVTIVTATHDL-KMVDVSDRIIWIRDGK 238
Cdd:PRK10982 164 SLtekEVNHLFTIIRKLKE----RGCGIVYISHKMeEIFQLCDEITILRDGQ 211
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
54-231 |
4.32e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.21 E-value: 4.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 54 VSIMGPSGSGKTTLFNMIGGLDRPTGGKvYIDGVDI-AMLDAY---EL----AWLRAK------KIGYIFQtfnlipvlt 119
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSGELIPNLGD-YEEEPSWdEVLKRFrgtELqnyfKKLYNGeikvvhKPQYVDL--------- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 120 avenvmLPMIFVGTPYE-----DAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDL 194
Cdd:PRK13409 172 ------IPKVFKGKVREllkkvDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDI 245
|
170 180 190
....*....|....*....|....*....|....*...
gi 502908369 195 HTGLKLINLLKEINEKKGVTIVtaTHDLKMVD-VSDRI 231
Cdd:PRK13409 246 RQRLNVARLIRELAEGKYVLVV--EHDLAVLDyLADNV 281
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
31-232 |
5.03e-12 |
|
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: 62.73 E-value: 5.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 31 YKMGKFIVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGgldrptggkvyidgvdiamldaYELAWLRAKKigyifq 110
Cdd:cd03238 1 LTVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL----------------------YASGKARLIS------ 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 111 tfnlipvltavenvmlpmiFVGTPYEDAIVKAKKLLEL--VGLGKF-IHHKPAELSGGQQQRVAAARALANDP--SIILA 185
Cdd:cd03238 53 -------------------FLPKFSRNKLIFIDQLQFLidVGLGYLtLGQKLSTLSGGELQRVKLASELFSEPpgTLFIL 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 502908369 186 DEPTGNLDLHTGLKLINLLKEINEkKGVTIVTATHDLKMVDVSDRII 232
Cdd:cd03238 114 DEPSTGLHQQDINQLLEVIKGLID-LGNTVILIEHNLDVLSSADWII 159
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
48-232 |
1.37e-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: 61.43 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 48 VKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAmldayelawlrakkigyifqtfnlipvltavenvmlp 127
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV------------------------------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 128 mifvgtpyedaiVKAKKLlelvglgkfihhkpaELSGGQQQRVAAARALANDPSIILADEPTGNLDLHTGLKLINLLKEI 207
Cdd:cd03222 65 ------------YKPQYI---------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
|
170 180
....*....|....*....|....*.
gi 502908369 208 NEKKGVTIVTATHDLKMVD-VSDRII 232
Cdd:cd03222 118 SEEGKKTALVVEHDLAVLDyLSDRIH 143
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
21-196 |
1.42e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 63.80 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 21 VVEAVEVKKYYkmGKFIVkaLDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYI-DGVdiamldayelaw 99
Cdd:TIGR03719 322 VIEAENLTKAF--GDKLL--IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETV------------ 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 100 lrakKIGYIFQTF-NLIPVLTAVENVM--LPMIFVGtpyeDAIVKAKKLlelvgLGKF------IHHKPAELSGGQQQRV 170
Cdd:TIGR03719 386 ----KLAYVDQSRdALDPNKTVWEEISggLDIIKLG----KREIPSRAY-----VGRFnfkgsdQQKKVGQLSGGERNRV 452
|
170 180
....*....|....*....|....*.
gi 502908369 171 AAARALANDPSIILADEPTGNLDLHT 196
Cdd:TIGR03719 453 HLAKTLKSGGNVLLLDEPTNDLDVET 478
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
38-240 |
1.60e-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: 63.69 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 38 VKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMI-GGLDRPTGGKVYIDGVDIAM---LDAYE----LAWLRAKKIGyif 109
Cdd:TIGR02633 273 RKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPVDIrnpAQAIRagiaMVPEDRKRHG--- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 110 qtfnLIPVLTAVENVMLPMI--FVGTPYEDAIVKAKKLLELVGLGKFIHHKP----AELSGGQQQRVAAARALANDPSII 183
Cdd:TIGR02633 350 ----IVPILGVGKNITLSVLksFCFKMRIDAAAELQIIGSAIQRLKVKTASPflpiGRLSGGNQQKAVLAKMLLTNPRVL 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502908369 184 LADEPTGNLDL---HTGLKLINLLKeineKKGVTIVTATHDLKMV-DVSDRIIWIRDGKIE 240
Cdd:TIGR02633 426 ILDEPTRGVDVgakYEIYKLINQLA----QEGVAIIVVSSELAEVlGLSDRVLVIGEGKLK 482
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
41-239 |
2.13e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 62.54 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGG----LDRPTG----GKVYIDGVDIAMLDAYELAWLRA-----KKIGY 107
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltgGGAPRGarvtGDVTLNGEPLAAIDAPRLARLRAvlpqaAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 108 IFqtfnlipvlTAVENVML---PMIFVG--TPYEDAIVkAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALAN---- 178
Cdd:PRK13547 97 AF---------SAREIVLLgryPHARRAgaLTHRDGEI-AWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpp 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502908369 179 -----DPSIILADEPTGNLDLHTGLKLINLLKEINEKKGVTIVTATHDLKM-VDVSDRIIWIRDGKI 239
Cdd:PRK13547 167 hdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLaARHADRIAMLADGAI 233
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-255 |
2.27e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 63.64 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 21 VVEAVEVKkyYKMGKFIVkaLDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAmldAYELAWL 100
Cdd:PTZ00243 1310 VFEGVQMR--YREGLPLV--LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIG---AYGLREL 1382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 101 RakkigyifQTFNLIPvltavenvMLPMIFVGT------PYEDAI---VKAKklLELVGLGKfihHKPAELSG------- 164
Cdd:PTZ00243 1383 R--------RQFSMIP--------QDPVLFDGTvrqnvdPFLEASsaeVWAA--LELVGLRE---RVASESEGidsrvle 1441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 165 -------GQQQRVAAARALANDPS-IILADEPTGNLDlhtglklINLLKEINEK-----KGVTIVTATHDLKMVDVSDRI 231
Cdd:PTZ00243 1442 ggsnysvGQRQLMCMARALLKKGSgFILMDEATANID-------PALDRQIQATvmsafSAYTVITIAHRLHTVAQYDKI 1514
|
250 260
....*....|....*....|....
