|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
9-233 |
6.78e-123 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 347.80 E-value: 6.78e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 9 PAISLSNIYKCYGAGAGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAV 88
Cdd:COG1136 3 PLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 89 IRGKHLGFIFQFFNLMPVLNVFDNVYFPLVLNGqFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAH 168
Cdd:COG1136 83 LRRRHIGFVFQFFNLLPELTALENVALPLLLAG-VSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15830546 169 EPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSELKARARRVVEIQDGVLIHDS 233
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVSDE 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
11-229 |
4.37e-107 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 307.49 E-value: 4.37e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGAGAGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAVIR 90
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 GKHLGFIFQFFNLMPVLNVFDNVYFPLVLNGQFsKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEP 170
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVP-KKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15830546 171 MVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSELKARARRVVEIQDGVL 229
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
9-235 |
1.52e-94 |
|
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: 276.24 E-value: 1.52e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 9 PAISLSNIYKCYGAGAGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAV 88
Cdd:COG4181 7 PIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 89 IRGKHLGFIFQFFNLMPVLNVFDNVYFPLVLNGQfskKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAH 168
Cdd:COG4181 87 LRARHVGFVFQSFQLLPTLTALENVMLPLELAGR---RDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFAT 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830546 169 EPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSELKARARRVVEIQDGVLIHDSDA 235
Cdd:COG4181 164 EPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTAA 230
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
11-232 |
4.65e-90 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 264.61 E-value: 4.65e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGAGagkVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAVIR 90
Cdd:COG2884 2 IRFENVSKRYPGG---REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 gKHLGFIFQFFNLMPVLNVFDNVYFPLVLNGqFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEP 170
Cdd:COG2884 79 -RRIGVVFQDFRLLPDRTVYENVALPLRVTG-KSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15830546 171 MVVIADEPTGNLDLATGEAILDLLLTINqQTGTTFVISTHSSEL-KARARRVVEIQDGVLIHD 232
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEIN-RRGTTVLIATHDLELvDRMPKRVLELEDGRLVRD 218
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
9-224 |
9.06e-80 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 239.99 E-value: 9.06e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 9 PAISLSNIYKCYGAGAGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLpeeqlav 88
Cdd:COG1116 6 PALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGP------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 89 irGKHLGFIFQFFNLMPVLNVFDNVYFPLVLNGqFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAH 168
Cdd:COG1116 79 --GPDRGVVFQEPALLPWLTVLDNVALGLELRG-VPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAN 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830546 169 EPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSE-----------LKARARRVVEI 224
Cdd:COG1116 156 DPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDeavfladrvvvLSARPGRIVEE 222
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
11-230 |
9.52e-77 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 234.97 E-value: 9.52e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGAGAGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAVIR 90
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 gKHLGFIFQFFNLMPVLNVFDNVYFPLVLNGqFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEP 170
Cdd:COG1135 82 -RKIGMIFQHFNLLSSRTVAENVALPLEIAG-VPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830546 171 MVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSE-LKARARRVVEIQDGVLI 230
Cdd:COG1135 160 KVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDvVRRICDRVAVLENGRIV 220
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
11-222 |
2.03e-73 |
|
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: 222.35 E-value: 2.03e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGAGAGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQlpeeqlaviR 90
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG---------P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 GKHLGFIFQFFNLMPVLNVFDNVYFPLVLNGQfSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEP 170
Cdd:cd03293 72 GPDRGYVFQQDALLPWLTVLDNVALGLELQGV-PKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDP 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15830546 171 MVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHS-SELKARARRVV 222
Cdd:cd03293 151 DVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDiDEAVFLADRVV 203
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
9-213 |
1.31e-71 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 222.28 E-value: 1.31e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 9 PAISLSNIYKCYGAgagkVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQlav 88
Cdd:COG3842 4 PALELENVSKRYGD----VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 89 iRGkhLGFIFQFFNLMPVLNVFDNVYFPLVLNGqFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAH 168
Cdd:COG3842 77 -RN--VGMVFQDYALFPHLTVAENVAFGLRMRG-VPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15830546 169 EPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSE 213
Cdd:COG3842 153 EPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQE 197
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
11-230 |
1.45e-71 |
|
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: 218.22 E-value: 1.45e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGAGAGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAVIR 90
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 gKHLGFIFQFFNLMPVLNVFDNVYFPLVLNGQfSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEP 170
Cdd:cd03258 82 -RRIGMIFQHFNLLSSRTVFENVALPLEIAGV-PKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830546 171 MVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSE-LKARARRVVEIQDGVLI 230
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEvVKRICDRVAVMEKGEVV 220
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
9-232 |
5.40e-70 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 214.54 E-value: 5.40e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 9 PAISLSNIYKCYgagAGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAV 88
Cdd:COG3638 1 PMLELRNLSKRY---PGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 89 IRGKhLGFIFQFFNLMPVLNVFDNV------YFPLV--LNGQFSKKEaTERTLHYLDSVGLSGFGDRKPGQLSGGQQQRV 160
Cdd:COG3638 78 LRRR-IGMIFQQFNLVPRLSVLTNVlagrlgRTSTWrsLLGLFPPED-RERALEALERVGLADKAYQRADQLSGGQQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830546 161 AIARALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSELkAR--ARRVVEIQDGVLIHD 232
Cdd:COG3638 156 AIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDL-ARryADRIIGLRDGRVVFD 228
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
11-227 |
1.21e-69 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 212.49 E-value: 1.21e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGAGagkVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAVIR 90
Cdd:TIGR02673 2 IEFHNVSKAYPGG---VAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 gKHLGFIFQFFNLMPVLNVFDNVYFPLVLNGQfSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEP 170
Cdd:TIGR02673 79 -RRIGVVFQDFRLLPDRTVYENVALPLEVRGK-KEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15830546 171 MVVIADEPTGNLDLATGEAILDLLLTINQQtGTTFVISTHSSEL-KARARRVVEIQDG 227
Cdd:TIGR02673 157 PLLLADEPTGNLDPDLSERILDLLKRLNKR-GTTVIVATHDLSLvDRVAHRVIILDDG 213
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
11-229 |
6.25e-69 |
|
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: 210.73 E-value: 6.25e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGAGagkVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAVIR 90
Cdd:cd03292 1 IEFINVTKTYPNG---TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 gKHLGFIFQFFNLMPVLNVFDNVYFPLVLNGQfSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEP 170
Cdd:cd03292 78 -RKIGVVFQDFRLLPDRNVYENVAFALEVTGV-PPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 171 MVVIADEPTGNLDLATGEAILDLLLTINQQtGTTFVISTHSSELKARAR-RVVEIQDGVL 229
Cdd:cd03292 156 TILIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRhRVIALERGKL 214
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
11-229 |
2.25e-68 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 209.57 E-value: 2.25e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGAGAGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAVIR 90
Cdd:NF038007 2 LNMQNAEKCYITKTIKTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 GKHLGFIFQFFNLMPVLNVFDNVYFPLVLNGqFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEP 170
Cdd:NF038007 82 RELIGYIFQSFNLIPHLSIFDNVALPLKYRG-VAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15830546 171 MVVIADEPTGNLDLATGEAILDLLLTINQQtGTTFVISTHSSELKARARRVVEIQDGVL 229
Cdd:NF038007 161 ALLLADEPTGNLDSKNARAVLQQLKYINQK-GTTIIMVTHSDEASTYGNRIINMKDGKL 218
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
11-235 |
5.53e-68 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 209.08 E-value: 5.53e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGagagKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNqLPEEQLAVIR 90
Cdd:COG1126 2 IEIENLHKSFG----DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 gKHLGFIFQFFNLMPVLNVFDNVYFPLVLNGQFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEP 170
Cdd:COG1126 77 -RKVGMVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 171 MVVIADEPTGNLD--LaTGEaILDLLLTInQQTGTTFVISTHssELK-AR--ARRVVEIQDGVLIHDSDA 235
Cdd:COG1126 156 KVMLFDEPTSALDpeL-VGE-VLDVMRDL-AKEGMTMVVVTH--EMGfARevADRVVFMDGGRIVEEGPP 220
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
9-232 |
2.15e-67 |
|
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: 207.52 E-value: 2.15e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 9 PAISLSNIYKCYGagaGKVdALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAV 88
Cdd:COG1127 4 PMIEVRNLTKSFG---DRV-VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 89 IRgKHLGFIFQF---FNLMpvlNVFDNVYFPLVLNGQFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARA 165
Cdd:COG1127 80 LR-RRIGMLFQGgalFDSL---TVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15830546 166 LAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHS-SELKARARRVVEIQDGVLIHD 232
Cdd:COG1127 156 LALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDlDSAFAIADRVAVLADGKIIAE 223
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
7-232 |
3.67e-67 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 206.98 E-value: 3.67e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 7 SLPAISLSNIYKCYGAGAGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQL 86
Cdd:PRK11629 2 NKILLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 87 AVIRGKHLGFIFQFFNLMPVLNVFDNVYFPLVLNGQfSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARAL 166
Cdd:PRK11629 82 AELRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKK-KPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15830546 167 AHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSELKARARRVVEIQDGVLIHD 232
Cdd:PRK11629 161 VNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAE 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
9-230 |
1.93e-66 |
|
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: 213.61 E-value: 1.93e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 9 PAISLSNIYKCYGA-GAGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLA 87
Cdd:COG1123 259 PLLEVRNLSKRYPVrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 88 VIRgKHLGFIFQ--FFNLMPVLNVFDNVYFPLVLNGQFSKKEATERTLHYLDSVGLS-GFGDRKPGQLSGGQQQRVAIAR 164
Cdd:COG1123 339 ELR-RRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830546 165 ALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSELKAR-ARRVVEIQDGVLI 230
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIV 484
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
11-232 |
3.24e-65 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 202.03 E-value: 3.24e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGAGagkVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAVIR 90
Cdd:cd03256 1 IEVENLSKTYPNG---KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 gKHLGFIFQFFNLMPVLNVFDNVYFPL--------VLNGQFSKKEaTERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAI 162
Cdd:cd03256 78 -RQIGMIFQQFNLIERLSVLENVLSGRlgrrstwrSLFGLFPKEE-KQRALAALERVGLLDKAYQRADQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830546 163 ARALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSEL-KARARRVVEIQDGVLIHD 232
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLaREYADRIVGLKDGRIVFD 226
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
11-230 |
6.09e-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: 198.13 E-value: 6.09e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGagagKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQlavir 90
Cdd:cd03259 1 LELKGLSKTYG----SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 gKHLGFIFQFFNLMPVLNVFDNVYFPLVLNGqFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEP 170
Cdd:cd03259 72 -RNIGMVFQDYALFPHLTVAENIAFGLKLRG-VPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830546 171 MVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHS-SELKARARRVVEIQDGVLI 230
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDqEEALALADRIAVMNEGRIV 210
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
10-210 |
1.03e-63 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 201.84 E-value: 1.03e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 10 AISLSNIYKCYGagagKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQlavi 89
Cdd:COG3839 3 SLELENVSKSYG----GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 90 RGkhLGFIFQFFNLMPVLNVFDNVYFPLVLNGqFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHE 169
Cdd:COG3839 75 RN--IAMVFQSYALYPHMTVYENIAFPLKLRK-VPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVRE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15830546 170 PMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTH 210
Cdd:COG3839 152 PKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTH 192
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
11-210 |
1.22e-63 |
|
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: 197.73 E-value: 1.22e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGAGAGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAvIR 90
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRK-IR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 GKHLGFIFQ--FFNLMPVLNVFDNVYFPLVLNGQFSKKEATERTLHY-LDSVGLS-GFGDRKPGQLSGGQQQRVAIARAL 166
Cdd:cd03257 81 RKEIQMVFQdpMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLlLVGVGLPeEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15830546 167 AHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTH 210
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITH 204
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
11-230 |
3.76e-63 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 200.03 E-value: 3.76e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGAGAGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAVIR 90
