|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-224 |
2.85e-117 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 334.32 E-value: 2.85e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSYGNKHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAEF 82
Cdd:COG1136 4 LLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 83 RKQHLGFIFQEYNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEP 162
Cdd:COG1136 84 RRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1112987593 163 SIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDPVAASFCSRVVFIKDGQIYTQ 224
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-221 |
3.66e-109 |
|
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: 313.66 E-value: 3.66e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGNKHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAEFR 83
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 84 KQHLGFIFQEYNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPS 163
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1112987593 164 IIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDPVAASFCSRVVFIKDGQI 221
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
3-221 |
9.92e-74 |
|
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: 224.24 E-value: 9.92e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSYGNKHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAEF 82
Cdd:COG4181 8 IIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 83 RKQHLGFIFQEYNLLDTLTVKENILLPLSITkiSKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEP 162
Cdd:COG4181 88 RARHVGFVFQSFQLLPTLTALENVMLPLELA--GRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1112987593 163 SIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDPVAASFCSRVVFIKDGQI 221
Cdd:COG4181 166 AILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRL 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
2-221 |
6.54e-73 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 221.85 E-value: 6.54e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 2 MIlEAKKIRKSYGNKHnkhEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAE 81
Cdd:COG2884 1 MI-RFENVSKRYPGGR---EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 82 FRkQHLGFIFQEYNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHE 161
Cdd:COG2884 77 LR-RRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1112987593 162 PSIIFADEPTGALDSKSASDLLNKLSQLNQkRRATIVMVTHDP-VAASFCSRVVFIKDGQI 221
Cdd:COG2884 156 PELLLADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLeLVDRMPKRVLELEDGRL 215
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-203 |
6.39e-68 |
|
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: 208.87 E-value: 6.39e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGNKHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNmkekqlaefR 83
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG---------P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 84 KQHLGFIFQEYNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPS 163
Cdd:cd03293 72 GPDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1112987593 164 IIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHD 203
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHD 191
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
3-222 |
2.34e-67 |
|
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: 207.59 E-value: 2.34e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSYGNKHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAEF 82
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 83 RKQHLGFIFQEYNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEP 162
Cdd:TIGR02211 81 RNKKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 163 SIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDPVAASFCSRVVFIKDGQIY 222
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDGQLF 220
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-214 |
4.33e-67 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 208.41 E-value: 4.33e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 1 MMILEAKKIRKSYGNKHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNmkekqla 80
Cdd:COG1116 5 APALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 81 efRKQHLGFIFQEYNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIH 160
Cdd:COG1116 78 --PGPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1112987593 161 EPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDPV-AASFCSRVV 214
Cdd:COG1116 156 DPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDeAVFLADRVV 210
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
7-216 |
2.24e-66 |
|
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: 204.77 E-value: 2.24e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 7 KKIRKSYGNKHnkheVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAEFRKQH 86
Cdd:TIGR03608 2 KNISKKFGDKV----ILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 87 LGFIFQEYNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPSIIF 166
Cdd:TIGR03608 78 LGYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLIL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1112987593 167 ADEPTGALDSKSASDLLNKLSQLNQKRRaTIVMVTHDPVAASFCSRVVFI 216
Cdd:TIGR03608 158 ADEPTGSLDPKNRDEVLDLLLELNDEGK-TIIIVTHDPEVAKQADRVIEL 206
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-221 |
4.07e-66 |
|
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: 204.74 E-value: 4.07e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSYGNKHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAEF 82
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 83 RkQHLGFIFQEYNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEP 162
Cdd:cd03258 81 R-RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 163 SIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHD-PVAASFCSRVVFIKDGQI 221
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEmEVVKRICDRVAVMEKGEV 219
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
2-221 |
1.07e-65 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 207.24 E-value: 1.07e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 2 MIlEAKKIRKSYGNKHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAE 81
Cdd:COG1135 1 MI-ELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 82 FRKQhLGFIFQEYNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHE 161
Cdd:COG1135 80 ARRK-IGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1112987593 162 PSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHD-PVAASFCSRVVFIKDGQI 221
Cdd:COG1135 159 PKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEmDVVRRICDRVAVLENGRI 219
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-221 |
2.61e-65 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 206.85 E-value: 2.61e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 1 MMILEAKKIRKSYGNkhnkHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQla 80
Cdd:COG3839 1 MASLELENVSKSYGG----VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 81 efRkqHLGFIFQEYNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIH 160
Cdd:COG3839 75 --R--NIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1112987593 161 EPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDPV-AASFCSRVVFIKDGQI 221
Cdd:COG3839 151 EPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVeAMTLADRIAVMNDGRI 212
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-221 |
3.22e-64 |
|
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: 199.28 E-value: 3.22e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGNKHnkheVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEkqlaefR 83
Cdd:cd03259 1 LELKGLSKTYGSVR----ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPP------E 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 84 KQHLGFIFQEYNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPS 163
Cdd:cd03259 71 RRNIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1112987593 164 IIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDPV-AASFCSRVVFIKDGQI 221
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEeALALADRIAVMNEGRI 209
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-221 |
4.85e-61 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 192.13 E-value: 4.85e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSYGNkhnkHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLL---NVLSSIDqvsGGTININQAEMTnMKEKQL 79
Cdd:COG1126 1 MIEIENLHKSFGD----LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLrciNLLEEPD---SGTITVDGEDLT-DSKKDI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 80 AEFRkQHLGFIFQEYNLLDTLTVKENILL-PLSITKISKKEAgqkfEEVAKEL----GIFELKDKYPNEISGGQKQRTSA 154
Cdd:COG1126 73 NKLR-RKVGMVFQQFNLFPHLTVLENVTLaPIKVKKMSKAEA----EERAMELlervGLADKADAYPAQLSGGQQQRVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1112987593 155 ARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLnQKRRATIVMVTHD-PVAASFCSRVVFIKDGQI 221
Cdd:COG1126 148 ARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDL-AKEGMTMVVVTHEmGFAREVADRVVFMDGGRI 214
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-221 |
5.44e-61 |
|
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: 192.12 E-value: 5.44e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSYGNKHnkheVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAEF 82
Cdd:COG1127 5 MIEVRNLTKSFGDRV----VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 83 RKQhLGFIFQEYNLLDTLTVKENILLPLSI-TKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHE 161
Cdd:COG1127 81 RRR-IGMLFQGGALFDSLTVFENVAFPLREhTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1112987593 162 PSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHD-PVAASFCSRVVFIKDGQI 221
Cdd:COG1127 160 PEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDlDSAFAIADRVAVLADGKI 220
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
3-221 |
6.14e-60 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 199.95 E-value: 6.14e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSYGNKHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAEF 82
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 83 RKQHLGFIFQEYNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEP 162
Cdd:PRK10535 84 RREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1112987593 163 SIIFADEPTGALDSKSASDLLNKLSQLNQkRRATIVMVTHDPVAASFCSRVVFIKDGQI 221
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQLRD-RGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-221 |
6.77e-60 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 189.50 E-value: 6.77e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 2 MILEAKKIRKSYGNKHnkhEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAE 81
Cdd:COG3638 1 PMLELRNLSKRYPGGT---PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 82 FRKQhLGFIFQEYNLLDTLTVKENIL--------LPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTS 153
Cdd:COG3638 78 LRRR-IGMIFQQFNLVPRLSVLTNVLagrlgrtsTWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1112987593 154 AARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDP-VAASFCSRVVFIKDGQI 221
Cdd:COG3638 157 IARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVdLARRYADRIIGLRDGRV 225
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
13-221 |
1.95e-59 |
|
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: 187.53 E-value: 1.95e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 13 YGNKHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAEFRKQhLGFIFQ 92
Cdd:TIGR02982 11 YGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQLRRR-IGYIFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 93 EYNLLDTLTVKENILLPLSI-TKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPSIIFADEPT 171
Cdd:TIGR02982 90 AHNLLGFLTARQNVQMALELqPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1112987593 172 GALDSKSASDLLNKLSQLNQKRRATIVMVTHDPVAASFCSRVVFIKDGQI 221
Cdd:TIGR02982 170 AALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRILDVADRILQMEDGKL 219
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-221 |
2.10e-59 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 191.46 E-value: 2.10e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 1 MMILEAKKIRKSYGNKHnkheVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKekqlA 80
Cdd:COG3842 3 MPALELENVSKRYGDVT----ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLP----P 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 81 EFRkqHLGFIFQEYNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIH 160
Cdd:COG3842 75 EKR--NVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1112987593 161 EPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDPV-AASFCSRVVFIKDGQI 221
Cdd:COG3842 153 EPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEeALALADRIAVMNDGRI 214
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-221 |
3.10e-59 |
|
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: 187.33 E-value: 3.10e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSYGNKHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAEF 82
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 83 RKqHLGFIFQE-YNLLD-TLTVKENILLPLSITKISKKEAgQKFEEVAKELGIFELK----DKYPNEISGGQKQRTSAAR 156
Cdd:cd03257 81 RK-EIQMVFQDpMSSLNpRMTIGEQIAEPLRIHGKLSKKE-ARKEAVLLLLVGVGLPeevlNRYPHELSGGQRQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1112987593 157 AFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHD-PVAASFCSRVVFIKDGQI 221
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDlGVVAKIADRVAVMYAGKI 224
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-221 |
1.22e-58 |
|
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: 185.04 E-value: 1.22e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGNKHnkheVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNmKEKQLAEFR 83
Cdd:cd03262 1 IEIKNLHKSFGDFH----VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 84 kQHLGFIFQEYNLLDTLTVKENILL-PLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEP 162
Cdd:cd03262 76 -QKVGMVFQQFNLFPHLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 163 SIIFADEPTGALDSKSASDLLNKLSQLNQKRRaTIVMVTHD-PVAASFCSRVVFIKDGQI 221
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEEGM-TMVVVTHEmGFAREVADRVIFMDDGRI 213
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-221 |
3.06e-58 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 184.88 E-value: 3.06e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGNKHnkheVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTnmkeKQLAEFR 83
Cdd:COG1131 1 IEVRGLTKRYGDKT----ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA----RDPAEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 84 kQHLGFIFQEYNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPS 163
Cdd:COG1131 73 -RRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1112987593 164 IIFADEPTGALDSKSASDLLNKLSQLNqKRRATIVMVTHD-PVAASFCSRVVFIKDGQI 221
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELA-AEGKTVLLSTHYlEEAERLCDRVAIIDKGRI 209
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-224 |
3.64e-58 |
|
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: 185.25 E-value: 3.64e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSYGNKhnkhEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAef 82
Cdd:COG1120 1 MLEAENLSVGYGGR----PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELA-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 83 rkQHLGFIFQEYNLLDTLTVKENILL---P-LSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAF 158
Cdd:COG1120 75 --RRIAYVPQEPPAPFGLTVRELVALgryPhLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1112987593 159 IHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDP-VAASFCSRVVFIKDGQIYTQ 224
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLnLAARYADRLVLLKDGRIVAQ 219
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-221 |
1.11e-57 |
|
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: 191.27 E-value: 1.11e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSYG-NKHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAE 81
Cdd:COG1123 260 LLEVRNLSKRYPvRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 82 FRKqHLGFIFQE-YNLLD-TLTVKENILLPLSITKI-SKKEAGQKFEEVAKELGIF-ELKDKYPNEISGGQKQRTSAARA 157
Cdd:COG1123 340 LRR-RVQMVFQDpYSSLNpRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIARA 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1112987593 158 FIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHD-PVAASFCSRVVFIKDGQI 221
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDlAVVRYIADRVAVMYDGRI 483
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-221 |
1.11e-56 |
|
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: 181.15 E-value: 1.11e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGNKHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININqaeMTNMKEKQLAEFR 83
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFD---GRPVTRRRRKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 84 KQhLGFIFQE-YNLLD-TLTVKENILLPLSITKIskKEAGQKFEEVAKELGI-FELKDKYPNEISGGQKQRTSAARAFIH 160
Cdd:COG1124 79 RR-VQMVFQDpYASLHpRHTVDRILAEPLRIHGL--PDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1112987593 161 EPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDP-VAASFCSRVVFIKDGQI 221
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLaVVAHLCDRVAVMQNGRI 217
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-221 |
2.53e-55 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 177.31 E-value: 2.53e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGNKHnkheVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAEFR 83
Cdd:cd03261 1 IELRGLTKSFGGRT----VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 84 KQhLGFIFQEYNLLDTLTVKENILLPLSI-TKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEP 162
Cdd:cd03261 77 RR-MGMLFQSGALFDSLTVFENVAFPLREhTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 163 SIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHD-PVAASFCSRVVFIKDGQI 221
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDlDTAFAIADRIAVLYDGKI 215
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-221 |
8.44e-55 |
|
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: 176.22 E-value: 8.44e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGNKHNkheVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAEFR 83
Cdd:cd03256 1 IEVENLSKTYPNGKK---ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 84 KqHLGFIFQEYNLLDTLTVKENIL------------LPLSITKISKKEAGQKFEEVakelGIFELKDKYPNEISGGQKQR 151
Cdd:cd03256 78 R-QIGMIFQQFNLIERLSVLENVLsgrlgrrstwrsLFGLFPKEEKQRALAALERV----GLLDKAYQRADQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1112987593 152 TSAARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDP-VAASFCSRVVFIKDGQI 221
Cdd:cd03256 153 VAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVdLAREYADRIVGLKDGRI 223
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-221 |
1.20e-53 |
|
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: 172.44 E-value: 1.20e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGNKHnkheVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKqlaefr 83
Cdd:cd03301 1 VELENVTKRFGNVT----ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 84 KQHLGFIFQEYNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPS 163
Cdd:cd03301 71 DRDIAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1112987593 164 IIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDPVAA-SFCSRVVFIKDGQI 221
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAmTMADRIAVMNDGQI 209
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-221 |
1.95e-53 |
|
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: 172.52 E-value: 1.95e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYgnkHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQaemTNMKEKQLAEFR 83
Cdd:COG1122 1 IELENLSFSY---PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDG---KDITKKNLRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 84 kQHLGFIFQ--EYNLLDTlTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHE 161
Cdd:COG1122 75 -RKVGLVFQnpDDQLFAP-TVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAME 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1112987593 162 PSIIFADEPTGALDSKSASDLLNKLSQLNQKRRaTIVMVTHDP-VAASFCSRVVFIKDGQI 221
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLKRLNKEGK-TVIIVTHDLdLVAELADRVIVLDDGRI 212
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-221 |
2.87e-53 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 172.04 E-value: 2.87e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGNKHnkheVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKqlaefr 83
Cdd:cd03300 1 IELENVSKFYGGFV----ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 84 KQHLGFIFQEYNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPS 163
Cdd:cd03300 71 KRPVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1112987593 164 IIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDPVAA-SFCSRVVFIKDGQI 221
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEAlTMSDRIAVMNKGKI 209
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
3-221 |
3.72e-53 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 171.50 E-value: 3.72e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSYGNKHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAEF 82
Cdd:PRK10584 6 IVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 83 RKQHLGFIFQEYNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEP 162
Cdd:PRK10584 86 RAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1112987593 163 SIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDPVAASFCSRVVFIKDGQI 221
Cdd:PRK10584 166 DVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
2-221 |
1.34e-52 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 173.83 E-value: 1.34e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 2 MIlEAKKIRKSYGNKHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAE 81
Cdd:PRK11153 1 MI-ELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 82 FRkQHLGFIFQEYNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHE 161
Cdd:PRK11153 80 AR-RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1112987593 162 PSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHD-PVAASFCSRVVFIKDGQI 221
Cdd:PRK11153 159 PKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEmDVVKRICDRVAVIDAGRL 219
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-221 |
2.39e-52 |
|
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: 170.17 E-value: 2.39e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSYGNKHnkhEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAEF 82
Cdd:TIGR02315 1 MLEVENLSKVYPNGK---QALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 83 RkQHLGFIFQEYNLLDTLTVKENILLPL--------SITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSA 154
Cdd:TIGR02315 78 R-RRIGMIFQHYNLIERLTVLENVLHGRlgykptwrSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1112987593 155 ARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHD-PVAASFCSRVVFIKDGQI 221
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQvDLAKKYADRIVGLKAGEI 224
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-220 |
3.91e-52 |
|
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: 167.36 E-value: 3.91e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGNKHnkheVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMkEKQLAEFR 83
Cdd:cd03229 1 LELKNVSKRYGQKT----VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDL-EDELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 84 kQHLGFIFQEYNLLDTLTVKENILLPLsitkiskkeagqkfeevakelgifelkdkypneiSGGQKQRTSAARAFIHEPS 163
Cdd:cd03229 76 -RRIGMVFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1112987593 164 IIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDP-VAASFCSRVVFIKDGQ 220
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLdEAARLADRVVVLRDGK 178
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-221 |
4.01e-52 |
|
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: 168.74 E-value: 4.01e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGNKHnkhEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAEFR 83
Cdd:cd03292 1 IEFINVTKTYPNGT---AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 84 kQHLGFIFQEYNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPS 163
Cdd:cd03292 78 -RKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1112987593 164 IIFADEPTGALDSKSASDLLNKLSQLNqKRRATIVMVTHDP-VAASFCSRVVFIKDGQI 221
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKIN-KAGTTVVVATHAKeLVDTTRHRVIALERGKL 214
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-220 |
5.76e-52 |
|
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: 168.03 E-value: 5.76e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 5 EAKKIRKSYGNKhnKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININqaeMTNMKEKQLAEFRK 84
Cdd:cd03225 1 ELKNLSFSYPDG--ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVD---GKDLTKLSLKELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 85 qHLGFIFQ--EYNLLdTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEP 162
Cdd:cd03225 76 -KVGLVFQnpDDQFF-GPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1112987593 163 SIIFADEPTGALDSKSASDLLNKLSQLNQKRRaTIVMVTHDP-VAASFCSRVVFIKDGQ 220
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAEGK-TIIIVTHDLdLLLELADRVIVLEDGK 211
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-235 |
2.62e-51 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 167.62 E-value: 2.62e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 1 MMILEAKKIRKSYgnkhNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMK----E 76
Cdd:PRK11264 1 MSAIEVKNLVKKF----HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARslsqQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 77 KQLAEFRKQHLGFIFQEYNLLDTLTVKENILL-PLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAA 155
Cdd:PRK11264 77 KGLIRQLRQHVGFVFQNFNLFPHRTVLENIIEgPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 156 RAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRaTIVMVTHD-PVAASFCSRVVFIKDGQIYTQlnkgGQDRQM 234
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEmSFARDVADRAIFMDQGRIVEQ----GPAKAL 231
|
.
gi 1112987593 235 F 235
Cdd:PRK11264 232 F 232
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-224 |
3.37e-51 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 164.92 E-value: 3.37e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 5 EAKKIRKSYGNKhnkhEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAefrk 84
Cdd:cd03214 1 EVENLSVGYGGR----TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELA---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 85 QHLGFIFQeynlldtltvkenillplsitkiskkeagqkfeeVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPSI 164
Cdd:cd03214 73 RKIAYVPQ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPI 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1112987593 165 IFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDP-VAASFCSRVVFIKDGQIYTQ 224
Cdd:cd03214 119 LLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLnLAARYADRVILLKDGRIVAQ 179
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
4-221 |
1.15e-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: 169.06 E-value: 1.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGNkhnkHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKqlaefr 83
Cdd:TIGR03265 5 LSIDNIRKRFGA----FTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQ------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 84 KQHLGFIFQEYNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPS 163
Cdd:TIGR03265 75 KRDYGIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1112987593 164 IIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDPVAA-SFCSRVVFIKDGQI 221
Cdd:TIGR03265 155 LLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEAlSMADRIVVMNHGVI 213
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
4-221 |
4.30e-50 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 164.20 E-value: 4.30e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGNkhnkHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKekqlaeFR 83
Cdd:TIGR00968 1 IEIANISKRFGS----FQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVH------AR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 84 KQHLGFIFQEYNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPS 163
Cdd:TIGR00968 71 DRKIGFVFQHYALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQ 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1112987593 164 IIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDPV-AASFCSRVVFIKDGQI 221
Cdd:TIGR00968 151 VLLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEeAMEVADRIVVMSNGKI 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-221 |
1.40e-49 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 170.08 E-value: 1.40e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSYGnkHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSG---GTININQAEMTNMKEKQl 79
Cdd:COG1123 4 LLEVRDLSVRYP--GGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEAL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 80 aefRKQHLGFIFQEY-NLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAF 158
Cdd:COG1123 81 ---RGRRIGMVFQDPmTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1112987593 159 IHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDP-VAASFCSRVVFIKDGQI 221
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLgVVAEIADRVVVMDDGRI 221
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-221 |
1.62e-49 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 165.71 E-value: 1.62e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 2 MILEAKKIRKSYGNKHnkheVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININ-QAEMTNMKEkqla 80
Cdd:COG1118 1 MSIEVRNISKRFGSFT----LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNgRDLFTNLPP---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 81 efRKQHLGFIFQEYNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIH 160
Cdd:COG1118 73 --RERRVGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1112987593 161 EPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDPV-AASFCSRVVFIKDGQI 221
Cdd:COG1118 151 EPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEeALELADRVVVMNQGRI 212
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-222 |
7.79e-49 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 160.69 E-value: 7.79e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGNKHnkhevlKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTnmkeKQLAEFR 83
Cdd:COG3840 2 LRLDDLTYRYGDFP------LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLT----ALPPAER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 84 KqhLGFIFQEYNLLDTLTVKENILLPLSIT-KISKKEAgQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEP 162
Cdd:COG3840 72 P--VSMLFQENNLFPHLTVAQNIGLGLRPGlKLTAEQR-AQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1112987593 163 SIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDPV-AASFCSRVVFIKDGQIY 222
Cdd:COG3840 149 PILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEdAARIADRVLLVADGRIA 209
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-214 |
1.07e-48 |
|
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: 162.92 E-value: 1.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSYGNKHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTL----LNVLSSIDQVSGgTININQAEMTNMKEKQ 78
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLaraiLGLLPPPGITSG-EILFDGEDLLKLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 79 LAEFRKQHLGFIFQE-YNLLD-TLTVKENILLPLSI-TKISKKEAGQKFEEVAKELGI---FELKDKYPNEISGGQKQRT 152
Cdd:COG0444 80 LRKIRGREIQMIFQDpMTSLNpVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1112987593 153 SAARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHD-PVAASFCSRVV 214
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDlGVVAEIADRVA 222
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-221 |
5.50e-48 |
|
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: 156.40 E-value: 5.50e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGNKhnkhEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQlaefr 83
Cdd:cd03230 1 IEVRNLSKRYGKK----TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEV----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 84 KQHLGFIFQEYNLLDTLTVKENILLplsitkiskkeagqkfeevakelgifelkdkypneiSGGQKQRTSAARAFIHEPS 163
Cdd:cd03230 72 KRRIGYLPEEPSLYENLTVRENLKL------------------------------------SGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1112987593 164 IIFADEPTGALDSKSASDLLNKLSQLNqKRRATIVMVTHD-PVAASFCSRVVFIKDGQI 221
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELK-KEGKTILLSSHIlEEAERLCDRVAILNNGRI 173
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
3-225 |
8.11e-48 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 158.06 E-value: 8.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSYGNKHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAEF 82
Cdd:PRK11629 5 LLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 83 RKQHLGFIFQEYNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEP 162
Cdd:PRK11629 85 RNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1112987593 163 SIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDPVAASFCSRVVFIKDGQIYTQL 225
Cdd:PRK11629 165 RLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAEL 227
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-221 |
1.95e-47 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 158.04 E-value: 1.95e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGNkhnkHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQaEMTNMK-------- 75
Cdd:COG4598 9 LEVRDLHKSFGD----LEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGG-EEIRLKpdrdgelv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 76 ---EKQLAEFRKQhLGFIFQEYNLLDTLTVKENILL-PLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQR 151
Cdd:COG4598 84 padRRQLQRIRTR-LGMVFQSFNLWSHMTVLENVIEaPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1112987593 152 TSAARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRaTIVMVTHD-PVAASFCSRVVFIKDGQI 221
Cdd:COG4598 163 AAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGR-TMLVVTHEmGFARDVSSHVVFLHQGRI 232
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-221 |
1.95e-46 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 153.82 E-value: 1.95e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGNKhnkhEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKekqLAEFR 83
Cdd:COG4619 1 LELEGLSFRVGGK----PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMP---PPEWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 84 KQhLGFIFQEYNLLDTlTVKENILLPLSITKisKKEAGQKFEEVAKELGI-FELKDKYPNEISGGQKQRTSAARAFIHEP 162
Cdd:COG4619 74 RQ-VAYVPQEPALWGG-TVRDNLPFPFQLRE--RKFDRERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 163 SIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDP-VAASFCSRVVFIKDGQI 221
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPeQIERVADRVLTLEAGRL 209
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-221 |
1.09e-45 |
|
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: 152.88 E-value: 1.09e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 2 MILEAKKIRKSYGNkhnkHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKekqlae 81
Cdd:cd03296 1 MSIEVRNVSKRFGD----FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 82 FRKQHLGFIFQEYNLLDTLTVKENILLPLSITKI----SKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARA 157
Cdd:cd03296 71 VQERNVGFVFQHYALFRHMTVFDNVAFGLRVKPRserpPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1112987593 158 FIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDPVAA-SFCSRVVFIKDGQI 221
Cdd:cd03296 151 LAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEAlEVADRVVVMNKGRI 215
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
2-221 |
1.22e-45 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 152.70 E-value: 1.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 2 MIlEAKKIRKSYGNKHnkheVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEmtnmKEKQLAE 81
Cdd:COG4555 1 MI-EVENLSKKYGKVP----ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGED----VRKEPRE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 82 FRKQhLGFIFQEYNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHE 161
Cdd:COG4555 72 ARRQ-IGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1112987593 162 PSIIFADEPTGALDSKSASDLLNKLSQLNQKRRaTIVMVTHDP-VAASFCSRVVFIKDGQI 221
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLLREILRALKKEGK-TVLFSSHIMqEVEALCDRVVILHKGKV 210
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-220 |
1.37e-45 |
|
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: 150.23 E-value: 1.37e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGNKHnkHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQaemTNMKEKQLAEFR 83
Cdd:cd03228 1 IEFKNVSFSYPGRP--KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDG---VDLRDLDLESLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 84 KqHLGFIFQEYNLLDTlTVKENILlplsitkiskkeagqkfeevakelgifelkdkypneiSGGQKQRTSAARAFIHEPS 163
Cdd:cd03228 76 K-NIAYVPQDPFLFSG-TIRENIL-------------------------------------SGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1112987593 164 IIFADEPTGALDSKSASDLLNKLSQLNQKRraTIVMVTHDPVAASFCSRVVFIKDGQ 220