gi 502908369 232 IWIRDGKIEKIELRRDIeaVMGEQ 255
Cdd:PTZ00243 1515 IVMDHGAVAEMGSPREL--VMNRQ 1536
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
41-239 |
2.65e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 63.22 E-value: 2.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDayeLAWLRaKKIGYIFQTfnlipvlta 120
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFG---LMDLR-KVLGIIPQA--------- 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 121 venvmlPMIFVGT------PY-EDAIVKAKKLLELVGLGKFIHHKP----AEL-------SGGQQQRVAAARALANDPSI 182
Cdd:PLN03130 1322 ------PVLFSGTvrfnldPFnEHNDADLWESLERAHLKDVIRRNSlgldAEVseagenfSVGQRQLLSLARALLRRSKI 1395
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502908369 183 ILADEPTGNLDLHTGlKLINllKEINEK-KGVTIVTATHDLKMVDVSDRIIWIRDGKI 239
Cdd:PLN03130 1396 LVLDEATAAVDVRTD-ALIQ--KTIREEfKSCTMLIIAHRLNTIIDCDRILVLDAGRV 1450
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
41-241 |
7.15e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.92 E-value: 7.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFN-MIGGLDRPTGGKVYIDGVDiamldAYelawlrAKKIGYIFQTfnlipvlT 119
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGSV-----AY------VPQVSWIFNA-------T 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 120 AVENVMLPMIFVGTPYEDAI-VKA-KKLLELVGLGKF--IHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLH 195
Cdd:PLN03232 695 VRENILFGSDFESERYWRAIdVTAlQHDLDLLPGRDLteIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAH 774
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 502908369 196 TGLKLIN-LLKEinEKKGVTIVTATHDLKMVDVSDRIIWIRDGKIEK 241
Cdd:PLN03232 775 VAHQVFDsCMKD--ELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKE 819
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
34-220 |
8.27e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 61.68 E-value: 8.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 34 GKFIvkALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVY-----IDGVDIAMldayelawlRaKKIGYI 108
Cdd:NF033858 277 GDFT--AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWlfgqpVDAGDIAT---------R-RRVGYM 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 109 FQTFNLIPVLTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEP 188
Cdd:NF033858 345 SQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEP 424
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 502908369 189 TGNLD---------LhtglkLINLLKEinekKGVTIVTATH 220
Cdd:NF033858 425 TSGVDpvardmfwrL-----LIELSRE----DGVTIFISTH 456
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
19-221 |
1.29e-10 |
|
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: 61.10 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 19 EYVVEAVEVKKYYKMGKFIvkaLDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKvyidgvdiamldayelA 98
Cdd:TIGR03719 2 QYIYTMNRVSKVVPPKKEI---LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE----------------A 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 99 WLRAK-KIGYIFQTFNLIPVLTAVENVMLPM------------IFVGTPYEDAivKAKKLLELVG-LGKFIHHKPA---- 160
Cdd:TIGR03719 63 RPQPGiKVGYLPQEPQLDPTKTVRENVEEGVaeikdaldrfneISAKYAEPDA--DFDKLAAEQAeLQEIIDAADAwdld 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 161 --------------------ELSGGQQQRVAAARALANDPSIILADEPTGNLDLHTGLKLINLLKEInekKGvTIVTATH 220
Cdd:TIGR03719 141 sqleiamdalrcppwdadvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY---PG-TVVAVTH 216
|
.
gi 502908369 221 D 221
Cdd:TIGR03719 217 D 217
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
40-223 |
1.62e-10 |
|
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: 61.18 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 40 ALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDI--AMLDAYElawlrakKIGYIFQTFNLIPV 117
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIltNISDVHQ-------NMGYCPQFDAIDDL 2026
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 118 LTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLHTG 197
Cdd:TIGR01257 2027 LTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQAR 2106
|
170 180
....*....|....*....|....*.
gi 502908369 198 LKLINLLKEInEKKGVTIVTATHDLK 223
Cdd:TIGR01257 2107 RMLWNTIVSI-IREGRAVVLTSHSME 2131
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
54-231 |
1.79e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 60.57 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 54 VSIMGPSGSGKTTLFNMIGGLDRPTGGKvYIDGVDI-AMLDAYelawlRAKKIGYIFQTF--NLIPVLTAVENV-MLPMI 129
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGELKPNLGD-YDEEPSWdEVLKRF-----RGTELQDYFKKLanGEIKVAHKPQYVdLIPKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 130 FVGTPYE-----DAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLHTGLKLINLL 204
Cdd:COG1245 176 FKGTVREllekvDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLI 255
|
170 180
....*....|....*....|....*....