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 gKHLGFIFQFFNLMPVLNVFDNVYFPLVLNGQfSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEP 170
Cdd:PRK11153 82 -RQIGMIFQHFNLLSSRTVFDNVALPLELAGT-PKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830546 171 MVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSE-LKARARRVVEIQDGVLI 230
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDvVKRICDRVAVIDAGRLV 220
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
18-229 |
4.30e-63 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 196.54 E-value: 4.30e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 18 KCYGAGAGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAVIRGKHLGFI 97
Cdd:PRK10584 14 KSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKHVGFV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 98 FQFFNLMPVLNVFDNVYFPLVLNGQfSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADE 177
Cdd:PRK10584 94 FQSFMLIPTLNALENVELPALLRGE-SSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15830546 178 PTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSELKARARRVVEIQDGVL 229
Cdd:PRK10584 173 PTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
11-213 |
3.64e-62 |
|
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: 193.99 E-value: 3.64e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGAGAgkvdALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQlavir 90
Cdd:cd03300 1 IELENVSKFYGGFV----ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 gKHLGFIFQFFNLMPVLNVFDNVYFPLVLNGqFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEP 170
Cdd:cd03300 72 -RPVNTVFQNYALFPHLTVFENIAFGLRLKK-LPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15830546 171 MVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSE 213
Cdd:cd03300 150 KVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQE 192
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
11-229 |
6.51e-62 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 192.74 E-value: 6.51e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGagagKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQlPEEQLAVIR 90
Cdd:cd03262 1 IEIKNLHKSFG----DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 gKHLGFIFQFFNLMPVLNVFDNVYFPLVLNGQFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEP 170
Cdd:cd03262 76 -QKVGMVFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830546 171 MVVIADEPTGNLDlatGEAILDLLLTINQ--QTGTTFVISTHssELK-AR--ARRVVEIQDGVL 229
Cdd:cd03262 155 KVMLFDEPTSALD---PELVGEVLDVMKDlaEEGMTMVVVTH--EMGfARevADRVIFMDDGRI 213
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
11-232 |
6.75e-62 |
|
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: 193.32 E-value: 6.75e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGagaGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNqlpEEQLAVIR 90
Cdd:COG1122 1 IELENLSFSYP---GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDIT---KKNLRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 gKHLGFIFQ-----FFnlMPvlNVFDNVYFPLvLNGQFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARA 165
Cdd:COG1122 75 -RKVGLVFQnpddqLF--AP--TVEEDVAFGP-ENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15830546 166 LAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQtGTTFVISTHSSELKAR-ARRVVEIQDGVLIHD 232
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAElADRVIVLDDGRIVAD 215
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
11-230 |
9.08e-62 |
|
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: 193.10 E-value: 9.08e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGagaGKVdALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAVIR 90
Cdd:cd03261 1 IELRGLTKSFG---GRT-VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 gKHLGFIFQFFNLMPVLNVFDNVYFPLVLNGQFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEP 170
Cdd:cd03261 77 -RRMGMLFQSGALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830546 171 MVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHS-SELKARARRVVEIQDGVLI 230
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDlDTAFAIADRIAVLYDGKIV 216
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
12-227 |
6.28e-61 |
|
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: 190.37 E-value: 6.28e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 12 SLSNIYKCYGAGAGKvdALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAvirg 91
Cdd:cd03225 1 ELKNLSFSYPDGARP--ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELR---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 92 KHLGFIFQ-----FFNLmpvlNVFDNVYFPLvLNGQFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARAL 166
Cdd:cd03225 75 RKVGLVFQnpddqFFGP----TVEEEVAFGL-ENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830546 167 AHEPMVVIADEPTGNLDLATGEAILDLLLTINQQtGTTFVISTHS-SELKARARRVVEIQDG 227
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDlDLLLELADRVIVLEDG 210
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
13-235 |
7.08e-61 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 201.88 E-value: 7.08e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 13 LSNIYKCYGAGAGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAVIRGK 92
Cdd:PRK10535 7 LKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 93 HLGFIFQFFNLMPVLNVFDNVYFPLVLNGqFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMV 172
Cdd:PRK10535 87 HFGFIFQRYHLLSHLTAAQNVEVPAVYAG-LERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQV 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15830546 173 VIADEPTGNLDLATGEAILDLLLTINQQtGTTFVISTHSSELKARARRVVEIQDGVLIHDSDA 235
Cdd:PRK10535 166 ILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPA 227
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
11-232 |
1.45e-59 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 187.89 E-value: 1.45e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGAGagkVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAVIR 90
Cdd:TIGR02315 2 LEVENLSKVYPNG---KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 gKHLGFIFQFFNLMPVLNVFDNVYFPLV--------LNGQFSKKEaTERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAI 162
Cdd:TIGR02315 79 -RRIGMIFQHYNLIERLTVLENVLHGRLgykptwrsLLGRFSEED-KERALSALERVGLADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830546 163 ARALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSEL-KARARRVVEIQDGVLIHD 232
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLaKKYADRIVGLKAGEIVFD 227
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
11-230 |
1.83e-59 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 187.19 E-value: 1.83e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGagagKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTViflnKLLNQLPEEQLAVIR 90
Cdd:COG1131 1 IEVRGLTKRYG----DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEV----RVLGEDVARDPAEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 gKHLGFIFQFFNLMPVLNVFDNVYFPLVLNGqFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEP 170
Cdd:COG1131 73 -RRIGYVPQEPALYPDLTVRENLRFFARLYG-LPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830546 171 MVVIADEPTGNLDLATGEAILDLLLTINQQtGTTFVISTHS-SELKARARRVVEIQDGVLI 230
Cdd:COG1131 151 ELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYlEEAERLCDRVAIIDKGRIV 210
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
10-230 |
5.20e-59 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 186.55 E-value: 5.20e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 10 AISLSNIYKCYGAGAGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAvi 89
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 90 rgKHLGFIFQ--FFNLMPVLNVFDNVYFPLVLNGqfsKKEATERTLHYLDSVGL-SGFGDRKPGQLSGGQQQRVAIARAL 166
Cdd:COG1124 79 --RRVQMVFQdpYASLHPRHTVDRILAEPLRIHG---LPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15830546 167 AHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSELKAR-ARRVVEIQDGVLI 230
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIV 218
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
13-224 |
2.07e-58 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 183.59 E-value: 2.07e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 13 LSNIYKCYGagaGKVdALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAVIRGK 92
Cdd:TIGR03608 1 LKNISKKFG---DKV-ILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 93 HLGFIFQFFNLMPVLNVFDNVYFPLVLNgQFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMV 172
Cdd:TIGR03608 77 KLGYLFQNFALIENETVEENLDLGLKYK-KLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15830546 173 VIADEPTGNLDLATGEAILDLLLTINQQtGTTFVISTHSSELKARARRVVEI 224
Cdd:TIGR03608 156 ILADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDPEVAKQADRVIEL 206
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
11-210 |
1.70e-57 |
|
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: 184.87 E-value: 1.70e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGAGAGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKP---TSGTVIFLNKLLNQLPEEQLA 87
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 88 VIRGKHLGFIFQ--FFNLMPVLNVFDNVYFPLVLNGQFSKKEATERTLHYLDSVGLSG---FGDRKPGQLSGGQQQRVAI 162
Cdd:COG0444 82 KIRGREIQMIFQdpMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDperRLDRYPHELSGGMRQRVMI 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15830546 163 ARALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTH 210
Cdd:COG0444 162 ARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITH 209
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
9-213 |
3.36e-57 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 182.37 E-value: 3.36e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 9 PAISLSNIYKCYGAGAGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTViflnkLLNQLPEEQLAV 88
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEI-----TLDGVPVTGPGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 89 IRGkhlgFIFQFFNLMPVLNVFDNVYFPLVLNGQfSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAH 168
Cdd:COG4525 77 DRG----VVFQKDALLPWLNVLDNVAFGLRLRGV-PKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15830546 169 EPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSE 213
Cdd:COG4525 152 DPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVE 196
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
11-230 |
1.12e-55 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 181.11 E-value: 1.12e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGAgagkVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLN-QLPeeqlavI 89
Cdd:COG1118 3 IEVRNISKRFGS----FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtNLP------P 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 90 RGKHLGFIFQFFNLMPVLNVFDNVYFPL-VLNGqfSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAH 168
Cdd:COG1118 73 RERRVGFVFQHYALFPHMTVAENIAFGLrVRPP--SKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15830546 169 EPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSELKAR-ARRVVEIQDGVLI 230
Cdd:COG1118 151 EPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALElADRVVVMNQGRIE 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
9-235 |
3.93e-55 |
|
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: 183.95 E-value: 3.93e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 9 PAISLSNIykCYGAGAGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPT---SGTVIFLNKLLNQLPEEq 85
Cdd:COG1123 3 PLLEVRDL--SVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 86 lavIRGKHLGFIFQFF--NLMPVlNVFDNVYFPLvLNGQFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIA 163
Cdd:COG1123 80 ---LRGRRIGMVFQDPmtQLNPV-TVGDQIAEAL-ENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15830546 164 RALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSELKAR-ARRVVEIQDGVLIHDSDA 235
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPP 227
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
11-227 |
2.86e-53 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 169.68 E-value: 2.86e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGagagKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLpEEQLAVIR 90
Cdd:cd03229 1 LELKNVSKRYG----QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDL-EDELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 gKHLGFIFQFFNLMPVLNVFDNVYFPlvlngqfskkeatertlhyldsvglsgfgdrkpgqLSGGQQQRVAIARALAHEP 170
Cdd:cd03229 76 -RRIGMVFQDFALFPHLTVLENIALG-----------------------------------LSGGQQQRVALARALAMDP 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15830546 171 MVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHS-SELKARARRVVEIQDG 227
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDlDEAARLADRVVVLRDG 177
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
11-229 |
5.17e-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: 170.13 E-value: 5.17e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGagagKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQlavir 90
Cdd:cd03301 1 VELENVTKRFG----NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 gKHLGFIFQFFNLMPVLNVFDNVYFPLVLNGqFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEP 170
Cdd:cd03301 72 -RDIAMVFQNYALYPHMTVYDNIAFGLKLRK-VPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 171 MVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHS-SELKARARRVVEIQDGVL 229
Cdd:cd03301 150 KVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDqVEAMTMADRIAVMNDGQI 209
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-213 |
7.32e-53 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 174.75 E-value: 7.32e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 1 MQSTIKSLPAISLSNIYKCYGagaGKvDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQ 80
Cdd:PRK09452 5 NKQPSSLSPLVELRGISKSFD---GK-EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 81 LPEEQlavirgKHLGFIFQFFNLMPVLNVFDNVYFPLVLNgQFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRV 160
Cdd:PRK09452 81 VPAEN------RHVNTVFQSYALFPHMTVFENVAFGLRMQ-KTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15830546 161 AIARALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSE 213
Cdd:PRK09452 154 AIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQE 206
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
11-232 |
9.88e-53 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 171.48 E-value: 9.88e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGAG-AGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAVI 89
Cdd:TIGR04521 1 IKLKNVSYIYQPGtPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 90 RgKHLGFIFQF-----FNLmpvlNVFDNVYF-PLvlNGQFSKKEATERTLHYLDSVGLS-GFGDRKPGQLSGGQQQRVAI 162
Cdd:TIGR04521 81 R-KKVGLVFQFpehqlFEE----TVYKDIAFgPK--NLGLSEEEAEERVKEALELVGLDeEYLERSPFELSGGQMRRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830546 163 ARALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSELKAR-ARRVVEIQDGVLIHD 232
Cdd:TIGR04521 154 AGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEyADRVIVMHKGKIVLD 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
11-230 |
2.17e-52 |
|
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: 170.13 E-value: 2.17e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYG-----------AGAGKVDALKS---------INLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGT 70
Cdd:cd03294 1 IKIKGLYKIFGknpqkafkllaKGKSKEEILKKtgqtvgvndVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 71 VIFLNKLLNQLPEEQLAVIRGKHLGFIFQFFNLMPVLNVFDNVYFPLVLNGQfSKKEATERTLHYLDSVGLSGFGDRKPG 150
Cdd:cd03294 81 VLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVLENVAFGLEVQGV-PRAEREERAAEALELVGLEGWEHKYPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 151 QLSGGQQQRVAIARALAHEPMVVIADEPTGNLD-LATGEaILDLLLTINQQTGTTFVISTHSSELKAR-ARRVVEIQDGV 228
Cdd:cd03294 160 ELSGGMQQRVGLARALAVDPDILLMDEAFSALDpLIRRE-MQDELLRLQAELQKTIVFITHDLDEALRlGDRIAIMKDGR 238
|
..