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAKGK--TVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-222 |
1.85e-45 |
|
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: 151.50 E-value: 1.85e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGNKHNKheVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEM-TNMKEkqlaef 82
Cdd:cd03263 1 LQIRNLTKTYKKGTKP--AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIrTDRKA------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 83 RKQHLGFIFQEYNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEP 162
Cdd:cd03263 73 ARQSLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1112987593 163 SIIFADEPTGALDSKSASDLLNKLSQLNQKRraTIVMVTHDP-VAASFCSRVVFIKDGQIY 222
Cdd:cd03263 153 SVLLLDEPTSGLDPASRRAIWDLILEVRKGR--SIILTTHSMdEAEALCDRIAIMSDGKLR 211
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-221 |
2.05e-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: 151.56 E-value: 2.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGNKHnkheVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLS-SIDQVSG----GTININQAEMTNMKEKQ 78
Cdd:cd03260 1 IELRDLNVYYGDKH----ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNrLNDLIPGapdeGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 79 LaEFRKQhLGFIFQEYNLLDtLTVKENILLPLSITKI-SKKEAGQKFEEVAKELGIF-ELKDK-YPNEISGGQKQRTSAA 155
Cdd:cd03260 77 L-ELRRR-VGMVFQKPNPFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWdEVKDRlHALGLSGGQQQRLCLA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 156 RAFIHEPSIIFADEPTGALDSKSAS---DLLNKLsqlnqKRRATIVMVTHDPVAASFCS-RVVFIKDGQI 221
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAkieELIAEL-----KKEYTIVIVTHNMQQAARVAdRTAFLLNGRL 218
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
4-221 |
4.42e-45 |
|
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: 152.03 E-value: 4.42e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGNK-----------HNKHEVLKG---------IDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGT 63
Cdd:cd03294 1 IKIKGLYKIFGKNpqkafkllakgKSKEEILKKtgqtvgvndVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 64 ININQAEMTNMKEKQLAEFRKQHLGFIFQEYNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNE 143
Cdd:cd03294 81 VLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1112987593 144 ISGGQKQRTSAARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDPVAA-SFCSRVVFIKDGQI 221
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEAlRLGDRIAIMKDGRL 239
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-222 |
1.29e-44 |
|
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: 149.79 E-value: 1.29e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGNKHnkhevLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKqlaefr 83
Cdd:cd03299 1 LKVENLSKDWKEFK-----LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 84 KQHLGFIFQEYNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPS 163
Cdd:cd03299 70 KRDISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPK 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 164 IIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDPV-AASFCSRVVFIKDGQIY 222
Cdd:cd03299 150 ILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEeAWALADKVAIMLNGKLI 209
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-221 |
1.69e-44 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 149.78 E-value: 1.69e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 2 MILEAKKIRKSYGNkhnkHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEM---TNMKEKQ 78
Cdd:COG4161 1 MSIQLKNINCFYGS----HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 79 LAEFRkQHLGFIFQEYNLLDTLTVKENIL-LPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARA 157
Cdd:COG4161 77 IRLLR-QKVGMVFQQYNLWPHLTVMENLIeAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1112987593 158 FIHEPSIIFADEPTGALD---SKSASDLLNKLSQLNqkrrATIVMVTHD-PVAASFCSRVVFIKDGQI 221
Cdd:COG4161 156 LMMEPQVLLFDEPTAALDpeiTAQVVEIIRELSQTG----ITQVIVTHEvEFARKVASQVVYMEKGRI 219
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
3-221 |
3.77e-44 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 151.77 E-value: 3.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSYgnkhnKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKqlaef 82
Cdd:NF040840 1 MIRIENLSKDW-----KEFKLRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPE----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 83 rKQHLGFIFQEYNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEP 162
Cdd:NF040840 71 -KRGIAYVYQNYMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 163 SIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHD-PVAASFCSRVVFIKDGQI 221
Cdd:NF040840 150 KLLLLDEPLSALDVQTRDELIREMKRWHREFGFTAIHVTHNfEEALSLADRVGIMLNGRL 209
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-221 |
8.12e-44 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 147.93 E-value: 8.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSYGnkhnKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTInINQAEMTNMKEKQLAEF 82
Cdd:PRK09493 1 MIEFKNVSKHFG----PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDL-IVDGLKVNDPKVDERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 83 RkQHLGFIFQEYNLLDTLTVKENILL-PLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHE 161
Cdd:PRK09493 76 R-QEAGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1112987593 162 PSIIFADEPTGALDSKSASDLLNKLSQLNQKrRATIVMVTHD-PVAASFCSRVVFIKDGQI 221
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEiGFAEKVASRLIFIDKGRI 214
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-221 |
1.44e-43 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 150.62 E-value: 1.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 2 MILEAKKIRKSYGNKhnkhEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEkqlae 81
Cdd:PRK10851 1 MSIEIANIKKSFGRT----QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 82 fRKQHLGFIFQEYNLLDTLTVKENILLPLSI--------TKISKKEAGQKFEEVakELGifELKDKYPNEISGGQKQRTS 153
Cdd:PRK10851 72 -RDRKVGFVFQHYALFRHMTVFDNIAFGLTVlprrerpnAAAIKAKVTQLLEMV--QLA--HLADRYPAQLSGGQKQRVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1112987593 154 AARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHD-PVAASFCSRVVFIKDGQI 221
Cdd:PRK10851 147 LARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDqEEAMEVADRVVVMSQGNI 215
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-224 |
3.33e-43 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 146.70 E-value: 3.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 2 MILEAKKIRKSYGNkhnkHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEM---TNMKEKQ 78
Cdd:PRK11124 1 MSIQLNGINCFYGA----HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 79 LAEFRkQHLGFIFQEYNLLDTLTVKEN-ILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARA 157
Cdd:PRK11124 77 IRELR-RNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1112987593 158 FIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKrRATIVMVTHD-PVAASFCSRVVFIKDGQIYTQ 224
Cdd:PRK11124 156 LMMEPQVLLFDEPTAALDPEITAQIVSIIRELAET-GITQVIVTHEvEVARKTASRVVYMENGHIVEQ 222
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
23-171 |
3.76e-43 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 143.56 E-value: 3.76e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 23 LKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLaefrKQHLGFIFQEYNLLDTLTV 102
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSL----RKEIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1112987593 103 KENILLPLSITKISKKEAGQKFEEVAKELGIFELKD----KYPNEISGGQKQRTSAARAFIHEPSIIFADEPT 171
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
23-219 |
1.35e-42 |
|
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: 144.53 E-value: 1.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 23 LKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAefrkqhlgfIFQEYNLLDTLTV 102
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV---------VFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 103 KENILLPLS--ITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPSIIFADEPTGALDSKSAS 180
Cdd:TIGR01184 72 RENIALAVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1112987593 181 DLLNKLSQLNQKRRATIVMVTHDPVAASFCS-RVVFIKDG 219
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHDVDEALLLSdRVVMLTNG 191
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-221 |
6.69e-42 |
|
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: 143.21 E-value: 6.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGNKHnkhEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLaefr 83
Cdd:cd03295 1 IEFENVTKRYGGGK---KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVEL---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 84 KQHLGFIFQEYNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAK--ELGIFELKDKYPNEISGGQKQRTSAARAFIHE 161
Cdd:cd03295 74 RRKIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLAlvGLDPAEFADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1112987593 162 PSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDpVAASFC--SRVVFIKDGQI 221
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHD-IDEAFRlaDRIAIMKNGEI 214
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-222 |
1.90e-41 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 142.15 E-value: 1.90e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 1 MMILEAKKIRKSYGNkhnkHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININqaemtnmkeKQLA 80
Cdd:COG1121 4 MPAIELENLTVSYGG----RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLF---------GKPP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 81 EFRKQHLGFIFQEYNLLDT--LTVKENILL----PLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSA 154
Cdd:COG1121 71 RRARRRIGYVPQRAEVDWDfpITVRDVVLMgrygRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1112987593 155 ARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRaTIVMVTHDP-VAASFCSRVVFIKDGQIY 222
Cdd:COG1121 151 ARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGK-TILVVTHDLgAVREYFDRVLLLNRGLVA 218
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
27-221 |
1.95e-41 |
|
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: 141.15 E-value: 1.95e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 27 DLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTnmkekQLAEFRKQhLGFIFQEYNLLDTLTVKENI 106
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHT-----GLAPYQRP-VSMLFQENNLFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 107 LLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPSIIFADEPTGALDSKSASDLLNKL 186
Cdd:TIGR01277 92 GLGLHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALV 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 1112987593 187 SQLNQKRRATIVMVTHDPV-AASFCSRVVFIKDGQI 221
Cdd:TIGR01277 172 KQLCSERQRTLLMVTHHLSdARAIASQIAVVSQGKI 207
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-221 |
1.96e-41 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 148.75 E-value: 1.96e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGNKHNkheVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAefr 83
Cdd:COG4988 337 IELEDVSFSYPGGRP---ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWR--- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 84 kQHLGFIFQEYNLLDTlTVKENILLplsitkiSKKEAG-QKFEEVAKELGIFELKDKYPN-------E----ISGGQKQR 151
Cdd:COG4988 411 -RQIAWVPQNPYLFAG-TIRENLRL-------GRPDASdEELEAALEAAGLDEFVAALPDgldtplgEggrgLSGGQAQR 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 152 TSAARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRraTIVMVTHDPVAASFCSRVVFIKDGQI 221
Cdd:COG4988 482 LALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLAQADRILVLDDGRI 549
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
23-221 |
1.99e-41 |
|
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: 140.89 E-value: 1.99e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 23 LKGIDLQIQ---KGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAEFRKQHLGFIFQEYNLLDT 99
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 100 LTVKENILLPLSitKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPSIIFADEPTGALDSKSA 179
Cdd:cd03297 90 LNVRENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1112987593 180 SDLLNKLSQLNQKRRATIVMVTHDPVAA-SFCSRVVFIKDGQI 221
Cdd:cd03297 168 LQLLPELKQIKKNLNIPVIFVTHDLSEAeYLADRIVVMEDGRL 210
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3-221 |
3.29e-41 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 145.09 E-value: 3.29e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSYGNKhnkhEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKekqlAEf 82
Cdd:PRK09452 14 LVELRGISKSFDGK----EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP----AE- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 83 rKQHLGFIFQEYNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEP 162
Cdd:PRK09452 85 -NRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 163 SIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDPVAA-SFCSRVVFIKDGQI 221
Cdd:PRK09452 164 KVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEAlTMSDRIVVMRDGRI 223
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
4-224 |
6.20e-41 |
|
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: 139.94 E-value: 6.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGNKhNKHevlkgIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMkekqlaEFR 83
Cdd:cd03298 1 VRLDKIRFSYGEQ-PMH-----FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAA------PPA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 84 KQHLGFIFQEYNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPS 163
Cdd:cd03298 69 DRPVSMLFQENNLFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1112987593 164 IIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDPV-AASFCSRVVFIKDGQIYTQ 224
Cdd:cd03298 149 VLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEdAKRLAQRVVFLDNGRIAAQ 210
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-221 |
9.01e-41 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 140.87 E-value: 9.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGnkhnKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEK--QLAE 81
Cdd:PRK10619 6 LNVIDLHKRYG----EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgQLKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 82 FRKQHL-------GFIFQEYNLLDTLTVKENIL-LPLSITKISKKEAGQKFEEVAKELGIFE-LKDKYPNEISGGQKQRT 152
Cdd:PRK10619 82 ADKNQLrllrtrlTMVFQHFNLWSHMTVLENVMeAPIQVLGLSKQEARERAVKYLAKVGIDErAQGKYPVHLSGGQQQRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 153 SAARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRaTIVMVTHD-PVAASFCSRVVFIKDGQI 221
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEmGFARHVSSHVIFLHQGKI 230
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-203 |
1.57e-40 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 140.00 E-value: 1.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 1 MMILEAKKIRKSYGNKHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTnmkeKQLA 80
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVT----GPGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 81 EfRkqhlGFIFQEYNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIH 160
Cdd:COG4525 77 D-R----GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1112987593 161 EPSIIFADEPTGALDS---KSASDLLNKLSQLNQKrraTIVMVTHD 203
Cdd:COG4525 152 DPRFLLMDEPFGALDAltrEQMQELLLDVWQRTGK---GVFLITHS 194
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-221 |
5.03e-40 |
|
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: 146.52 E-value: 5.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGNkhNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKekqLAEFR 83
Cdd:COG2274 474 IELENVSFRYPG--DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID---PASLR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 84 KQhLGFIFQEYNLLDTlTVKENILlpLSITKISKKEAgqkfEEVAKELGIFELKDKYPN-----------EISGGQKQRT 152
Cdd:COG2274 549 RQ-IGVVLQDVFLFSG-TIRENIT--LGDPDATDEEI----IEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRL 620
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1112987593 153 SAARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRraTIVMVTHDPVAASFCSRVVFIKDGQI 221
Cdd:COG2274 621 AIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGR--TVIIIAHRLSTIRLADRIIVLDKGRI 687
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-220 |
3.00e-39 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 133.52 E-value: 3.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 5 EAKKIRKSYGNKHnkheVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLaefrK 84
Cdd:cd00267 1 EIENLSFRYGGRT----ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 85 QHLGFIFQeynlldtltvkenillplsitkiskkeagqkfeevakelgifelkdkypneISGGQKQRTSAARAFIHEPSI 164
Cdd:cd00267 73 RRIGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1112987593 165 IFADEPTGALDSKSASDLLNKLSQLNQKRRaTIVMVTHDP-VAASFCSRVVFIKDGQ 220
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEEGR-TVIIVTHDPeLAELAADRVIVLKDGK 157
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-221 |
7.62e-39 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 135.58 E-value: 7.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGNKhnkhEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEkqlaEFR 83
Cdd:PRK11247 13 LLLNAVSKRYGER----TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARE----DTR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 84 kqhlgFIFQEYNLLDTLTVKENILLPLSITkiSKKEAGQKFEEVakelGIFELKDKYPNEISGGQKQRTSAARAFIHEPS 163
Cdd:PRK11247 85 -----LMFQDARLLPWKKVIDNVGLGLKGQ--WRDAALQALAAV----GLADRANEWPAALSGGQKQRVALARALIHRPG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1112987593 164 IIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHD-PVAASFCSRVVFIKDGQI 221
Cdd:PRK11247 154 LLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDvSEAVAMADRVLLIEEGKI 212
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-221 |
1.46e-38 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 137.67 E-value: 1.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 1 MMILEAKKIRKSYGNKHnkhEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNM--KEKQ 78
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKT---QVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELepADRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 79 LAefrkqhlgFIFQEYNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAF 158
Cdd:PRK11650 78 IA--------MVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1112987593 159 IHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDPVAA-SFCSRVVFIKDGQI 221
Cdd:PRK11650 150 VREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAmTLADRVVVMNGGVA 213
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
20-221 |
3.71e-38 |
|
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: 134.50 E-value: 3.71e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 20 HEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAEFRKQhLGFIFQ--EYNLL 97
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLRKK-VGLVFQfpEHQLF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 98 DTlTVKENILLPLSITKISKKEAGQKFEEVAKELGIFE-LKDKYPNEISGGQKQRTSAARAFIHEPSIIFADEPTGALDS 176
Cdd:TIGR04521 97 EE-TVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEeYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDP 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1112987593 177 KSASDLLNKLSQLNQKRRATIVMVTHD-PVAASFCSRVVFIKDGQI 221
Cdd:TIGR04521 176 KGRKEILDLFKRLHKEKGLTVILVTHSmEDVAEYADRVIVMHKGKI 221
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-222 |
6.11e-38 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 133.60 E-value: 6.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSYgnkhNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIdqVSGGTININQAEM---TNMKEKQL 79
Cdd:PRK09984 4 IIRVEKLAKTF----NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL--ITGDKSAGSHIELlgrTVQREGRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 80 A-EFRKQ--HLGFIFQEYNLLDTLTVKENILL------PL------SITKISKKEAGQKFEEVakelGIFELKDKYPNEI 144
Cdd:PRK09984 78 ArDIRKSraNTGYIFQQFNLVNRLSVLENVLIgalgstPFwrtcfsWFTREQKQRALQALTRV----GMVHFAHQRVSTL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1112987593 145 SGGQKQRTSAARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHD-PVAASFCSRVVFIKDGQIY 222
Cdd:PRK09984 154 SGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQvDYALRYCERIVALRQGHVF 232
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-221 |
1.06e-37 |
|
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: 130.03 E-value: 1.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGNkhNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLaefr 83
Cdd:cd03246 1 LEVENVSFRYPG--AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNEL---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 84 KQHLGFIFQEYNLLDTlTVKENILlplsitkiskkeagqkfeevakelgifelkdkypneiSGGQKQRTSAARAFIHEPS 163
Cdd:cd03246 75 GDHVGYLPQDDELFSG-SIAENIL-------------------------------------SGGQRQRLGLARALYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1112987593 164 IIFADEPTGALDSKSASDLLNKLSQLnQKRRATIVMVTHDPVAASFCSRVVFIKDGQI 221
Cdd:cd03246 117 ILVLDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
27-222 |
1.14e-37 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 132.01 E-value: 1.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 27 DLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQlaefrkQHLGFIFQEYNLLDTLTVKENI 106
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR------RPVSMLFQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 107 LLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPSIIFADEPTGALDSKSASDLLNKL 186
Cdd:PRK10771 93 GLGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLV 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 1112987593 187 SQLNQKRRATIVMVTH---DpvAASFCSRVVFIKDGQIY 222
Cdd:PRK10771 173 SQVCQERQLTLLMVSHsleD--AARIAPRSLVVADGRIA 209
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-221 |
1.32e-37 |
|
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: 131.34 E-value: 1.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGNkhnkHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTnmkeKQLAEFR 83
Cdd:cd03265 1 IEVENLVKKYGD----FEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV----REPREVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 84 KQhLGFIFQEYNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPS 163
Cdd:cd03265 73 RR-IGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1112987593 164 IIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHD-PVAASFCSRVVFIKDGQI 221
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYmEEAEQLCDRVAIIDHGRI 210
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-221 |
7.57e-37 |
|
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: 129.24 E-value: 7.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGNKHnkheVLKGIDLQIQKGEFVsIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKqlaeFR 83
Cdd:cd03264 1 LQLENLTKRYGKKR----ALDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK----LR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 84 kQHLGFIFQEYNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPS 163
Cdd:cd03264 72 -RRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 164 IIFADEPTGALDSKSASDLLNKLSQLNQKRraTIVMVTHDpVA--ASFCSRVVFIKDGQI 221
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHI-VEdvESLCNQVAVLNKGKL 207
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
12-221 |
1.64e-36 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 135.68 E-value: 1.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 12 SYGNKHnkhEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQaemTNMKEKQLAEFRKqHLGFIF 91
Cdd:COG1132 348 SYPGDR---PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDG---VDIRDLTLESLRR-QIGVVP 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 92 QEYNLLDTlTVKENILLplsitkiSKKEAG-QKFEEVAKELGIFELKDKYPN-----------EISGGQKQRTSAARAFI 159
Cdd:COG1132 421 QDTFLFSG-TIRENIRY-------GRPDATdEEVEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARALL 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1112987593 160 HEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRraTIVMVTHDPVAASFCSRVVFIKDGQI 221
Cdd:COG1132 493 KDPPILILDEATSALDTETEALIQEALERLMKGR--TTIVIAHRLSTIRNADRILVLDDGRI 552
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-224 |
1.82e-36 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 129.43 E-value: 1.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 1 MMILEAKKIRKSYGNKHnkheVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSS-IDQVSGGTINI--NQAEMTNMKEk 77
Cdd:COG1119 1 DPLLELRNVTVRRGGKT----ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRLfgERRGGEDVWE- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 78 qLaefrKQHLGFI---FQEYnLLDTLTVKENIL--------LPLSITKISKKEAgqkfEEVAKELGIFELKDKYPNEISG 146
Cdd:COG1119 76 -L----RKRIGLVspaLQLR-FPRDETVLDVVLsgffdsigLYREPTDEQRERA----RELLELLGLAHLADRPFGTLSQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 147 GQKQRTSAARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTH--DPVAASFcSRVVFIKDGQIYTQ 224
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHhvEEIPPGI-THVLLLKDGRVVAA 224
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
2-203 |
2.87e-36 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 130.21 E-value: 2.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 2 MIlEAKKIRKSYGNKHnkhEVLKGIDLQIQKGEFVSIMGPSGSGKTTLL---NVLssIDQvSGGTININQAEMTNMKEKQ 78
Cdd:COG1125 1 MI-EFENVTKRYPDGT---VAVDDLSLTIPAGEFTVLVGPSGCGKTTTLrmiNRL--IEP-TSGRILIDGEDIRDLDPVE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 79 LaefrKQHLGFIFQEYNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIF--ELKDKYPNEISGGQKQRTSAAR 156
Cdd:COG1125 74 L----RRRIGYVIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLDpeEYRDRYPHELSGGQQQRVGVAR 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1112987593 157 AFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHD 203
Cdd:COG1125 150 ALAADPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHD 196
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-221 |
5.99e-36 |
|
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: 133.74 E-value: 5.99e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGNkhNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAefr 83
Cdd:COG4987 334 LELEDVSFRYPG--AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLR--- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 84 kQHLGFIFQEYNLLDTlTVKENILLplsitkiSKKEAG-QKFEEVAKELGIFELKDKYPN-------E----ISGGQKQR 151
Cdd:COG4987 409 -RRIAVVPQRPHLFDT-TLRENLRL-------ARPDATdEELWAALERVGLGDWLAALPDgldtwlgEggrrLSGGERRR 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 152 TSAARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRraTIVMVTHDPVAASFCSRVVFIKDGQI 221
Cdd:COG4987 480 LALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLAGLERMDRILVLEDGRI 547
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
7-207 |
1.05e-35 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 130.15 E-value: 1.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 7 KKIRKSYGNKHnkheVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKqlaefrKQH 86
Cdd:PRK11000 7 RNVTKAYGDVV----ISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA------ERG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 87 LGFIFQEYNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPSIIF 166
Cdd:PRK11000 77 VGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1112987593 167 ADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDPVAA 207
Cdd:PRK11000 157 LDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEA 197
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-221 |
1.60e-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: 125.45 E-value: 1.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 5 EAKKIRKSYgnkHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININqaemtnmKEKQLAEFRK 84
Cdd:cd03226 1 RIENISFSY---KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLN-------GKPIKAKERR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 85 QHLGFIFQE--YNLLdTLTVKENILLPLSITKiskkEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEP 162
Cdd:cd03226 71 KSIGYVMQDvdYQLF-TDSVREELLLGLKELD----AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGK 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1112987593 163 SIIFADEPTGALDS---KSASDLLNKLsqlnQKRRATIVMVTHDP-VAASFCSRVVFIKDGQI 221
Cdd:cd03226 146 DLLIFDEPTSGLDYknmERVGELIREL----AAQGKAVIVITHDYeFLAKVCDRVLLLANGAI 204
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-221 |
2.91e-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: 125.17 E-value: 2.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSYGNKHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTINInqAEMTNMKEKQLAef 82
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATV--DGFDVVKEPAEA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 83 rKQHLGFIFQEYNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEP 162
Cdd:cd03266 77 -RRRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1112987593 163 SIIFADEPTGALDSKSASDLLNKLSQLnqkRRA--TIVMVTHD-PVAASFCSRVVFIKDGQI 221
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQL---RALgkCILFSTHImQEVERLCDRVVVLHRGRV 214
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-221 |
3.01e-35 |
|
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: 126.31 E-value: 3.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 1 MMILEAKKIRKSYGnkhnKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLA 80
Cdd:COG0411 2 DPLLEVRGLTKRFG----GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 81 efrkqHLGFI--FQEYNLLDTLTVKENI---------------LLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNE 143
Cdd:COG0411 78 -----RLGIArtFQNPRLFPELTVLENVlvaaharlgrgllaaLLRLPRARREEREARERAEELLERVGLADRADEPAGN 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1112987593 144 ISGGQKQRTSAARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHD-PVAASFCSRVVFIKDGQI 221
Cdd:COG0411 153 LSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDmDLVMGLADRIVVLDFGRV 231
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
12-217 |
3.27e-35 |
|
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: 124.95 E-value: 3.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 12 SYGNkhnkHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQaemtnmkeKQLAEFRKQhLGFIF 91
Cdd:cd03235 8 SYGG----HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG--------KPLEKERKR-IGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 92 QEYNLLDT--LTVKENILLPL-----SITKISKKEAgQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPSI 164
Cdd:cd03235 75 QRRSIDRDfpISVRDVVLMGLyghkgLFRRLSKADK-AKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1112987593 165 IFADEPTGALDSKSASDLLNKLSQLNQKRRaTIVMVTHDPVAAS-FCSRVVFIK 217
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLRELRREGM-TILVVTHDLGLVLeYFDRVLLLN 206
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-221 |
3.87e-35 |
|
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: 125.35 E-value: 3.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGnkhnKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAefr 83
Cdd:cd03218 1 LRAENLSKRYG----KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 84 kqHLGFIF--QEYNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHE 161
Cdd:cd03218 74 --RLGIGYlpQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATN 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1112987593 162 PSIIFADEPTGALDSKSASDLLNKLSQLnqKRRATIVMVTHDPV--AASFCSRVVFIKDGQI 221
Cdd:cd03218 152 PKFLLLDEPFAGVDPIAVQDIQKIIKIL--KDRGIGVLITDHNVreTLSITDRAYIIYEGKV 211
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2-222 |
9.45e-35 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 124.88 E-value: 9.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 2 MILEAKKIRKSYGNKhnkhEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAE 81
Cdd:PRK13548 1 AMLEARNLSVRLGGR----TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 82 FR---KQH--LGFIFqeynlldtlTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDK-YPnEISGGQKQRTSAA 155
Cdd:PRK13548 77 RRavlPQHssLSFPF---------TVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRdYP-QLSGGEQQRVQLA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1112987593 156 RAFI------HEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHD-PVAASFCSRVVFIKDGQIY 222
Cdd:PRK13548 147 RVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDlNLAARYADRIVLLHQGRLV 220
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-221 |
1.05e-34 |
|
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: 124.47 E-value: 1.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGnkhnKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAefr 83
Cdd:cd03219 1 LEVRGLTKRFG----GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 84 kqHLGFI--FQEYNLLDTLTVKENILLP----------LSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQR 151
Cdd:cd03219 74 --RLGIGrtFQIPRLFPELTVLENVMVAaqartgsgllLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1112987593 152 TSAARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRaTIVMVTHD-PVAASFCSRVVFIKDGQI 221
Cdd:cd03219 152 LEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGI-TVLLVEHDmDVVMSLADRVTVLDQGRV 221
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
38-221 |
1.54e-34 |
|
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: 126.07 E-value: 1.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 38 IMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKekqlAEFRkqHLGFIFQEYNLLDTLTVKENILLPLSITKISK 117
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVP----PHLR--HINMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 118 KEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATI 197
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITF 154
|
170 180
....*....|....*....|....*
gi 1112987593 198 VMVTHDPVAA-SFCSRVVFIKDGQI 221
Cdd:TIGR01187 155 VFVTHDQEEAmTMSDRIAIMRKGKI 179
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
21-233 |
2.36e-34 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 123.06 E-value: 2.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 21 EVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAEFRKQhLGFIFQEYNLLDTL 100
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQ-IGMIFQDHHLLMDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 101 TVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPSIIFADEPTGALDSKSAS 180
Cdd:PRK10908 95 TVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1112987593 181 DLLNKLSQLNqKRRATIVMVTHD-PVAASFCSRVVFIKDGQIYtqlnkGGQDRQ 233
Cdd:PRK10908 175 GILRLFEEFN-RVGVTVLMATHDiGLISRRSYRMLTLSDGHLH-----GGVGGE 222
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2-213 |
3.67e-34 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 121.82 E-value: 3.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 2 MILEAKKIRKSYGNkhnkHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEmtnmKEKQLAE 81
Cdd:COG4133 1 MMLEAENLSCRRGE----RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEP----IRDARED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 82 FRkQHLGFIFQEYNLLDTLTVKENILLPLSITKISkkEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHE 161
Cdd:COG4133 73 YR-RRLAYLGHADGLKPELTVRENLRFWAALYGLR--ADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1112987593 162 PSIIFADEPTGALDSKSASDLLNKLSQLNQKRRAtIVMVTHDPVAASFCSRV 213
Cdd:COG4133 150 APLWLLDEPFTALDAAGVALLAELIAAHLARGGA-VLLTTHQPLELAAARVL 200
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
4-221 |
4.14e-34 |
|
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: 122.31 E-value: 4.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGNKhnKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQaemTNMKEKQLAEFR 83
Cdd:cd03245 3 IEFRNVSFSYPNQ--EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDG---TDIRQLDPADLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 84 kQHLGFIFQEYNLLDTlTVKENILLPLSITKiskkeaGQKFEEVAKELGIFELKDKYPN-----------EISGGQKQRT 152
Cdd:cd03245 78 -RNIGYVPQDVTLFYG-TLRDNITLGAPLAD------DERILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1112987593 153 SAARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRraTIVMVTHDPVAASFCSRVVFIKDGQI 221
Cdd:cd03245 150 ALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDK--TLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-244 |
4.24e-34 |
|
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: 123.69 E-value: 4.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGNKHNKheVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQaeMTNMKEKQLAEFR 83
Cdd:TIGR04520 1 IEVENVSFSYPESEKP--ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENLWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 84 kQHLGFIFQE-YNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEP 162
Cdd:TIGR04520 77 -KKVGMVFQNpDNQFVGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 163 SIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDPVAASFCSRVVFIKDGQIYTQlnkgGQDRQMFFQ-DIMK 241
Cdd:TIGR04520 156 DIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAE----GTPREIFSQvELLK 231
|
...