gi 502908369 205 KEI-NEKKGVTIVtaTHDLKMVD-VSDRI 231
Cdd:COG1245 256 RELaEEGKYVLVV--EHDLAILDyLADYV 282
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
38-239 |
1.83e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 60.33 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 38 VKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMI-GGLDRPTGGKVYIDG--VDI-----AMldAYELAWL---RaKKIG 106
Cdd:PRK13549 275 IKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLfGAYPGRWEGEIFIDGkpVKIrnpqqAI--AQGIAMVpedR-KRDG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 107 yifqtfnLIPVLTAVENVMLPMIfvgtpyeDAIVKAKKL---LELVGLGKFIHH----------KPAELSGGQQQRVAAA 173
Cdd:PRK13549 352 -------IVPVMGVGKNITLAAL-------DRFTGGSRIddaAELKTILESIQRlkvktaspelAIARLSGGNQQKAVLA 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 174 RALANDPSIILADEPTGNLDL---HTGLKLINLLKeineKKGVTIVTATHDLKMV-DVSDRIIWIRDGKI 239
Cdd:PRK13549 418 KCLLLNPKILILDEPTRGIDVgakYEIYKLINQLV----QQGVAIIVISSELPEVlGLSDRVLVMHEGKL 483
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
41-237 |
1.99e-10 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 59.49 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGvdiamldayelawlrakKIGYIFQTFNLIPVlTA 120
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-----------------RISFSSQFSWIMPG-TI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 121 VENvmlpmIFVGTPYED----AIVKAKKLLElvGLGKF-------IHHKPAELSGGQQQRVAAARALANDPSIILADEPT 189
Cdd:cd03291 115 KEN-----IIFGVSYDEyrykSVVKACQLEE--DITKFpekdntvLGEGGITLSGGQRARISLARAVYKDADLYLLDSPF 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502908369 190 GNLDLHTGlklinllKEINEK------KGVTIVTATHDLKMVDVSDRIIWIRDG 237
Cdd:cd03291 188 GYLDVFTE-------KEIFEScvcklmANKTRILVTSKMEHLKKADKILILHEG 234
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
34-241 |
4.32e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.58 E-value: 4.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 34 GKFIVKaldGVTFNVKRREYVSIMGPSGSGKTTLFN-MIGGLdRPTGGKVYI-DGVDIAMLDAYelawlRAkkigyifqt 111
Cdd:PRK11147 331 GKQLVK---DFSAQVQRGDKIALIGPNGCGKTTLLKlMLGQL-QADSGRIHCgTKLEVAYFDQH-----RA--------- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 112 fNLIPVLTAVENVmlpmifvGTPYEDAIVKAKKLLELVGLGKFIHH-KPA-----ELSGGQQQRVAAARALANDPSIILA 185
Cdd:PRK11147 393 -ELDPEKTVMDNL-------AEGKQEVMVNGRPRHVLGYLQDFLFHpKRAmtpvkALSGGERNRLLLARLFLKPSNLLIL 464
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502908369 186 DEPTGNLDLHTglklINLLKEINEKKGVTIVTATHDLKMVD--VSDRIIWIRDGKIEK 241
Cdd:PRK11147 465 DEPTNDLDVET----LELLEELLDSYQGTVLLVSHDRQFVDntVTECWIFEGNGKIGR 518
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
41-239 |
5.11e-10 |
|
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: 57.27 E-value: 5.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTG---GKVYIDGVDIAmldayELAWLRAKKIGYIFQTFNLIPV 117
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYK-----EFAEKYPGEIIYVSEEDVHFPT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 118 LTAVENvmlpMIFVGTPYEDAIVKAkkllelvglgkfihhkpaeLSGGQQQRVAAARALANDPSIILADEPTGNLDLHTG 197
Cdd:cd03233 98 LTVRET----LDFALRCKGNEFVRG-------------------ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 502908369 198 LKLINLLKEI-NEKKGVTIVTATH-DLKMVDVSDRIIWIRDGKI 239
Cdd:cd03233 155 LEILKCIRTMaDVLKTTTFVSLYQaSDEIYDLFDKVLVLYEGRQ 198
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
21-196 |
1.08e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.21 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 21 VVEAVEVKKYYKmGKFIVkalDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYI-DGVdiamldayelaw 99
Cdd:PRK11819 324 VIEAENLSKSFG-DRLLI---DDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIgETV------------ 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 100 lrakKIGYIFQTF-NLIPVLTAVENVM--LPMIFVGTpYE---DAIVKA---------KKllelVGlgkfihhkpaELSG 164
Cdd:PRK11819 388 ----KLAYVDQSRdALDPNKTVWEEISggLDIIKVGN-REipsRAYVGRfnfkggdqqKK----VG----------VLSG 448
|
170 180 190
....*....|....*....|....*....|..
gi 502908369 165 GQQQRVAAARALANDPSIILADEPTGNLDLHT 196
Cdd:PRK11819 449 GERNRLHLAKTLKQGGNVLLLDEPTNDLDVET 480
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
41-239 |
1.16e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.09 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAwlrAKKIGYIFQTFN---LIPV 117
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGL---ANGIVYISEDRKrdgLVLG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 118 LTAVENVMLPMIfvgTPYEDAIVKAKKLLELVGLGKFIH----HKPA------ELSGGQQQRVAAARALANDPSIILADE 187
Cdd:PRK10762 345 MSVKENMSLTAL---RYFSRAGGSLKHADEQQAVSDFIRlfniKTPSmeqaigLLSGGNQQKVAIARGLMTRPKVLILDE 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502908369 188 PTGNLDLhtGLK-----LINLLKeineKKGVTIVTATHDLKMV-DVSDRIIWIRDGKI 239
Cdd:PRK10762 422 PTRGVDV--GAKkeiyqLINQFK----AEGLSIILVSSEMPEVlGMSDRILVMHEGRI 473
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
41-237 |
1.18e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 58.38 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGvdiamldayelawlrakKIGYIFQTFNLIPVlTA 120
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-----------------RISFSPQTSWIMPG-TI 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 121 VENvmlpmIFVGTPYED----AIVKAKKLLELVGLGKFIHHKP-----AELSGGQQQRVAAARALANDPSIILADEPTGN 191