gi 15830546 229 LI 230
Cdd:cd03294 239 LV 240
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
10-235 |
1.44e-50 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 164.80 E-value: 1.44e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 10 AISLSNIYKCYGagagKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNK---LLNQLPEEQL 86
Cdd:COG4161 2 SIQLKNINCFYG----SHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdFSQKPSEKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 87 AVIRGKhLGFIFQFFNLMPVLNVFDN-VYFPLVLNGQfSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARA 165
Cdd:COG4161 78 RLLRQK-VGMVFQQYNLWPHLTVMENlIEAPCKVLGL-SKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830546 166 LAHEPMVVIADEPTGNLDLATGEAILDLLLTInQQTGTTFVISTHSSELkAR--ARRVVEIQDGVLIHDSDA 235
Cdd:COG4161 156 LMMEPQVLLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVEF-ARkvASQVVYMEKGRIIEQGDA 225
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
7-229 |
5.38e-50 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 166.75 E-value: 5.38e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 7 SLPAISLSNIYKCYGAGAgkvdALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQl 86
Cdd:TIGR03265 1 SSPYLSIDNIRKRFGAFT----ALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQK- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 87 avirgKHLGFIFQFFNLMPVLNVFDNVYFPLVlNGQFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARAL 166
Cdd:TIGR03265 76 -----RDYGIVFQSYALFPNLTVADNIAYGLK-NRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARAL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830546 167 AHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTH-SSELKARARRVVEIQDGVL 229
Cdd:TIGR03265 150 ATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHdQEEALSMADRIVVMNHGVI 213
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
10-235 |
6.83e-50 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 163.26 E-value: 6.83e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 10 AISLSNIYKCYGAGagkvDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNK---LLNQLPEEQL 86
Cdd:PRK11124 2 SIQLNGINCFYGAH----QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfdFSKTPSDKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 87 AVIRgKHLGFIFQFFNLMPVLNVFDN-VYFPLVLNGqFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARA 165
Cdd:PRK11124 78 RELR-RNVGMVFQQYNLWPHLTVQQNlIEAPCRVLG-LSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830546 166 LAHEPMVVIADEPTGNLDLATGEAILDLLLTInQQTGTTFVISTHSSELkAR--ARRVVEIQDGVLIHDSDA 235
Cdd:PRK11124 156 LMMEPQVLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEV-ARktASRVVYMENGHIVEQGDA 225
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
10-213 |
7.60e-50 |
|
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: 162.89 E-value: 7.60e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 10 AISLSNIYKCYGAgagkVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPeeqlavI 89
Cdd:cd03296 2 SIEVRNVSKRFGD----FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP------V 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 90 RGKHLGFIFQFFNLMPVLNVFDNVYFPLVL---NGQFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARAL 166
Cdd:cd03296 72 QERNVGFVFQHYALFRHMTVFDNVAFGLRVkprSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARAL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15830546 167 AHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSE 213
Cdd:cd03296 152 AVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQE 198
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
9-233 |
9.22e-49 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 160.25 E-value: 9.22e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 9 PAISLSNIYKCYGagagKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQlpeeqlav 88
Cdd:COG1121 5 PAIELENLTVSYG----GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 89 iRGKHLGFIFQFFNL---MPVlNVFDnvyfpLVLNG--------QFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQ 157
Cdd:COG1121 73 -ARRRIGYVPQRAEVdwdFPI-TVRD-----VVLMGrygrrglfRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830546 158 QRVAIARALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQtGTTFVISTHS-SELKARARRVVEIQDGVLIHDS 233
Cdd:COG1121 146 QRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDlGAVREYFDRVLLLNRGLVAHGP 221
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
11-210 |
2.02e-48 |
|
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: 159.39 E-value: 2.02e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGAGAgkvDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAvir 90
Cdd:cd03295 1 IEFENVTKRYGGGK---KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELR--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 gKHLGFIFQFFNLMPVLNVFDNVYFPLVLNGqFSKKEATERTLHYLDSVGL--SGFGDRKPGQLSGGQQQRVAIARALAH 168
Cdd:cd03295 75 -RKIGYVIQQIGLFPHMTVEENIALVPKLLK-WPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15830546 169 EPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTH 210
Cdd:cd03295 153 DPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTH 194
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
10-232 |
4.77e-48 |
|
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: 158.67 E-value: 4.77e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 10 AISLSNIykcyGAGAGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAvi 89
Cdd:COG1120 1 MLEAENL----SVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELA-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 90 rgKHLGFIFQFFNLMPVLNVFDNVY---FP-LVLNGQFSKKEAtERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARA 165
Cdd:COG1120 75 --RRIAYVPQEPPAPFGLTVRELVAlgrYPhLGLFGRPSAEDR-EAVEEALERTGLEHLADRPVDELSGGERQRVLIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15830546 166 LAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSELKAR-ARRVVEIQDGVLIHD 232
Cdd:COG1120 152 LAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARyADRLVLLKDGRIVAQ 219
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
11-232 |
6.50e-48 |
|
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: 158.10 E-value: 6.50e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGagagKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLavir 90
Cdd:COG4555 2 IEVENLSKKYG----KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREAR---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 gKHLGFIFQFFNLMPVLNVFDNVYFPLVLNGQFsKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEP 170
Cdd:COG4555 74 -RQIGVLPDERGLYDRLTVRENIRYFAELYGLF-DEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15830546 171 MVVIADEPTGNLDLATGEAILDLLLTINQQtGTTFVISTHS-SELKARARRVVEIQDGVLIHD 232
Cdd:COG4555 152 KVLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHImQEVEALCDRVVILHKGKVVAQ 213
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
9-183 |
8.51e-48 |
|
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: 8.51e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 9 PAISLSNIYKCYGAgagkVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIF--------LNKLLNQ 80
Cdd:COG4598 7 PALEVRDLHKSFGD----LEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVggeeirlkPDRDGEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 81 LPEE--QLAVIRGKhLGFIFQFFNLMPVLNVFDNVYF-PLVLNGQfSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQ 157
Cdd:COG4598 83 VPADrrQLQRIRTR-LGMVFQSFNLWSHMTVLENVIEaPVHVLGR-PKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQ 160
|
170 180
....*....|....*....|....*.