gi 1112987593 242 TQG 244
Cdd:TIGR04520 232 EIG 234
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
16-221 |
1.87e-33 |
|
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: 120.90 E-value: 1.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 16 KHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININqaemTNMKEKQLAEFRKQhLGFIF-QEY 94
Cdd:cd03267 30 KYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVA----GLVPWKRRKKFLRR-IGVVFgQKT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 95 NLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPSIIFADEPTGAL 174
Cdd:cd03267 105 QLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1112987593 175 DSKSASDLLNKLSQLNQKRRATIVMVTHD--PVAAsFCSRVVFIKDGQI 221
Cdd:cd03267 185 DVVAQENIRNFLKEYNRERGTTVLLTSHYmkDIEA-LARRVLVIDKGRL 232
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
4-221 |
2.57e-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: 120.86 E-value: 2.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGNKhnkhEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAefr 83
Cdd:TIGR03864 2 LEVAGLSFRYGAR----RALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVAGHDLRRAPRAALA--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 84 kqHLGFIFQEYNL-LDtLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEP 162
Cdd:TIGR03864 75 --RLGVVFQQPTLdLD-LSVRQNLRYHAALHGLSRAEARARIAELLARLGLAERADDKVRELNGGHRRRVEIARALLHRP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1112987593 163 SIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTH--DPVAASfcSRVVFIKDGQI 221
Cdd:TIGR03864 152 ALLLLDEPTVGLDPASRAAITAHVRALARDQGLSVLWATHlvDEIEAS--DRLVVLHRGRV 210
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3-235 |
3.01e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 121.72 E-value: 3.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSYgnkHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMtNMKEKQLAEF 82
Cdd:PRK13639 1 ILETRDLKYSY---PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 83 RKQhLGFIFQeyNLLDTL---TVKENILL-PLSItKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAF 158
Cdd:PRK13639 77 RKT-VGIVFQ--NPDDQLfapTVEEDVAFgPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGIL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1112987593 159 IHEPSIIFADEPTGALDSKSASDLLNKLSQLNqKRRATIVMVTHD-PVAASFCSRVVFIKDGQIYtqlnKGGQDRQMF 235
Cdd:PRK13639 153 AMKPEIIVLDEPTSGLDPMGASQIMKLLYDLN-KEGITIIISTHDvDLVPVYADKVYVMSDGKII----KEGTPKEVF 225
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-221 |
4.83e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 121.73 E-value: 4.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 2 MILEAKKIRKSYGNKHNKH-EVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTINI---NQAEMTNMKE- 76
Cdd:PRK13651 1 MQIKVKNIVKIFNKKLPTElKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkDEKNKKKTKEk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 77 -----------------KQLAEFRKQhLGFIFQ--EYNLLDTLTVKENILLPLSItKISKKEAGQKFEEVAKELGI-FEL 136
Cdd:PRK13651 81 ekvleklviqktrfkkiKKIKEIRRR-VGVVFQfaEYQLFEQTIEKDIIFGPVSM-GVSKEEAKKRAAKYIELVGLdESY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 137 KDKYPNEISGGQKQRTSAARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRaTIVMVTHD-PVAASFCSRVVF 215
Cdd:PRK13651 159 LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDlDNVLEWTKRTIF 237
|
....*.
gi 1112987593 216 IKDGQI 221
Cdd:PRK13651 238 FKDGKI 243
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-182 |
7.88e-33 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 119.36 E-value: 7.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 1 MMILEAKKIRKSYGNKhnkhEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLA 80
Cdd:COG1137 1 MMTLEAENLVKSYGKR----TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 81 efrKQHLGFIFQEYNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIH 160
Cdd:COG1137 77 ---RLGIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALAT 153
|
170 180
....*....|....*....|..
gi 1112987593 161 EPSIIFADEPTGALDSKSASDL 182
Cdd:COG1137 154 NPKFILLDEPFAGVDPIAVADI 175
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1-222 |
1.02e-32 |
|
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: 118.04 E-value: 1.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 1 MMILEAKKIRKSYGNKHNKH--EVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSidQVSG----GTININQaemTNM 74
Cdd:cd03213 1 GVTLSFRNLTVTVKSSPSKSgkQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAG--RRTGlgvsGEVLING---RPL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 75 KEKQLaefrKQHLGFIFQEYNLLDTLTVKENILLplsitkiskkeagqkfeeVAKELGifelkdkypneISGGQKQRTSA 154
Cdd:cd03213 76 DKRSF----RKIIGYVPQDDILHPTLTVRETLMF------------------AAKLRG-----------LSGGERKRVSI 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1112987593 155 ARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRaTIVMVTHDPVAASF--CSRVVFIKDGQ-IY 222
Cdd:cd03213 123 ALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGR-TIICSIHQPSSEIFelFDKLLLLSQGRvIY 192
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
26-221 |
1.23e-32 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 121.75 E-value: 1.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 26 IDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININ------QAEMTNMKekqlAEFRkqHLGFIFQEYNLLDT 99
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGgevlqdSARGIFLP----PHRR--RIGYVFQEARLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 100 LTVKENILLplSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPSIIFADEPTGALDSKSA 179
Cdd:COG4148 92 LSVRGNLLY--GRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARK 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1112987593 180 SDLLNKLSQLNQKRRATIVMVTHDPV-AASFCSRVVFIKDGQI 221
Cdd:COG4148 170 AEILPYLERLRDELDIPILYVSHSLDeVARLADHVVLLEQGRV 212
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-221 |
2.02e-32 |
|
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: 123.64 E-value: 2.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 1 MMILEAKKIRKSYGNKHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKT----TLLNVLSSIDQVSGGTININQAEMTNMKE 76
Cdd:COG4172 4 MPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 77 KQLAEFRKQHLGFIFQE----YNLLdtLTVKENILLPLSI-TKISKKEAGQKFEEVAKELGIFELK---DKYPNEISGGQ 148
Cdd:COG4172 84 RELRRIRGNRIAMIFQEpmtsLNPL--HTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDPErrlDAYPHQLSGGQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1112987593 149 KQRTSAARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHD-PVAASFCSRVVFIKDGQI 221
Cdd:COG4172 162 RQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDlGVVRRFADRVAVMRQGEI 235
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
19-221 |
4.29e-32 |
|
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: 123.23 E-value: 4.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 19 KHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAEfrkqHLGFIFQEYNLLD 98
Cdd:TIGR01842 330 KKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGK----HIGYLPQDVELFP 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 99 TlTVKENIllplsiTKISKKEAGQKFEEVAKELGIFELKDKYPN-----------EISGGQKQRTSAARAFIHEPSIIFA 167
Cdd:TIGR01842 406 G-TVAENI------ARFGENADPEKIIEAAKLAGVHELILRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVVL 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1112987593 168 DEPTGALDSKSASDLLNKLSQLnQKRRATIVMVTHDPVAASFCSRVVFIKDGQI 221
Cdd:TIGR01842 479 DEPNSNLDEEGEQALANAIKAL-KARGITVVVITHRPSLLGCVDKILVLQDGRI 531
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-221 |
5.12e-32 |
|
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: 122.49 E-value: 5.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSY-------GNKHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTL-LNVLSSIDqvSGGTININQAEMTNM 74
Cdd:COG4172 275 LLEARDLKVWFpikrglfRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALLRLIP--SEGEIRFDGQDLDGL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 75 KEKQLAEFRKqHLGFIFQE-YNLLDT-LTVKENILLPLSI--TKISKKEAGQKFEEVAKELGI-FELKDKYPNEISGGQK 149
Cdd:COG4172 353 SRRALRPLRR-RMQVVFQDpFGSLSPrMTVGQIIAEGLRVhgPGLSAAERRARVAEALEEVGLdPAARHRYPHEFSGGQR 431
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1112987593 150 QRTSAARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHD-PVAASFCSRVVFIKDGQI 221
Cdd:COG4172 432 QRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDlAVVRALAHRVMVMKDGKV 504
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-221 |
5.74e-32 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 119.82 E-value: 5.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGnkhnKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQlaefr 83
Cdd:PRK11432 7 VVLKNITKRFG----SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 84 kQHLGFIFQEYNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAK--ELGIFElkDKYPNEISGGQKQRTSAARAFIHE 161
Cdd:PRK11432 78 -RDICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALElvDLAGFE--DRYVDQISGGQQQRVALARALILK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1112987593 162 PSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDPVAASFCS-RVVFIKDGQI 221
Cdd:PRK11432 155 PKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSdTVIVMNKGKI 215
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-221 |
9.41e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 116.94 E-value: 9.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 1 MMILEAKKIRKSYGNKhnkhEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVS-----GGTININQAEMTNMk 75
Cdd:PRK14247 1 MNKIEIRDLKVSFGQV----EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKM- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 76 ekQLAEFRKQhLGFIFQEYNLLDTLTVKENILLPLSITKI--SKKEAGQKFEEVAKELGIF-ELKDKY---PNEISGGQK 149
Cdd:PRK14247 76 --DVIELRRR-VQMVFQIPNPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLWdEVKDRLdapAGKLSGGQQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1112987593 150 QRTSAARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLnqKRRATIVMVTHDPV-AASFCSRVVFIKDGQI 221
Cdd:PRK14247 153 QRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLEL--KKDMTIVLVTHFPQqAARISDYVAFLYKGQI 223
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-221 |
1.14e-31 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 117.06 E-value: 1.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSYGNKHnkheVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSI-DQVSG----GTI-----NINQAEMt 72
Cdd:COG1117 11 KIEVRNLNVYYGDKQ----ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMnDLIPGarveGEIlldgeDIYDPDV- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 73 nmkekQLAEFRKQhLGFIFQEYNLLdTLTVKENILLPLSITKI-SKKEAGQKFEEVAKELGIF-ELKDK---YPNEISGG 147
Cdd:COG1117 86 -----DVVELRRR-VGMVFQKPNPF-PKSIYDNVAYGLRLHGIkSKSELDEIVEESLRKAALWdEVKDRlkkSALGLSGG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1112987593 148 QKQRTSAARAFIHEPSIIFADEPTGALDSKSAS---DLLNKLsqlnqKRRATIVMVTHDPVAASFCS-RVVFIKDGQI 221
Cdd:COG1117 159 QQQRLCIARALAVEPEVLLMDEPTSALDPISTAkieELILEL-----KKDYTIVIVTHNMQQAARVSdYTAFFYLGEL 231
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
18-221 |
1.33e-31 |
|
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: 116.17 E-value: 1.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 18 NKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLaefrKQHLGFIFQEYNLL 97
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSL----RSMIGVVLQDTFLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 98 DTlTVKENILLPlsiTKISKKEagqKFEEVAKELGIFELKDKYPN-----------EISGGQKQRTSAARAFIHEPSIIF 166
Cdd:cd03254 90 SG-TIMENIRLG---RPNATDE---EVIEAAKEAGAHDFIMKLPNgydtvlgenggNLSQGERQLLAIARAMLRDPKILI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1112987593 167 ADEPTGALDSKSASDLLNKLSQLNQKRraTIVMVTHDPVAASFCSRVVFIKDGQI 221
Cdd:cd03254 163 LDEATSNIDTETEKLIQEALEKLMKGR--TSIIIAHRLSTIKNADKILVLDDGKI 215
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-221 |
1.68e-31 |
|
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: 115.61 E-value: 1.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGNKHnkheVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAefr 83
Cdd:cd03224 1 LEVENLNAGYGKSQ----ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 84 KQHLGFIFQEYNLLDTLTVKENILLPLSITKISKKEAgqKFEEVakeLGIF----ELKDKYPNEISGGQKQRTSAARAFI 159
Cdd:cd03224 74 RAGIGYVPEGRRIFPELTVEENLLLGAYARRRAKRKA--RLERV---YELFprlkERRKQLAGTLSGGEQQMLAIARALM 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1112987593 160 HEPSIIFADEPTGALDSKSASDLLNKLSQLNqKRRATIVMVTHD-PVAASFCSRVVFIKDGQI 221
Cdd:cd03224 149 SRPKLLLLDEPSEGLAPKIVEEIFEAIRELR-DEGVTILLVEQNaRFALEIADRAYVLERGRV 210
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
15-221 |
1.73e-31 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 115.83 E-value: 1.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 15 NKHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSG---GTININQAEMTNmkekqlAEFRKqHLGFIF 91
Cdd:cd03234 15 NWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKP------DQFQK-CVAYVR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 92 QEYNLLDTLTVKENIL--LPLSITKISKKEAGQKFEEVA--KELGIFELKDKYPNEISGGQKQRTSAARAFIHEPSIIFA 167
Cdd:cd03234 88 QDDILLPGLTVRETLTytAILRLPRKSSDAIRKKRVEDVllRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1112987593 168 DEPTGALDSKSASDLLNKLSQLnqKRRATIVMVT-HDPVAASF--CSRVVFIKDGQI 221
Cdd:cd03234 168 DEPTSGLDSFTALNLVSTLSQL--ARRNRIVILTiHQPRSDLFrlFDRILLLSSGEI 222
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-203 |
3.69e-31 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 118.40 E-value: 3.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSYGNKHnkheVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQlaef 82
Cdd:PRK11607 19 LLEIRNLTKSFDGQH----AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 83 rkQHLGFIFQEYNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEP 162
Cdd:PRK11607 91 --RPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRP 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1112987593 163 SIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHD 203
Cdd:PRK11607 169 KLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHD 209
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
17-214 |
6.14e-31 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 113.73 E-value: 6.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 17 HNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNV----LSSIDQVSgGTININQAEMTNMKekqlAEFRkqHLGFIFQ 92
Cdd:COG4136 11 LGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAiagtLSPAFSAS-GEVLLNGRRLTALP----AEQR--RIGILFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 93 EYNLLDTLTVKENILLPLSiTKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPSIIFADEPTG 172
Cdd:COG4136 84 DDLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFS 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1112987593 173 ALDsksaSDLLNKLSQL--NQKRRATI--VMVTHDPVAASFCSRVV 214
Cdd:COG4136 163 KLD----AALRAQFREFvfEQIRQRGIpaLLVTHDEEDAPAAGRVL 204
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-224 |
1.22e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 114.70 E-value: 1.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 2 MIlEAKKIRKSYGNKHNKheVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTnmkEKQLAE 81
Cdd:PRK13632 7 MI-KVENVSFSYPNSENN--ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIS---KENLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 82 FRKqHLGFIFQEY-NLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIH 160
Cdd:PRK13632 81 IRK-KIGIIFQNPdNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1112987593 161 EPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDPVAASFCSRVVFIKDGQIYTQ 224
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQ 223
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-221 |
1.54e-30 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 114.40 E-value: 1.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 1 MMILEAKKIRKSYGN-----KHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMK 75
Cdd:PRK10419 1 MTLLNVSGLSHHYAHgglsgKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 76 EKQLAEFRKQhLGFIFQeynllDTL-------TVKENILLPLS-ITKISKKEAGQKFEEVAKELGI-FELKDKYPNEISG 146
Cdd:PRK10419 81 RAQRKAFRRD-IQMVFQ-----DSIsavnprkTVREIIREPLRhLLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1112987593 147 GQKQRTSAARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHD-PVAASFCSRVVFIKDGQI 221
Cdd:PRK10419 155 GQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDlRLVERFCQRVMVMDNGQI 230
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
23-235 |
1.83e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 114.76 E-value: 1.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 23 LKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKqLAEFRKQhLGFIFQ--EYNLLDTl 100
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVK-LSDIRKK-VGLVFQypEYQLFEE- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 101 TVKENILLPLSITKISKKEAGQKFEEVAKELGIF--ELKDKYPNEISGGQKQRTSAARAFIHEPSIIFADEPTGALDSKS 178
Cdd:PRK13637 100 TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKG 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1112987593 179 ASDLLNKLSQLNQKRRATIVMVTH--DPVaASFCSRVVFIKDGQIYTQlnkgGQDRQMF 235
Cdd:PRK13637 180 RDEILNKIKELHKEYNMTIILVSHsmEDV-AKLADRIIVMNKGKCELQ----GTPREVF 233
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-221 |
3.48e-30 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 117.43 E-value: 3.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 1 MMILEAKKIRKSY-GNKhnkheVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQl 79
Cdd:COG1129 2 EPLLEMRGISKSFgGVK-----ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRD- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 80 AefrkQHLG--FIFQEYNLLDTLTVKENILLPLSITK---ISKKEAGQKFEEVAKELGIfelkDKYPN----EISGGQKQ 150
Cdd:COG1129 76 A----QAAGiaIIHQELNLVPNLSVAENIFLGREPRRgglIDWRAMRRRARELLARLGL----DIDPDtpvgDLSVAQQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1112987593 151 RTSAARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLnQKRRATIVMVTH--DPVAAsFCSRVVFIKDGQI 221
Cdd:COG1129 148 LVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHrlDEVFE-IADRVTVLRDGRL 218
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
21-214 |
3.61e-30 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 117.39 E-value: 3.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 21 EVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLaefrKQHLGFIFQEYNLLDTl 100
Cdd:TIGR02857 336 PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW----RDQIAWVPQHPFLFAG- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 101 TVKENILL------PLSITKISKKEAGQKFEEVAkELGIFELKDKYPNEISGGQKQRTSAARAFIHEPSIIFADEPTGAL 174
Cdd:TIGR02857 411 TIAENIRLarpdasDAEIREALERAGLDEFVAAL-PQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHL 489
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1112987593 175 DSKSASDLLNKLSQLNQKRraTIVMVTHDPVAASFCSRVV 214
Cdd:TIGR02857 490 DAETEAEVLEALRALAQGR--TVLLVTHRLALAALADRIV 527
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-221 |
4.76e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 112.63 E-value: 4.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 1 MMILEAKKIRKSYGNKHnkheVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNV------LSSIDQVSGGT----ININQAE 70
Cdd:PRK14267 2 KFAIETVNLRVYYGSNH----VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrlleLNEEARVEGEVrlfgRNIYSPD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 71 MTNMkekqlaEFRKQhLGFIFQEYNLLDTLTVKENILLPLSITKI--SKKEAGQKFEEVAKELGIF-ELKDK---YPNEI 144
Cdd:PRK14267 78 VDPI------EVRRE-VGMVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALWdEVKDRlndYPSNL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1112987593 145 SGGQKQRTSAARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLnqKRRATIVMVTHDPVAASFCSR-VVFIKDGQI 221
Cdd:PRK14267 151 SGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSDyVAFLYLGKL 226
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
26-221 |
4.80e-30 |
|
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: 114.82 E-value: 4.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 26 IDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAEFRKQHLGFIFQEYNLLDTLTVKEN 105
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 106 ILLPLSITKISKKEAgqKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPSIIFADEPTGALDSKSASDLLNK 185
Cdd:TIGR02142 96 LRYGMKRARPSERRI--SFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPY 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 1112987593 186 LSQLNQKRRATIVMVTHDPV-AASFCSRVVFIKDGQI 221
Cdd:TIGR02142 174 LERLHAEFGIPILYVSHSLQeVLRLADRVVVLEDGRV 210
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
22-221 |
6.54e-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: 6.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 22 VLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAefrkQHLGFIFQEYNLLDTlT 101
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELG----RHIGYLPQDVELFDG-T 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 102 VKENI--LLPLSITKISK--KEAGqkfeevAKELgIFELKDKYPNEI-------SGGQKQRTSAARAFIHEPSIIFADEP 170
Cdd:COG4618 422 IAENIarFGDADPEKVVAaaKLAG------VHEM-ILRLPDGYDTRIgeggarlSGGQRQRIGLARALYGDPRLVVLDEP 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1112987593 171 TGALDSKSASDLLNKLSQLnQKRRATIVMVTHDPVAASFCSRVVFIKDGQI 221
Cdd:COG4618 495 NSNLDDEGEAALAAAIRAL-KARGATVVVITHRPSLLAAVDKLLVLRDGRV 544
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
21-237 |
2.28e-29 |
|
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: 110.40 E-value: 2.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 21 EVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQaemTNMKEKQLAEFRKqHLGFIFQEYNLLDTl 100
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDG---QDIREVTLDSLRR-AIGVVPQDTVLFND- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 101 TVKENIllplsitKISKKEAG-QKFEEVAKELGIFE----LKDKYPNE-------ISGGQKQRTSAARAFIHEPSIIFAD 168
Cdd:cd03253 90 TIGYNI-------RYGRPDATdEEVIEAAKAAQIHDkimrFPDGYDTIvgerglkLSGGEKQRVAIARAILKNPPILLLD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1112987593 169 EPTGALDSKSASDLLNKLSQLNQKRraTIVMVTHDPVAASFCSRVVFIKDGQIYTQ------LNKGGQDRQMFFQ 237
Cdd:cd03253 163 EATSALDTHTEREIQAALRDVSKGR--TTIVIAHRLSTIVNADKIIVLKDGRIVERgtheelLAKGGLYAEMWKA 235
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
23-235 |
3.20e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 111.27 E-value: 3.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 23 LKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTN-MKEKQLAEFRKqHLGFIFQ--EYNLLDT 99
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgKKNKKLKPLRK-KVGIVFQfpEHQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 100 lTVKENILLPLSITKISKKEAGQKFEEVAKELGIFE-LKDKYPNEISGGQKQRTSAARAFIHEPSIIFADEPTGALDSKS 178
Cdd:PRK13634 102 -TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKG 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 179 ASDLLNKLSQLNQKRRATIVMVTH---DpvAASFCSRVVFIKDGQIYTQlnkgGQDRQMF 235
Cdd:PRK13634 181 RKEMMEMFYKLHKEKGLTTVLVTHsmeD--AARYADQIVVMHKGTVFLQ----GTPREIF 234
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
5-221 |
3.75e-29 |
|
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: 109.94 E-value: 3.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 5 EAKKIRKSYGNKHNkHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQaemTNMKEKQLAEFRK 84
Cdd:cd03249 2 EFKNVSFRYPSRPD-VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDG---VDIRDLNLRWLRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 85 QhLGFIFQEYNLLDTlTVKENILLplSITKISKKEAgqkfEEVAKELGIFELKDKYPN-----------EISGGQKQRTS 153
Cdd:cd03249 78 Q-IGLVSQEPVLFDG-TIAENIRY--GKPDATDEEV----EEAAKKANIHDFIMSLPDgydtlvgergsQLSGGQKQRIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1112987593 154 AARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRraTIVMVTHDPVAASFCSRVVFIKDGQI 221
Cdd:cd03249 150 IARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGR--TTIVIAHRLSTIRNADLIAVLQNGQV 215
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-221 |
3.86e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 110.56 E-value: 3.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSYgNKH--NKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQla 80
Cdd:COG1101 1 MLELKNLSKTF-NPGtvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYK-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 81 efRKQHLGFIFQEyNLLDT---LTVKENILL--------PLSITKISKKEAgqKFEEVAKELGIfELKDKYPNEI---SG 146
Cdd:COG1101 78 --RAKYIGRVFQD-PMMGTapsMTIEENLALayrrgkrrGLRRGLTKKRRE--LFRELLATLGL-GLENRLDTKVgllSG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1112987593 147 GQKQRTSAARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTH---DpvAASFCSRVVFIKDGQI 221
Cdd:COG1101 152 GQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHnmeQ--ALDYGNRLIMMHEGRI 227
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
3-220 |
7.00e-29 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 109.06 E-value: 7.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSYgNKHNKH----EVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAE----MTNM 74
Cdd:COG4778 4 LLEVENLSKTF-TLHLQGgkrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdLAQA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 75 KEKQLAEFRKQHLGFIFQeynLLDTL-------TVKEnillPLSITKISKKEAGQKFEEVAKELGIFE-LKDKYPNEISG 146
Cdd:COG4778 83 SPREILALRRRTIGYVSQ---FLRVIprvsaldVVAE----PLLERGVDREEARARARELLARLNLPErLWDLPPATFSG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1112987593 147 GQKQRTSAARAFIHEPSIIFADEPTGALDSKSAS---DLLNKLsqlnqKRR-ATIVMVTHDP-VAASFCSRVVFIKDGQ 220
Cdd:COG4778 156 GEQQRVNIARGFIADPPLLLLDEPTASLDAANRAvvvELIEEA-----KARgTAIIGIFHDEeVREAVADRVVDVTPFS 229
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
3-203 |
1.56e-28 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 110.21 E-value: 1.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSY----GNKHNKHEVLK---GIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMK 75
Cdd:COG4608 7 LLEVRDLKKHFpvrgGLFGRTVGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 76 EKQLAEFRKqHLGFIFQE-YNLLDT-LTVKENILLPLSITKI-SKKEAGQKFEEVAKELGIF-ELKDKYPNEISGGQKQR 151
Cdd:COG4608 87 GRELRPLRR-RMQMVFQDpYASLNPrMTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLRpEHADRYPHEFSGGQRQR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1112987593 152 TSAARAFIHEPSIIFADEPTGALD-SKSASdLLNKLSQLNQKRRATIVMVTHD 203
Cdd:COG4608 166 IGIARALALNPKLIVCDEPVSALDvSIQAQ-VLNLLEDLQDELGLTYLFISHD 217
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
7-221 |
1.69e-28 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 113.22 E-value: 1.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 7 KKIRKSYGNKHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVL---SSIDQVSGGTININQAEMTnmkekqlAEFR 83
Cdd:TIGR00955 25 SRLRGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALafrSPKGVKGSGSVLLNGMPID-------AKEM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 84 KQHLGFIFQEYNLLDTLTVKENIL------LPLSITKISKKEAgqkFEEVAKELGIFELKDK---YPNE---ISGGQKQR 151
Cdd:TIGR00955 98 RAISAYVQQDDLFIPTLTVREHLMfqahlrMPRRVTKKEKRER---VDEVLQALGLRKCANTrigVPGRvkgLSGGERKR 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1112987593 152 TSAARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRaTIVMVTHDPVAASFC--SRVVFIKDGQI 221
Cdd:TIGR00955 175 LAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGK-TIICTIHQPSSELFElfDKIILMAEGRV 245
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-224 |
5.76e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 107.79 E-value: 5.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIrkSYGNKHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTnmkEKQLAEF 82
Cdd:PRK13635 5 IIRVEHI--SFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLS---EETVWDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 83 RKQhLGFIFQEY-NLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHE 161
Cdd:PRK13635 80 RRQ-VGMVFQNPdNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQ 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1112987593 162 PSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDPVAASFCSRVVFIKDGQIYTQ 224
Cdd:PRK13635 159 PDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEE 221
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-221 |
6.42e-28 |
|
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: 106.60 E-value: 6.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 1 MMILEAKKIRKSYGNKHnkheVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLA 80
Cdd:COG0410 1 MPMLEVENLHAGYGGIH----VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 81 efrKQHLGFIFQEYNLLDTLTVKENILLPLSITKiSKKEAGQKFEEVakeLGIF----ELKDKYPNEISGGQKQRTSAAR 156
Cdd:COG0410 77 ---RLGIGYVPEGRRIFPSLTVEENLLLGAYARR-DRAEVRADLERV---YELFprlkERRRQRAGTLSGGEQQMLAIGR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1112987593 157 AFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQkRRATIVMVTHD-PVAASFCSRVVFIKDGQI 221
Cdd:COG0410 150 ALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNR-EGVTILLVEQNaRFALEIADRAYVLERGRI 214
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
23-221 |
1.50e-27 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 108.97 E-value: 1.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 23 LKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAEFRKQHLGFIFQEYNLLDTLTV 102
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 103 KENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPSIIFADEPTGALDSKSASDL 182
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1112987593 183 LNKLSQLNQKRRATIVMVTHD-PVAASFCSRVVFIKDGQI 221
Cdd:PRK10070 204 QDELVKLQAKHQRTIVFISHDlDEAMRIGDRIAIMQNGEV 243
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-221 |
2.52e-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: 104.28 E-value: 2.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGnkhnKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININqaemtnmkEKQLAEFR 83
Cdd:cd03269 1 LEVENVTKRFG----RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFD--------GKPLDIAA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 84 KQHLGFIFQEYNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPS 163
Cdd:cd03269 69 RNRIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 164 IIFADEPTGALDSKSASDLLNKLSQLNQKRRaTIVMVTH--DPVAAsFCSRVVFIKDGQI 221
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIRELARAGK-TVILSTHqmELVEE-LCDRVLLLNKGRA 206
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-209 |
2.53e-27 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 105.55 E-value: 2.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSYGNKhnkhEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQlaef 82
Cdd:PRK11248 1 MLQISHLYADYGGK----PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 83 rkqhlGFIFQEYNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEP 162
Cdd:PRK11248 73 -----GVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANP 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1112987593 163 SIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDPVAASF 209
Cdd:PRK11248 148 QLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVF 194
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
22-221 |
2.96e-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: 104.62 E-value: 2.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 22 VLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQaemTNMKEKQLAEFRKQhLGFIFQEYNLLDTlT 101
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDG---HDVRDYTLASLRRQ-IGLVSQDVFLFND-T 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 102 VKENILlplsitkISKKEAGQK-FEEVAKELG----IFELKDKYPNEI-------SGGQKQRTSAARAFIHEPSIIFADE 169
Cdd:cd03251 92 VAENIA-------YGRPGATREeVEEAARAANahefIMELPEGYDTVIgergvklSGGQRQRIAIARALLKDPPILILDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1112987593 170 PTGALDSKSASDLLNKLSQLnQKRRATIVmVTHDPVAASFCSRVVFIKDGQI 221
Cdd:cd03251 165 ATSALDTESERLVQAALERL-MKNRTTFV-IAHRLSTIENADRIVVLEDGKI 214
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
20-235 |
3.21e-27 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 109.41 E-value: 3.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 20 HEVLKGIDLQIQKGEFVSIMGPSGSGK-TTLLNVLSSIDqvSGGTININQAEMTNMKEKQLAEFRKQhLGFIFQEYN--L 96
Cdd:PRK15134 299 NVVVKNISFTLRPGETLGLVGESGSGKsTTGLALLRLIN--SQGEIWFDGQPLHNLNRRQLLPVRHR-IQVVFQDPNssL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 97 LDTLTVKENILLPLSI--TKISKKEAGQKFEEVAKELGI-FELKDKYPNEISGGQKQRTSAARAFIHEPSIIFADEPTGA 173
Cdd:PRK15134 376 NPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSS 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1112987593 174 LDSKSASDLLNKLSQLNQKRRATIVMVTHD-PVAASFCSRVVFIKDGQIYTQlnkgGQDRQMF 235
Cdd:PRK15134 456 LDKTVQAQILALLKSLQQKHQLAYLFISHDlHVVRALCHQVIVLRQGEVVEQ----GDCERVF 514
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
23-224 |
3.23e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 105.60 E-value: 3.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 23 LKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNmkeKQLAEFRKqHLGFIFQE-YNLLDTLT 101
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITD---DNFEKLRK-HIGIVFQNpDNQFVGSI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 102 VKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPSIIFADEPTGALDSKSASD 181
Cdd:PRK13648 101 VKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQN 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1112987593 182 LLNKLSQLNQKRRATIVMVTHDPVAASFCSRVVFIKDGQIYTQ 224
Cdd:PRK13648 181 LLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKE 223
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
21-224 |
4.17e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 105.59 E-value: 4.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 21 EVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKqlaEFRKQhLGFIFQEYNllDTL 100
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEK---WVRSK-VGLVFQDPD--DQV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 101 ---TVKENILL-PLSItKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPSIIFADEPTGALDS 176
Cdd:PRK13647 93 fssTVWDDVAFgPVNM-GLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDP 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1112987593 177 KSASDLLNKLSQLNQkRRATIVMVTHD-PVAASFCSRVVFIKDGQIYTQ 224
Cdd:PRK13647 172 RGQETLMEILDRLHN-QGKTVIVATHDvDLAAEWADQVIVLKEGRVLAE 219
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-237 |
6.95e-27 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 105.96 E-value: 6.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 1 MMILEAKKIRKSYGNKHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKT----TLLNVLSSiDQVSGGTININQAEMTNMKE 76
Cdd:PRK09473 10 DALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAA-NGRIGGSATFNGREILNLPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 77 KQLAEFRKQHLGFIFQeynllDTLT-------VKENILLPLSITK-ISKKEAgqkFEEVAKELGIFELKDK------YPN 142
Cdd:PRK09473 89 KELNKLRAEQISMIFQ-----DPMTslnpymrVGEQLMEVLMLHKgMSKAEA---FEESVRMLDAVKMPEArkrmkmYPH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 143 EISGGQKQRTSAARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHD-PVAASFCSRVVFIKDGQI 221
Cdd:PRK09473 161 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDlGVVAGICDKVLVMYAGRT 240
|
250
....*....|....*...