Cdd:TIGR01271 504 KDN-----IIFGLSYDEyrytSVIKACQLEEDIALFPEKDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFTH 578
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502908369 192 LDLHTGlklinllKEINEK------KGVTIVTATHDLKMVDVSDRIIWIRDG 237
Cdd:TIGR01271 579 LDVVTE-------KEIFESclcklmSNKTRILVTSKLEHLKKADKILLLHEG 623
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
41-239 |
1.54e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.06 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAmldAYELAWLRakkigyifQTFNLIPvlta 120
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVA---KFGLTDLR--------RVLSIIP---- 1316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 121 venvMLPMIFVGT------PY-EDAIVKAKKLLELVGLGKFIHHKPAEL-----------SGGQQQRVAAARALANDPSI 182
Cdd:PLN03232 1317 ----QSPVLFSGTvrfnidPFsEHNDADLWEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKI 1392
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502908369 183 ILADEPTGNLDLHTGLKLINLLKEinEKKGVTIVTATHDLKMVDVSDRIIWIRDGKI 239
Cdd:PLN03232 1393 LVLDEATASVDVRTDSLIQRTIRE--EFKSCTMLVIAHRLNTIIDCDKILVLSSGQV 1447
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
55-193 |
2.58e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 57.55 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 55 SIMGPSGSGKTTLFNMIGGldRPTGGkvYIDGvDIAMLDAYELAWLRAKKIGYIFQTFNLIPVLTAVENVM------LP- 127
Cdd:PLN03140 910 ALMGVSGAGKTTLMDVLAG--RKTGG--YIEG-DIRISGFPKKQETFARISGYCEQNDIHSPQVTVRESLIysaflrLPk 984
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502908369 128 -------MIFVGTPYEdaivkakkLLELVGLGKFIHHKPA--ELSGGQQQRVAAARALANDPSIILADEPTGNLD 193
Cdd:PLN03140 985 evskeekMMFVDEVME--------LVELDNLKDAIVGLPGvtGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
146-221 |
2.81e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.88 E-value: 2.81e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502908369 146 LELVGLGKfiHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLHTGLKLINLLKEInekKGvTIVTATHD 221
Cdd:PRK11147 143 LAQLGLDP--DAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTF---QG-SIIFISHD 212
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
56-220 |
3.15e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 55.26 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 56 IMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMldayelawLRAKKIGYIFQTFNLIPVLTAVEN-VMLPMIFVGTP 134
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINN--------IAKPYCTYIGHNLGLKLEMTVFENlKFWSEIYNSAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 135 YEDAIVKAKKLLELvglgkfIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDlHTGLKLINLLKEINEKKGVT 214
Cdd:PRK13541 103 TLYAAIHYFKLHDL------LDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS-KENRDLLNNLIVMKANSGGI 175
|
....*.
gi 502908369 215 IVTATH 220
Cdd:PRK13541 176 VLLSSH 181
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
31-239 |
1.12e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 55.25 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 31 YKMGKFIVKALDgvtFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYidgvdiamldayelawlRAKKIGYIFQ 110
Cdd:PLN03073 518 YPGGPLLFKNLN---FGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF-----------------RSAKVRMAVF 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 111 TFNLIPVLTAVENVMLPMI--FVGTPYEdaivKAKKLLELVGLGKFIHHKPA-ELSGGQQQRVAAARALANDPSIILADE 187
Cdd:PLN03073 578 SQHHVDGLDLSSNPLLYMMrcFPGVPEQ----KLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDE 653
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502908369 188 PTGNLDLHTGLKLINLLKEIneKKGVTIVtaTHDLKMVDVSDRIIW-IRDGKI 239
Cdd:PLN03073 654 PSNHLDLDAVEALIQGLVLF--QGGVLMV--SHDEHLISGSVDELWvVSEGKV 702
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
41-255 |
1.27e-08 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 54.48 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLdRPTGGKVYIDGVDIAMLDAYElaWLRAkkigyifqtFNLIPvlta 120
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWNSVPLQK--WRKA---------FGVIP---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 121 vENVmlpMIFVGT------PYED-AIVKAKKLLELVGLGKFIHHKPAE-----------LSGGQQQRVAAARALANDPSI 182
Cdd:cd03289 84 -QKV---FIFSGTfrknldPYGKwSDEEIWKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502908369 183 ILADEPTGNLDLHTGLKLINLLKEinEKKGVTIVTATHDLKMVDVSDRIIWIRDGKIEKIElrrDIEAVMGEQ 255
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQ--AFADCTVILSEHRIEAMLECQRFLVIEENKVRQYD---SIQKLLNEK 227
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
25-241 |
1.27e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 55.34 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 25 VEVKKY---YKMGKFIVkaLDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYELAWlr 101
Cdd:TIGR00957 1285 VEFRNYclrYREDLDLV--LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRF-- 1360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 102 akKIGYIFQTfnlipvltavenvmlPMIFVGT---------PYEDAIVKAKklLELVGLGKFIHHKPAEL---------- 162
Cdd:TIGR00957 1361 --KITIIPQD---------------PVLFSGSlrmnldpfsQYSDEEVWWA--LELAHLKTFVSALPDKLdhecaeggen 1421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 163 -SGGQQQRVAAARALANDPSIILADEPTGNLDLHTGlkliNLLKEI--NEKKGVTIVTATHDLKMVDVSDRIIWIRDGKI 239
Cdd:TIGR00957 1422 lSVGQRQLVCLARALLRKTKILVLDEATAAVDLETD----NLIQSTirTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEV 1497
|
..