gi 15830546 158 QRVAIARALAHEPMVVIADEPTGNLD 183
Cdd:COG4598 161 QRAAIARALAMEPEVMLFDEPTSALD 186
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
30-179 |
1.42e-46 |
|
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: 151.65 E-value: 1.42e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 30 LKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLavirGKHLGFIFQFFNLMPVLNV 109
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSL----RKEIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830546 110 FDNVYFPLVLNGqFSKKEATERTLHYLDSVGLSGFGDRK----PGQLSGGQQQRVAIARALAHEPMVVIADEPT 179
Cdd:pfam00005 77 RENLRLGLLLKG-LSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
11-230 |
2.08e-46 |
|
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: 153.49 E-value: 2.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGagagKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGI-----DKPTSGTVIFLNKLLNQLPEEQ 85
Cdd:cd03260 1 IELRDLNVYYG----DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 86 LAVIRGkhLGFIFQFFNLMPvLNVFDNVYFPLVLNGQFSKKEATERTLHYLDSVGLSG-FGDR-KPGQLSGGQQQRVAIA 163
Cdd:cd03260 77 LELRRR--VGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDeVKDRlHALGLSGGQQQRLCLA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15830546 164 RALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQtgTTFVISTHSSELKAR-ARRVVEIQDGVLI 230
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARvADRTAFLLNGRLV 219
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
30-229 |
2.63e-46 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 152.66 E-value: 2.63e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 30 LKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLaviRgKHLGFIFQffnlMPVL-- 107
Cdd:COG4619 16 LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEW---R-RQVAYVPQ----EPALwg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 108 -NVFDNVYFPLVLNGqfsKKEATERTLHYLDSVGLS-GFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNLDLA 185
Cdd:COG4619 88 gTVRDNLPFPFQLRE---RKFDRERALELLERLGLPpDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPE 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15830546 186 TGEAILDLLLTINQQTGTTFVISTHSSELKAR-ARRVVEIQDGVL 229
Cdd:COG4619 165 NTRRVEELLREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
30-235 |
3.61e-46 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 153.75 E-value: 3.61e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 30 LKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTV------IFLNKLLNQlpeeQLAVIRG--KHLGFIFQFF 101
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgditIDTARSLSQ----QKGLIRQlrQHVGFVFQNF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 102 NLMPVLNVFDNVY-FPLVLNGQfSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTG 180
Cdd:PRK11264 95 NLFPHRTVLENIIeGPVIVKGE-PKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTS 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15830546 181 NLDlatGEAILDLLLTINQ--QTGTTFVISTHSSELkAR--ARRVVEIQDGVLIHDSDA 235
Cdd:PRK11264 174 ALD---PELVGEVLNTIRQlaQEKRTMVIVTHEMSF-ARdvADRAIFMDQGRIVEQGPA 228
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
11-229 |
5.51e-46 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 150.63 E-value: 5.51e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGagagKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLavir 90
Cdd:cd03230 1 IEVRNLSKRYG----KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVK---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 gKHLGFIFQFFNLMPVLNVFDNVYfplvlngqfskkeatertlhyldsvglsgfgdrkpgqLSGGQQQRVAIARALAHEP 170
Cdd:cd03230 73 -RRIGYLPEEPSLYENLTVRENLK-------------------------------------LSGGMKQRLALAQALLHDP 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 171 MVVIADEPTGNLDLATGEAILDLLLTINQQtGTTFVISTHS-SELKARARRVVEIQDGVL 229
Cdd:cd03230 115 ELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHIlEEAERLCDRVAILNNGRI 173
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
11-232 |
7.19e-46 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 152.22 E-value: 7.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGagagkvDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAVir 90
Cdd:COG3840 2 LRLDDLTYRYG------DFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPV-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 gkhlGFIFQFFNLMPVLNVFDNVYFPLVLNGQFSKKEaTERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEP 170
Cdd:COG3840 74 ----SMLFQENNLFPHLTVAQNIGLGLRPGLKLTAEQ-RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15830546 171 MVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSELKAR-ARRVVEIQDGVLIHD 232
Cdd:COG3840 149 PILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARiADRVLLVADGRIAAD 211
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
11-234 |
8.10e-46 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 152.55 E-value: 8.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGagagKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQlPEEQLAVIR 90
Cdd:PRK09493 2 IEFKNVSKHFG----PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVND-PKVDERLIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 gKHLGFIFQFFNLMPVLNVFDNVYF-PLVLNGQfSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHE 169
Cdd:PRK09493 77 -QEAGMVFQQFYLFPHLTALENVMFgPLRVRGA-SKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830546 170 PMVVIADEPTGNLDLATGEAILDLLLTINQQtGTTFVISTHSSELkAR--ARRVVEIQDGVLIHDSD 234
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGF-AEkvASRLIFIDKGRIAEDGD 219
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
11-232 |
8.52e-45 |
|
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: 150.66 E-value: 8.52e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGAGagKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNklLNQLPEEQLAVIR 90
Cdd:TIGR04520 1 IEVENVSFSYPES--EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENLWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 gKHLGFIFQffnlmpvlN---------VFDNVYFPLVlNGQFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVA 161
Cdd:TIGR04520 77 -KKVGMVFQ--------NpdnqfvgatVEDDVAFGLE-NLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830546 162 IARALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTfVIS-THSSELKARARRVVEIQDGVLIHD 232
Cdd:TIGR04520 147 IAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGIT-VISiTHDMEEAVLADRVIVMNKGKIVAE 217
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
30-227 |
1.12e-44 |
|
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: 149.15 E-value: 1.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 30 LKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAVirgkhlgfiFQFFNLMPVLNV 109
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVV---------FQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 110 FDNVYFPL-VLNGQFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNLDLATGE 188
Cdd:TIGR01184 72 RENIALAVdRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15830546 189 AILDLLLTINQQTGTTFVISTHS-SELKARARRVVEIQDG 227
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHDvDEALLLSDRVVMLTNG 191
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
25-210 |
1.21e-44 |
|
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: 149.51 E-value: 1.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 25 GKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAvirgkHLGFI--FQFFN 102
Cdd:cd03219 11 GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIA-----RLGIGrtFQIPR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 103 LMPVLNVFDNV---------YFPLVLNGQFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVV 173
Cdd:cd03219 86 LFPELTVLENVmvaaqartgSGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 15830546 174 IADEPTGNLDLATGEAILDLLLTINQQtGTTFVISTH 210
Cdd:cd03219 166 LLDEPAAGLNPEETEELAELIRELRER-GITVLLVEH 201
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
11-210 |
1.41e-44 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 151.40 E-value: 1.41e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGagaGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLaviR 90
Cdd:COG1125 2 IEFENVTKRYP---DGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVEL---R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 gKHLGFIFQFFNLMPVLNVFDNVYFPLVLNGqFSKKEATERTLHYLDSVGL--SGFGDRKPGQLSGGQQQRVAIARALAH 168
Cdd:COG1125 76 -RRIGYVIQQIGLFPHMTVAENIATVPRLLG-WDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15830546 169 EPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTH 210
Cdd:COG1125 154 DPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTH 195
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
30-231 |
1.65e-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: 149.02 E-value: 1.65e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 30 LKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQlaviRGKhlGFIFQFFNLMPVLNV 109
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK----RDI--SYVPQNYALFPHMTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 110 FDNVYFPLVLNgQFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNLDLATGEA 189
Cdd:cd03299 89 YKNIAYGLKKR-KVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEK 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15830546 190 ILDLLLTINQQTGTTFVISTHS-SELKARARRVVEIQDGVLIH 231
Cdd:cd03299 168 LREELKKIRKEFGVTVLHVTHDfEEAWALADKVAIMLNGKLIQ 210
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
12-232 |
8.03e-44 |
|
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: 145.27 E-value: 8.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 12 SLSNIYKCYGagagKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAvirg 91
Cdd:cd03214 1 EVENLSVGYG----GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELA---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 92 KHLGFIFQffnlmpvlnvfdnvyfplvlngqfskkeatertlhYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPM 171
Cdd:cd03214 73 RKIAYVPQ-----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPP 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830546 172 VVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSELKAR-ARRVVEIQDGVLIHD 232
Cdd:cd03214 118 ILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARyADRVILLKDGRIVAQ 179
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
9-207 |
1.46e-43 |
|
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: 147.11 E-value: 1.46e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 9 PAISLSNIYKCYGAgagkVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAv 88
Cdd:COG0411 3 PLLEVRGLTKRFGG----LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIA- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 89 irgkHLGFI--FQFFNLMPVLNVFDNV-----------YFPLVLNGQFSKK---EATERTLHYLDSVGLSGFGDRKPGQL 152
Cdd:COG0411 78 ----RLGIArtFQNPRLFPELTVLENVlvaaharlgrgLLAALLRLPRARReerEARERAEELLERVGLADRADEPAGNL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15830546 153 SGGQQQRVAIARALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVI 207
Cdd:COG0411 154 SYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILL 208
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
45-234 |
1.47e-43 |
|
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: 149.18 E-value: 1.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 45 LCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQlavirgKHLGFIFQFFNLMPVLNVFDNVYFPLVLNGQfS 124
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHL------RHINMVFQSYALFPHMTVEENVAFGLKMRKV-P 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 125 KKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTT 204
Cdd:TIGR01187 74 RAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGIT 153
|
170 180 190
....*....|....*....|....*....|.
gi 15830546 205 FVISTH-SSELKARARRVVEIQDGVLIHDSD 234
Cdd:TIGR01187 154 FVFVTHdQEEAMTMSDRIAIMRKGKIAQIGT 184
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
21-210 |
8.94e-43 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 147.19 E-value: 8.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 21 GAGAGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAVIRgKHLGFIFQ- 99
Cdd:COG4608 25 GRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLR-RRMQMVFQd 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 100 -FFNLMPVLNVFDNVYFPLVLNGQFSKKEATERTLHYLDSVGLS-GFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADE 177
Cdd:COG4608 104 pYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRpEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDE 183
|
170 180 190
....*....|....*....|....*....|...
gi 15830546 178 PTGNLDLATGEAILDLLLTINQQTGTTFVISTH 210
Cdd:COG4608 184 PVSALDVSIQAQVLNLLEDLQDELGLTYLFISH 216
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
10-213 |
2.25e-42 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 144.07 E-value: 2.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 10 AISLSNIYKCYGagaGKvDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQlavi 89
Cdd:PRK11248 1 MLQISHLYADYG---GK-PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 90 rgkhlGFIFQFFNLMPVLNVFDNVYFPLVLNGqFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHE 169
Cdd:PRK11248 73 -----GVVFQNEGLLPWRNVQDNVAFGLQLAG-VEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAAN 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15830546 170 PMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSE 213
Cdd:PRK11248 147 PQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIE 190
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
20-230 |
3.60e-42 |
|
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: 149.83 E-value: 3.60e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 20 YGAGAGKVDALKSINLDINKGEFLALCGPSGSGKS----TLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAVIRGKHLG 95
Cdd:COG4172 16 FGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRIRGNRIA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 96 FIFQ--FFNLMPVLNVFDNVYFPLVLNGQFSKKEATERTLHYLDSVG-------LSGFgdrkPGQLSGGQQQRVAIARAL 166
Cdd:COG4172 96 MIFQepMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGipdperrLDAY----PHQLSGGQRQRVMIAMAL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15830546 167 AHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSELKAR-ARRVVEIQDGVLI 230
Cdd:COG4172 172 ANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRfADRVAVMRQGEIV 236
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
10-229 |
3.85e-42 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 146.38 E-value: 3.85e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 10 AISLSNIYKCYGagagKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEeqlavi 89
Cdd:PRK10851 2 SIEIANIKKSFG----RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 90 RGKHLGFIFQFFNLMPVLNVFDNVYFPL-VL------NGQFSKKEATErtlhYLDSVGLSGFGDRKPGQLSGGQQQRVAI 162
Cdd:PRK10851 72 RDRKVGFVFQHYALFRHMTVFDNIAFGLtVLprrerpNAAAIKAKVTQ----LLEMVQLAHLADRYPAQLSGGQKQRVAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15830546 163 ARALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSELKAR-ARRVVEIQDGVL 229
Cdd:PRK10851 148 ARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEvADRVVVMSQGNI 215
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
11-185 |
4.95e-42 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 146.33 E-value: 4.95e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGagagKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQlaviR 90
Cdd:PRK11000 4 VTLRNVTKAYG----DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 GkhLGFIFQFFNLMPVLNVFDNVYFPLVLNGQfSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEP 170
Cdd:PRK11000 76 G--VGMVFQSYALYPHLSVAENMSFGLKLAGA-KKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEP 152
|
170
....*....|....*
gi 15830546 171 MVVIADEPTGNLDLA 185
Cdd:PRK11000 153 SVFLLDEPLSNLDAA 167
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
11-229 |
7.08e-42 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 141.94 E-value: 7.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGAGAgkvDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAVIR 90
Cdd:PRK10908 2 IRFEHVSKAYLGGR---QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 gKHLGFIFQFFNLMPVLNVFDNVYFPLVLNGQfSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEP 170
Cdd:PRK10908 79 -RQIGMIFQDHHLLMDRTVYDNVAIPLIIAGA-SGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 171 MVVIADEPTGNLDLATGEAILDLLLTINqQTGTTFVISTHSSELKA-RARRVVEIQDGVL 229
Cdd:PRK10908 157 AVLLADEPTGNLDDALSEGILRLFEEFN-RVGVTVLMATHDIGLISrRSYRMLTLSDGHL 215
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
11-227 |
1.46e-41 |
|
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: 139.44 E-value: 1.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGAGAGKVdaLKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAvir 90
Cdd:cd03228 1 IEFKNVSFSYPGRPKPV--LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLR--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 gKHLGFIFQFFNLMPvLNVFDNVyfplvlngqfskkeatertlhyldsvglsgfgdrkpgqLSGGQQQRVAIARALAHEP 170
Cdd:cd03228 76 -KNIAYVPQDPFLFS-GTIRENI--------------------------------------LSGGQRQRIAIARALLRDP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15830546 171 MVVIADEPTGNLDLATGEAILDLLLTINQQTgTTFVIsTHSSELKARARRVVEIQDG 227
Cdd:cd03228 116 PILILDEATSALDPETEALILEALRALAKGK-TVIVI-AHRLSTIRDADRIIVLDDG 170
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
29-210 |
1.88e-41 |
|
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: 140.36 E-value: 1.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 29 ALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTViflnKLLNQLPEEQlavirGKHLGFIFQFFNL---MP 105
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSI----RVFGKPLEKE-----RKRIGYVPQRRSIdrdFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 106 VlNVFDNV----YFPLVLNGQFSKKEAtERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGN 181
Cdd:cd03235 85 I-SVRDVVlmglYGHKGLFRRLSKADK-AKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAG 162
|
170 180
....*....|....*....|....*....