gi 1112987593 222 --YtqlnkgGQDRQMFFQ 237
Cdd:PRK09473 241 meY------GNARDVFYQ 252
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-203 |
1.41e-26 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 105.17 E-value: 1.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 19 KHEVLK---GIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAEFRKQhLGFIFQE-- 93
Cdd:PRK15079 30 PPKTLKavdGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSD-IQMIFQDpl 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 94 YNLLDTLTVKENILLPLSI--TKISKKEAGQKFEEVAKELGIFE-LKDKYPNEISGGQKQRTSAARAFIHEPSIIFADEP 170
Cdd:PRK15079 109 ASLNPRMTIGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEP 188
|
170 180 190
....*....|....*....|....*....|...
gi 1112987593 171 TGALDSKSASDLLNKLSQLNQKRRATIVMVTHD 203
Cdd:PRK15079 189 VSALDVSIQAQVVNLLQQLQREMGLSLIFIAHD 221
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-235 |
1.64e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 104.16 E-value: 1.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSYGNKHnkhEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMtNMKEKQLAEF 82
Cdd:PRK13636 5 ILKVEELNYNYSDGT---HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 83 RkQHLGFIFQEY-NLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHE 161
Cdd:PRK13636 81 R-ESVGMVFQDPdNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVME 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1112987593 162 PSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHD-PVAASFCSRVVFIKDGQIYTQlnkgGQDRQMF 235
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDiDIVPLYCDNVFVMKEGRVILQ----GNPKEVF 230
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-221 |
2.02e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 104.40 E-value: 2.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSY-----------GNKH----NKHEV--LKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTIN 65
Cdd:COG4586 1 IIEVENLSKTYrvyekepglkgALKGlfrrEYREVeaVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 66 INQaeMTNMKEKQlaEFRKQhLGFIF-QEYNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEI 144
Cdd:COG4586 81 VLG--YVPFKRRK--EFARR-IGVVFgQRSQLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 145 SGGQKQRTSAARAFIHEPSIIFADEPTGALD--SKSAsdLLNKLSQLNQKRRATIVMVTHDP--VAAsFCSRVVFIKDGQ 220
Cdd:COG4586 156 SLGQRMRCELAAALLHRPKILFLDEPTIGLDvvSKEA--IREFLKEYNRERGTTILLTSHDMddIEA-LCDRVIVIDHGR 232
|
.
gi 1112987593 221 I 221
Cdd:COG4586 233 I 233
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
4-221 |
2.75e-26 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 106.87 E-value: 2.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGNkhNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTnmkekQL--AE 81
Cdd:TIGR03375 464 IEFRNVSFAYPG--QETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIR-----QIdpAD 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 82 FRkQHLGFIFQEYNLLdTLTVKENILL-PLSITKiskkeagQKFEEVAKELGIFELKDKYPN-----------EISGGQK 149
Cdd:TIGR03375 537 LR-RNIGYVPQDPRLF-YGTLRDNIALgAPYADD-------EEILRAAELAGVTEFVRRHPDgldmqigergrSLSGGQR 607
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1112987593 150 QRTSAARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRraTIVMVTHDPVAASFCSRVVFIKDGQI 221
Cdd:TIGR03375 608 QAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGK--TLVLVTHRTSLLDLVDRIIVMDNGRI 677
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
12-221 |
2.84e-26 |
|
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: 100.85 E-value: 2.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 12 SYGNKHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKqlaefRKQHLGFIF 91
Cdd:cd03247 7 SFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-----LSSLISVLN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 92 QEYNLLDTlTVKENIllplsitkiskkeaGQKFeevakelgifelkdkypneiSGGQKQRTSAARAFIHEPSIIFADEPT 171
Cdd:cd03247 82 QRPYLFDT-TLRNNL--------------GRRF--------------------SGGERQRLALARILLQDAPIVLLDEPT 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1112987593 172 GALDSKSASDLLNKL-SQLNQKrraTIVMVTHDPVAASFCSRVVFIKDGQI 221
Cdd:cd03247 127 VGLDPITERQLLSLIfEVLKDK---TLIWITHHLTGIEHMDKILFLENGKI 174
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-203 |
4.89e-26 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 102.22 E-value: 4.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 1 MMILEAKKIRKSYGN-----KHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMK 75
Cdd:COG4167 2 SALLEVRNLSKTFKYrtglfRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 76 EKQlaefRKQHLGFIFQEYNllDTLTVKENI--LL--PLSI-TKISKKEAGQKFEEVAKELGIF-ELKDKYPNEISGGQK 149
Cdd:COG4167 82 YKY----RCKHIRMIFQDPN--TSLNPRLNIgqILeePLRLnTDLTAEEREERIFATLRLVGLLpEHANFYPHMLSSGQK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1112987593 150 QRTSAARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHD 203
Cdd:COG4167 156 QRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQH 209
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-221 |
4.93e-26 |
|
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: 100.75 E-value: 4.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGNKHnkheVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQlaefr 83
Cdd:cd03268 1 LKTNDLTKTYGKKR----VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 84 kQHLGFIFQEYNLLDTLTVKENILLPLSITKISKKEAgqkfEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPS 163
Cdd:cd03268 72 -RRIGALIEAPGFYPNLTARENLRLLARLLGIRKKRI----DEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1112987593 164 IIFADEPTGALDSKSASDLLNKLSQLNqKRRATIVMVTH-----DPVAasfcSRVVFIKDGQI 221
Cdd:cd03268 147 LLILDEPTNGLDPDGIKELRELILSLR-DQGITVLISSHllseiQKVA----DRIGIINKGKL 204
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
3-244 |
7.50e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 102.09 E-value: 7.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSY--GNKHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININqaEMTNMKEKQLA 80
Cdd:PRK13633 4 MIKCKNVSYKYesNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVD--GLDTSDEENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 81 EFRkQHLGFIFQEY-NLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFI 159
Cdd:PRK13633 82 DIR-NKAGMVFQNPdNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 160 HEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDPVAASFCSRVVFIKDGQIYtqlnKGGQDRQMFFQ-D 238
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVV----MEGTPKEIFKEvE 236
|
....*.
gi 1112987593 239 IMKTQG 244
Cdd:PRK13633 237 MMKKIG 242
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
3-221 |
9.35e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 101.73 E-value: 9.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSYGNKHNKHeVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTnmkEKQLAEF 82
Cdd:PRK13650 4 IIEVKNLTFKYKEDQEKY-TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLT---EENVWDI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 83 RkQHLGFIFQEY-NLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHE 161
Cdd:PRK13650 80 R-HKIGMVFQNPdNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 162 PSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDPVAASFCSRVVFIKDGQI 221
Cdd:PRK13650 159 PKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
22-220 |
1.01e-25 |
|
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: 99.85 E-value: 1.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 22 VLKGIDLQIQKGEFVSIMGPSGSGKTTLLN-VLSSIDQVSGgTININQaemtnmkekqlaefrkqHLGFIFQEYNLLDTl 100
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGELEKLSG-SVSVPG-----------------SIAYVSQEPWIQNG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 101 TVKENILLPLSITKiskkeagQKFEEVAK------ELGIFELKDKYpnEI-------SGGQKQRTSAARAFIHEPSIIFA 167
Cdd:cd03250 81 TIRENILFGKPFDE-------ERYEKVIKacalepDLEILPDGDLT--EIgekginlSGGQKQRISLARAVYSDADIYLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1112987593 168 DEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDPVAASFCSRVVFIKDGQ 220
Cdd:cd03250 152 DDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
17-235 |
2.12e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 100.24 E-value: 2.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 17 HNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVS-----GGTININQAEMTNMKEKQLaEFRKQhLGFIF 91
Cdd:PRK14239 15 YNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIYSPRTDTV-DLRKE-IGMVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 92 QEYNLLdTLTVKENILLPLSITKISKKEA-GQKFEEVAKELGIF-ELKDKYPNE---ISGGQKQRTSAARAFIHEPSIIF 166
Cdd:PRK14239 93 QQPNPF-PMSIYENVVYGLRLKGIKDKQVlDEAVEKSLKGASIWdEVKDRLHDSalgLSGGQQQRVCIARVLATSPKIIL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 167 ADEPTGALDSKSASDLLNKLsqLNQKRRATIVMVTHDPVAASFCS-RVVFIKDGqiytQLNKGGQDRQMF 235
Cdd:PRK14239 172 LDEPTSALDPISAGKIEETL--LGLKDDYTMLLVTRSMQQASRISdRTGFFLDG----DLIEYNDTKQMF 235
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-204 |
2.30e-25 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 103.98 E-value: 2.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGNKHnkhEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAefr 83
Cdd:TIGR02868 335 LELRDLSAGYPGAP---PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVR--- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 84 kQHLGFIFQEYNLLDTlTVKENILLplsitkiSKKEA-GQKFEEVAKELGIFELKDKYPN-----------EISGGQKQR 151
Cdd:TIGR02868 409 -RRVSVCAQDAHLFDT-TVRENLRL-------ARPDAtDEELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQR 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1112987593 152 TSAARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRraTIVMVTHDP 204
Cdd:TIGR02868 480 LALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGR--TVVLITHHL 530
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
2-224 |
3.27e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 100.09 E-value: 3.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 2 MILEAKKIRKSYGNKhnkhEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAe 81
Cdd:PRK11231 1 MTLRTENLTVGYGTK----RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 82 frkQHLGFIFQEYNLLDTLTVKENI------LLPLsITKISKKEAgQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAA 155
Cdd:PRK11231 76 ---RRLALLPQHHLTPEGITVRELVaygrspWLSL-WGRLSAEDN-ARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 156 RAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRaTIVMVTHDPVAAS-FCSRVVFIKDGQIYTQ 224
Cdd:PRK11231 151 MVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGK-TVVTVLHDLNQASrYCDHLVVLANGHVMAQ 219
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
25-221 |
3.81e-25 |
|
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: 98.98 E-value: 3.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 25 GIDLQIQKGEFVSIMGPSGSGKTT----LLNVLSSIDQVSGGTININQAEMTNMKekqlaeFRKQHLGFIFQE----YNL 96
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLtclaILGLLPPGLTQTSGEILLDGRPLLPLS------IRGRHIATIMQNprtaFNP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 97 LDTLT--VKENILLPLSITKISKKEAGQKFEEVAKELGIfELKDKYPNEISGGQKQRTSAARAFIHEPSIIFADEPTGAL 174
Cdd:TIGR02770 78 LFTMGnhAIETLRSLGKLSKQARALILEALEAVGLPDPE-EVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1112987593 175 DSKSASDLLNKLSQLNQKRRATIVMVTHD-PVAASFCSRVVFIKDGQI 221
Cdd:TIGR02770 157 DVVNQARVLKLLRELRQLFGTGILLITHDlGVVARIADEVAVMDDGRI 204
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
25-221 |
4.83e-25 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 102.96 E-value: 4.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 25 GIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQA-EMTNMKEKQLAE--FRKQHLGFIFQEYNL----- 96
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGdEWVDMTKPGPDGrgRAKRYIGILHQEYDLyphrt 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 97 -LDTLTVKENILLPLSITK----ISKKEAGqkFEEVAKElgifELKDKYPNEISGGQKQRTSAARAFIHEPSIIFADEPT 171
Cdd:TIGR03269 382 vLDNLTEAIGLELPDELARmkavITLKMVG--FDEEKAE----EILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPT 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1112987593 172 GALDS----KSASDLLNKLSQLNQkrraTIVMVTHD-PVAASFCSRVVFIKDGQI 221
Cdd:TIGR03269 456 GTMDPitkvDVTHSILKAREEMEQ----TFIIVSHDmDFVLDVCDRAALMRDGKI 506
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
20-214 |
9.38e-25 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 96.92 E-value: 9.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 20 HEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTininqaemtnmkekqLAEFRKQHLGFIFQEYNLLDT 99
Cdd:NF040873 5 RPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGT---------------VRRAGGARVAYVPQRSEVPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 100 L--TVKENILL----PLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPSIIFADEPTGA 173
Cdd:NF040873 70 LplTVRDLVAMgrwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1112987593 174 LDSKSASDLLNKLSQLnQKRRATIVMVTHDPVAASFCSRVV 214
Cdd:NF040873 150 LDAESRERIIALLAEE-HARGATVVVVTHDLELVRRADPCV 189
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-221 |
1.20e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 98.58 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 18 NKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEM---TNMKEKQLAEFRKQhLGFIFQEY 94
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgKDIFQIDAIKLRKE-VGMVFQQP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 95 NLLDTLTVKENILLPLSITKIS-KKEAGQKFEEVAKELGIF-ELKDKY---PNEISGGQKQRTSAARAFIHEPSIIFADE 169
Cdd:PRK14246 100 NPFPHLSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLWkEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1112987593 170 PTGALDSKSASDLLNKLSQLnqKRRATIVMVTHDP-VAASFCSRVVFIKDGQI 221
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITEL--KNEIAIVIVSHNPqQVARVADYVAFLYNGEL 230
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-220 |
1.76e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 101.26 E-value: 1.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 1 MMILEAKKIRKSYGNKHnkheVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTnMKEKQLA 80
Cdd:COG3845 3 PPALELRGITKRFGGVV----ANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVR-IRSPRDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 81 efRKQHLGFIFQEYNLLDTLTVKENILL---PLSITKISKKEAGQKFEEVAKELGiFELK-DKYPNEISGGQKQRTSAAR 156
Cdd:COG3845 78 --IALGIGMVHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARARIRELSERYG-LDVDpDAKVEDLSVGEQQRVEILK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1112987593 157 AFIHEPSIIFADEPTGALDSKSASDLLNKLSQLnQKRRATIVMVTH--DPVAAsFCSRVVFIKDGQ 220
Cdd:COG3845 155 ALYRGARILILDEPTAVLTPQEADELFEILRRL-AAEGKSIIFITHklREVMA-IADRVTVLRRGK 218
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
22-204 |
5.68e-24 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 100.34 E-value: 5.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 22 VLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSG--GTININQAEMTnmkeKQLAefrkQHLGFIFQEYNLLDT 99
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPT----KQIL----KRTGFVTQDDILYPH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 100 LTVKENIL------LPLSITKISKKEAGqkfEEVAKELGIFE-----LKDKYPNEISGGQKQRTSAARAFIHEPSIIFAD 168
Cdd:PLN03211 155 LTVRETLVfcsllrLPKSLTKQEKILVA---ESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILD 231
|
170 180 190
....*....|....*....|....*....|....*.
gi 1112987593 169 EPTGALDSKSASDLLNKLSQLNQKRRaTIVMVTHDP 204
Cdd:PLN03211 232 EPTSGLDATAAYRLVLTLGSLAQKGK-TIVTSMHQP 266
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
10-222 |
5.88e-24 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 95.68 E-value: 5.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 10 RKSYGNKHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININqaemtnMKEKQLAEFrkqHLGF 89
Cdd:cd03220 25 ILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVR------GRVSSLLGL---GGGF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 90 ifqeynlLDTLTVKENILLPLSITKISKKEAGQKFEEVAK--ELGIFelKDKYPNEISGGQKQRTSAARAFIHEPSIIFA 167
Cdd:cd03220 96 -------NPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEfsELGDF--IDLPVKTYSSGMKARLAFAIATALEPDILLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1112987593 168 DEPTGALDSKSASDLLNKLSQLnQKRRATIVMVTHDPVA-ASFCSRVVFIKDGQIY 222
Cdd:cd03220 167 DEVLAVGDAAFQEKCQRRLREL-LKQGKTVILVSHDPSSiKRLCDRALVLEKGKIR 221
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
23-239 |
6.82e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 97.12 E-value: 6.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 23 LKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNM-KEKQLAEFRKqHLGFIFQ--EYNLLDT 99
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsKNKDIKQIRK-KVGLVFQfpESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 100 LTVKENILLPLSItKISKKEAGQKFEEVAKELGIFE-LKDKYPNEISGGQKQRTSAARAFIHEPSIIFADEPTGALDSKS 178
Cdd:PRK13649 102 TVLKDVAFGPQNF-GVSQEEAEALAREKLALVGISEsLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1112987593 179 ASDLLNKLSQLNQKrRATIVMVTH--DPVaASFCSRVVFIKDGQIYtqlnKGGQDRQMfFQDI 239
Cdd:PRK13649 181 RKELMTLFKKLHQS-GMTIVLVTHlmDDV-ANYADFVYVLEKGKLV----LSGKPKDI-FQDV 236
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
4-224 |
9.26e-24 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 96.21 E-value: 9.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGNKhnkhEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAefr 83
Cdd:PRK10253 8 LRGEQLTLGYGKY----TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 84 kQHLGFIFQEYNLLDTLTVKENIL------LPLsITKISKKEAgqkfEEVAKEL---GIFELKDKYPNEISGGQKQRTSA 154
Cdd:PRK10253 81 -RRIGLLAQNATTPGDITVQELVArgryphQPL-FTRWRKEDE----EAVTKAMqatGITHLADQSVDTLSGGQRQRAWI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1112987593 155 ARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHD-PVAASFCSRVVFIKDGQIYTQ 224
Cdd:PRK10253 155 AMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDlNQACRYASHLIALREGKIVAQ 225
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-221 |
1.16e-23 |
|
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: 99.11 E-value: 1.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGNKhnkhEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQ------------------------- 58
Cdd:TIGR03269 1 IEVKNLTKKFDGK----EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyeptsgriiyhvalcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 59 -------VSGGTININQAEMTNMKEKQLAEFRKQhLGFIFQE-YNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKE 130
Cdd:TIGR03269 77 kvgepcpVCGGTLEPEEVDFWNLSDKLRRRIRKR-IAIMLQRtFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 131 LGIFELKDKYPNEISGGQKQRTSAARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDP-VAASF 209
Cdd:TIGR03269 156 VQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPeVIEDL 235
|
250
....*....|..