gi 502908369 240 EK 241
Cdd:TIGR00957 1498 AE 1499
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
41-239 |
1.35e-08 |
|
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: 54.14 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTL----FNMIGGLDrptgGKVYIDGVDIAMLdayELAWLRAKkIGYIFQT----- 111
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKL---PLHTLRSR-LSIILQDpilfs 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 112 ----FNLIPVLTAVENVMLPMIfvgtpyedAIVKAKKLLELV--GLGKFIHHKPAELSGGQQQRVAAARALANDPSIILA 185
Cdd:cd03288 109 gsirFNLDPECKCTDDRLWEAL--------EIAQLKNMVKSLpgGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIM 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502908369 186 DEPTGNLDLHTGlkliNLLKEI--NEKKGVTIVTATHDLKMVDVSDRIIWIRDGKI 239
Cdd:cd03288 181 DEATASIDMATE----NILQKVvmTAFADRTVVTIAHRVSTILDADLVLVLSRGIL 232
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
41-249 |
1.44e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 53.88 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGldRP----TGGKVYIDGVDIAMLDAYElawlRAKK-IGYIFQTFNLI 115
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPaykiLEGDILFKGESILDLEPEE----RAHLgIFLAFQYPIEI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 116 PVLTAVENVMLPM----IFVGTPYEDAI-----VKAKklLELVGLG-KFIHHKPAE-LSGGQQQRVAAARALANDPSIIL 184
Cdd:CHL00131 97 PGVSNADFLRLAYnskrKFQGLPELDPLefleiINEK--LKLVGMDpSFLSRNVNEgFSGGEKKRNEILQMALLDSELAI 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502908369 185 ADEPTGNLDlhtglklINLLKEINE------KKGVTIVTATHDLKMVD--VSDRIIWIRDGKIEK---IELRRDIE 249
Cdd:CHL00131 175 LDETDSGLD-------IDALKIIAEginklmTSENSIILITHYQRLLDyiKPDYVHVMQNGKIIKtgdAELAKELE 243
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1-231 |
1.46e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.04 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 1 MQNAEEAKnvKLPSRRKLEYVveavEVKKYYKMGKfIVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGG 80
Cdd:PTZ00265 368 VENNDDGK--KLKDIKKIQFK----NVRFHYDTRK-DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEG 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 81 KVYIDgvDIAMLDAYELAWLRAKkIGYIFQ-------------TFNLIPV--LTAVENVMLPMIF--------------- 130
Cdd:PTZ00265 441 DIIIN--DSHNLKDINLKWWRSK-IGVVSQdpllfsnsiknniKYSLYSLkdLEALSNYYNEDGNdsqenknkrnscrak 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 131 --------VGTPYEDAIVKAKKLL------ELVGLGK------FIHHKP-----------AELSGGQQQRVAAARALAND 179
Cdd:PTZ00265 518 cagdlndmSNTTDSNELIEMRKNYqtikdsEVVDVSKkvlihdFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRN 597
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 502908369 180 PSIILADEPTGNLDLHTGL---KLINLLKEiNEKKgVTIVTAtHDLKMVDVSDRI 231
Cdd:PTZ00265 598 PKILILDEATSSLDNKSEYlvqKTINNLKG-NENR-ITIIIA-HRLSTIRYANTI 649
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
56-237 |
3.03e-08 |
|
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: 51.61 E-value: 3.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 56 IMGPSGSGKTTLFNMIGG-LDRPTGGKVYIDGVDIAMLDAYELawlrakkigyifqtfnlipvltavenvmlpmifvgtp 134
Cdd:smart00382 7 IVGPPGSGKTTLARALAReLGPPGGGVIYIDGEDILEEVLDQL------------------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 135 yedaivkakkllelvgLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLHTGLKLI-----NLLKEINE 209
Cdd:smart00382 50 ----------------LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelRLLLLLKS 113
|
170 180 190
....*....|....*....|....*....|....
gi 502908369 210 KKGVTIVTATHDLK------MVDVSDRIIWIRDG 237
Cdd:smart00382 114 EKNLTVILTTNDEKdlgpalLRRRFDRRIVLLLI 147
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
44-248 |
3.04e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.90 E-value: 3.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 44 VTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYE-----LAWLRAKKigyifQTFNLI--- 115
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrlargLVYLPEDR-----QSSGLYlda 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 116 PVLTAVENVM--LPMIFVGTPYEDAIVKakKLLELVGLgKFIH-HKPAE-LSGGQQQRVAAARALANDPSIILADEPTGN 191
Cdd:PRK15439 357 PLAWNVCALThnRRGFWIKPARENAVLE--RYRRALNI-KFNHaEQAARtLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502908369 192 LDLHTGLKLINLLKEInEKKGVTIVTATHDL-KMVDVSDRIIWIRDGKIEKIELRRDI 248
Cdd:PRK15439 434 VDVSARNDIYQLIRSI-AAQNVAVLFISSDLeEIEQMADRVLVMHQGEISGALTGAAI 490
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
150-240 |
3.38e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.01 E-value: 3.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 150 GLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLHTGLKLIN--LLKEInekKGVTIVTATHDLKMVDV 227
Cdd:PTZ00243 771 GLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEecFLGAL---AGKTRVLATHQVHVVPR 847
|
90
....*....|...
gi 502908369 228 SDRIIWIRDGKIE 240
Cdd:PTZ00243 848 ADYVVALGDGRVE 860
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
21-189 |
4.11e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.59 E-value: 4.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 21 VVEAVEVKKYYkmGKfiVKALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAmlDAyelAWL 100
Cdd:NF033858 1 VARLEGVSHRY--GK--TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA--DA---RHR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 101 RA--KKIGYIFQTF--NLIPVLTAVENVMlpmiFVGTPY-EDAIVKAKK---LLELVGLGKFiHHKPA-ELSGGQQQRVA 171
Cdd:NF033858 72 RAvcPRIAYMPQGLgkNLYPTLSVFENLD----FFGRLFgQDAAERRRRideLLRATGLAPF-ADRPAgKLSGGMKQKLG 146
|
170
....*....|....*...
gi 502908369 172 AARALANDPSIILADEPT 189
Cdd:NF033858 147 LCCALIHDPDLLILDEPT 164
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
41-220 |
4.61e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.57 E-value: 4.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGldRPTGGkvYIDGvDIAMLDAYELAWLRAKKIGYIFQTFNLIPVLTA 120
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTG--VITG-GDRLVNGRPLDSSFQRSIGYVQQQDLHLPTSTV 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 121 VENVMLPMiFVGTP----------YEDAIVkakKLLELVGLGKFIHHKPAE-LSGGQQQRVAAARALANDP-SIILADEP 188
Cdd:TIGR00956 854 RESLRFSA-YLRQPksvsksekmeYVEEVI---KLLEMESYADAVVGVPGEgLNVEQRKRLTIGVELVAKPkLLLFLDEP 929
|
170 180 190
....*....|....*....|....*....|..