gi 15830546 182 LDLATGEAILDLLLTINQQtGTTFVISTH 210
Cdd:cd03235 163 VDPKTQEDIYELLRELRRE-GMTILVVTH 190
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
30-233 |
4.97e-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: 139.35 E-value: 4.97e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 30 LKSINLDIN---KGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQ------LPEEQlavirgKHLGFIFQF 100
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkinLPPQQ------RKIGLVFQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 101 FNLMPVLNVFDNVYFPLVLNGQFSKKEATERTLhylDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTG 180
Cdd:cd03297 84 YALFPHLNVRENLAFGLKRKRNREDRISVDELL---DLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15830546 181 NLDLATGEAILDLLLTINQQTGTTFVISTHS-SELKARARRVVEIQDGVLIHDS 233
Cdd:cd03297 161 ALDRALRLQLLPELKQIKKNLNIPVIFVTHDlSEAEYLADRIVVMEDGRLQYIG 214
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
29-232 |
2.60e-40 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 138.99 E-value: 2.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 29 ALKSINLDINKGEFLALCGPSGSGKSTLLNILSGI---DKPTSGTVIFLNKLLNQlpEEQLAV-IRGK--HLGFIFQFFN 102
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQR--EGRLARdIRKSraNTGYIFQQFN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 103 LMPVLNVFDNVYFPLVLNGQFSK-------KEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIA 175
Cdd:PRK09984 97 LVNRLSVLENVLIGALGSTPFWRtcfswftREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILA 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15830546 176 DEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSELKAR-ARRVVEIQDGVLIHD 232
Cdd:PRK09984 177 DEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRyCERIVALRQGHVFYD 234
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
25-227 |
4.53e-40 |
|
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: 135.06 E-value: 4.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 25 GKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAvirgKHLGFIFQffnlm 104
Cdd:cd00267 10 GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELR----RRIGYVPQ----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 105 pvlnvfdnvyfplvlngqfskkeatertlhyldsvglsgfgdrkpgqLSGGQQQRVAIARALAHEPMVVIADEPTGNLDL 184
Cdd:cd00267 81 -----------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDP 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15830546 185 ATGEAILDLLLTINQQtGTTFVISTHSSELKARAR-RVVEIQDG 227
Cdd:cd00267 114 ASRERLLELLRELAEE-GRTVIIVTHDPELAELAAdRVIVLKDG 156
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
11-231 |
4.55e-40 |
|
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: 137.25 E-value: 4.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGAGagKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQlpeeQLAVIR 90
Cdd:cd03263 1 LQIRNLTKTYKKG--TKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT----DRKAAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 gKHLGFIFQFFNLMPVLNVFDNVYFPLVLNGqFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEP 170
Cdd:cd03263 75 -QSLGYCPQFDALFDELTVREHLRFYARLKG-LPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830546 171 MVVIADEPTGNLDLATGEAILDLLLTInqQTGTTFVISTHS-SELKARARRVVEIQDGVLIH 231
Cdd:cd03263 153 SVLLLDEPTSGLDPASRRAIWDLILEV--RKGRSIILTTHSmDEAEALCDRIAIMSDGKLRC 212
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
30-226 |
5.39e-40 |
|
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: 136.45 E-value: 5.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 30 LKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEqlaviRGKHLGFIFQFFNLMPVLNV 109
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED-----YRRRLAYLGHADGLKPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 110 FDNVYFplvLNGQFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNLDlATGEA 189
Cdd:COG4133 93 RENLRF---WAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALD-AAGVA 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 15830546 190 ILDLLLTINQQTGTTFVISTHsSELKARARRVVEIQD 226
Cdd:COG4133 169 LLAELIAAHLARGGAVLLTTH-QPLELAAARVLDLGD 204
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
11-227 |
1.49e-39 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 137.12 E-value: 1.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGAGAgkvdALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEqlavIR 90
Cdd:PRK11247 13 LLLNAVSKRYGERT----VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARED----TR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 gkhlgFIFQFFNLMPVLNVFDNVyfPLVLNGQFSkkeatERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEP 170
Cdd:PRK11247 85 -----LMFQDARLLPWKKVIDNV--GLGLKGQWR-----DAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15830546 171 MVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHS-SELKARARRVVEIQDG 227
Cdd:PRK11247 153 GLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDvSEAVAMADRVLLIEEG 210
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
9-230 |
1.50e-39 |
|
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: 142.97 E-value: 1.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 9 PAISLSNIYKCYGAGAgkvDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAv 88
Cdd:COG4988 335 PSIELEDVSFSYPGGR---PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWR- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 89 irgKHLGFIFQffnlMPVL---NVFDNVyfplvlngQFSKKEATERTLHY-LDSVGLSGFGDRKPG-----------QLS 153
Cdd:COG4988 411 ---RQIAWVPQ----NPYLfagTIRENL--------RLGRPDASDEELEAaLEAAGLDEFVAALPDgldtplgeggrGLS 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830546 154 GGQQQRVAIARALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQqtGTTFVISTHSSELKARARRVVEIQDGVLI 230
Cdd:COG4988 476 GGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQADRILVLDDGRIV 550
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
8-232 |
2.54e-39 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 136.74 E-value: 2.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 8 LPAISLSNIYKCYG--AGAGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQ 85
Cdd:PRK10419 4 LNVSGLSHHYAHGGlsGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 86 LAVIRGKhLGFIFQ----FFNlmPVLNVFDNVYFPLVLNGQFSKKEATERTLHYLDSVGLS-GFGDRKPGQLSGGQQQRV 160
Cdd:PRK10419 84 RKAFRRD-IQMVFQdsisAVN--PRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15830546 161 AIARALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSELKAR-ARRVVEIQDGVLIHD 232
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIVET 233
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
9-230 |
7.76e-39 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 141.06 E-value: 7.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 9 PAISLSNIYKCYGAGAGkvDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAv 88
Cdd:COG4987 332 PSLELEDVSFRYPGAGR--PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLR- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 89 irgKHLGFIFQ---FFNlMPVLNvfdnvyfplvlNGQFSKKEATERTL-HYLDSVGLSGFGDRKPG-----------QLS 153
Cdd:COG4987 409 ---RRIAVVPQrphLFD-TTLRE-----------NLRLARPDATDEELwAALERVGLGDWLAALPDgldtwlgeggrRLS 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830546 154 GGQQQRVAIARALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQqtGTTFVISTHSSELKARARRVVEIQDGVLI 230
Cdd:COG4987 474 GGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLERMDRILVLEDGRIV 548
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
10-234 |
9.37e-39 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 134.73 E-value: 9.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 10 AISLSNIYKCYGagagKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDK-----PTSGTVIFLNKLLNQlPEE 84
Cdd:TIGR00972 1 AIEIENLNLFYG----EKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDlvpgvRIEGKVLFDGQDIYD-KKI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 85 QLAVIRgKHLGFIFQFFNLMPvLNVFDNVYFPLVLNGQFSKKEATERTLHYLDSVGL----------SGFGdrkpgqLSG 154
Cdd:TIGR00972 76 DVVELR-RRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIKDKKELDEIVEESLKKAALwdevkdrlhdSALG------LSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 155 GQQQRVAIARALAHEPMVVIADEPTGNLD-LATGEaILDLLLTINQQtgTTFVISTHSSELKAR-ARRVVEIQDGVLIHD 232
Cdd:TIGR00972 148 GQQQRLCIARALAVEPEVLLLDEPTSALDpIATGK-IEELIQELKKK--YTIVIVTHNMQQAARiSDRTAFFYDGELVEY 224
|
..
gi 15830546 233 SD 234
Cdd:TIGR00972 225 GP 226
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
11-232 |
1.68e-38 |
|
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: 132.70 E-value: 1.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGAGagkvDALKSINLDINKGeFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEqlavIR 90
Cdd:cd03264 1 LQLENLTKRYGKK----RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK----LR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 gKHLGFIFQFFNLMPVLNVFDNVYFPLVLNGqFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEP 170
Cdd:cd03264 72 -RRIGYLPQEFGVYPNFTVREFLDYIAWLKG-IPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15830546 171 MVVIADEPTGNLDLATGEAILDLLltINQQTGTTFVISTH-SSELKARARRVVEIQDGVLIHD 232
Cdd:cd03264 150 SILIVDEPTAGLDPEERIRFRNLL--SELGEDRIVILSTHiVEDVESLCNQVAVLNKGKLVFE 210
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
35-227 |
4.85e-38 |
|
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: 131.85 E-value: 4.85e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 35 LDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAVirgkhlGFIFQFFNLMPVLNVFDNVY 114
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPV------SMLFQENNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 115 FPLVLNGQFSKkEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNLDLATGEAILDLL 194
Cdd:cd03298 93 LGLSPGLKLTA-EDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190
....*....|....*....|....*....|....