gi 1112987593 210 CSRVVFIKDGQI 221
Cdd:TIGR03269 236 SDKAIWLENGEI 247
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
9-221 |
1.29e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 95.53 E-value: 1.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 9 IRKSYGNKHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININqaemtnMKEKQLAEfrkqhLG 88
Cdd:COG1134 28 LLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVN------GRVSALLE-----LG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 89 FIFQEynlldTLTVKENILLPLSITKISKKEAGQKFEEVAK--ELGIF---ELKdKYpneiSGGQKqrtsaAR-AF---I 159
Cdd:COG1134 97 AGFHP-----ELTGRENIYLNGRLLGLSRKEIDEKFDEIVEfaELGDFidqPVK-TY----SSGMR-----ARlAFavaT 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1112987593 160 H-EPSIIFADEPTGALDS----KSasdlLNKLSQLnQKRRATIVMVTHDP-VAASFCSRVVFIKDGQI 221
Cdd:COG1134 162 AvDPDILLVDEVLAVGDAafqkKC----LARIREL-RESGRTVIFVSHSMgAVRRLCDRAIWLEKGRL 224
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-221 |
1.95e-23 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 92.88 E-value: 1.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGNkhnkHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEmtnmkekqlaefr 83
Cdd:cd03216 1 LELRGITKRFGG----VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKE------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 84 kqhlgfifqeynlLDTLTVKEnillplsitkiskkeagqkfeevAKELGI---FELkdkypneiSGGQKQRTSAARAFIH 160
Cdd:cd03216 64 -------------VSFASPRD-----------------------ARRAGIamvYQL--------SVGERQMVEIARALAR 99
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1112987593 161 EPSIIFADEPTGALDSKSASDLLNKLSQLnQKRRATIVMVTH--DPVAAsFCSRVVFIKDGQI 221
Cdd:cd03216 100 NARLLILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHrlDEVFE-IADRVTVLRDGRV 160
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
26-223 |
2.01e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 95.96 E-value: 2.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 26 IDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNM-KEKQLAEFRKQhLGFIFQ--EYNLLDTLTV 102
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTsKQKEIKPVRKK-VGVVFQfpESQLFEETVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 103 KENILLPLSItKISKKEAGQKFEEVAKELGIF-ELKDKYPNEISGGQKQRTSAARAFIHEPSIIFADEPTGALDSKSASD 181
Cdd:PRK13643 104 KDVAFGPQNF-GIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIE 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1112987593 182 LLNKLSQLNQKRRaTIVMVTH--DPVaASFCSRVVFIKDGQIYT 223
Cdd:PRK13643 183 MMQLFESIHQSGQ-TVVLVTHlmDDV-ADYADYVYLLEKGHIIS 224
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-221 |
6.17e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 94.39 E-value: 6.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSYGNKHNKHEvLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLaef 82
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQ-LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNL--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 83 rKQHLGFIFQEY-NLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHE 161
Cdd:PRK13642 80 -RRKIGMVFQNPdNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 162 PSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDPVAASFCSRVVFIKDGQI 221
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEI 218
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-221 |
7.40e-23 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 92.97 E-value: 7.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGNKHnkheVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAefr 83
Cdd:TIGR03410 1 LEVSNLNVYYGQSH----ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 84 KQHLGFIFQEYNLLDTLTVKENILLPLSitkiSKKEAGQKFEEVAKEL--GIFELKDKYPNEISGGQKQRTSAARAFIHE 161
Cdd:TIGR03410 74 RAGIAYVPQGREIFPRLTVEENLLTGLA----ALPRRSRKIPDEIYELfpVLKEMLGRRGGDLSGGQQQQLAIARALVTR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1112987593 162 PSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMV-THDPVAASFCSRVVFIKDGQI 221
Cdd:TIGR03410 150 PKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVeQYLDFARELADRYYVMERGRV 210
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-220 |
7.87e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 94.49 E-value: 7.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSYGNKhnkhEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMtnmkeKQLAEF 82
Cdd:PRK13537 7 PIDFRNVEKRYGDK----LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV-----PSRARH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 83 RKQHLGFIFQEYNLLDTLTVKENILLPLSITKISkkeAGQKFEEVAKELGIFELKDKYP---NEISGGQKQRTSAARAFI 159
Cdd:PRK13537 78 ARQRVGVVPQFDNLDPDFTVRENLLVFGRYFGLS---AAAARALVPPLLEFAKLENKADakvGELSGGMKRRLTLARALV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1112987593 160 HEPSIIFADEPTGALDSKSASDLLNKLSQLnQKRRATIVMVTH-DPVAASFCSRVVFIKDGQ 220
Cdd:PRK13537 155 NDPDVLVLDEPTTGLDPQARHLMWERLRSL-LARGKTILLTTHfMEEAERLCDRLCVIEEGR 215
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-221 |
8.61e-23 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 93.03 E-value: 8.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 1 MMILEAKKIRKSYGNKhnkhEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKekqLA 80
Cdd:PRK10895 1 MATLTAKNLAKAYKGR----RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLP---LH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 81 EFRKQHLGFIFQEYNLLDTLTVKENILLPLSITK-ISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFI 159
Cdd:PRK10895 74 ARARRGIGYLPQEASIFRRLSVYDNLMAVLQIRDdLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1112987593 160 HEPSIIFADEPTGALDSKSASDLLNKLSQLnqKRRATIVMVTHDPVAASF--CSRVVFIKDGQI 221
Cdd:PRK10895 154 ANPKFILLDEPFAGVDPISVIDIKRIIEHL--RDSGLGVLITDHNVRETLavCERAYIVSQGHL 215
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-219 |
1.15e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 96.39 E-value: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGNKHnkheVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAEFr 83
Cdd:PRK09700 6 ISMAGIGKSFGPVH----ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 84 kqHLGFIFQEYNLLDTLTVKENILLPLSITK-------ISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAAR 156
Cdd:PRK09700 81 --GIGIIYQELSVIDELTVLENLYIGRHLTKkvcgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1112987593 157 AFIHEPSIIFADEPTGALDSKSASDLLNKLSQLnQKRRATIVMVTHD-PVAASFCSRVVFIKDG 219
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQL-RKEGTAIVYISHKlAEIRRICDRYTVMKDG 221
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3-225 |
2.14e-22 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 92.30 E-value: 2.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSYGNKHNKHEVlkgiDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAEF 82
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDV----SFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 83 RKQHL-----GFIFQeyNLLDTL----TVKENILLPLSIT------KIsKKEAGQKFEEVakELGIFELKDKyPNEISGG 147
Cdd:PRK11701 82 ERRRLlrtewGFVHQ--HPRDGLrmqvSAGGNIGERLMAVgarhygDI-RATAGDWLERV--EIDAARIDDL-PTTFSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 148 QKQRTSAARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHD-PVAASFCSRVVFIKDGQI----- 221
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDlAVARLLAHRLLVMKQGRVvesgl 235
|
250
....*....|....*
gi 1112987593 222 -----------YTQL 225
Cdd:PRK11701 236 tdqvlddpqhpYTQL 250
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
18-220 |
2.99e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 95.26 E-value: 2.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 18 NKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEmtnmkekqlaefrkqHLGFIFQE-YNL 96
Cdd:COG4178 374 DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGA---------------RVLFLPQRpYLP 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 97 LDTLtvKENILLPLSITKISKKEAgqkfEEVAKELGIFELKDKY------PNEISGGQKQRTSAARAFIHEPSIIFADEP 170
Cdd:COG4178 439 LGTL--REALLYPATAEAFSDAEL----REALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEA 512
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1112987593 171 TGALDSKSASDLLNKLSQlnQKRRATIVMVTHDPVAASFCSRVVFIKDGQ 220
Cdd:COG4178 513 TSALDEENEAALYQLLRE--ELPGTTVISVGHRSTLAAFHDRVLELTGDG 560
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
3-221 |
3.53e-22 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 91.82 E-value: 3.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSYGNKHNkhevLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAEF 82
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKG----CRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 83 RKQHL-----GFIFQeyNLLDTL----TVKENI---LLPLSITKISK--KEAGQKFEEVAKELGIFelkDKYPNEISGGQ 148
Cdd:TIGR02323 79 ERRRLmrtewGFVHQ--NPRDGLrmrvSAGANIgerLMAIGARHYGNirATAQDWLEEVEIDPTRI---DDLPRAFSGGM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1112987593 149 KQRTSAARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHD-PVAASFCSRVVFIKDGQI 221
Cdd:TIGR02323 154 QQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDlGVARLLAQRLLVMQQGRV 227
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-224 |
4.76e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 92.17 E-value: 4.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSYgnKHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTT---LLNVLSSIDQVSGGTININQAEMTnmkEKQL 79
Cdd:PRK13640 5 IVEFKHVSFTY--PDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLT---AKTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 80 AEFRKQhLGFIFQEY-NLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAF 158
Cdd:PRK13640 80 WDIREK-VGIVFQNPdNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGIL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1112987593 159 IHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDPVAASFCSRVVFIKDGQIYTQ 224
Cdd:PRK13640 159 AVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQ 224
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
16-227 |
6.71e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 94.14 E-value: 6.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 16 KHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSsidqvsG-----GTININQAEMTNMKEKQLaefrKQHLGFI 90
Cdd:PRK11174 359 SPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALL------GflpyqGSLKINGIELRELDPESW----RKHLSWV 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 91 FQEYNLLDTlTVKENILLplsitkiSKKEAG-QKFEEVAKELGIFELKDKYPN-----------EISGGQKQRTSAARAF 158
Cdd:PRK11174 429 GQNPQLPHG-TLRDNVLL-------GNPDASdEQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARAL 500
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1112987593 159 IHEPSIIFADEPTGALDSKSASDLLNKLSQLnqKRRATIVMVTH--DPVAAsfCSRVVFIKDGQI-----YTQLNK 227
Cdd:PRK11174 501 LQPCQLLLLDEPTASLDAHSEQLVMQALNAA--SRRQTTLMVTHqlEDLAQ--WDQIWVMQDGQIvqqgdYAELSQ 572
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
4-224 |
1.18e-21 |
|
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: 93.65 E-value: 1.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGNKHNkheVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLaefr 83
Cdd:TIGR01193 474 IVINDVSYSYGYGSN---ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTL---- 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 84 KQHLGFIFQEYNLLDTlTVKENILLPlsitkiSKKEAGQkfEEVAKELGIFELKDKYPN--------------EISGGQK 149
Cdd:TIGR01193 547 RQFINYLPQEPYIFSG-SILENLLLG------AKENVSQ--DEIWAACEIAEIKDDIENmplgyqtelseegsSISGGQK 617
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1112987593 150 QRTSAARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKrraTIVMVTHDPVAASFCSRVVFIKDGQIYTQ 224
Cdd:TIGR01193 618 QRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQSDKIIVLDHGKIIEQ 689
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
12-224 |
1.23e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 93.35 E-value: 1.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 12 SYGNKHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLaefrKQHLGFIF 91
Cdd:PRK11160 345 SFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAL----RQAISVVS 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 92 QEYNLLDTlTVKENILLplsitkiSKKEAG-QKFEEVAKELGIFELKDKYP----------NEISGGQKQRTSAARAFIH 160
Cdd:PRK11160 421 QRVHLFSA-TLRDNLLL-------AAPNASdEALIEVLQQVGLEKLLEDDKglnawlgeggRQLSGGEQRRLGIARALLH 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1112987593 161 EPSIIFADEPTGALDSKSASDLLNKLSQLNQKRraTIVMVTHDPVAASFCSRVVFIKDGQIYTQ 224
Cdd:PRK11160 493 DAPLLLLDEPTEGLDAETERQILELLAEHAQNK--TVLMITHRLTGLEQFDRICVMDNGQIIEQ 554
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
23-203 |
1.67e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 90.66 E-value: 1.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 23 LKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMT-NMKEKQLAEFRKQ-HLGFIFQEYNLLDTL 100
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpETGNKNLKKLRKKvSLVFQFPEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 101 TVKENILLPLSItKISKKEAGQKFEEVAKELGIFE-LKDKYPNEISGGQKQRTSAARAFIHEPSIIFADEPTGALDSKSA 179
Cdd:PRK13641 103 VLKDVEFGPKNF-GFSEDEAKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGR 181
|
170 180
....*....|....*....|....
gi 1112987593 180 SDLLnKLSQLNQKRRATIVMVTHD 203
Cdd:PRK13641 182 KEMM-QLFKDYQKAGHTVILVTHN 204
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
21-224 |
1.74e-21 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 89.47 E-value: 1.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 21 EVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMkekQLAEFRKQhLGFIFQEyNLLDTL 100
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALA---DPAWLRRQ-VGVVLQE-NVLFNR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 101 TVKENILLP---LSITKIskkeagqkfEEVAKELG----IFELKDKYPN-------EISGGQKQRTSAARAFIHEPSIIF 166
Cdd:cd03252 91 SIRDNIALAdpgMSMERV---------IEAAKLAGahdfISELPEGYDTivgeqgaGLSGGQRQRIAIARALIHNPRILI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1112987593 167 ADEPTGALDSKSASDLLNKLSQLNQKRraTIVMVTHDPVAASFCSRVVFIKDGQIYTQ 224
Cdd:cd03252 162 FDEATSALDYESEHAIMRNMHDICAGR--TVIIIAHRLSTVKNADRIIVMEKGRIVEQ 217
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
3-203 |
2.72e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 90.79 E-value: 2.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSY------GNKHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININ-QAEMTNMK 75
Cdd:PRK11308 5 LLQAIDLKKHYpvkrglFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQgQDLLKADP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 76 EKQLAefRKQHLGFIFQE-YNLLDTLTVKENILL-PLSI-TKISKKEAGQKFEEVAKELGIF-ELKDKYPNEISGGQKQR 151
Cdd:PRK11308 85 EAQKL--LRQKIQIVFQNpYGSLNPRKKVGQILEePLLInTSLSAAERREKALAMMAKVGLRpEHYDRYPHMFSGGQRQR 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1112987593 152 TSAARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHD 203
Cdd:PRK11308 163 IAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHD 214
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-203 |
3.07e-21 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 88.62 E-value: 3.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 2 MILEAKKIrksyGNKHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQlae 81
Cdd:PRK10247 6 PLLQLQNV----GYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEI--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 82 FRKQhLGFIFQEYNLLDTlTVKENILLPLSITKISKKEagQKFeevAKELGIFELKD----KYPNEISGGQKQRTSAARA 157
Cdd:PRK10247 79 YRQQ-VSYCAQTPTLFGD-TVYDNLIFPWQIRNQQPDP--AIF---LDDLERFALPDtiltKNIAELSGGEKQRISLIRN 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1112987593 158 FIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHD 203
Cdd:PRK10247 152 LQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
23-203 |
3.38e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 90.07 E-value: 3.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 23 LKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSS-IDQVSGGTININQAEMTNMKE-KQLAEFRKQhLGFIFQ--EYNLLD 98
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGlIISETGQTIVGDYAIPANLKKiKEVKRLRKE-IGLVFQfpEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 99 TLTVKENILLPLSITKiSKKEAGQKFEEVakeLGIFELKDKY----PNEISGGQKQRTSAARAFIHEPSIIFADEPTGAL 174
Cdd:PRK13645 106 ETIEKDIAFGPVNLGE-NKQEAYKKVPEL---LKLVQLPEDYvkrsPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGL 181
|
170 180
....*....|....*....|....*....
gi 1112987593 175 DSKSASDLLNKLSQLNQKRRATIVMVTHD 203
Cdd:PRK13645 182 DPKGEEDFINLFERLNKEYKKRIIMVTHN 210
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-238 |
6.10e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 89.07 E-value: 6.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 19 KHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTN-MKEKQLAEFRKQhLGFIFQ--EYN 95
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHkTKDKYIRPVRKR-IGMVFQfpESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 96 LLDTLTVKENILLPLSItKISKKEAGQKFEEVAKELGI-FELKDKYPNEISGGQKQRTSAARAFIHEPSIIFADEPTGAL 174
Cdd:PRK13646 98 LFEDTVEREIIFGPKNF-KMNLDEVKNYAHRLLMDLGFsRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1112987593 175 DSKSASDLLNKLSQLNQKRRATIVMVTHD-PVAASFCSRVVFIKDGQIYTQLNKggqdRQMFFQD 238
Cdd:PRK13646 177 DPQSKRQVMRLLKSLQTDENKTIILVSHDmNEVARYADEVIVMKEGSIVSQTSP----KELFKDK 237
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-221 |
1.19e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 89.03 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 1 MMILEAKKIRKSYGNKHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKT-TLLNVLSSID---QVSGGTININQAEMTNMKE 76
Cdd:PRK11022 1 MALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDypgRVMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 77 KQLAEFRKQHLGFIFQE--YNLLDTLTVKENILLPLSITKI-SKKEAGQKFEEVAKELGIFELK---DKYPNEISGGQKQ 150
Cdd:PRK11022 81 KERRNLVGAEVAMIFQDpmTSLNPCYTVGFQIMEAIKVHQGgNKKTRRQRAIDLLNQVGIPDPAsrlDVYPHQLSGGMSQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1112987593 151 RTSAARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHD-PVAASFCSRVVFIKDGQI 221
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDlALVAEAAHKIIVMYAGQV 232
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-221 |
2.12e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 87.86 E-value: 2.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSYGNKHnkheVLKGIDLQIQKGEFVSIMGPSGSGKTTL----LNVLSSidqvSGGTININQAEMTnmkekq 78
Cdd:COG4152 1 MLELKGLTKRFGDKT----AVDDVSFTVPKGEIFGLLGPNGAGKTTTiriiLGILAP----DSGEVLWDGEPLD------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 79 lAEFRkQHLGFIFQEYNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAF 158
Cdd:COG4152 67 -PEDR-RRIGYLPEERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAAL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1112987593 159 IHEPSIIFADEPTGALDSKSASDLLNKLsqLNQKRR-ATIVMVTHD-PVAASFCSRVVFIKDGQI 221
Cdd:COG4152 145 LHDPELLILDEPFSGLDPVNVELLKDVI--RELAAKgTTVIFSSHQmELVEELCDRIVIINKGRK 207
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
26-202 |
2.56e-20 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 88.39 E-value: 2.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 26 IDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAEFRKQHLGFIFQEYNLLDTLTVKEN 105
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLPPEKRRIGYVFQDARLFPHYKVRGN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 106 ILLplsitKISKKEAGQkFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPSIIFADEPTGALDSKSASDLLNK 185
Cdd:PRK11144 97 LRY-----GMAKSMVAQ-FDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPY 170
|
170
....*....|....*..
gi 1112987593 186 LSQLNQKRRATIVMVTH 202
Cdd:PRK11144 171 LERLAREINIPILYVSH 187
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-223 |
2.59e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.35 E-value: 2.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 6 AKKIRKSYGNKhnkhEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININqaemtnmkekqlaefRKQ 85
Cdd:COG0488 1 LENLSKSFGGR----PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP---------------KGL 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 86 HLGFIFQEYNLLDTLTVKENIL--------LPLSITKISKK------------EAGQKFEE------------VAKELGI 133
Cdd:COG0488 62 RIGYLPQEPPLDDDLTVLDTVLdgdaelraLEAELEELEAKlaepdedlerlaELQEEFEAlggweaearaeeILSGLGF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 134 FELK-DKYPNEISGGQKQRTSAARAFIHEPSIIFADEPTGALDSKSasdlLNKLSQLNQKRRATIVMVTHDpvaASF--- 209
Cdd:COG0488 142 PEEDlDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES----IEWLEEFLKNYPGTVLVVSHD---RYFldr 214
|
250
....*....|....*
gi 1112987593 210 -CSRVVFIKDGQIYT 223
Cdd:COG0488 215 vATRILELDRGKLTL 229
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-221 |
2.63e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 89.34 E-value: 2.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSYGNKhnkhEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQlaef 82
Cdd:PRK15439 11 LLCARSISKQYSGV----EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAK---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 83 rKQHLG--FIFQEYNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAKEL------GIFELKDKYPNEIsggqkqrtsa 154
Cdd:PRK15439 83 -AHQLGiyLVPQEPLLFPNLSVKENILFGLPKRQASMQKMKQLLAALGCQLdldssaGSLEVADRQIVEI---------- 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1112987593 155 ARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLnQKRRATIVMVTHD-PVAASFCSRVVFIKDGQI 221
Cdd:PRK15439 152 LRGLMRDSRILILDEPTASLTPAETERLFSRIREL-LAQGVGIVFISHKlPEIRQLADRISVMRDGTI 218
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
3-203 |
3.06e-20 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 86.74 E-value: 3.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSYGNKhnkhEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAEF 82
Cdd:PRK11831 7 LVDMRGVSFTRGNR----CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 83 RKQhLGFIFQEYNLLDTLTVKENILLPLsitkiskKEAGQKFEEVAKELGIFELK--------DKYPNEISGGQKQRTSA 154
Cdd:PRK11831 83 RKR-MSMLFQSGALFTDMNVFDNVAYPL-------REHTQLPAPLLHSTVMMKLEavglrgaaKLMPSELSGGMARRAAL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1112987593 155 ARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHD 203
Cdd:PRK11831 155 ARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHD 203
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
12-246 |
3.77e-20 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 89.40 E-value: 3.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 12 SYGNKHNKhEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLaefrKQHLGFIF 91
Cdd:TIGR00958 487 SYPNRPDV-PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYL----HRQVALVG 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 92 QEyNLLDTLTVKENILLPLSITKISKKEAgqkfeeVAKELG----IFELKDKYPNEI-------SGGQKQRTSAARAFIH 160
Cdd:TIGR00958 562 QE-PVLFSGSVRENIAYGLTDTPDEEIMA------AAKAANahdfIMEFPNGYDTEVgekgsqlSGGQKQRIAIARALVR 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 161 EPSIIFADEPTGALDSKSASdllnKLSQLNQKRRATIVMVTHDPVAASFCSRVVFIKDGQIYTQLNkggqdrqmfFQDIM 240
Cdd:TIGR00958 635 KPRVLILDEATSALDAECEQ----LLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGT---------HKQLM 701
|
....*.
gi 1112987593 241 KTQGVL 246
Cdd:TIGR00958 702 EDQGCY 707
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
22-218 |
9.14e-20 |
|
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: 83.36 E-value: 9.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 22 VLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEmtnmkekqlaefrkqHLGFIFQE-YnlLDTL 100
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE---------------DLLFLPQRpY--LPLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 101 TVKENILLPLSitkiskkeagqkfeevaKELgifelkdkypneiSGGQKQRTSAARAFIHEPSIIFADEPTGALDSKSAS 180
Cdd:cd03223 79 TLREQLIYPWD-----------------DVL-------------SGGEQQRLAFARLLLHKPKFVFLDEATSALDEESED 128
|
170 180 190
....*....|....*....|....*....|....*...
gi 1112987593 181 DLLNKLsqlnQKRRATIVMVTHDPVAASFCSRVVFIKD 218
Cdd:cd03223 129 RLYQLL----KELGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
33-221 |
1.90e-19 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 87.22 E-value: 1.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 33 GEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAEFRKQhLGFIFQE-YNLLDT-LTVKENILLPL 110
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRD-IQFIFQDpYASLDPrQTVGDSIMEPL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 111 SITKISKKEAGQK-FEEVAKELGIF-ELKDKYPNEISGGQKQRTSAARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQ 188
Cdd:PRK10261 429 RVHGLLPGKAAAArVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLD 508
|
170 180 190
....*....|....*....|....*....|....
gi 1112987593 189 LNQKRRATIVMVTHD-PVAASFCSRVVFIKDGQI 221
Cdd:PRK10261 509 LQRDFGIAYLFISHDmAVVERISHRVAVMYLGQI 542
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
20-221 |
2.41e-19 |
|
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: 83.67 E-value: 2.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 20 HEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAEfrkqHLGFIFQEYNLLdT 99
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHS----KVSLVGQEPVLF-A 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 100 LTVKENILLPL-SITKISKKEAGQKFEE----VAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPSIIFADEPTGAL 174
Cdd:cd03248 102 RSLQDNIAYGLqSCSFECVKEAAQKAHAhsfiSELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSAL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1112987593 175 DSKSASDLLNKLSQLNQKRraTIVMVTHDPVAASFCSRVVFIKDGQI 221
Cdd:cd03248 182 DAESEQQVQQALYDWPERR--TVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-243 |
2.95e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 84.47 E-value: 2.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 1 MMILEAKKIRKSY-GNKHnkheVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTnmkEKQL 79
Cdd:PRK13652 1 MHLIETRDLCYSYsGSKE----ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPIT---KENI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 80 AEFRKqHLGFIFQeyNLLDTL---TVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAAR 156
Cdd:PRK13652 74 REVRK-FVGLVFQ--NPDDQIfspTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 157 AFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHD-PVAASFCSRVVFIKDGQIYTQlnkgGQDRQMF 235
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQlDLVPEMADYIYVMDKGRIVAY----GTVEEIF 226
|
....*...
gi 1112987593 236 FQDIMKTQ 243
Cdd:PRK13652 227 LQPDLLAR 234
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
22-221 |
3.37e-19 |
|
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: 82.09 E-value: 3.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 22 VLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNmkeKQLAEFRKQHLGFI---FQEYNLLD 98
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTR---RSPRDAIRAGIAYVpedRKREGLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 99 TLTVKENILLPLSitkiskkeagqkfeevakelgifelkdkypneISGGQKQRTSAARAFIHEPSIIFADEPTGALDSKS 178
Cdd:cd03215 92 DLSVAENIALSSL--------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1112987593 179 ASDLLNKLSQLNQKRRAtIVMVTHD-PVAASFCSRVVFIKDGQI 221
Cdd:cd03215 140 KAEIYRLIRELADAGKA-VLLISSElDELLGLCDRILVMYEGRI 182
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
23-220 |
1.24e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 84.91 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 23 LKGIDLQIQKGEFVSIMGPSGSGKT-TLLNVLSSIDQvSGGTININQA----------EMTNMKEKQLAEFRKQHLGFIF 91
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-AGGLVQCDKMllrrrsrqviELSEQSAAQMRHVRGADMAMIF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 92 QE--YNLLDTLTVKENILLPLSITK-ISKKEAGQKFEEVAKELGIFELK---DKYPNEISGGQKQRTSAARAFIHEPSII 165
Cdd:PRK10261 111 QEpmTSLNPVFTVGEQIAESIRLHQgASREEAMVEAKRMLDQVRIPEAQtilSRYPHQLSGGMRQRVMIAMALSCRPAVL 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1112987593 166 FADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHD-PVAASFCSRVVFIKDGQ 220
Cdd:PRK10261 191 IADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDmGVVAEIADRVLVMYQGE 246
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
25-203 |
1.57e-18 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 81.96 E-value: 1.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 25 GIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAefRKqhlGFI--FQEYNLLDTLTV 102
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA--RM---GVVrtFQHVRLFREMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 103 KENILLP------------LSITKISKKEAGQKFEEVA---KELGIFELKDKYPNEISGGQKQRTSAARAFIHEPSIIFA 167
Cdd:PRK11300 98 IENLLVAqhqqlktglfsgLLKTPAFRRAESEALDRAAtwlERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILML 177
|
170 180 190
....*....|....*....|....*....|....*.
gi 1112987593 168 DEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHD 203
Cdd:PRK11300 178 DEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHD 213
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-220 |
2.44e-18 |
|
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: 83.72 E-value: 2.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSYGNKhnkhEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSG--GTININQAEmtnMKEKQLA 80
Cdd:TIGR02633 1 LLEMKGIVKTFGGV----KALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSP---LKASNIR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 81 EFRKQHLGFIFQEYNLLDTLTVKENILLPLSIT----KISKKEAGQKFEEVAKELGIFELKDKYP-NEISGGQKQRTSAA 155
Cdd:TIGR02633 74 DTERAGIVIIHQELTLVPELSVAENIFLGNEITlpggRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1112987593 156 RAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIvMVTH--DPVAAsFCSRVVFIKDGQ 220
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACV-YISHklNEVKA-VCDTICVIRDGQ 218
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-235 |
4.92e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 80.91 E-value: 4.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 22 VLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSI-DQVSG----GTININQAEMTNMKEkqLAEFRKQhLGFIFQEYNL 96
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMnDKVSGyrysGDVLLGGRSIFNYRD--VLEFRRR-VGMLFQRPNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 97 LdTLTVKENILLPLSITKISKKeagQKFEEVAK----ELGIFE-LKDKY---PNEISGGQKQRTSAARAFIHEPSIIFAD 168
Cdd:PRK14271 113 F-PMSIMDNVLAGVRAHKLVPR---KEFRGVAQarltEVGLWDaVKDRLsdsPFRLSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1112987593 169 EPTGALDSKSASDLLNKLSQLNQkrRATIVMVTHD-PVAASFCSRVVFIKDGQIYTQlnkgGQDRQMF 235
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLAD--RLTVIIVTHNlAQAARISDRAALFFDGRLVEE----GPTEQLF 250
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-219 |
6.09e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 81.80 E-value: 6.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 1 MMILEAKKIRKSYGNKhnkhEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTnmKEKQLA 80
Cdd:PRK13536 39 TVAIDLAGVSKSYGDK----AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP--ARARLA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 81 EFRkqhLGFIFQEYNLLDTLTVKENILLPLSITKISKKEagqkFEEVAKELGIF---ELK-DKYPNEISGGQKQRTSAAR 156
Cdd:PRK13536 113 RAR---IGVVPQFDNLDLEFTVRENLLVFGRYFGMSTRE----IEAVIPSLLEFarlESKaDARVSDLSGGMKRRLTLAR 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1112987593 157 AFIHEPSIIFADEPTGALDSKSASDLLNKLSQLnQKRRATIVMVTH-DPVAASFCSRVVFIKDG 219
Cdd:PRK13536 186 ALINDPQLLILDEPTTGLDPHARHLIWERLRSL-LARGKTILLTTHfMEEAERLCDRLCVLEAG 248
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
23-220 |
6.73e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 82.27 E-value: 6.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 23 LKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEM--TNMKEKQLAefrkqHLGFIFQEYNLLDTL 100
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfASTTAALAA-----GVAIIYQELHLVPEM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 101 TVKENILL---PLSITKISKKEAGQKFEEVAKELGIfelkDKYPN----EISGGQKQRTSAARAFIHEPSIIFADEPTGA 173
Cdd:PRK11288 95 TVAENLYLgqlPHKGGIVNRRLLNYEAREQLEHLGV----DIDPDtplkYLSIGQRQMVEIAKALARNARVIAFDEPTSS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1112987593 174 LDSKSASDLLNKLSQLNQKRRAtIVMVTH--DPVAAsFCSRVVFIKDGQ 220
Cdd:PRK11288 171 LSAREIEQLFRVIRELRAEGRV-ILYVSHrmEEIFA-LCDAITVFKDGR 217
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
2-201 |
1.00e-17 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 79.83 E-value: 1.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 2 MILEAKKIRKSY----GNKHNKH-EVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKE 76
Cdd:PRK15112 3 TLLEVRNLSKTFryrtGWFRRQTvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 77 KqlaeFRKQHLGFIFQE-YNLLDTLTVKENIL-LPLSI-TKISKKEAGQKFEEVAKELGIfeLKDK---YPNEISGGQKQ 150
Cdd:PRK15112 83 S----YRSQRIRMIFQDpSTSLNPRQRISQILdFPLRLnTDLEPEQREKQIIETLRQVGL--LPDHasyYPHMLAPGQKQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1112987593 151 RTSAARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVT 201
Cdd:PRK15112 157 RLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVT 207
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-202 |
1.01e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 80.66 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSYGNKH-NKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTINI----------NQAEM 71
Cdd:PRK13631 21 ILRVKNLYCVFDEKQeNELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 72 TNMKEKQLAEFRK--QHLGFIFQ--EYNLLDTlTVKENILLPLSITKISKKEAGQKfeeVAKELGIFELKDKY----PNE 143
Cdd:PRK13631 101 TNPYSKKIKNFKElrRRVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKL---AKFYLNKMGLDDSYlersPFG 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1112987593 144 ISGGQKQRTSAARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRaTIVMVTH 202
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNK-TVFVITH 234
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1-222 |
1.17e-17 |
|
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: 78.46 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 1 MMILEAKKIRKSYGNKHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSG---GTININqaemtNMKEK 77
Cdd:cd03233 1 ASTLSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYN-----GIPYK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 78 QLAEFRKQHLGFIFQEYNLLDTLTVKENIllplsitkiskkeagqKFeeVAKELGifelkDKYPNEISGGQKQRTSAARA 157
Cdd:cd03233 76 EFAEKYPGEIIYVSEEDVHFPTLTVRETL----------------DF--ALRCKG-----NEFVRGISGGERKRVSIAEA 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1112987593 158 FIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDP---VAASFcSRVVFIKDG-QIY 222
Cdd:cd03233 133 LVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQAsdeIYDLF-DKVLVLYEGrQIY 200
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
21-205 |
1.67e-17 |
|
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: 78.17 E-value: 1.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 21 EVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTnmkekQLAEFRKQHLGFIFQEYNLLDTL 100
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLA-----EQRDEPHENILYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 101 TVKENILLPLSITKISKKEAGQKFEEVakelGIFELKDKYPNEISGGQKQRTSAARAFIHEPSIIFADEPTGALDsKSAS 180
Cdd:TIGR01189 89 SALENLHFWAAIHGGAQRTIEDALAAV----GLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD-KAGV 163
|
170 180
....*....|....*....|....*
gi 1112987593 181 DLLNKLSQLNQKRRATIVMVTHDPV 205
Cdd:TIGR01189 164 ALLAGLLRAHLARGGIVLLTTHQDL 188
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
21-221 |
3.12e-17 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 78.19 E-value: 3.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 21 EVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSID--QVSGGTININQAEMTNMKekqlAEFR-KQHLGFIFQE---- 93
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELS----PDERaRAGIFLAFQYpvei 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 94 -----YNLLdtLTVKENILLPlsitKISKKEAGQKFEEVAKELGIFE-LKDKYPNE-ISGGQKQRTSAARAFIHEPSIIF 166
Cdd:COG0396 90 pgvsvSNFL--RTALNARRGE----ELSAREFLKLLKEKMKELGLDEdFLDRYVNEgFSGGEKKRNEILQMLLLEPKLAI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 167 ADEPTGALDSKSASDLLNKLSQLNQKRRATIVmVTH-----DPVAASFcsrVVFIKDGQI 221
Cdd:COG0396 164 LDETDSGLDIDALRIVAEGVNKLRSPDRGILI-ITHyqrilDYIKPDF---VHVLVDGRI 219
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
23-221 |
3.57e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 78.49 E-value: 3.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 23 LKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKekQLAEFRKQhLGFIFQ--EYNLLDTl 100
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFS--KLQGIRKL-VGIVFQnpETQFVGR- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 101 TVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPSIIFADEPTGALDSKSAS 180
Cdd:PRK13644 94 TVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1112987593 181 DLLNKLSQLNQKRRaTIVMVTHDPVAASFCSRVVFIKDGQI 221
Cdd:PRK13644 174 AVLERIKKLHEKGK-TIVYITHNLEELHDADRIIVMDRGKI 213
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
26-222 |
5.66e-17 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 80.06 E-value: 5.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 26 IDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMtnmkEKQLAEFRkQHLGFIFQEYNLLDTLTVKEN 105
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNLDAVR-QSLGMCPQHNILFHHLTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 106 ILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPSIIFADEPTGALDSKSASDLLNK 185
Cdd:TIGR01257 1024 ILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDL 1103
|
170 180 190
....*....|....*....|....*....|....*...