gi 502908369 189 TGNLDLHTGLKLINLLKEInEKKGVTIVTATH 220
Cdd:TIGR00956 930 TSGLDSQTAWSICKLMRKL-ADHGQAILCTIH 960
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
162-232 |
1.06e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 50.05 E-value: 1.06e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502908369 162 LSGGQQQRVAAARALAN-----DPSIILaDEPTGNLDLHTGLKLINLLKEINeKKGVTIVTATHDLKMVDVSDRII 232
Cdd:cd03227 78 LSGGEKELSALALILALaslkpRPLYIL-DEIDRGLDPRDGQALAEAILEHL-VKGAQVIVITHLPELAELADKLI 151
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
58-225 |
1.28e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 51.82 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 58 GPSGSGKTTLFNMIGGLDRPTGGKVyidgvdiaMLDAYE-LAWLRAKKIGYifQTFNLIPV-------LTAV-------- 121
Cdd:PRK15064 34 GANGCGKSTFMKILGGDLEPSAGNV--------SLDPNErLGKLRQDQFAF--EEFTVLDTvimghteLWEVkqerdriy 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 122 -------ENVM----LPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKP-AELSGGQQQRVAAARALANDPSIILADEPT 189
Cdd:PRK15064 104 alpemseEDGMkvadLEVKFAEMDGYTAEARAGELLLGVGIPEEQHYGLmSEVAPGWKLRVLLAQALFSNPDILLLDEPT 183
|
170 180 190
....*....|....*....|....*....|....*....
gi 502908369 190 GNLDLHTglklINLLKEINEKKGVTIVTATHD---LKMV 225
Cdd:PRK15064 184 NNLDINT----IRWLEDVLNERNSTMIIISHDrhfLNSV 218
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
29-193 |
1.82e-07 |
|
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: 51.83 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 29 KYYKMGKFIvkaLDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLdRPTGGKVYIDGVDiamLDAYEL-AWLRAkkigy 107
Cdd:TIGR01271 1226 KYTEAGRAV---LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVS---WNSVTLqTWRKA----- 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 108 ifqtFNLIPvltavENVMlpmIFVGT------PYED-AIVKAKKLLELVGLGKFIHHKPAEL-----------SGGQQQR 169
Cdd:TIGR01271 1294 ----FGVIP-----QKVF---IFSGTfrknldPYEQwSDEEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQL 1361
|
170 180
....*....|....*....|....
gi 502908369 170 VAAARALANDPSIILADEPTGNLD 193
Cdd:TIGR01271 1362 MCLARSILSKAKILLLDEPSAHLD 1385
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
41-232 |
1.98e-07 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 50.33 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 41 LDGVTFNVKRREYVSIMGPSGSGKTTL-FNMIGGldrpTGGKVYIDGvdiamLDAYELAWLRAKKIGYIFQTFNLIPVLt 119
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLaFDTIYA----EGQRRYVES-----LSAYARQFLGQMDKPDVDSIEGLSPAI- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 120 AVENVML---PMIFVGTPYE-----------DAIVKAKKLLELVGLGKFIHHKPAE-LSGGQQQRVAAARALANDPSIIL 184
Cdd:cd03270 81 AIDQKTTsrnPRSTVGTVTEiydylrllfarVGIRERLGFLVDVGLGYLTLSRSAPtLSGGEAQRIRLATQIGSGLTGVL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 502908369 185 --ADEPTGNLDLHTGLKLINLLKEInEKKGVTIVTATHDLKMVDVSDRII 232
Cdd:cd03270 161 yvLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDTIRAADHVI 209
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
19-221 |
2.45e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 51.27 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 19 EYVVEAVEVKKYYKMGKFIvkaLDGVTFN----VKrreyVSIMGPSGSGKTTLFNMIGGLDRPTGGKvyidgvdiamlda 94
Cdd:PRK11819 4 QYIYTMNRVSKVVPPKKQI---LKDISLSffpgAK----IGVLGLNGAGKSTLLRIMAGVDKEFEGE------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 95 yelAWLRAK-KIGYIFQTFNLIPVLTAVENVMLPM--IF--------VGTPYEDAIVKAKKLLELVG-LGKFIHHK---- 158
Cdd:PRK11819 64 ---ARPAPGiKVGYLPQEPQLDPEKTVRENVEEGVaeVKaaldrfneIYAAYAEPDADFDALAAEQGeLQEIIDAAdawd 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 159 ---------------PAE-----LSGGQQQRVAAARALANDPSIILADEPTGNLDLHTGLKLINLLKEInekKGvTIVTA 218
Cdd:PRK11819 141 ldsqleiamdalrcpPWDakvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDY---PG-TVVAV 216
|
...
gi 502908369 219 THD 221
Cdd:PRK11819 217 THD 219
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
138-232 |
3.23e-07 |
|
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: 50.78 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 138 AIVKAKKLLELVGLGKFIHHKPA-ELSGGQQQRVAAARAL---ANDPSIILADEPTGNLDLHTGLKLINLLKEInEKKGV 213
Cdd:TIGR00630 805 SISRKLQTLCDVGLGYIRLGQPAtTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRL-VDKGN 883
|
90
....*....|....*....
gi 502908369 214 TIVTATHDLKMVDVSDRII 232
Cdd:TIGR00630 884 TVVVIEHNLDVIKTADYII 902
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
45-220 |
3.32e-07 |
|
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: 50.90 E-value: 3.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 45 TFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDgvdiamldayelawlRAKKIGYIFQTfnliPVL---TAV 121
Cdd:TIGR00954 472 SFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP---------------AKGKLFYVPQR----PYMtlgTLR 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 122 ENVMLPMI---FVGTPYEDAIVKakKLLELVGLGKFIHHKPA---------ELSGGQQQRVAAARALANDPSIILADEPT 189
Cdd:TIGR00954 533 DQIIYPDSsedMKRRGLSDKDLE--QILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECT 610
|
170 180 190
....*....|....*....|....*....|.