gi 15830546 195 LTINQQTGTTFVISTHS-SELKARARRVVEIQDG 227
Cdd:cd03298 172 LDLHAETKMTVLMVTHQpEDAKRLAQRVVFLDNG 205
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
11-234 |
1.63e-37 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 131.85 E-value: 1.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGAGA-----GKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQ 85
Cdd:TIGR02769 3 LEVRDVTHTYRTGGlfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 86 LAVIRgKHLGFIFQ----FFNlmPVLNVFDNVYFPLVLNGQFSKKEATERTLHYLDSVGL-SGFGDRKPGQLSGGQQQRV 160
Cdd:TIGR02769 83 RRAFR-RDVQLVFQdspsAVN--PRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15830546 161 AIARALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSELKAR-ARRVVEIQDGVLIHDSD 234
Cdd:TIGR02769 160 NIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEECD 234
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
10-183 |
3.84e-37 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 133.04 E-value: 3.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 10 AISLSNIYKCYgagAGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQL-PEEqlav 88
Cdd:PRK11650 3 GLKLQAVRKSY---DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELePAD---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 89 iRGkhLGFIFQFFNLMPVLNVFDNVYFPLVLNGqFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAH 168
Cdd:PRK11650 76 -RD--IAMVFQNYALYPHMSVRENMAYGLKIRG-MPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVR 151
|
170
....*....|....*
gi 15830546 169 EPMVVIADEPTGNLD 183
Cdd:PRK11650 152 EPAVFLFDEPLSNLD 166
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
30-224 |
4.92e-37 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 129.14 E-value: 4.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 30 LKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKP---TSGTVIFLNKLLNQLPEEQlavirgKHLGFIFQFFNLMPV 106
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQ------RRIGILFQDDLLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 107 LNVFDNVYFPLVlnGQFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNLDLAT 186
Cdd:COG4136 91 LSVGENLAFALP--PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAAL 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 15830546 187 GEAILDLLLTINQQTGTTFVISTHSSELKARARRVVEI 224
Cdd:COG4136 169 RAQFREFVFEQIRQRGIPALLVTHDEEDAPAAGRVLDL 206
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
11-234 |
5.36e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 131.75 E-value: 5.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGAG-AGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTV--IFLNKLLNQLPEEQLA 87
Cdd:PRK13651 3 IKVKNIVKIFNKKlPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewIFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 88 V-------------------IRgKHLGFIFQF--FNLMPVLNVFDNVYFPLVLNgqFSKKEATERTLHYLDSVGLS-GFG 145
Cdd:PRK13651 83 VleklviqktrfkkikkikeIR-RRVGVVFQFaeYQLFEQTIEKDIIFGPVSMG--VSKEEAKKRAAKYIELVGLDeSYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 146 DRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQtGTTFVISTHS-SELKARARRVVEI 224
Cdd:PRK13651 160 QRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDlDNVLEWTKRTIFF 238
|
250
....*....|
gi 15830546 225 QDGVLIHDSD 234
Cdd:PRK13651 239 KDGKIIKDGD 248
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
9-213 |
5.54e-37 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 133.42 E-value: 5.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 9 PAISLSNIYKCYGaGAGKVDalkSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQlav 88
Cdd:PRK11607 18 PLLEIRNLTKSFD-GQHAVD---DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 89 irgKHLGFIFQFFNLMPVLNVFDNVYFPLVLNgQFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAH 168
Cdd:PRK11607 91 ---RPINMMFQSYALFPHMTVEQNIAFGLKQD-KLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAK 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15830546 169 EPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSE 213
Cdd:PRK11607 167 RPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQE 211
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
11-221 |
5.64e-37 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 130.47 E-value: 5.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGagagKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLN-------QLP- 82
Cdd:PRK10619 6 LNVIDLHKRYG----EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgQLKv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 83 --EEQLAVIRGKhLGFIFQFFNLMPVLNVFDNVYFPLVLNGQFSKKEATERTLHYLDSVGLSGFGDRK-PGQLSGGQQQR 159
Cdd:PRK10619 82 adKNQLRLLRTR-LTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830546 160 VAIARALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQtGTTFVISTHSSELkarARRV 221
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGF---ARHV 218
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
11-231 |
1.07e-36 |
|
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: 128.17 E-value: 1.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGAgagkVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNK--------LLNQLP 82
Cdd:cd03269 1 LEVENVTKRFGR----VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKpldiaarnRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 83 EEqlaviRGkhlgfifqffnLMPVLNVFDNVYFPLVLNGqFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAI 162
Cdd:cd03269 77 EE-----RG-----------LYPKMKVIDQLVYLAQLKG-LKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQF 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 163 ARALAHEPMVVIADEPTGNLDLATGEAILDLLLTInQQTGTTFVISTHSSELKAR-ARRVVEIQDGVLIH 231
Cdd:cd03269 140 IAAVIHDPELLILDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEElCDRVLLLNKGRAVL 208
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
29-230 |
1.17e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 129.81 E-value: 1.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 29 ALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAVirGKHLGFIFQffnlmpvlN 108
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEV--RKTVGIVFQ--------N 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 109 VFDNVYFPLV--------LNGQFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTG 180
Cdd:PRK13639 87 PDDQLFAPTVeedvafgpLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTS 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15830546 181 NLDLATGEAILDLLLTINQQtGTTFVISTHSSEL-KARARRVVEIQDGVLI 230
Cdd:PRK13639 167 GLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLvPVYADKVYVMSDGKII 216
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
9-235 |
1.49e-36 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 133.99 E-value: 1.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 9 PAISLSNIYKCYGAgagkVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKllnqlPEEQLAV 88
Cdd:COG1129 3 PLLEMRGISKSFGG----VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGE-----PVRFRSP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 89 IRGKHLG--FIFQFFNLMPVLNVFDNVYF--PLVLNGQFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIAR 164
Cdd:COG1129 74 RDAQAAGiaIIHQELNLVPNLSVAENIFLgrEPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830546 165 ALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQtGTTFV-ISTHSSELKARARRVVEIQDGVLIHDSDA 235
Cdd:COG1129 154 ALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIyISHRLDEVFEIADRVTVLRDGRLVGTGPV 224
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
29-227 |
1.68e-36 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 129.75 E-value: 1.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 29 ALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNqlpEEQLAVIRgKHLGFIFQ-----FFNL 103
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLS---EETVWDVR-RQVGMVFQnpdnqFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 104 mpvlNVFDNVYFPLVLNGqFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNLD 183
Cdd:PRK13635 98 ----TVQDDVAFGLENIG-VPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15830546 184 LATGEAILDLLLTINQQTGTTfVIS-THSSELKARARRVVEIQDG 227
Cdd:PRK13635 173 PRGRREVLETVRQLKEQKGIT-VLSiTHDLDEAAQADRVIVMNKG 216
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
11-230 |
1.86e-36 |
|
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: 127.33 E-value: 1.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGagagKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQlavir 90
Cdd:cd03268 1 LKTNDLTKTYG----KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 gKHLGFIFQFFNLMPVLNVFDNVYFPLVLNGQfsKKEATERTLhylDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEP 170
Cdd:cd03268 72 -RRIGALIEAPGFYPNLTARENLRLLARLLGI--RKKRIDEVL---DVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNP 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830546 171 MVVIADEPTGNLDLATGEAILDLLLTINQQtGTTFVISTHS-SELKARARRVVEIQDGVLI 230
Cdd:cd03268 146 DLLILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLlSEIQKVADRIGIINKGKLI 205
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
9-232 |
1.87e-36 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 135.73 E-value: 1.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 9 PAISLSNIykCYGAGAGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTvIFLNKL-LNQLPeeqLA 87
Cdd:COG2274 472 GDIELENV--SFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGR-ILIDGIdLRQID---PA 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 88 VIRgKHLGFIFQ---FFNlmpvLNVFDNVyfplvlngQFSKKEATERTLHY-LDSVGLSGFGDRKP-----------GQL 152
Cdd:COG2274 546 SLR-RQIGVVLQdvfLFS----GTIRENI--------TLGDPDATDEEIIEaARLAGLHDFIEALPmgydtvvgeggSNL 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 153 SGGQQQRVAIARALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQqtGTTFVISTHSSELKARARRVVEIQDGVLIHD 232
Cdd:COG2274 613 SGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRLADRIIVLDKGRIVED 690
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
9-230 |
2.27e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 128.96 E-value: 2.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 9 PAISLSNIYKCYGAGagKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQlpeEQLAV 88
Cdd:PRK13632 6 VMIKVENVSFSYPNS--ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISK---ENLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 89 IRgKHLGFIFQ-----FFNLmpvlNVFDNVYFPLVlNGQFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIA 163
Cdd:PRK13632 81 IR-KKIGIIFQnpdnqFIGA----TVEDDIAFGLE-NKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15830546 164 RALAHEPMVVIADEPTGNLDLATGEAILDLLLTInQQTGTTFVIS-THSSELKARARRVVEIQDGVLI 230
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDL-RKTRKKTLISiTHDMDEAILADKVIVFSEGKLI 221
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
25-221 |
8.30e-36 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 127.08 E-value: 8.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 25 GKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDK--P---TSGTVIFLNKLLNQlPEEQLAVIRgKHLGFIFQ 99
Cdd:COG1117 22 GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDIYD-PDVDVVELR-RRVGMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 100 FFNLMPvLNVFDNVYFPLVLNGQFSKKEATERTLHYLDSVGL----------SGFGdrkpgqLSGGQQQRVAIARALAHE 169
Cdd:COG1117 100 KPNPFP-KSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALwdevkdrlkkSALG------LSGGQQQRLCIARALAVE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15830546 170 PMVVIADEPTGNLD-LATGeAILDLLLTINQQtgTTFVISTHSselKARARRV 221
Cdd:COG1117 173 PEVLLMDEPTSALDpISTA-KIEELILELKKD--YTIVIVTHN---MQQAARV 219
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
11-230 |
1.00e-35 |
|
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: 125.95 E-value: 1.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGagagKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEqlavIR 90
Cdd:cd03265 1 IEVENLVKKYG----DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE----VR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 gKHLGFIFQFFNLMPVLNVFDNVYFPLVLNGqFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEP 170
Cdd:cd03265 73 -RRIGIVFQDLSVDDELTGWENLYIHARLYG-VPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830546 171 MVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHS-SELKARARRVVEIQDGVLI 230
Cdd:cd03265 151 EVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYmEEAEQLCDRVAIIDHGRII 211
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
28-217 |
1.09e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 127.83 E-value: 1.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 28 DALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLL-NQLPEEQLAVIRgKHLGFIFQFfnlmPV 106
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItAGKKNKKLKPLR-KKVGIVFQF----PE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 107 LNVF------DNVYFPLvlNGQFSKKEATERTLHYLDSVGLS-GFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPT 179
Cdd:PRK13634 96 HQLFeetvekDICFGPM--NFGVSEEDAKQKAREMIELVGLPeELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPT 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 15830546 180 GNLDLATGEAILDLLLTINQQTGTTFVISTHSSELKAR 217
Cdd:PRK13634 174 AGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAAR 211
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
10-234 |
2.04e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 126.77 E-value: 2.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 10 AISLSNIYKCYGAGAgkvDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQlavI 89
Cdd:PRK13647 4 IIEVEDLHFRYKDGT---KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKW---V 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 90 RGKhLGFIFQ-----FFNLmpvlNVFDNVYF-PLvlNGQFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIA 163
Cdd:PRK13647 78 RSK-VGLVFQdpddqVFSS----TVWDDVAFgPV--NMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830546 164 RALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQtGTTFVISTHSSELKAR-ARRVVEIQDGVLIHDSD 234
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGD 221
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
30-227 |
2.06e-35 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 126.04 E-value: 2.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 30 LKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAVIRG-----KHLGFIFqffnlm 104
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAvlpqhSSLSFPF------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 105 PVLNVfdnvyfplVLNG----QFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALA------HEPMVVI 174
Cdd:PRK13548 92 TVEEV--------VAMGraphGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15830546 175 ADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSELKAR-ARRVVEIQDG 227
Cdd:PRK13548 164 LDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARyADRIVLLHQG 217
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
8-230 |
4.37e-35 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 127.00 E-value: 4.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 8 LPAISLSNIY---KCYGAGAGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEE 84
Cdd:PRK11308 6 LQAIDLKKHYpvkRGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 85 QLAVIRGKhLGFIFQ--FFNLMPVLNVFDNVYFPLVLNGQFSKKEATERTLHYLDSVGL-SGFGDRKPGQLSGGQQQRVA 161
Cdd:PRK11308 86 AQKLLRQK-IQIVFQnpYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 162 IARALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHssELKararrVVE-IQDGVLI 230
Cdd:PRK11308 165 IARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISH--DLS-----VVEhIADEVMV 227