gi 1112987593 186 LSQLNQKRraTIVMVTHDPVAASFC-SRVVFIKDGQIY 222
Cdd:TIGR01257 1104 LLKYRSGR--TIIMSTHHMDEADLLgDRIAIISQGRLY 1139
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
18-246 |
9.92e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 79.23 E-value: 9.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 18 NKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLaefrKQHLGFIFQEYNLL 97
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASL----RRNIAVVFQDAGLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 98 DTlTVKENI------------LLPLSITK----ISKKEAGqkFEEVAKELGifelkdkypNEISGGQKQRTSAARAFIHE 161
Cdd:PRK13657 422 NR-SIEDNIrvgrpdatdeemRAAAERAQahdfIERKPDG--YDTVVGERG---------RQLSGGERQRLAIARALLKD 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 162 PSIIFADEPTGALDSKSASDLLNKLSQLNQKRraTIVMVTHDPVAASFCSRVVFIKDGQI-----YTQL-NKGGQdrqmf 235
Cdd:PRK13657 490 PPILILDEATSALDVETEAKVKAALDELMKGR--TTFIIAHRLSTVRNADRILVFDNGRVvesgsFDELvARGGR----- 562
|
250
....*....|.
gi 1112987593 236 FQDIMKTQGVL 246
Cdd:PRK13657 563 FAALLRAQGML 573
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
17-235 |
1.07e-16 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 78.99 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 17 HNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMkekQLAEFRKQ-----HLGFIF 91
Cdd:PRK10789 325 QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---QLDSWRSRlavvsQTPFLF 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 92 QEynlldtlTVKENILLplsitkiSKKEAGQ-KFEEVAK----ELGIFELKDKYPNEI-------SGGQKQRTSAARAFI 159
Cdd:PRK10789 402 SD-------TVANNIAL-------GRPDATQqEIEHVARlasvHDDILRLPQGYDTEVgergvmlSGGQKQRISIARALL 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 160 HEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRraTIVMVTHDPVAASFCSRVVFIKDGQIYTQ------LNKGGQDRQ 233
Cdd:PRK10789 468 LNAEILILDDALSAVDGRTEHQILHNLRQWGEGR--TVIISAHRLSALTEASEILVMQHGHIAQRgnhdqlAQQSGWYRD 545
|
..
gi 1112987593 234 MF 235
Cdd:PRK10789 546 MY 547
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-220 |
1.22e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 78.82 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 1 MM--ILEAKKIRKSYGNKhnkhEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVS--GGTININQAEmtnMKE 76
Cdd:PRK13549 1 MMeyLLEMKNITKTFGGV----KALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEE---LQA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 77 KQLAEFRKQHLGFIFQEYNLLDTLTVKENILLPLSITK---ISKKEAGQKFEEVAKELGIfelkDKYPN----EISGGQK 149
Cdd:PRK13549 74 SNIRDTERAGIAIIHQELALVKELSVLENIFLGNEITPggiMDYDAMYLRAQKLLAQLKL----DINPAtpvgNLGLGQQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1112987593 150 QRTSAARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLnQKRRATIVMVTH--DPVAAsFCSRVVFIKDGQ 220
Cdd:PRK13549 150 QLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDL-KAHGIACIYISHklNEVKA-ISDTICVIRDGR 220
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-221 |
1.43e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 78.34 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 1 MMILEAKKIRKSYGNKhnkhEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLA 80
Cdd:PRK09536 1 MPMIDVSDLSVEFGDT----TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 81 efrkQHLGFIFQEYNLLDTLTVKENILL---PLSITKISKKEAGQKFEEVAKE-LGIFELKDKYPNEISGGQKQRTSAAR 156
Cdd:PRK09536 77 ----RRVASVPQDTSLSFEFDVRQVVEMgrtPHRSRFDTWTETDRAAVERAMErTGVAQFADRPVTSLSGGERQRVLLAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1112987593 157 AFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRaTIVMVTHD-PVAASFCSRVVFIKDGQI 221
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGK-TAVAAIHDlDLAARYCDELVLLADGRV 217
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-220 |
1.74e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 78.12 E-value: 1.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSY-GNKhnkheVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMT--NMKEKQL 79
Cdd:PRK10762 4 LLQLKGIDKAFpGVK-----ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfnGPKSSQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 80 AefrkqHLGFIFQEYNLLDTLTVKENILLPLSIT----KISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAA 155
Cdd:PRK10762 79 A-----GIGIIHQELNLIPQLTIAENIFLGREFVnrfgRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1112987593 156 RAFIHEPSIIFADEPTGAL-DSKSASdLLNKLSQLNQKRRAtIVMVTHDpVAASF--CSRVVFIKDGQ 220
Cdd:PRK10762 154 KVLSFESKVIIMDEPTDALtDTETES-LFRVIRELKSQGRG-IVYISHR-LKEIFeiCDDVTVFRDGQ 218
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
20-224 |
2.03e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 78.21 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 20 HEVLKGIDLQIQKGEFVSIMGPSGSGKT-TLLNVL----SSIDQVSGGTININQAEMTNMKEKQLAEFRKQHLGFIFQE- 93
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSvTALSILrllpSPPVVYPSGDIRFHGESLLHASEQTLRGVRGNKIAMIFQEp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 94 ---YNLLDTLtvKENILLPLSITKISKKEAG-----QKFEEVAKELGIFELKDkYPNEISGGQKQRTSAARAFIHEPSII 165
Cdd:PRK15134 102 mvsLNPLHTL--EKQLYEVLSLHRGMRREAArgeilNCLDRVGIRQAAKRLTD-YPHQLSGGERQRVMIAMALLTRPELL 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 166 FADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHD-PVAASFCSRVVFIKDGQIYTQ 224
Cdd:PRK15134 179 IADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNlSIVRKLADRVAVMQNGRCVEQ 238
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-203 |
2.21e-16 |
|
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: 78.05 E-value: 2.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSYGNKHnkhEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGtininqaemtnmkEKQLAEF 82
Cdd:TIGR03719 4 IYTMNRVSKVVPPKK---EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG-------------EARPQPG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 83 RKqhLGFIFQEYNLLDTLTVKENILLPLSITK--------ISKK--EAGQKFEEVAKELGifELKDKY------------ 140
Cdd:TIGR03719 68 IK--VGYLPQEPQLDPTKTVRENVEEGVAEIKdaldrfneISAKyaEPDADFDKLAAEQA--ELQEIIdaadawdldsql 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1112987593 141 ---------P------NEISGGQKQRTSAARAFIHEPSIIFADEPTGALDSKSASDLLNKLsqlnQKRRATIVMVTHD 203
Cdd:TIGR03719 144 eiamdalrcPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL----QEYPGTVVAVTHD 217
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
4-241 |
2.62e-16 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 75.13 E-value: 2.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGNKHnkheVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTnmkEKQLaefr 83
Cdd:TIGR03740 1 LETKNLSKRFGKQT----AVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWT---RKDL---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 84 kQHLGFIFQEYNLLDTLTVKENILLPLSITKISKkeagQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPS 163
Cdd:TIGR03740 70 -HKIGSLIESPPLYENLTARENLKVHTTLLGLPD----SRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 164 IIFADEPTGALDSKSASDlLNKLSQLNQKRRATIVMVTHD----PVAASFcsrVVFIKDGQI-YTQLNKGGQDRQMFFQD 238
Cdd:TIGR03740 145 LLILDEPTNGLDPIGIQE-LRELIRSFPEQGITVILSSHIlsevQQLADH---IGIISEGVLgYQGKINKSENLEKLFVE 220
|
...
gi 1112987593 239 IMK 241
Cdd:TIGR03740 221 VVK 223
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-203 |
2.71e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 75.84 E-value: 2.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 11 KSYGNKHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEM--TNMKEKQ--LAEFRKQh 86
Cdd:PRK14258 11 NNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFfnQNIYERRvnLNRLRRQ- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 87 LGFIFQEYNLLdTLTVKENILLPLSITKISKK-EAGQKFEEVAKELGIF-ELKDKYPN---EISGGQKQRTSAARAFIHE 161
Cdd:PRK14258 90 VSMVHPKPNLF-PMSVYDNVAYGVKIVGWRPKlEIDDIVESALKDADLWdEIKHKIHKsalDLSGGQQQRLCIARALAVK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1112987593 162 PSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHD 203
Cdd:PRK14258 169 PKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHN 210
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-221 |
3.79e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 77.41 E-value: 3.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSYGNKhnkhEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININqaemTNMKekqlaef 82
Cdd:COG0488 315 VLELEGLSKSYGDK----TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG----ETVK------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 83 rkqhLGFIFQEYNLLD-TLTVKENIllplsitkiskKEAGQKFEE--VAKELGIF----ELKDKYPNEISGGQKQRTSAA 155
Cdd:COG0488 380 ----IGYFDQHQEELDpDKTVLDEL-----------RDGAPGGTEqeVRGYLGRFlfsgDDAFKPVGVLSGGEKARLALA 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1112987593 156 RAFIHEPSIIFADEPTGALD--SKSAsdLLNKLSQLNqkrrATIVMVTHDPvaaSF----CSRVVFIKDGQI 221
Cdd:COG0488 445 KLLLSPPNVLLLDEPTNHLDieTLEA--LEEALDDFP----GTVLLVSHDR---YFldrvATRILEFEDGGV 507
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-239 |
4.11e-16 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 77.46 E-value: 4.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 16 KHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSsiDQVSGGTININQaEMTNMKEKQlAEFRKQhLGFIFQEYN 95
Cdd:TIGR00956 772 KKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTGVITGGD-RLVNGRPLD-SSFQRS-IGYVQQQDL 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 96 LLDTLTVKENILLPLSI---TKISKKEAGQKFEEVAKELGIFELKDKYPNEISGG----QKQRTSAARAFIHEP-SIIFA 167
Cdd:TIGR00956 847 HLPTSTVRESLRFSAYLrqpKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGlnveQRKRLTIGVELVAKPkLLLFL 926
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1112987593 168 DEPTGALDSKSA---SDLLNKLSQLNQkrraTIVMVTHDPVAASFCS--RVVFikdgqiytqLNKGGQdrQMFFQDI 239
Cdd:TIGR00956 927 DEPTSGLDSQTAwsiCKLMRKLADHGQ----AILCTIHQPSAILFEEfdRLLL---------LQKGGQ--TVYFGDL 988
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
22-203 |
4.43e-16 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 76.10 E-value: 4.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 22 VLKGIDLQIQKGEFVSIMGPSGSGKT----TLLNVLSSIDQVSGGTININQAEMTNMKEKQLAEFRKQHLGFIFQEYN-L 96
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSliakAICGITKDNWHVTADRFRWNGIDLLKLSPRERRKIIGREIAMIFQEPSsC 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 97 LD-TLTVKENIllplsITKISKKEAGQKF-------EEVAKEL----GIFELKD---KYPNEISGGQKQRTSAARAFIHE 161
Cdd:COG4170 102 LDpSAKIGDQL-----IEAIPSWTFKGKWwqrfkwrKKRAIELlhrvGIKDHKDimnSYPHELTEGECQKVMIAMAIANQ 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1112987593 162 PSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHD 203
Cdd:COG4170 177 PRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHD 218
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
5-204 |
7.05e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 74.22 E-value: 7.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 5 EAKKIRKSYGNKHN--KHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLssidqvsggtininQAEMTNMKEKQLAEF 82
Cdd:COG2401 26 RVAIVLEAFGVELRvvERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLL--------------AGALKGTPVAGCVDV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 83 RKQHLGfifQEYNLLDTLTVKENILlplsitkiskkeagqkfeEVAKELGIFELKDKY-----PNEISGGQKQRTSAARA 157
Cdd:COG2401 92 PDNQFG---REASLIDAIGRKGDFK------------------DAVELLNAVGLSDAVlwlrrFKELSTGQKFRFRLALL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1112987593 158 FIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDP 204
Cdd:COG2401 151 LAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHY 197
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
22-221 |
1.14e-15 |
|
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: 73.30 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 22 VLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLaefrKQHLGFIFQEYNLLDTlT 101
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDL----RSRISIIPQDPVLFSG-T 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 102 VKENiLLPLSitKISKKEAGQKFEEVA-KELgIFELKDKYPNEI-------SGGQKQRTSAARAFIHEPSIIFADEPTGA 173
Cdd:cd03244 94 IRSN-LDPFG--EYSDEELWQALERVGlKEF-VESLPGGLDTVVeeggenlSVGQRQLLCLARALLRKSKILVLDEATAS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1112987593 174 LDSKSASdLLNKLSQLNQKRRaTIVMVTH--DPVAAsfCSRVVFIKDGQI 221
Cdd:cd03244 170 VDPETDA-LIQKTIREAFKDC-TVLTIAHrlDTIID--SDRILVLDKGRV 215
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-208 |
1.41e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 74.05 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSYGNkhnkHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSI-DQVSG----GTININQAEMtNMKEK 77
Cdd:PRK14243 10 VLRTENLNVYYGS----FLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLnDLIPGfrveGKVTFHGKNL-YAPDV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 78 QLAEFRKQhLGFIFQEYNLLDTlTVKENILLPLSITKIsKKEAGQKFEEVAKELGIF-ELKDKYPNE---ISGGQKQRTS 153
Cdd:PRK14243 85 DPVEVRRR-IGMVFQKPNPFPK-SIYDNIAYGARINGY-KGDMDELVERSLRQAALWdEVKDKLKQSglsLSGGQQQRLC 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1112987593 154 AARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLnqKRRATIVMVTHDPVAAS 208
Cdd:PRK14243 162 IARAIAVQPEVILMDEPCSALDPISTLRIEELMHEL--KEQYTIIIVTHNMQQAA 214
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
16-219 |
1.80e-15 |
|
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: 72.28 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 16 KHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSS--IDQVSGGTININQAEMTnmkekqlAEFRKQhLGFIFQE 93
Cdd:cd03232 16 KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLD-------KNFQRS-TGYVEQQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 94 YNLLDTLTVKENILlplsitkiskkeagqkFEEVAKELGIfelkdkypneisgGQKQRTSAARAFIHEPSIIFADEPTGA 173
Cdd:cd03232 88 DVHSPNLTVREALR----------------FSALLRGLSV-------------EQRKRLTIGVELAAKPSILFLDEPTSG 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1112987593 174 LDSKSAS---DLLNKLSQLNQkrraTIVMVTHDPVAASFCS--RVVFIKDG 219
Cdd:cd03232 139 LDSQAAYnivRFLKKLADSGQ----AILCTIHQPSASIFEKfdRLLLLKRG 185
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
22-224 |
5.34e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 72.51 E-value: 5.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 22 VLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAefRKqhLGFIFQEYNLLDTLT 101
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFA--RK--VAYLPQQLPAAEGMT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 102 VKEnillplsITKISK-----------KEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPSIIFADEP 170
Cdd:PRK10575 102 VRE-------LVAIGRypwhgalgrfgAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEP 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1112987593 171 TGALDSKSASDLLNKLSQLNQKRRATIVMVTHD-PVAASFCSRVVFIKDGQIYTQ 224
Cdd:PRK10575 175 TSALDIAHQVDVLALVHRLSQERGLTVIAVLHDiNMAARYCDYLVALRGGEMIAQ 229
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-200 |
2.36e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 70.29 E-value: 2.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 1 MMILEAKKIRKSYGnkhnKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMkekQLA 80
Cdd:PRK11614 3 KVMLSFDKVSAHYG----KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDW---QTA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 81 EFRKQHLGFIFQEYNLLDTLTVKENilLPLSITKISKKEAGQKFEEVAKELG-IFELKDKYPNEISGGQKQRTSAARAFI 159
Cdd:PRK11614 76 KIMREAVAIVPEGRRVFSRMTVEEN--LAMGGFFAERDQFQERIKWVYELFPrLHERRIQRAGTMSGGEQQMLAIGRALM 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1112987593 160 HEPSIIFADEPTGALDSKSASDLLNKLSQLNQKrRATIVMV 200
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLV 193
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
7-203 |
3.92e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 69.76 E-value: 3.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 7 KKIRKSYGNKhnkhEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTINinqaemtnmKEKQLaefrkqH 86
Cdd:PRK09544 8 ENVSVSFGQR----RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---------RNGKL------R 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 87 LGFIFQEYNLLDTLtvkenillPLSITKISKKEAGQKFEEVA---KELGIFELKDKYPNEISGGQKQRTSAARAFIHEPS 163
Cdd:PRK09544 69 IGYVPQKLYLDTTL--------PLTVNRFLRLRPGTKKEDILpalKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQ 140
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1112987593 164 IIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHD 203
Cdd:PRK09544 141 LLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHD 180
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
20-198 |
5.53e-14 |
|
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: 71.00 E-value: 5.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 20 HEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQaemTNMKEKQLAEFRkQHLGFIFQeynllDT 99
Cdd:COG5265 371 RPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDG---QDIRDVTQASLR-AAIGIVPQ-----DT 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 100 L----TVKENILLplsitkiSKKEAGQ-KFEEVAK--ELGIF--ELKDKYPNEI-------SGGQKQRTSAARAFIHEPS 163
Cdd:COG5265 442 VlfndTIAYNIAY-------GRPDASEeEVEAAARaaQIHDFieSLPDGYDTRVgerglklSGGEKQRVAIARTLLKNPP 514
|
170 180 190
....*....|....*....|....*....|....*
gi 1112987593 164 IIFADEPTGALDSKSASDLLNKLSQLnQKRRATIV 198
Cdd:COG5265 515 ILIFDEATSALDSRTERAIQAALREV-ARGRTTLV 548
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
22-204 |
5.64e-14 |
|
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: 68.29 E-value: 5.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 22 VLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMtnmkeKQLAEFRKQHLGFIFQEYNLLDTLT 101
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL-----DFQRDSIARGLLYLGHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 102 VKENillplsITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPSIIFADEPTGALDSKSASD 181
Cdd:cd03231 90 VLEN------LRFWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
170 180
....*....|....*....|...
gi 1112987593 182 LLNKLSQLNQkRRATIVMVTHDP 204
Cdd:cd03231 164 FAEAMAGHCA-RGGMVVLTTHQD 185
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
18-217 |
7.50e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 69.14 E-value: 7.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 18 NKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAEFRKQHlgfifQEYNLL 97
Cdd:PRK15056 18 NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQS-----EEVDWS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 98 DTLTVKENILLP----LSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPSIIFADEPTGA 173
Cdd:PRK15056 93 FPVLVEDVVMMGryghMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1112987593 174 LDSKSASDLLNKLSQLNQKRRaTIVMVTHDPVAAS-FCSRVVFIK 217
Cdd:PRK15056 173 VDVKTEARIISLLRELRDEGK-TMLVSTHNLGSVTeFCDYTVMVK 216
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
21-202 |
1.55e-13 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 67.17 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 21 EVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLS--SIDQVSGGTI-----NINQAEMTnmkekqlaEFRKQHLGFIFQE 93
Cdd:cd03217 14 EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMghPKYEVTEGEIlfkgeDITDLPPE--------ERARLGIFLAFQY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 94 ynlldtltvkenillPLSITkiskkeaGQKFEEVAKELgifelkdkypNE-ISGGQKQRTSAARAFIHEPSIIFADEPTG 172
Cdd:cd03217 86 ---------------PPEIP-------GVKNADFLRYV----------NEgFSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190
....*....|....*....|....*....|
gi 1112987593 173 ALDSKSASDLLNKLSQLNQKRRATIVmVTH 202
Cdd:cd03217 134 GLDIDALRLVAEVINKLREEGKSVLI-ITH 162
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-203 |
1.83e-13 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 65.55 E-value: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGNKhnkhEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAemtnmkekqlaefr 83
Cdd:cd03221 1 IELENLSKTYGGK----LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST-------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 84 kqhlgfifqeynlldtltvkenillplsiTKISkkeagqkfeevakelgifelkdkYPNEISGGQKQRTSAARAFIHEPS 163
Cdd:cd03221 63 -----------------------------VKIG-----------------------YFEQLSGGEKMRLALAKLLLENPN 90
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1112987593 164 IIFADEPTGALDSKSASDLLNKLSQLNQkrraTIVMVTHD 203
Cdd:cd03221 91 LLLLDEPTNHLDLESIEALEEALKEYPG----TVILVSHD 126
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
23-219 |
1.85e-13 |
|
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: 67.36 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 23 LKGIDLQIQKGEFVSIMGPSGSGKTTLL-NVLSSIDQVSGGTININQAEMTNMKEKQLAEFRKQhLGFIFQEYNLLDTlT 101
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYS-VAYAAQKPWLLNA-T 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 102 VKENILLPLSITKiskkeagQKFEEVAKELGIFELKDKYPN-----------EISGGQKQRTSAARAFIHEPSIIFADEP 170
Cdd:cd03290 95 VEENITFGSPFNK-------QRYKAVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1112987593 171 TGALDSKSASDLLNK-LSQLNQKRRATIVMVTHDPVAASFCSRVVFIKDG 219
Cdd:cd03290 168 FSALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
24-221 |
1.89e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 67.80 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 24 KGIDLQIQKGEFVSIMGPSGSGKTtlLNVLSSIDQVSGGTININQAEMTNMKEKQLAEFRKQHLGFIFQE----YNLLDT 99
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTAGRVLLDGKPVAPCALRGRKIATIMQNprsaFNPLHT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 100 LT--VKENILlplsitKISKKEAGQKFEEVAKELGIFELK---DKYPNEISGGQKQRTSAARAFIHEPSIIFADEPTGAL 174
Cdd:PRK10418 98 MHthARETCL------ALGKPADDATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1112987593 175 DSKSASDLLNKLSQLNQKRRATIVMVTHD-PVAASFCSRVVFIKDGQI 221
Cdd:PRK10418 172 DVVAQARILDLLESIVQKRALGMLLVTHDmGVVARLADDVAVMSHGRI 219
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-252 |
1.90e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 69.62 E-value: 1.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 23 LKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSidqvsggtiNINQAEMTNMKEKQLAEFRKQhLGFIFQEynlldtlTV 102
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG---------ELSHAETSSVVIRGSVAYVPQ-VSWIFNA-------TV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 103 KENILLPlsiTKISKKEAGQKFEEVA--KELGIF------ELKDKYPNeISGGQKQRTSAARAFIHEPSIIFADEPTGAL 174
Cdd:PLN03232 696 RENILFG---SDFESERYWRAIDVTAlqHDLDLLpgrdltEIGERGVN-ISGGQKQRVSMARAVYSNSDIYIFDDPLSAL 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 175 DSKSASDLLNKLSQlNQKRRATIVMVTHDPVAASFCSRVVFIKDGQI-----YTQLNKGGQdrqmFFQDIMKTQGVLGGV 249
Cdd:PLN03232 772 DAHVAHQVFDSCMK-DELKGKTRVLVTNQLHFLPLMDRIILVSEGMIkeegtFAELSKSGS----LFKKLMENAGKMDAT 846
|
...
gi 1112987593 250 QHE 252
Cdd:PLN03232 847 QEV 849
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
21-221 |
1.93e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 69.28 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 21 EVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQ--------LAEFRKQHlGfifq 92
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairagiayVPEDRKGE-G---- 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 93 eynLLDTLTVKENILLPL--SITK---ISKKEAGQKFEEVAKELGIfelkdKYPN------EISGGQKQRTSAARAFIHE 161
Cdd:COG1129 341 ---LVLDLSIRENITLASldRLSRgglLDRRRERALAEEYIKRLRI-----KTPSpeqpvgNLSGGNQQKVVLAKWLATD 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1112987593 162 PSIIFADEPT-----GAldsKsaSDLLNKLSQLNQKRRAtIVMVTHD-PVAASFCSRVVFIKDGQI 221
Cdd:COG1129 413 PKVLILDEPTrgidvGA---K--AEIYRLIRELAAEGKA-VIVISSElPELLGLSDRILVMREGRI 472
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
23-198 |
2.14e-13 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 69.28 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 23 LKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQaemTNMKEKQLAEFRKQhLGFIFQEYNLLDTlTV 102
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDG---HDLRDYTLASLRNQ-VALVSQNVHLFND-TI 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 103 KENILLPlSITKISKKEagqkFEEVAKELGIFELKDKYPN-----------EISGGQKQRTSAARAFIHEPSIIFADEPT 171
Cdd:PRK11176 434 ANNIAYA-RTEQYSREQ----IEEAARMAYAMDFINKMDNgldtvigengvLLSGGQRQRIAIARALLRDSPILILDEAT 508
|
170 180
....*....|....*....|....*..