gi 502908369 190 GNLDLHTGLKLINLLKEinekKGVTIVTATH 220
Cdd:TIGR00954 611 SAVSVDVEGYMYRLCRE----FGITLFSVSH 637
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
144-232 |
3.95e-07 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 49.92 E-value: 3.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 144 KLLELVGLGKFIHHKPA-ELSGGQQQRVAAARAL---ANDPSIILADEPTGNLDLHTGLKLINLLKEINEkKGVTIVTAT 219
Cdd:cd03271 151 QTLCDVGLGYIKLGQPAtTLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVD-KGNTVVVIE 229
|
90
....*....|...
gi 502908369 220 HDLKMVDVSDRII 232
Cdd:cd03271 230 HNLDVIKCADWII 242
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
160-237 |
4.97e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 50.60 E-value: 4.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 160 AELSGGQQQRVAAARALANDPSII--LADEPTGNLDLHTGLKLINLLKEINEKkGVTIVTATHDLKMVDVSDRIIWIRDG 237
Cdd:PRK00635 475 ATLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQ-GNTVLLVEHDEQMISLADRIIDIGPG 553
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
54-231 |
5.19e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 49.29 E-value: 5.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 54 VSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLDAYE-------LAWLRAKKIGYIF--QTFNLIPvlTAVENV 124
Cdd:cd03236 29 LGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDEILDEFRgselqnyFTKLLEGDVKVIVkpQYVDLIP--KAVKGK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 125 MLPMIfvgtPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLHTGLKLINLL 204
Cdd:cd03236 107 VGELL----KKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLI 182
|
170 180
....*....|....*....|....*...
gi 502908369 205 KEINEKKGVTIVTaTHDLKMVD-VSDRI 231
Cdd:cd03236 183 RELAEDDNYVLVV-EHDLAVLDyLSDYI 209
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
24-245 |
6.82e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 49.35 E-value: 6.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 24 AVEVKKYYK-MGKfiVKALDGVTFNVKRREYVSIMGPSGSGKTTlfnmiGGLdrptggKVYIDGVDIAMLDAYELAWLRA 102
Cdd:NF000106 13 AVEVRGLVKhFGE--VKAVDGVDLDVREGTVLGVLGP*GAA**R-----GAL------PAHV*GPDAGRRPWRF*TWCAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 103 KKIgyIFQTFNL-IPV-------LTAVENVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAAR 174
Cdd:NF000106 80 RRA--LRRTIG*hRPVr*grresFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502908369 175 ALANDPSIILADEPTGNLDLHTGLKLINLLKEInEKKGVTIVTATHDLKMVD-------VSDRIIWIRDGKIEKIELR 245
Cdd:NF000106 158 SMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSM-VRDGATVLLTTQYMEEAEqlaheltVIDRGRVIADGKVDELKTK 234
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
162-235 |
7.16e-07 |
|
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: 48.37 E-value: 7.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 162 LSGGQQQ------RVAAARALANDPSIILADEPTGNLDL-HTGLKLINLLKEINEKKGVTIVTATHDLKMVDVSDRIIWI 234
Cdd:cd03240 116 CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHDEELVDAADHIYRV 195
|
.
gi 502908369 235 R 235
Cdd:cd03240 196 E 196
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
40-239 |
7.67e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 49.71 E-value: 7.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 40 ALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVYIDGVDIAMLdayELAWLRAKkigyiFQTFNLIPVL- 118
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---QLDSWRSR-----LAVVSQTPFLf 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 119 --TAVENVMLpmifvGTP--YEDAIVKAKKL-------LEL-VGLGKFIHHKPAELSGGQQQRVAAARALANDPSIILAD 186
Cdd:PRK10789 402 sdTVANNIAL-----GRPdaTQQEIEHVARLasvhddiLRLpQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILD 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502908369 187 EPTGNLDLHTGLKLINLLKEINEKKgvTIVTATHDLKMVDVSDRIIWIRDGKI 239
Cdd:PRK10789 477 DALSAVDGRTEHQILHNLRQWGEGR--TVIISAHRLSALTEASEILVMQHGHI 527
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
37-239 |
4.27e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.41 E-value: 4.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 37 IVKALDGVtfnVKRREYVSIMGPSGSGKTTLFNMIG----GLDRPTGGKVYIDGVDIAMLDAYelawLRAKKIgYIFQTF 112
Cdd:TIGR00956 76 ILKPMDGL---IKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKH----YRGDVV-YNAETD 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 113 NLIPVLTAVENVMLP--MIFVGTPYE--DAIVKAKKLLELV----GLGkfiHHKPAE--------LSGGQQQRVAAARAL 176
Cdd:TIGR00956 148 VHFPHLTVGETLDFAarCKTPQNRPDgvSREEYAKHIADVYmatyGLS---HTRNTKvgndfvrgVSGGERKRVSIAEAS 224
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502908369 177 ANDPSIILADEPTGNLDLHTGLKLINLLKEI----NEKKGVTIVTATHDlkMVDVSDRIIWIRDGKI 239
Cdd:TIGR00956 225 LGGAKIQCWDNATRGLDSATALEFIRALKTSanilDTTPLVAIYQCSQD--AYELFDKVIVLYEGYQ 289
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
162-242 |
5.37e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.03 E-value: 5.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 162 LSGGQQQRVAAARALANDPSIILADEPTGNLDLHTGLKLINLLKEINEK-KGVTIVTATHDlKMVDVSDRIIWIRDGKIE 240
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKdKGIIIISSEMP-ELLGITDRILVMSNGLVA 470
|
..