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
13-210 |
6.75e-35 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 127.14 E-value: 6.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 13 LSNIYKCYGagagKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTvIFLNKllnqlpeEQLA--VIR 90
Cdd:PRK11432 9 LKNITKRFG----SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQ-IFIDG-------EDVThrSIQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 GKHLGFIFQFFNLMPVLNVFDNVYFPLVLNGQfSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEP 170
Cdd:PRK11432 77 QRDICMVFQSYALFPHMSLGENVGYGLKMLGV-PKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15830546 171 MVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTH 210
Cdd:PRK11432 156 KVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTH 195
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
29-227 |
1.17e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 125.16 E-value: 1.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 29 ALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTvIFLNKLLNQLPEEQLAVIRgKHLGFIFQFfnlmPVLN 108
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGK-IIIDGVDITDKKVKLSDIR-KKVGLVFQY----PEYQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 109 VF------DNVYFPLVLNgqFSKKEATERTLHYLDSVGLS--GFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTG 180
Cdd:PRK13637 96 LFeetiekDIAFGPINLG--LSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15830546 181 NLDLATGEAILDLLLTINQQTGTTFVISTHSSELKAR-ARRVVEIQDG 227
Cdd:PRK13637 174 GLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKlADRIIVMNKG 221
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
24-232 |
1.27e-34 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 124.07 E-value: 1.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 24 AGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAVIRG-----KHLGFIF 98
Cdd:COG4559 11 LGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAvlpqhSSLAFPF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 99 qffnlmPVLNVfdnvyfplV----LNGQFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALA--HEPMV 172
Cdd:COG4559 91 ------TVEEV--------ValgrAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlWEPVD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15830546 173 VIA-----DEPTGNLDLATGEAILDLLLTINQQTGTTFVIsTHSSELKAR-ARRVVEIQDGVLIHD 232
Cdd:COG4559 157 GGPrwlflDEPTSALDLAHQHAVLRLARQLARRGGGVVAV-LHDLNLAAQyADRILLLHQGRLVAQ 221
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
9-213 |
1.71e-34 |
|
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: 123.66 E-value: 1.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 9 PAISLSNIYKCYGagaGKVdALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLnkLLNQLPEEQLAV 88
Cdd:COG1119 2 PLLELRNVTVRRG---GKT-ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRL--FGERRGGEDVWE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 89 IRgKHLGFI-----FQFFNLMPVLNVfdnvyfplVLNGQFS--------KKEATERTLHYLDSVGLSGFGDRKPGQLSGG 155
Cdd:COG1119 76 LR-KRIGLVspalqLRFPRDETVLDV--------VLSGFFDsiglyrepTDEQRERARELLELLGLAHLADRPFGTLSQG 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15830546 156 QQQRVAIARALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSE 213
Cdd:COG1119 147 EQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVE 204
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
14-210 |
1.85e-34 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 123.79 E-value: 1.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 14 SNIYKCYGAGAG-----KVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQlav 88
Cdd:COG4167 8 RNLSKTFKYRTGlfrrqQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 89 iRGKHLGFIFQFFN--LMPVLNVFDNVYFPLVLNGQFSKKEATERTLHYLDSVGLSG-FGDRKPGQLSGGQQQRVAIARA 165
Cdd:COG4167 85 -RCKHIRMIFQDPNtsLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLLPeHANFYPHMLSSGQKQRVALARA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15830546 166 LAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTH 210
Cdd:COG4167 164 LILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQ 208
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
10-210 |
4.00e-34 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 123.68 E-value: 4.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 10 AISLSNIYKCYGagagKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQ--------L 81
Cdd:COG4152 1 MLELKGLTKRFG----DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPedrrrigyL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 82 PEEqlaviRGkhlgfifqffnLMPVLNVFDNVYFPLVLNGQfSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVA 161
Cdd:COG4152 77 PEE-----RG-----------LYPKMKVGEQLVYLARLKGL-SKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQ 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15830546 162 IARALAHEPMVVIADEPTGNLD-LATgEAILDLLLTINQQtGTTFVISTH 210
Cdd:COG4152 140 LIAALLHDPELLILDEPFSGLDpVNV-ELLKDVIRELAAK-GTTVIFSSH 187
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
21-227 |
1.16e-33 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 126.72 E-value: 1.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 21 GAGAGKVDALKSINLDINKGEFLALCGPSGSGKSTL-LNILSGIdkPTSGTVIFLNKLLNQLPEEQLAVIRgKHLGFIFQ 99
Cdd:COG4172 293 RRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALLRLI--PSEGEIRFDGQDLDGLSRRALRPLR-RRMQVVFQ 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 100 --FFNLMPVLNVFDNVYFPLVLNG-QFSKKEATERTLHYLDSVGLS-GFGDRKPGQLSGGQQQRVAIARALAHEPMVVIA 175
Cdd:COG4172 370 dpFGSLSPRMTVGQIIAEGLRVHGpGLSAAERRARVAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVL 449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15830546 176 DEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHssELK---ARARRVVEIQDG 227
Cdd:COG4172 450 DEPTSALDVSVQAQILDLLRDLQREHGLAYLFISH--DLAvvrALAHRVMVMKDG 502
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
12-227 |
8.93e-33 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 117.74 E-value: 8.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 12 SLSNIYKCYGagaGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNqlpeeqlAVIRG 91
Cdd:cd03226 1 RIENISFSYK---KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK-------AKERR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 92 KHLGFI-----FQFFnlmpvlnvFDNVYFPLVL-NGQFSKKEatERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARA 165
Cdd:cd03226 71 KSIGYVmqdvdYQLF--------TDSVREELLLgLKELDAGN--EQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15830546 166 LAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVIsTHSSELKAR-ARRVVEIQDG 227
Cdd:cd03226 141 LLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVI-THDYEFLAKvCDRVLLLANG 202
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
11-232 |
1.54e-32 |
|
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: 117.47 E-value: 1.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGAGAGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPeeqLAVIR 90
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEP---AEARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 GkhLGFIFQFFNLMPVLNVFDNVYFPLVLNGqFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEP 170
Cdd:cd03266 79 R--LGFVSDSTGLYDRLTARENLEYFAGLYG-LKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15830546 171 MVVIADEPTGNLDLATGEAILDLLLTINQQtGTTFVISTHS-SELKARARRVVEIQDGVLIHD 232
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHImQEVERLCDRVVVLHRGRVVYE 217
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
10-222 |
2.06e-32 |
|
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: 117.78 E-value: 2.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 10 AISLSNIYKCYGAGAgkvdALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAvi 89
Cdd:TIGR03864 1 ALEVAGLSFRYGARR----ALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVAGHDLRRAPRAALA-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 90 rgkHLGFIFQFFNLMPVLNVFDNVYFPLVLNGqFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHE 169
Cdd:TIGR03864 75 ---RLGVVFQQPTLDLDLSVRQNLRYHAALHG-LSRAEARARIAELLARLGLAERADDKVRELNGGHRRRVEIARALLHR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15830546 170 PMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTH-SSELKARARRVV 222
Cdd:TIGR03864 151 PALLLLDEPTVGLDPASRAAITAHVRALARDQGLSVLWATHlVDEIEASDRLVV 204
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
22-207 |
3.52e-32 |
|
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: 116.76 E-value: 3.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 22 AGAGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAViRGkhLGFIFQFF 101
Cdd:cd03224 8 AGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERAR-AG--IGYVPEGR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 102 NLMPVLNVFDNvyfpLVLNGQFSKKEATERTlhyLDSV-----GLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIAD 176
Cdd:cd03224 85 RIFPELTVEEN----LLLGAYARRRAKRKAR---LERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLD 157
|
170 180 190
....*....|....*....|....*....|.
gi 15830546 177 EPTGNLDLATGEAILDLLLTINQQtGTTFVI 207
Cdd:cd03224 158 EPSEGLAPKIVEEIFEAIRELRDE-GVTILL 187
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
23-227 |
4.51e-32 |
|
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: 116.76 E-value: 4.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 23 GAGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKL----LNQLPEEQLAVIRGKHLGFIF 98
Cdd:COG4778 20 GGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdLAQASPREILALRRRTIGYVS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 99 QFFNLMPVLNVFDNVYFPLVLNGqFSKKEATERTLHYLDSVGLsgfgDRK-----PGQLSGGQQQRVAIARALAHEPMVV 173
Cdd:COG4778 100 QFLRVIPRVSALDVVAEPLLERG-VDREEARARARELLARLNL----PERlwdlpPATFSGGEQQRVNIARGFIADPPLL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15830546 174 IADEPTGNLDLATGEAILDLLLTINQQtGTTFVISTHSSELKAR-ARRVVEIQDG 227
Cdd:COG4778 175 LLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAvADRVVDVTPF 228
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
27-233 |
9.56e-32 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 115.89 E-value: 9.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 27 VDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTViflnKLLNQLPEEQlaviRGKHL---GFIF----Q 99
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV----RVAGLVPWKR----RKKFLrriGVVFgqktQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 100 FFNLMPV---LNVFDNVYfplvlngQFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIAD 176
Cdd:cd03267 106 LWWDLPVidsFYLLAAIY-------DLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15830546 177 EPTGNLDLATGEAILDLLLTINQQTGTTFVISTHS-SELKARARRVVEIQDGVLIHDS 233
Cdd:cd03267 179 EPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYmKDIEALARRVLVIDKGRLLYDG 236
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
33-227 |
1.33e-31 |
|
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: 118.66 E-value: 1.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 33 INLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQ------LPEEQlaviRgkHLGFIFQFFNLMPV 106
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDsargifLPPHR----R--RIGYVFQEARLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 107 LNVFDNVYFplvlnGQfSKKEATERTLHyLDSV----GLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNL 182
Cdd:COG4148 92 LSVRGNLLY-----GR-KRAPRAERRIS-FDEVvellGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAAL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15830546 183 DLATGEAILDLLLTINQQTGTTFVISTHSSELKAR-ARRVVEIQDG 227
Cdd:COG4148 165 DLARKAEILPYLERLRDELDIPILYVSHSLDEVARlADHVVLLEQG 210
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
23-222 |
1.81e-31 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 113.87 E-value: 1.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 23 GAGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTViflnkllnqlpeeqlAVIRGKHLGFIFQFFN 102
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV---------------RRAGGARVAYVPQRSE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 103 L---MPvLNVFDnvyfpLVLNGQFSK--------KEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPM 171
Cdd:NF040873 66 VpdsLP-LTVRD-----LVAMGRWARrglwrrltRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEAD 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15830546 172 VVIADEPTGNLDLATGEAILDLLLTINQQtGTTFVISTHSSELKARARRVV 222
Cdd:NF040873 140 LLLLDEPTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRRADPCV 189
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
34-232 |
1.90e-31 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 115.06 E-value: 1.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 34 NLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAVirgkhlGFIFQFFNLMPVLNVFDNV 113
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPV------SMLFQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 114 yfPLVLNGQFSKKEATERTL-HYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNLDLATGEAILD 192
Cdd:PRK10771 93 --GLGLNPGLKLNAAQREKLhAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLT 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15830546 193 LLLTINQQTGTTFVISTHSSELKAR-ARRVVEIQDGVLIHD 232
Cdd:PRK10771 171 LVSQVCQERQLTLLMVSHSLEDAARiAPRSLVVADGRIAWD 211
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
11-229 |
3.05e-31 |
|
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: 113.08 E-value: 3.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIykCYGAGAGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLavir 90
Cdd:cd03246 1 LEVENV--SFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNEL---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 GKHLGFIFQFFNLMPVlNVFDNVyfplvlngqfskkeatertlhyldsvglsgfgdrkpgqLSGGQQQRVAIARALAHEP 170
Cdd:cd03246 75 GDHVGYLPQDDELFSG-SIAENI--------------------------------------LSGGQRQRLGLARALYGNP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15830546 171 MVVIADEPTGNLDLATGEAILDLLLTINQQtGTTFVISTHSSELKARARRVVEIQDGVL 229
Cdd:cd03246 116 RILVLDEPNSHLDVEGERALNQAIAALKAA-GATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
29-232 |
5.73e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 115.18 E-value: 5.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 29 ALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNklLNQLPEEQLAVIRGKhLGFIFQF-FNLMPVL 107
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEENLWDIRNK-AGMVFQNpDNQIVAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 108 NVFDNVYF-PLVLNgqFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNLDLAT 186
Cdd:PRK13633 102 IVEEDVAFgPENLG--IPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSG 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15830546 187 GEAILDLLLTINQQTGTTFVISTHSSELKARARRVVEIQDGVLIHD 232
Cdd:PRK13633 180 RREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVME 225
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
19-210 |
7.81e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 114.94 E-value: 7.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 19 CYGAGAGkVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNqLPEEQLAVIRgKHLGFIF 98
Cdd:PRK13636 12 NYNYSDG-THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID-YSRKGLMKLR-ESVGMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 99 QF-FNLMPVLNVFDNVYFPlVLNGQFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADE 177
Cdd:PRK13636 89 QDpDNQLFSASVYQDVSFG-AVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDE 167
|
170 180 190
....*....|....*....|....*....|...