gi 1112987593 172 GALDSKSASDLLNKLSQLnQKRRATIV 198
Cdd:PRK11176 509 SALDTESERAIQAALDEL-QKNRTSLV 534
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
2-204 |
7.03e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 65.67 E-value: 7.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 2 MILEAKKIRKSYGNKhnkhEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQaemtnmKEKQLAE 81
Cdd:PRK13539 1 MMLEGEDLACVRGGR----VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG------GDIDDPD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 82 FRKQ-----HLGFifqeynLLDTLTVKENILL--------PLSItkiskkEAGQKFEEVAkelGIFELKDKYpneISGGQ 148
Cdd:PRK13539 71 VAEAchylgHRNA------MKPALTVAENLEFwaaflggeELDI------AAALEAVGLA---PLAHLPFGY---LSAGQ 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1112987593 149 KQRTSAARAFIHEPSIIFADEPTGALDSkSASDLLNKLSQLNQKRRATIVMVTHDP 204
Cdd:PRK13539 133 KRRVALARLLVSNRPIWILDEPTAALDA-AAVALFAELIRAHLAQGGIVIAATHIP 187
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
30-219 |
7.96e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 67.73 E-value: 7.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 30 IQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTINI-NQAEMTNMKEKQlaefrkQHLGFIFQEYNLLDTLTVKENILL 108
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVaGKSILTNISDVH------QNMGYCPQFDAIDDLLTGREHLYL 2035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 109 PLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQ 188
Cdd:TIGR01257 2036 YARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVS 2115
|
170 180 190
....*....|....*....|....*....|..
gi 1112987593 189 LNQKRRAtIVMVTHD-PVAASFCSRVVFIKDG 219
Cdd:TIGR01257 2116 IIREGRA-VVLTSHSmEECEALCTRLAIMVKG 2146
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-203 |
1.08e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 67.07 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 7 KKIRKSYGNKHnkhEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGtininqaemtnmkEKQLAEFRKqh 86
Cdd:PRK11819 10 NRVSKVVPPKK---QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG-------------EARPAPGIK-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 87 LGFIFQEYNLLDTLTVKENILLPLSITK--------ISKK--EAGQKFEEVAKELGifELKDKY---------------- 140
Cdd:PRK11819 72 VGYLPQEPQLDPEKTVRENVEEGVAEVKaaldrfneIYAAyaEPDADFDALAAEQG--ELQEIIdaadawdldsqleiam 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1112987593 141 ------PNE-----ISGGQKQRTSAARAFIHEPSIIFADEPTGALDSKSASDLLNKLsqlnQKRRATIVMVTHD 203
Cdd:PRK11819 150 dalrcpPWDakvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFL----HDYPGTVVAVTHD 219
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
23-244 |
1.57e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 67.07 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 23 LKGIDLQIQKGEFVSIMGPSGSGKTTLLN-VLSSIDQVSGGTINInqaemtnmkeKQLAEFRKQhLGFIFQEynlldtlT 101
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVI----------RGTVAYVPQ-VSWIFNA-------T 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 102 VKENILLPLSITKiSKKEAGQKFEEVAKELGIF------ELKDKYPNeISGGQKQRTSAARAFIHEPSIIFADEPTGALD 175
Cdd:PLN03130 695 VRDNILFGSPFDP-ERYERAIDVTALQHDLDLLpggdltEIGERGVN-ISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1112987593 176 SKSASDLLNKL--SQLNQKRRatiVMVTHDPVAASFCSRVVFIKDGQI-----YTQLNKGGqdrqMFFQDIMKTQG 244
Cdd:PLN03130 773 AHVGRQVFDKCikDELRGKTR---VLVTNQLHFLSQVDRIILVHEGMIkeegtYEELSNNG----PLFQKLMENAG 841
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
17-203 |
2.85e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 65.82 E-value: 2.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 17 HNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKekqLAEFRKQHLGFIFQE--- 93
Cdd:COG3845 268 DRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLS---PRERRRLGVAYIPEDrlg 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 94 YNLLDTLTVKENILLPLSITK-------ISKKEAGQKFEEVAKELGIfelkdKYPNE------ISGGQKQRTSAARAFIH 160
Cdd:COG3845 345 RGLVPDMSVAENLILGRYRRPpfsrggfLDRKAIRAFAEELIEEFDV-----RTPGPdtparsLSGGNQQKVILARELSR 419
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1112987593 161 EPSIIFADEPTGALDSKSASDLLNKLsqLNQKRR-ATIVMVTHD 203
Cdd:COG3845 420 DPKLLIAAQPTRGLDVGAIEFIHQRL--LELRDAgAAVLLISED 461
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
25-207 |
8.61e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 62.51 E-value: 8.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 25 GIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMtnmkEKQLAEFRKQ-----HLGFIFQEynlldt 99
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI----RRQRDEYHQDllylgHQPGIKTE------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 100 LTVKENILLPLSITKISKKEA--------G-QKFEEV-AKELgifelkdkypneiSGGQKQRTSAARAFIHEPSIIFADE 169
Cdd:PRK13538 89 LTALENLRFYQRLHGPGDDEAlwealaqvGlAGFEDVpVRQL-------------SAGQQRRVALARLWLTRAPLWILDE 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 1112987593 170 PTGALDSKSASDLLNKLSQlNQKRRATIVMVTHDPVAA 207
Cdd:PRK13538 156 PFTAIDKQGVARLEALLAQ-HAEQGGMVILTTHQDLPV 192
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
22-202 |
1.14e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 64.28 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 22 VLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTI----NINQAEMTNMKEKQ-----------LAEFRKQH 86
Cdd:PTZ00265 1183 IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHivfkNEHTNDMTNEQDYQgdeeqnvgmknVNEFSLTK 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 87 LG------FIFQ-------------EYNLLD-----TLTVKENILLPLSI---TKISKKEAG-QKFEEVAKELGIFELKD 138
Cdd:PTZ00265 1263 EGgsgedsTVFKnsgkilldgvdicDYNLKDlrnlfSIVSQEPMLFNMSIyenIKFGKEDATrEDVKRACKFAAIDEFIE 1342
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1112987593 139 KYPNE-----------ISGGQKQRTSAARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTH 202
Cdd:PTZ00265 1343 SLPNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH 1417
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-221 |
2.16e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 63.26 E-value: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIrKSYGNKHnkhevLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTnmkEKQLAEF 82
Cdd:PRK09700 265 VFEVRNV-TSRDRKK-----VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS---PRSPLDA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 83 RKQHLGFIFQ---EYNLLDTLTVKENILLPLSITKISKKEA--------GQKFEEVAKELgiFELK----DKYPNEISGG 147
Cdd:PRK09700 336 VKKGMAYITEsrrDNGFFPNFSIAQNMAISRSLKDGGYKGAmglfhevdEQRTAENQREL--LALKchsvNQNITELSGG 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1112987593 148 QKQRTSAARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDPVAASFCSRVVFIKDGQI 221
Cdd:PRK09700 414 NQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
3-202 |
3.09e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 61.58 E-value: 3.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSYGNKhnkhEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSID--QVSGGTININQAEMTNMKEKQLA 80
Cdd:CHL00131 7 ILEIKNLHASVNEN----EILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 81 efrkqHLGfIFQEYNLLDTLTVKENI-LLPLSIT------KISKKEAGQKFEEVAKELGIFELK----DKYPNE-ISGGQ 148
Cdd:CHL00131 83 -----HLG-IFLAFQYPIEIPGVSNAdFLRLAYNskrkfqGLPELDPLEFLEIINEKLKLVGMDpsflSRNVNEgFSGGE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1112987593 149 KQRTSAARAFIHEPSIIFADEPTGALDS---KSASDLLNKLSQLNQkrraTIVMVTH 202
Cdd:CHL00131 157 KKRNEILQMALLDSELAILDETDSGLDIdalKIIAEGINKLMTSEN----SIILITH 209
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
11-204 |
3.53e-11 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 62.94 E-value: 3.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 11 KSYGNKHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSidQVSGGTINiNQAEMTNMKEKQlaEFRKQHLGFI 90
Cdd:PLN03140 884 KEQGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIE-GDIRISGFPKKQ--ETFARISGYC 958
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 91 FQEYNLLDTLTVKENIL------LPlsiTKISKKEAGQKFEEVAKELGIFELKDK---YP--NEISGGQKQRTSAARAFI 159
Cdd:PLN03140 959 EQNDIHSPQVTVRESLIysaflrLP---KEVSKEEKMMFVDEVMELVELDNLKDAivgLPgvTGLSTEQRKRLTIAVELV 1035
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1112987593 160 HEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRaTIVMVTHDP 204
Cdd:PLN03140 1036 ANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGR-TVVCTIHQP 1079
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
26-203 |
4.64e-11 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 61.74 E-value: 4.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 26 IDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQ----VSGGTININQAEMTNMKEKQLAEFRKQHLGFIFQEYNllDTLT 101
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDDIDLLRLSPRERRKLVGHNVSMIFQEPQ--SCLD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 102 VKENILLPLsITKIS----KKEAGQKFE-------EVAKELGIFELKD---KYPNEISGGQKQRTSAARAFIHEPSIIFA 167
Cdd:PRK15093 104 PSERVGRQL-MQNIPgwtyKGRWWQRFGwrkrraiELLHRVGIKDHKDamrSFPYELTEGECQKVMIAIALANQPRLLIA 182
|
170 180 190
....*....|....*....|....*....|....*.
gi 1112987593 168 DEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHD 203
Cdd:PRK15093 183 DEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHD 218
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-221 |
5.02e-11 |
|
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: 62.66 E-value: 5.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 23 LKGIDLQIQKGEFVSIMGPSGSGKTTLLN-VLSSIDQVSGgtininQAEMtnmkekqlaefrKQHLGFIFQEyNLLDTLT 101
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKVEG------HVHM------------KGSVAYVPQQ-AWIQNDS 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 102 VKENILLPlsiTKISKKEAGQKFEEVA--KELGIF------ELKDKYPNeISGGQKQRTSAARAFIHEPSIIFADEPTGA 173
Cdd:TIGR00957 715 LRENILFG---KALNEKYYQQVLEACAllPDLEILpsgdrtEIGEKGVN-LSGGQKQRVSLARAVYSNADIYLFDDPLSA 790
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1112987593 174 LDSKSASDLLNKL----SQLNQKRRatiVMVTHdpvAASFCSRVVFI---KDGQI 221
Cdd:TIGR00957 791 VDAHVGKHIFEHVigpeGVLKNKTR---ILVTH---GISYLPQVDVIivmSGGKI 839
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
21-221 |
5.88e-11 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 60.12 E-value: 5.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 21 EVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLaefrKQHLGFIFQEYNLLDTl 100
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL----RSSLTIIPQDPTLFSG- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 101 TVKENIllplsitkisKKEAGQKFEEVAKELGIFELKdkypNEISGGQKQRTSAARAFIHEPSIIFADEPTGALDskSAS 180
Cdd:cd03369 97 TIRSNL----------DPFDEYSDEEIYGALRVSEGG----LNLSQGQRQLLCLARALLKRPRVLVLDEATASID--YAT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1112987593 181 DLLNKLSQLNQKRRATIVMVTHDPVAASFCSRVVFIKDGQI 221
Cdd:cd03369 161 DALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEV 201
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-202 |
6.23e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 62.35 E-value: 6.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGNKHNKhEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEmtNMKEKQLAEFR 83
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDV-EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSH--NLKDINLKWWR 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 84 KQhLGFIFQEyNLLDTLTVKENILLPL------------------------------------SITKISKKEAGQKFEEV 127
Cdd:PTZ00265 460 SK-IGVVSQD-PLLFSNSIKNNIKYSLyslkdlealsnyynedgndsqenknkrnscrakcagDLNDMSNTTDSNELIEM 537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 128 AKELGIFE-------------------LKDKY-------PNEISGGQKQRTSAARAFIHEPSIIFADEPTGALDSKSASD 181
Cdd:PTZ00265 538 RKNYQTIKdsevvdvskkvlihdfvsaLPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYL 617
|
250 260
....*....|....*....|.
gi 1112987593 182 LLNKLSQLNQKRRATIVMVTH 202
Cdd:PTZ00265 618 VQKTINNLKGNENRITIIIAH 638
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
10-220 |
7.75e-11 |
|
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: 60.50 E-value: 7.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 10 RKSYGNKHNKHEVLKGidlQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAEFrkqhlgf 89
Cdd:cd03237 5 TMKKTLGEFTLEVEGG---SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADY------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 90 ifqeynlldTLTVKEnilLPLSITKISKKEAGQKfEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPSIIFADE 169
Cdd:cd03237 75 ---------EGTVRD---LLSSITKDFYTHPYFK-TEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDE 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1112987593 170 PTGALDSKS---ASDLLNKLSQLNQKrraTIVMVTHDPVAASFCSRVVFIKDGQ 220
Cdd:cd03237 142 PSAYLDVEQrlmASKVIRRFAENNEK---TAFVVEHDIIMIDYLADRLIVFEGE 192
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
22-175 |
2.14e-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: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 22 VLKGIDLQIQKGEFVSIMGPSGSGKTTLLnvlssidqvsggtininqaeMTNMKEKQLAEFRKQHLGFI--FQEYNLLDT 99
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLL--------------------MLILGELEPSEGKIKHSGRIsfSSQFSWIMP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 100 LTVKENILLPLSITKISKK---EAGQKFEEVAKelgiFELKDKYPN-----EISGGQKQRTSAARAFIHEPSIIFADEPT 171
Cdd:cd03291 112 GTIKENIIFGVSYDEYRYKsvvKACQLEEDITK----FPEKDNTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPF 187
|
....
gi 1112987593 172 GALD 175
Cdd:cd03291 188 GYLD 191
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
22-203 |
3.12e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 59.92 E-value: 3.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 22 VLKGIDLQIQKGEFVSIMGPSGSGKTTLLnvlssidqvsggtininqaeMTNMKEKQLAEFRKQHLGFI--FQEYNLLDT 99
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLL--------------------MMIMGELEPSEGKIKHSGRIsfSPQTSWIMP 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 100 LTVKENILLPLSITKI---SKKEAGQKFEEVAKelgiFELKDKYP-----NEISGGQKQRTSAARAFIHEPSIIFADEPT 171
Cdd:TIGR01271 501 GTIKDNIIFGLSYDEYrytSVIKACQLEEDIAL----FPEKDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPF 576
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1112987593 172 GALDSKSASDL----LNKL----------SQLNQKRRATIVMVTHD 203
Cdd:TIGR01271 577 THLDVVTEKEIfescLCKLmsnktrilvtSKLEHLKKADKILLLHE 622
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
29-204 |
3.63e-10 |
|
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: 59.76 E-value: 3.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 29 QIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININqaemtnmkekqlaefRKQHLGFIFQE-YNLLDTLtvKENIL 107
Cdd:TIGR00954 474 EVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP---------------AKGKLFYVPQRpYMTLGTL--RDQII 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 108 LPLSITKISKKEAGQK----------FEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPSIIFADEPTGALdsk 177
Cdd:TIGR00954 537 YPDSSEDMKRRGLSDKdleqildnvqLTHILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAV--- 613
|
170 180
....*....|....*....|....*..
gi 1112987593 178 sASDLLNKLSQLNQKRRATIVMVTHDP 204
Cdd:TIGR00954 614 -SVDVEGYMYRLCREFGITLFSVSHRK 639
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
18-207 |
4.52e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 57.94 E-value: 4.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 18 NKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNmkekqlAEfRKQHLGFIFQEYNLL 97
Cdd:PRK13543 22 NEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR------GD-RSRFMAYLGHLPGLK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 98 DTLTVKENILLplsITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPSIIFADEPTGALDSK 177
Cdd:PRK13543 95 ADLSTLENLHF---LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE 171
|
170 180 190
....*....|....*....|....*....|
gi 1112987593 178 SASdLLNKLSQLNQKRRATIVMVTHDPVAA 207
Cdd:PRK13543 172 GIT-LVNRMISAHLRGGGAALVTTHGAYAA 200
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-175 |
5.36e-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: 59.18 E-value: 5.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSYGNKhnkhEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAemtnmkekqlaef 82
Cdd:TIGR03719 322 VIEAENLTKAFGDK----LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGET------------- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 83 rkQHLGFIFQEYNLLD-TLTVKENILLPLSITKISKKEAGQKfeevaKELGIFELK----DKYPNEISGGQKQRTSAARA 157
Cdd:TIGR03719 385 --VKLAYVDQSRDALDpNKTVWEEISGGLDIIKLGKREIPSR-----AYVGRFNFKgsdqQKKVGQLSGGERNRVHLAKT 457
|
170
....*....|....*...
gi 1112987593 158 FIHEPSIIFADEPTGALD 175
Cdd:TIGR03719 458 LKSGGNVLLLDEPTNDLD 475
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-221 |
8.02e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 58.36 E-value: 8.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 4 LEAKKIRKSYGNKhnkhEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTIninqaemtnmkekQLAEfr 83
Cdd:PRK15064 320 LEVENLTKGFDNG----PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-------------KWSE-- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 84 KQHLGFIFQ--EYNLLDTLTVKEnillplsitKISK-KEAGQKFEEVAKELG--IFELKD--KYPNEISGGQKQRTSAAR 156
Cdd:PRK15064 381 NANIGYYAQdhAYDFENDLTLFD---------WMSQwRQEGDDEQAVRGTLGrlLFSQDDikKSVKVLSGGEKGRMLFGK 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1112987593 157 AFIHEPSIIFADEPTGALDSKSASDLLNKLsqlnQKRRATIVMVTHD-PVAASFCSRVVFIKDGQI 221
Cdd:PRK15064 452 LMMQKPNVLVMDEPTNHMDMESIESLNMAL----EKYEGTLIFVSHDrEFVSSLATRIIEITPDGV 513
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
22-202 |
8.09e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.88 E-value: 8.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 22 VLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTIninQAEMTNMKeKQLAEFRKQhLGFIFQEYNLLDTLT 101
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEI---LFERQSIK-KDLCTYQKQ-LCFVGHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 102 VKENILLPLSITKISKkeagqkfeEVAKELGIFELKD--KYP-NEISGGQKQRTSAARAFIHEPSIIFADEPTGALDSKS 178
Cdd:PRK13540 91 LRENCLYDIHFSPGAV--------GITELCRLFSLEHliDYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162
|
170 180
....*....|....*....|....
gi 1112987593 179 ASDLLNKLsQLNQKRRATIVMVTH 202
Cdd:PRK13540 163 LLTIITKI-QEHRAKGGAVLLTSH 185
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
26-202 |
8.95e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 58.60 E-value: 8.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 26 IDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGT-------ININqaemtNMkekqlaEFRKQhLGFIFQEYNLLD 98
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEawlfgqpVDAG-----DI------ATRRR-VGYMSQAFSLYG 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 99 TLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPSIIFADEPTGALDSkS 178
Cdd:NF033858 353 ELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDP-V 431
|
170 180
....*....|....*....|....*...
gi 1112987593 179 ASD----LLNKLSqlnQKRRATIVMVTH 202
Cdd:NF033858 432 ARDmfwrLLIELS---REDGVTIFISTH 456
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
22-202 |
1.18e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 58.19 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 22 VLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLaefrKQHLGFIFQEYNLL-DTL 100
Cdd:PRK10790 356 VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL----RQGVAMVQQDPVVLaDTF 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 101 TVkeNILLPlsiTKISKKEAGQKFE-----EVAKEL--GIFELKDKYPNEISGGQKQRTSAARAFIHEPSIIFADEPTGA 173
Cdd:PRK10790 432 LA--NVTLG---RDISEEQVWQALEtvqlaELARSLpdGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATAN 506
|
170 180
....*....|....*....|....*....
gi 1112987593 174 LDSKSASDLLNKLSQLnqKRRATIVMVTH 202
Cdd:PRK10790 507 IDSGTEQAIQQALAAV--REHTTLVVIAH 533
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
3-203 |
1.46e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.90 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSYGNkhNKHEVLKGidlQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTINinqaemtnmKEKQLAeF 82
Cdd:PRK13409 340 LVEYPDLTKKLGD--FSLEVEGG---EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD---------PELKIS-Y 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 83 RKQhlgFIFQEYNLldtlTVKENIllplsitkiskKEAGQKF------EEVAKELGIFELKDKYPNEISGGQKQRTSAAR 156
Cdd:PRK13409 405 KPQ---YIKPDYDG----TVEDLL-----------RSITDDLgssyykSEIIKPLQLERLLDKNVKDLSGGELQRVAIAA 466
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1112987593 157 AFIHEPSIIFADEPTGALDSK---SASDLLNKLSqlnQKRRATIVMVTHD 203
Cdd:PRK13409 467 CLSRDADLYLLDEPSAHLDVEqrlAVAKAIRRIA---EEREATALVVDHD 513
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
23-228 |
1.96e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.43 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 23 LKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTInINQAEMTNMKEKQlaEFRKQHLGFIFQEYNLLDTLTV 102
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSI-LFQGKEIDFKSSK--EALENGISMVHQELNLVLQRSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 103 KENILL---PLSITKISKKEAGQKFEEVAKELGI-FELKDKYPNeISGGQKQRTSAARAFIHEPSIIFADEPTGALDSKS 178
Cdd:PRK10982 91 MDNMWLgryPTKGMFVDQDKMYRDTKAIFDELDIdIDPRAKVAT-LSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1112987593 179 ASDLLNKLSQLnQKRRATIVMVTHD-PVAASFCSRVVFIKDGQ-IYTQLNKG 228
Cdd:PRK10982 170 VNHLFTIIRKL-KERGCGIVYISHKmEEIFQLCDEITILRDGQwIATQPLAG 220
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-203 |
2.25e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.13 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 30 IQKGEFVSIMGPSGSGKTTLLNVLSsidqvsGGTI-NINQAEMTNMKEKQLAEFRKQHLGFIFQEynlldtltVKEN--- 105
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILS------GELIpNLGDYEEEPSWDEVLKRFRGTELQNYFKK--------LYNGeik 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 106 -ILLPLSITKISK-------------KEAGqKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPSIIFADEPT 171
Cdd:PRK13409 162 vVHKPQYVDLIPKvfkgkvrellkkvDERG-KLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPT 240
|
170 180 190
....*....|....*....|....*....|....*
gi 1112987593 172 GALDSK---SASDLLNKLSqlnqKRRATIVmVTHD 203
Cdd:PRK13409 241 SYLDIRqrlNVARLIRELA----EGKYVLV-VEHD 270
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-203 |
2.44e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 57.10 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 31 QKGEFVSIMGPSGSGKTTLLNVLSsidqvsgGTI--NINQAEMTNMKEKQLAEFRkqhlGFIFQEY--NLLD-TLTVken 105
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILS-------GELkpNLGDYDEEPSWDEVLKRFR----GTELQDYfkKLANgEIKV--- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 106 ILLPLSITKISK-------------KEAGqKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPSIIFADEPTG 172
Cdd:COG1245 163 AHKPQYVDLIPKvfkgtvrellekvDERG-KLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSS 241
|
170 180 190
....*....|....*....|....*....|....
gi 1112987593 173 ALDSK---SASDLLNKLSQLNQkrraTIVMVTHD 203
Cdd:COG1245 242 YLDIYqrlNVARLIRELAEEGK----YVLVVEHD 271
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-203 |
2.55e-09 |
|
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: 56.22 E-value: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 33 GEFVSIMGPSGSGKTTLLNVLSS------------------IDQVSGGTIninQAEMTNMKEKQLAEFRK-QHLGFIFQe 93
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGklkpnlgkfddppdwdeiLDEFRGSEL---QNYFTKLLEGDVKVIVKpQYVDLIPK- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 94 ynlldtlTVKENILLPLSitkisKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPSIIFADEPTGA 173
Cdd:cd03236 102 -------AVKGKVGELLK-----KKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSY 169
|
170 180 190
....*....|....*....|....*....|
gi 1112987593 174 LDSKSASDLLNKLSQLNQKRRATIVmVTHD 203
Cdd:cd03236 170 LDIKQRLNAARLIRELAEDDNYVLV-VEHD 198
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
20-221 |
3.12e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 55.99 E-value: 3.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 20 HEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSG--------GTININQAEMTNMKEKQLAEFR-----KQH 86
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGEPLAAIDAPRLARLRavlpqAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 87 LGFIFqeynlldtlTVKENILL---PLSITKISKKEAGQKFEEVAKEL-GIFELKDKYPNEISGGQKQRTSAARAF---- 158
Cdd:PRK13547 94 PAFAF---------SAREIVLLgryPHARRAGALTHRDGEIAWQALALaGATALVGRDVTTLSGGELARVQFARVLaqlw 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1112987593 159 -----IHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDP-VAASFCSRVVFIKDGQI 221
Cdd:PRK13547 165 pphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPnLAARHADRIAMLADGAI 233
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
16-228 |
3.47e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 55.78 E-value: 3.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 16 KHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTInINQAEMTNMKEKQLAEFRKQhLGFIFQE-- 93
Cdd:PRK13638 10 RYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAV-LWQGKPLDYSKRGLLALRQQ-VATVFQDpe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 94 ----YNLLDTltvkeNILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPSIIFADE 169
Cdd:PRK13638 88 qqifYTDIDS-----DIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 170 PTGALDSKSASDLLNKLSQLNQKRRaTIVMVTHDPVAASFCSRVVFI-KDGQIYTQLNKG 228
Cdd:PRK13638 163 PTAGLDPAGRTQMIAIIRRIVAQGN-HVIISSHDIDLIYEISDAVYVlRQGQILTHGAPG 221
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
7-222 |
8.76e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.89 E-value: 8.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 7 KKIRKSygNKHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSS-IDQVSG---GTININQAEmtnmkekqLAEF 82
Cdd:TIGR00956 63 RKLKKF--RDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASnTDGFHIgveGVITYDGIT--------PEEI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 83 RKQHLG---FIFQEYNLLDTLTVKENILLP-------LSITKISKKEAGQKFEEV-AKELGIFELKD-KYPNE----ISG 146
Cdd:TIGR00956 133 KKHYRGdvvYNAETDVHFPHLTVGETLDFAarcktpqNRPDGVSREEYAKHIADVyMATYGLSHTRNtKVGNDfvrgVSG 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 147 GQKQRTSAARAFIHEPSIIFADEPTGALDSKSASDLLNKLSqlnqkrraTIVMVTHDP--VAASFCS--------RVVFI 216
Cdd:TIGR00956 213 GERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALK--------TSANILDTTplVAIYQCSqdayelfdKVIVL 284
|
....*..