gi 502908369 241 KI 242
Cdd:PRK10982 471 GI 472
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
156-200 |
1.19e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.01 E-value: 1.19e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 502908369 156 HHKPAELSGGQQQRVAAARALANDPSIILADEPTGNLDLHTGLKL 200
Cdd:PLN03073 339 VKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWL 383
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
24-239 |
7.84e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 43.34 E-value: 7.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 24 AVEVKKYYKmgKFIVKAL-DGVTFNVKRREYVSIMGPSGSGKTTLFNMIGGLDRPTGGKVyidgvdiamldayelAWLRA 102
Cdd:PRK15064 319 ALEVENLTK--GFDNGPLfKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV---------------KWSEN 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 103 KKIGYIFQTfnlipvlTAVE-----NVMLPMIFVGTPYEDAIVKAKKLLELVGLGKFIHHKPAELSGGQQQRVAAARALA 177
Cdd:PRK15064 382 ANIGYYAQD-------HAYDfendlTLFDWMSQWRQEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMM 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502908369 178 NDPSIILADEPTGNLDLHTGLKLINLLKEInekKGvTIVTATHDLKMVD-VSDRIIWIRDGKI 239
Cdd:PRK15064 455 QKPNVLVMDEPTNHMDMESIESLNMALEKY---EG-TLIFVSHDREFVSsLATRIIEITPDGV 513
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
34-217 |
1.01e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 42.47 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 34 GKFIVKALDgvtFNVKRREYVSIMGPSGSGKTTLFNMIGGLD--RPTGGKVYIDGVDIAMLDAYE-------LAWLRAKK 104
Cdd:PRK09580 13 DKAILRGLN---LEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDragegifMAFQYPVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 105 IGYIFQTFNLIPVLTAVENVMLPMIFVGTPYEDAIVKAKKLLELvglgkfihhkPAEL---------SGGQQQRVAAARA 175
Cdd:PRK09580 90 IPGVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKM----------PEDLltrsvnvgfSGGEKKRNDILQM 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 502908369 176 LANDPSIILADEPTGNLDLhTGLKL----INLLKeiNEKKGVTIVT 217
Cdd:PRK09580 160 AVLEPELCILDESDSGLDI-DALKIvadgVNSLR--DGKRSFIIVT 202
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
162-232 |
1.61e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 1.61e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502908369 162 LSGGQQQRVAAARALAN---DPSIILADEPTGNLDLHTGLKLINLLKEINEkKGVTIVTATHDLKMVDVSDRII 232
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTH-QGHTVVIIEHNMHVVKVADYVL 882
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
137-232 |
5.15e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.21 E-value: 5.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 137 DAIVKAKKLLEL---VGLGkFIH-HKPA-ELSGGQQQRVAAARAL---ANDPSIILADEPTgnldlhTGL------KLIN 202
Cdd:PRK00349 802 EAIPKIARKLQTlvdVGLG-YIKlGQPAtTLSGGEAQRVKLAKELskrSTGKTLYILDEPT------TGLhfedirKLLE 874
|
90 100 110
....*....|....*....|....*....|
gi 502908369 203 LLKEINEkKGVTIVTATHDLKMVDVSDRII 232
Cdd:PRK00349 875 VLHRLVD-KGNTVVVIEHNLDVIKTADWII 903
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
138-232 |
1.93e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 39.24 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 138 AIVKAKKLLELVGLGkFIH-HKPA-ELSGGQQQRVAAARALA---NDPSIILADEPTgnldlhTGL------KLINLLKE 206
Cdd:COG0178 802 KIARKLQTLQDVGLG-YIKlGQPAtTLSGGEAQRVKLASELSkrsTGKTLYILDEPT------TGLhfhdirKLLEVLHR 874
|
90 100
....*....|....*....|....*.
gi 502908369 207 INEkKGVTIVTATHDLKMVDVSDRII 232
Cdd:COG0178 875 LVD-KGNTVVVIEHNLDVIKTADWII 899
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
39-239 |
2.54e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 38.62 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 39 KALDGVTFNVKRREYVSIMGPSGSGKTTLFNMIGG--LDRPTGGKVYIDGVDIAML---DAYElawlraKKIGYIFQ--- 110
Cdd:NF040905 274 KVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGrsYGRNISGTVFKDGKEVDVStvsDAID------AGLAYVTEdrk 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 111 TFNLIPVLTAVENVMLPM---------------IFVGTPYEDAI-VKAKKLLELVGlgkfihhkpaELSGGQQQRVAAAR 174
Cdd:NF040905 348 GYGLNLIDDIKRNITLANlgkvsrrgvideneeIKVAEEYRKKMnIKTPSVFQKVG----------NLSGGNQQKVVLSK 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 175 ALANDPSIILADEPTGNLDLhtGLK-----LINLLKEinEKKGVtIVTATHDLKMVDVSDRIIWIRDGKI 239
Cdd:NF040905 418 WLFTDPDVLILDEPTRGIDV--GAKyeiytIINELAA--EGKGV-IVISSELPELLGMCDRIYVMNEGRI 482
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
163-234 |
4.30e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 38.23 E-value: 4.30e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502908369 163 SGGQQQRVAAARALANDPSIILADEPTGNLDLHTGLKLINLLKEINEkkgvTIVTATHDLKMVD-VSDRIIWI 234
Cdd:PRK10636 151 SGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG----TLILISHDRDFLDpIVDKIIHI 219
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
42-68 |
6.34e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 34.11 E-value: 6.34e-03
10 20
....*....|....*....|....*..
gi 502908369 42 DGVTFNVKRREYVSIMGPSGSGKTTLF 68
Cdd:pfam13555 13 DGHTIPIDPRGNTLLTGPSGSGKSTLL 39
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
149-232 |
9.56e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 37.30 E-value: 9.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502908369 149 VGLGKFIHHKPAE-LSGGQQQRVAAARALANDPSIIL--ADEPTGNLDLHTGLKLINLLKEInEKKGVTIVTATHDLKMV 225
Cdd:TIGR00630 475 VGLDYLSLSRAAGtLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHDEDTI 553
|
....*..
gi 502908369 226 DVSDRII 232
Cdd:TIGR00630 554 RAADYVI 560
|
|
| |