gi 1112987593 217 KDG-QIY 222
Cdd:TIGR00956 285 YEGyQIY 291
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
20-239 |
8.81e-09 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 54.86 E-value: 8.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 20 HEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSgGTININQAEMTNMKekqLAEFRKQhLGFIFQEYNLLdT 99
Cdd:cd03289 17 NAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVP---LQKWRKA-FGVIPQKVFIF-S 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 100 LTVKENiLLPLSitkiskKEAGQKFEEVAKELGIFELKDKYPNE-----------ISGGQKQRTSAARAFIHEPSIIFAD 168
Cdd:cd03289 91 GTFRKN-LDPYG------KWSDEEIWKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSVLSKAKILLLD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1112987593 169 EPTGALDSKSASDLLNKLSQLNQKrrATIVMVTHDPVAASFCSRVVFIKDGQI--YTQLNKGGQDRQMFFQDI 239
Cdd:cd03289 164 EPSAHLDPITYQVIRKTLKQAFAD--CTVILSEHRIEAMLECQRFLVIEENKVrqYDSIQKLLNEKSHFKQAI 234
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
29-203 |
9.00e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 54.55 E-value: 9.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 29 QIQKGEFVSIMGPSGSGKTTLLNVLSSIdQVSGGTININQAEMTNMKEKQLAEFRkqhlGFIFQEYNLLDTLTVKEniLL 108
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHR----AYLSQQQTPPFAMPVFQ--YL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 109 PLSITKISKKEAGQK-FEEVAKELGifeLKDKYP---NEISGGQKQRTSAARAF--IHePSI------IFADEPTGALD- 175
Cdd:PRK03695 91 TLHQPDKTRTEAVASaLNEVAEALG---LDDKLGrsvNQLSGGEWQRVRLAAVVlqVW-PDInpagqlLLLDEPMNSLDv 166
|
170 180
....*....|....*....|....*....
gi 1112987593 176 -SKSASDLLnkLSQLNQKRRAtIVMVTHD 203
Cdd:PRK03695 167 aQQAALDRL--LSELCQQGIA-VVMSSHD 192
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
22-221 |
2.53e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.21 E-value: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 22 VLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKekqLAEFRKQhLGFIFQEyNLLDTLT 101
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFG---LTDLRRV-LSIIPQS-PVLFSGT 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 102 VKENILlPLSitkiSKKEAGqkfeeVAKELGIFELKDKYPNE--------------ISGGQKQRTSAARAFIHEPSIIFA 167
Cdd:PLN03232 1326 VRFNID-PFS----EHNDAD-----LWEALERAHIKDVIDRNpfgldaevseggenFSVGQRQLLSLARALLRRSKILVL 1395
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1112987593 168 DEPTGALDSKsaSDLLNKLSQLNQKRRATIVMVTHDPVAASFCSRVVFIKDGQI 221
Cdd:PLN03232 1396 DEATASVDVR--TDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQV 1447
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-204 |
2.98e-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: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 32 KGEFVSIMGPSGSGKTTLLNVLssidqvsggtininqaemtnmkekqLAEFRKQHLGFIFQeynlldtltvkenillpls 111
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARAL-------------------------ARELGPPGGGVIYI------------------- 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 112 itkiskkeAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPSIIFADEPTGALDSKSASDLL-----NKL 186
Cdd:smart00382 37 --------DGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelRLL 108
|
170
....*....|....*...
gi 1112987593 187 SQLNQKRRATIVMVTHDP 204
Cdd:smart00382 109 LLLKSEKNLTVILTTNDE 126
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
22-175 |
4.29e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 53.63 E-value: 4.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 22 VLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKekqLAEFRKQhLGFIFQEYNLLDTlT 101
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYG---LRELRRQ-FSMIPQDPVLFDG-T 1399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 102 VKENiLLPLSitkiskkEAGQkfEEVAKELGIFELKDKYPNEISG--------------GQKQRTSAARAFIHEPS-IIF 166
Cdd:PTZ00243 1400 VRQN-VDPFL-------EASS--AEVWAALELVGLRERVASESEGidsrvleggsnysvGQRQLMCMARALLKKGSgFIL 1469
|
....*....
gi 1112987593 167 ADEPTGALD 175
Cdd:PTZ00243 1470 MDEATANID 1478
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
21-202 |
5.02e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 52.49 E-value: 5.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 21 EVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSID--QVSGGTININQAEMTNMKekqlAEFRKQHLGFIFQEYNlLD 98
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELS----PEDRAGEGIFMAFQYP-VE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 99 TLTVKENILLPLSITKISK---KEAGQKF------EEVAKELGIFE-LKDKYPNE-ISGGQKQRTSAARAFIHEPSIIFA 167
Cdd:PRK09580 90 IPGVSNQFFLQTALNAVRSyrgQEPLDRFdfqdlmEEKIALLKMPEdLLTRSVNVgFSGGEKKRNDILQMAVLEPELCIL 169
|
170 180 190
....*....|....*....|....*....|....*
gi 1112987593 168 DEPTGALDSKSASDLLNKLSQLNQKRRATIVmVTH 202
Cdd:PRK09580 170 DESDSGLDIDALKIVADGVNSLRDGKRSFII-VTH 203
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
27-200 |
5.12e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.09 E-value: 5.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 27 DLQIQKGEFVSIMGPSGSGKTTLLNVLS-SIDQVSGGTININQaEMTNMKEKQLaefrkQHLgfIFQEY-----NLL--- 97
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAgELPLLSGERQSQFS-HITRLSFEQL-----QKL--VSDEWqrnntDMLspg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 98 --DT-LTVKENILLPlsitkiSKKEAgqKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPSIIFADEPTGAL 174
Cdd:PRK10938 95 edDTgRTTAEIIQDE------VKDPA--RCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGL 166
|
170 180
....*....|....*....|....*.
gi 1112987593 175 DSKSASDLLNKLSQLNQKrRATIVMV 200
Cdd:PRK10938 167 DVASRQQLAELLASLHQS-GITLVLV 191
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
13-171 |
5.56e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.20 E-value: 5.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 13 YGnkhnKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQLAEFR----KQHLG 88
Cdd:NF033858 11 YG----KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCPRiaymPQGLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 89 fifqeYNLLDTLTVKENI-----LLPLsitkiSKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPS 163
Cdd:NF033858 87 -----KNLYPTLSVFENLdffgrLFGQ-----DAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPD 156
|
....*...
gi 1112987593 164 IIFADEPT 171
Cdd:NF033858 157 LLILDEPT 164
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
3-203 |
6.59e-08 |
|
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: 52.86 E-value: 6.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSYGNkhNKHEVLKGidlQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTINinqaemtnmKEKQLAeF 82
Cdd:COG1245 341 LVEYPDLTKSYGG--FSLEVEGG---EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD---------EDLKIS-Y 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 83 RKQHLGFIFQEynlldtlTVKENIllplsitkisKKEAGQKF------EEVAKELGIFELKDKYPNEISGGQKQRTSAAR 156
Cdd:COG1245 406 KPQYISPDYDG-------TVEEFL----------RSANTDDFgssyykTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAA 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1112987593 157 AFIHEPSIIFADEPTGALDSK---SASDLLNKLSqlnQKRRATIVMVTHD 203
Cdd:COG1245 469 CLSRDADLYLLDEPSAHLDVEqrlAVAKAIRRFA---ENRGKTAMVVDHD 515
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
3-202 |
1.24e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 51.71 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSY-GNKhnkheVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLS------SIDqvsgGTIninqaemtnMK 75
Cdd:NF040905 1 ILEMRGITKTFpGVK-----ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSgvyphgSYE----GEI---------LF 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 76 EKQLAEFRK----QHLGF--IFQEYNLLDTLTVKENILLPLSITK---ISKKEAGQKFEEVAKELGIFELKDKYPNEISG 146
Cdd:NF040905 63 DGEVCRFKDirdsEALGIviIHQELALIPYLSIAENIFLGNERAKrgvIDWNETNRRARELLAKVGLDESPDTLVTDIGV 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1112987593 147 GQKQRTSAARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLnQKRRATIVMVTH 202
Cdd:NF040905 143 GKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISH 197
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
16-224 |
1.31e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 52.16 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 16 KHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLS-SID---QVSG------------------GTININQAEMTN 73
Cdd:PLN03140 174 KKTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAgKLDpslKVSGeityngyrlnefvprktsAYISQNDVHVGV 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 74 MKEKQLAEF--RKQHLGfifQEYNLLDTLTVKEN---ILLPLSITKISKKEAGQKFEE------VAKELGIFELKDKYPN 142
Cdd:PLN03140 254 MTVKETLDFsaRCQGVG---TRYDLLSELARREKdagIFPEAEVDLFMKATAMEGVKSslitdyTLKILGLDICKDTIVG 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 143 E-----ISGGQKQRTSAARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDPVAASF--CSRVVF 215
Cdd:PLN03140 331 DemirgISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQPAPETFdlFDDIIL 410
|
....*....
gi 1112987593 216 IKDGQIYTQ 224
Cdd:PLN03140 411 LSEGQIVYQ 419
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-221 |
2.05e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 51.43 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 20 HEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTINInqaemtnmkekqlaefrKQHLGFIFQEYNLLDT 99
Cdd:PRK13545 37 HYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI-----------------KGSAALIAISSGLNGQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 100 LTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPSIIFADEPTGALDSKSA 179
Cdd:PRK13545 100 LTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFT 179
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1112987593 180 SDLLNKLSQLNQKRRaTIVMVTHD-PVAASFCSRVVFIKDGQI 221
Cdd:PRK13545 180 KKCLDKMNEFKEQGK-TIFFISHSlSQVKSFCTKALWLHYGQV 221
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
25-203 |
4.00e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.63 E-value: 4.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 25 GIDLQIQkgefVSIMGPSGSGKTTLLNVLSSIDQVSGGTInINQAEMtnmkekQLAEFRKQHLgfifqeynllDTLTVKE 104
Cdd:PLN03073 531 GIDLDSR----IAMVGPNGIGKSTILKLISGELQPSSGTV-FRSAKV------RMAVFSQHHV----------DGLDLSS 589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 105 NILLPLSITKISKKEagQKFEEVAKELGI---FELKDKYpnEISGGQKQRTSAARAFIHEPSIIFADEPTGALDSKSASD 181
Cdd:PLN03073 590 NPLLYMMRCFPGVPE--QKLRAHLGSFGVtgnLALQPMY--TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEA 665
|
170 180
....*....|....*....|..
gi 1112987593 182 LLNKLSQLnqkrRATIVMVTHD 203
Cdd:PLN03073 666 LIQGLVLF----QGGVLMVSHD 683
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
26-100 |
4.22e-07 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 50.18 E-value: 4.22e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1112987593 26 IDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTnmkEKQLAEFRkQHLGFIFQEYNLLDTL 100
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT---ADNREAYR-QLFSAVFSDFHLFDRL 421
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
15-221 |
4.93e-07 |
|
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: 50.21 E-value: 4.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 15 NKHNKHevLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVL-SSIDQVSGGTININQAEMtNMKEKQLA---------EFRK 84
Cdd:TIGR02633 270 NPHRKR--VDDVSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPV-DIRNPAQAiragiamvpEDRK 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 85 QHlgfifqeyNLLDTLTVKENILLPL--SITKISKKEAGQKFEEVAKELGIFELKDKYPN----EISGGQKQRTSAARAF 158
Cdd:TIGR02633 347 RH--------GIVPILGVGKNITLSVlkSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFlpigRLSGGNQQKAVLAKML 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1112987593 159 IHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDPVAASFCSRVVFIKDGQI 221
Cdd:TIGR02633 419 LTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-175 |
6.07e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.12 E-value: 6.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 22 VLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKekqLAEFRKQhLGFI----------- 90
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFG---LMDLRKV-LGIIpqapvlfsgtv 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 91 ------FQEYNLLDTLTVKENILLPLSITKISK------KEAGQKFeevakelgifelkdkypneiSGGQKQRTSAARAF 158
Cdd:PLN03130 1330 rfnldpFNEHNDADLWESLERAHLKDVIRRNSLgldaevSEAGENF--------------------SVGQRQLLSLARAL 1389
|
170
....*....|....*..
gi 1112987593 159 IHEPSIIFADEPTGALD 175
Cdd:PLN03130 1390 LRRSKILVLDEATAAVD 1406
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
15-220 |
7.09e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 48.09 E-value: 7.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 15 NKHNkhevLKGIDLQIQKGEFVSIMGPSGSGKTTLLNvlssidqvsggtiNINQAEMTNMKEKQLAEFRKQHLGFIFQEY 94
Cdd:cd03238 7 NVHN----LQNLDVSIPLNVLVVVTGVSGSGKSTLVN-------------EGLYASGKARLISFLPKFSRNKLIFIDQLQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 95 NLLDTltvkeNI-LLPLsitkiskkeaGQKFeevakelgifelkdkypNEISGGQKQRTS-AARAFIH-EPSIIFADEPT 171
Cdd:cd03238 70 FLIDV-----GLgYLTL----------GQKL-----------------STLSGGELQRVKlASELFSEpPGTLFILDEPS 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1112987593 172 GALDSKSASDLLNKLSQLNQKRRaTIVMVTHDPVAASFCSRVVFIKDGQ 220
Cdd:cd03238 118 TGLHQQDINQLLEVIKGLIDLGN-TVILIEHNLDVLSSADWIIDFGPGS 165
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
98-202 |
8.79e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 48.96 E-value: 8.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 98 DTLTVKENILLPLSITKISKKEAGQKFEEVAKELGIFELKDKYPNEISGGQKQRTSAARAFIHEPSIIFADEPTGALDSK 177
Cdd:NF000106 99 ESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPR 178
|
90 100
....*....|....*....|....*
gi 1112987593 178 SASDLLNKLSQLnQKRRATIVMVTH 202
Cdd:NF000106 179 TRNEVWDEVRSM-VRDGATVLLTTQ 202
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
23-203 |
1.10e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 49.20 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 23 LKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTnmkEKQLAEFRkQHLGFIFQEYNLLDTLTV 102
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT---AEQPEDYR-KLFSAVFTDFHLFDQLLG 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 103 KENillplsitKISKKEAGQKFeevakeLGIFELKDKYPNE--------ISGGQKQRTSAARAFIHEPSIIFADEPTGAL 174
Cdd:PRK10522 415 PEG--------KPANPALVEKW------LERLKMAHKLELEdgrisnlkLSKGQKKRLALLLALAEERDILLLDEWAADQ 480
|
170 180
....*....|....*....|....*....
gi 1112987593 175 DSKSASDLLNKLSQLNQKRRATIVMVTHD 203
Cdd:PRK10522 481 DPHFRREFYQVLLPLLQEMGKTIFAISHD 509
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-221 |
1.40e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.89 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 21 EVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQ--------LAEFRKQHLGFifq 92
Cdd:PRK15439 277 EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrlarglvyLPEDRQSSGLY--- 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 93 eynlLD--------TLTVKEnilLPLSITkiSKKEAgQKFEEVAKELGI-FELKDKYPNEISGGQKQRTSAARAFIHEPS 163
Cdd:PRK15439 354 ----LDaplawnvcALTHNR---RGFWIK--PAREN-AVLERYRRALNIkFNHAEQAARTLSGGNQQKVLIAKCLEASPQ 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1112987593 164 IIFADEPTGALDSKSASDLLNKLSQLNQKRRAtIVMVTHD-PVAASFCSRVVFIKDGQI 221
Cdd:PRK15439 424 LLIVDEPTRGVDVSARNDIYQLIRSIAAQNVA-VLFISSDlEEIEQMADRVLVMHQGEI 481
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-221 |
1.51e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 48.79 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 22 VLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQaemTNMKEKQLAEFRKQhLGFIFQEyNLLDTLT 101
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG---LNIAKIGLHDLRFK-ITIIPQD-PVLFSGS 1375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 102 VKENiLLPLSitKISKKEAGQKFEEVAKELGIFELKDKYPNE-------ISGGQKQRTSAARAFIHEPSIIFADEPTGAL 174
Cdd:TIGR00957 1376 LRMN-LDPFS--QYSDEEVWWALELAHLKTFVSALPDKLDHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAV 1452
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1112987593 175 DSKsaSDLLNKLSQLNQKRRATIVMVTHDPVAASFCSRVVFIKDGQI 221
Cdd:TIGR00957 1453 DLE--TDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEV 1497
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
22-239 |
1.57e-06 |
|
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: 48.75 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 22 VLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSgGTININQAEMTNMkekQLAEFRKQhLGFIFQEYNLLdTLT 101
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSV---TLQTWRKA-FGVIPQKVFIF-SGT 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 102 VKENiLLPlsitkiSKKEAGQKFEEVAKELGIFELKDKYPNE-----------ISGGQKQRTSAARAFIHEPSIIFADEP 170
Cdd:TIGR01271 1308 FRKN-LDP------YEQWSDEEIWKVAEEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSILSKAKILLLDEP 1380
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1112987593 171 TGALDSKSASDLLNKLSQlnQKRRATIVMVTHDPVAASFCSRVVFIKDGQI--YTQLNKGGQDRQMFFQDI 239
Cdd:TIGR01271 1381 SAHLDPVTLQIIRKTLKQ--SFSNCTVILSEHRVEALLECQQFLVIEGSSVkqYDSIQKLLNETSLFKQAM 1449
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
20-203 |
1.88e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.41 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 20 HEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQ------------LAEfRKQHL 87
Cdd:PRK11147 16 APLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDpprnvegtvydfVAE-GIEEQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 88 GFIFQEYNLLDTLTVK---ENILLPLS-ITKISKKEAGQKFE----EVAKELGIFelKDKYPNEISGGQKQRTSAARAFI 159
Cdd:PRK11147 95 AEYLKRYHDISHLVETdpsEKNLNELAkLQEQLDHHNLWQLEnrinEVLAQLGLD--PDAALSSLSGGWLRKAALGRALV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1112987593 160 HEPSIIFADEPTGALDsksaSDLLNKLSQLNQKRRATIVMVTHD 203
Cdd:PRK11147 173 SNPDVLLLDEPTNHLD----IETIEWLEGFLKTFQGSIIFISHD 212
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
15-51 |
1.94e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 48.47 E-value: 1.94e-06
10 20 30
....*....|....*....|....*....|....*..
gi 1112987593 15 NKHNkhevLKGIDLQIQKGEFVSIMGPSGSGKTTLLN 51
Cdd:TIGR00630 620 RENN----LKNITVSIPLGLFTCITGVSGSGKSTLIN 652
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-66 |
3.68e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.42 E-value: 3.68e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1112987593 3 ILEAKKIRKSYGNKhnkheVL-KGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTINI 66
Cdd:PRK11819 324 VIEAENLSKSFGDR-----LLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-244 |
5.92e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.09 E-value: 5.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIRKSYGNKhnkhEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSsidqvsgGTININQAEMTNMKEKQLAEF 82
Cdd:PRK10636 312 LLKMEKVSAGYGDR----IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLA-------GELAPVSGEIGLAKGIKLGYF 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 83 RKQHLGFIFQEYNLLDTLTvkenillplsitKISKKEAGQKFEEVakeLGIFELK-DKYPNE---ISGGQKQRTSAARAF 158
Cdd:PRK10636 381 AQHQLEFLRADESPLQHLA------------RLAPQELEQKLRDY---LGGFGFQgDKVTEEtrrFSGGEKARLVLALIV 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 159 IHEPSIIFADEPTGALDsksaSDLLNKLSQLNQKRRATIVMVTHDP-VAASFCSRVVFIKDGQIyTQLNKGGQDRQMFFQ 237
Cdd:PRK10636 446 WQRPNLLLLDEPTNHLD----LDMRQALTEALIDFEGALVVVSHDRhLLRSTTDDLYLVHDGKV-EPFDGDLEDYQQWLS 520
|
....*..
gi 1112987593 238 DIMKTQG 244
Cdd:PRK10636 521 DVQKQEN 527
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
143-220 |
8.44e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 44.87 E-value: 8.44e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1112987593 143 EISGGQKQRTSAARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDPVAASFCSRVVFIKDGQ 220
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEGE 148
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
17-49 |
1.27e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 46.17 E-value: 1.27e-05
10 20 30
....*....|....*....|....*....|...
gi 1112987593 17 HNkhevLKGIDLQIQKGEFVSIMGPSGSGKTTL 49
Cdd:COG0178 14 HN----LKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
33-175 |
1.70e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.62 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 33 GEFVSIMGPSGSGKTTLLN--VLSSID-------------QVSGGTININQAEM-TNMKEKQLAEFRKQhlgfIFQEYNL 96
Cdd:PLN03073 203 GRHYGLVGRNGTGKTTFLRymAMHAIDgipkncqilhveqEVVGDDTTALQCVLnTDIERTQLLEEEAQ----LVAQQRE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 97 LDTLTVKENILLPlSITKISKKEAGQKFEEVAKELGIF--------------------ELKDKYPNEISGGQKQRTSAAR 156
Cdd:PLN03073 279 LEFETETGKGKGA-NKDGVDKDAVSQRLEEIYKRLELIdaytaearaasilaglsftpEMQVKATKTFSGGWRMRIALAR 357
|
170
....*....|....*....
gi 1112987593 157 AFIHEPSIIFADEPTGALD 175
Cdd:PLN03073 358 ALFIEPDLLLLDEPTNHLD 376
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
23-221 |
3.06e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 44.61 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 23 LKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQ--------LAEFRKQHlgfifqey 94
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglangivyISEDRKRD-------- 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 95 NLLDTLTVKENILLPlSITKISKK----EAGQKFEEVAKELGIFELK----DKYPNEISGGQKQRTSAARAFIHEPSIIF 166
Cdd:PRK10762 340 GLVLGMSVKENMSLT-ALRYFSRAggslKHADEQQAVSDFIRLFNIKtpsmEQAIGLLSGGNQQKVAIARGLMTRPKVLI 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1112987593 167 ADEPTGALD---SKSASDLLNKLsqlnQKRRATIVMVTHD-PVAASFCSRVVFIKDGQI 221
Cdd:PRK10762 419 LDEPTRGVDvgaKKEIYQLINQF----KAEGLSIILVSSEmPEVLGMSDRILVMHEGRI 473
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
7-51 |
3.52e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 44.63 E-value: 3.52e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1112987593 7 KKIRKSYGNK--------HNkhevLKGIDLQIQKGEFVSIMGPSGSGKTTLLN 51
Cdd:COG0178 601 KKRRKGNGKFltikgareNN----LKNVDVEIPLGVLTCVTGVSGSGKSTLVN 649
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
15-51 |
4.68e-05 |
|
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: 43.37 E-value: 4.68e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1112987593 15 NKHNkhevLKGIDLQIQKGEFVSIMGPSGSGKTTLLN 51
Cdd:cd03271 7 RENN----LKNIDVDIPLGVLTCVTGVSGSGKSSLIN 39
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
15-51 |
7.07e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 43.52 E-value: 7.07e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1112987593 15 NKHNkhevLKGIDLQIQKGEFVSIMGPSGSGKTTLLN 51
Cdd:PRK00349 621 RENN----LKNVDVEIPLGKFTCVTGVSGSGKSTLIN 653
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
8-49 |
1.73e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 42.69 E-value: 1.73e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1112987593 8 KIRKSYGNKHNkhevLKGIDLQIQKGEFVSIMGPSGSGKTTL 49
Cdd:TIGR00630 1 KIIVRGAREHN----LKNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
14-241 |
3.50e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 40.95 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 14 GNKHNKHEVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLssidqvsGGTININQAEMTnmkekqlaefRKQHLGFIFQE 93
Cdd:PRK13546 31 KHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNII-------GGSLSPTVGKVD----------RNGEVSVIAIS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 94 YNLLDTLTVKENILLPLSITKISKKEAGQKFEEVAK--ELG--IFELKDKYpneiSGGQKQRTSAARAFIHEPSIIFADE 169
Cdd:PRK13546 94 AGLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEfsELGefIYQPVKKY----SSGMRAKLGFSINITVNPDILVIDE 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1112987593 170 PTGALDSKSASDLLNKLSQLNQKRRaTIVMVTHD-PVAASFCSRVVFIKDGQI--YTQLNKGGQDRQMFFQDIMK 241
Cdd:PRK13546 170 ALSVGDQTFAQKCLDKIYEFKEQNK-TIFFVSHNlGQVRQFCTKIAWIEGGKLkdYGELDDVLPKYEAFLNDFKK 243
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-221 |
3.84e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 41.45 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 3 ILEAKKIrkSYGNKHNKH-EVLKGIDLQIQKGEFVSIMGPSGSGKTTLLNVL-SSIDQVSGGTININQAEMTNMKEKQ-- 78
Cdd:PRK13549 259 ILEVRNL--TAWDPVNPHiKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLfGAYPGRWEGEIFIDGKPVKIRNPQQai 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 79 ------LAEFRKQHlgfifqeyNLLDTLTVKENILLPL--SITKISKKEAGQKFEEVAKElgIFELKDKYPN------EI 144
Cdd:PRK13549 337 aqgiamVPEDRKRD--------GIVPVMGVGKNITLAAldRFTGGSRIDDAAELKTILES--IQRLKVKTASpelaiaRL 406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1112987593 145 SGGQKQRTSAARAFIHEPSIIFADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDPVAASFCSRVVFIKDGQI 221
Cdd:PRK13549 407 SGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
17-49 |
4.46e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.21 E-value: 4.46e-04
10 20 30
....*....|....*....|....*....|...
gi 1112987593 17 HNkhevLKGIDLQIQKGEFVSIMGPSGSGKTTL 49
Cdd:PRK00349 14 HN----LKNIDLDIPRDKLVVFTGLSGSGKSSL 42
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
144-204 |
5.30e-04 |
|
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: 39.65 E-value: 5.30e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1112987593 144 ISGGQKQRTSAARAFIHE-----PSIIFaDEPTGALDSKSASDLLNKLSQLNQKRRATIVmVTHDP 204
Cdd:cd03227 78 LSGGEKELSALALILALAslkprPLYIL-DEIDRGLDPRDGQALAEAILEHLVKGAQVIV-ITHLP 141
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
17-49 |
8.91e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 39.55 E-value: 8.91e-04
10 20 30
....*....|....*....|....*....|...
gi 1112987593 17 HNkhevLKGIDLQIQKGEFVSIMGPSGSGKTTL 49
Cdd:cd03270 9 HN----LKNVDVDIPRNKLVVITGVSGSGKSSL 37
|
|
| UMPK_like |
cd02028 |
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the ... |
35-61 |
1.55e-03 |
|
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or uridine-cytidine kinase (UCK).
Pssm-ID: 238986 [Multi-domain] Cd Length: 179 Bit Score: 38.44 E-value: 1.55e-03
10 20
....*....|....*....|....*..
gi 1112987593 35 FVSIMGPSGSGKTTLLNVLSSIDQVSG 61
Cdd:cd02028 1 VVGIAGPSGSGKTTFAKKLSNQLRVNG 27
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
23-221 |
6.65e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 37.40 E-value: 6.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 23 LKGIDLQIQKGEFVSIMGPSGSGKTTLLNVLSSIDQVSGGTININQAEMTNMKEKQ--------LAEFRKQH--LGFIFQ 92
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEainhgfalVTEERRSTgiYAYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 93 EYN-LLDTLTVKENILLPLSITKISKKeagqkfeevaKELGIFELKDKYPNE------ISGGQKQRTSAARAFIHEPSII 165
Cdd:PRK10982 344 GFNsLISNIRNYKNKVGLLDNSRMKSD----------TQWVIDSMRVKTPGHrtqigsLSGGNQQKVIIGRWLLTQPEIL 413
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1112987593 166 FADEPTGALDSKSASDLLNKLSQLNQKRRATIVMVTHDPVAASFCSRVVFIKDGQI 221
Cdd:PRK10982 414 MLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
142-219 |
7.32e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 37.50 E-value: 7.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112987593 142 NEISGGQKQRTSAARAFIHEPSII--FADEPTGALDSKSAsdllNKLSQLNQKRR---ATIVMVTHDPVAASFCSRVVFI 216
Cdd:PRK00635 475 ATLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDT----HKLINVIKKLRdqgNTVLLVEHDEQMISLADRIIDI 550
|
...
gi 1112987593 217 KDG 219
Cdd:PRK00635 551 GPG 553
|
|
| |