gi 15830546 178 PTGNLDLATGEAILDLLLTINQQTGTTFVISTH 210
Cdd:PRK13636 168 PTAGLDPMGVSEIMKLLVEMQKELGLTIIIATH 200
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
9-210 |
8.34e-31 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 118.59 E-value: 8.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 9 PAISLSNIYKCYGAgagkVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTvIFLNkllnqlpeEQLAV 88
Cdd:COG3845 4 PALELRGITKRFGG----VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGE-ILID--------GKPVR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 89 IRGKH------LGFIFQFFNLMPVLNVFDNVyfplVL------NGQFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQ 156
Cdd:COG3845 71 IRSPRdaialgIGMVHQHFMLVPNLTVAENI----VLgleptkGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGE 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15830546 157 QQRVAIARALAHEPMVVIADEPTGNLdlaTGEAILDLLLTINQ--QTGTTFVISTH 210
Cdd:COG3845 147 QQRVEILKALYRGARILILDEPTAVL---TPQEADELFEILRRlaAEGKSIIFITH 199
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
10-210 |
1.27e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 114.46 E-value: 1.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 10 AISLSNIYKCYGAG---AGKvdALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLL-NQLPEEQ 85
Cdd:PRK13649 2 GINLQNVSYTYQAGtpfEGR--ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItSTSKNKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 86 LAVIRgKHLGFIFQFfnlmPVLNVFDNVYFPLVL----NGQFSKKEATERTLHYLDSVGLS-GFGDRKPGQLSGGQQQRV 160
Cdd:PRK13649 80 IKQIR-KKVGLVFQF----PESQLFEETVLKDVAfgpqNFGVSQEEAEALAREKLALVGISeSLFEKNPFELSGGQMRRV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15830546 161 AIARALAHEPMVVIADEPTGNLDLATGEAILDLLLTINqQTGTTFVISTH 210
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLH-QSGMTIVLVTH 203
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
11-232 |
2.07e-30 |
|
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: 110.60 E-value: 2.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGAgagkVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTViflnkllnqlpeeqlaVIR 90
Cdd:cd03216 1 LELRGITKRFGG----VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEI----------------LVD 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 GKHLGFIfqffnlmpvlnvfdnvyfplvlngqfSKKEATE---RTLHyldsvglsgfgdrkpgQLSGGQQQRVAIARALA 167
Cdd:cd03216 61 GKEVSFA--------------------------SPRDARRagiAMVY----------------QLSVGERQMVEIARALA 98
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15830546 168 HEPMVVIADEPTGNLDLATGEAILDLLLTINQQtGTTFVISTHS-SELKARARRVVEIQDGVLIHD 232
Cdd:cd03216 99 RNARLLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRlDEVFEIADRVTVLRDGRVVGT 163
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
10-233 |
3.56e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 113.39 E-value: 3.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 10 AISLSNIYKCYGAGAG-KVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLN-QLPEEQLA 87
Cdd:PRK13641 2 SIKFENVDYIYSPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpETGNKNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 88 VIRgKHLGFIFQFfnlmPVLNVFDNVYFPLV----LNGQFSKKEATERTLHYLDSVGLS-GFGDRKPGQLSGGQQQRVAI 162
Cdd:PRK13641 82 KLR-KKVSLVFQF----PEAQLFENTVLKDVefgpKNFGFSEDEAKEKALKWLKKVGLSeDLISKSPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15830546 163 ARALAHEPMVVIADEPTGNLDLATGEAILDLLLTInQQTGTTFVISTHS-SELKARARRVVEIQDGVLI-HDS 233
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDY-QKAGHTVILVTHNmDDVAEYADDVLVLEHGKLIkHAS 228
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
9-227 |
3.75e-30 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 116.81 E-value: 3.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 9 PAISLSNIYKCYGAgagkVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLpEEQLAV 88
Cdd:PRK09700 4 PYISMAGIGKSFGP----VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKL-DHKLAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 89 IRGkhLGFIFQFFNLMPVLNVFDNVYFPLVLNGQF------SKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAI 162
Cdd:PRK09700 79 QLG--IGIIYQELSVIDELTVLENLYIGRHLTKKVcgvniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15830546 163 ARALAHEPMVVIADEPTGNLdlaTGEAILDLLLTINQ--QTGTTFV-ISTHSSELKARARRVVEIQDG 227
Cdd:PRK09700 157 AKTLMLDAKVIIMDEPTSSL---TNKEVDYLFLIMNQlrKEGTAIVyISHKLAEIRRICDRYTVMKDG 221
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-222 |
4.63e-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: 116.62 E-value: 4.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 2 QSTIKSLPAISLSNIYKCYGagaGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQL 81
Cdd:TIGR02857 313 PVTAAPASSLEFSGVSVAYP---GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADA 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 82 PEEQLavirGKHLGFIFQFFNLMPVlNVFDNVyfplvlngQFSKKEATERTL-HYLDSVGLSGF------------GDRK 148
Cdd:TIGR02857 390 DADSW----RDQIAWVPQHPFLFAG-TIAENI--------RLARPDASDAEIrEALERAGLDEFvaalpqgldtpiGEGG 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830546 149 PGqLSGGQQQRVAIARALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQqtGTTFVISTHSSELKARARRVV 222
Cdd:TIGR02857 457 AG-LSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALADRIV 527
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-217 |
5.06e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 111.93 E-value: 5.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 25 GKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGI-----DKPTSGTVIFLNKLLNQLPEEQLAvirgKHLGFIFQ 99
Cdd:PRK14247 14 GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIELR----RRVQMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 100 FFNLMPVLNVFDNVYFPLVLNGQF-SKKEATERTLHYLDSVGL-SGFGDR---KPGQLSGGQQQRVAIARALAHEPMVVI 174
Cdd:PRK14247 90 IPNPIPNLSIFENVALGLKLNRLVkSKKELQERVRWALEKAQLwDEVKDRldaPAGKLSGGQQQRLCIARALAFQPEVLL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15830546 175 ADEPTGNLDLATGEAILDLLLTINQQtgTTFVISTHSSELKAR 217
Cdd:PRK14247 170 ADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAAR 210
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
26-232 |
6.98e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 113.41 E-value: 6.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 26 KVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAVIRG------------KH 93
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELITNPyskkiknfkelrRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 94 LGFIFQFfnlmPVLNVF------DNVYFPLVLnGQfSKKEATERTLHYLDSVGL-SGFGDRKPGQLSGGQQQRVAIARAL 166
Cdd:PRK13631 118 VSMVFQF----PEYQLFkdtiekDIMFGPVAL-GV-KKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGIL 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15830546 167 AHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVIsTHSSElkararRVVEIQDGVLIHD 232
Cdd:PRK13631 192 AIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVI-THTME------HVLEVADEVIVMD 250
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
30-227 |
8.42e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 112.13 E-value: 8.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 30 LKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNqlpEEQLAVIRgKHLGFIFQF-FNLMPVLN 108
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLT---EENVWDIR-HKIGMVFQNpDNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 109 VFDNVYFPLVlNGQFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNLDlatGE 188
Cdd:PRK13650 99 VEDDVAFGLE-NKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLD---PE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15830546 189 AILDLLLT---INQQTGTTfVIS-THSSELKARARRVVEIQDG 227
Cdd:PRK13650 175 GRLELIKTikgIRDDYQMT-VISiTHDLDEVALSDRVLVMKNG 216
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
27-234 |
8.83e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 112.87 E-value: 8.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 27 VDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTViflnKLLNQLP---EEQLAvirgKHLGFIF----Q 99
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEV----RVLGYVPfkrRKEFA----RRIGVVFgqrsQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 100 FFNLMPVLNVFDnvyfplvLNG---QFSKKEAtERTLHYLDSV-GLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIA 175
Cdd:COG4586 107 LWWDLPAIDSFR-------LLKaiyRIPDAEY-KKRLDELVELlDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFL 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 176 DEPTGNLDLATGEAILDLLLTINQQTGTTFVISTH-SSELKARARRVVEIQDGVLIHDSD 234
Cdd:COG4586 179 DEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHdMDDIEALCDRVIVIDHGRIIYDGS 238
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
34-227 |
1.21e-29 |
|
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: 109.95 E-value: 1.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 34 NLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAVirgkhlGFIFQFFNLMPVLNVFDNV 113
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPV------SMLFQENNLFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 114 YF----PLVLNG-QFSKKEATERtlhyldSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNLDLATGE 188
Cdd:TIGR01277 92 GLglhpGLKLNAeQQEKVVDAAQ------QVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLRE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15830546 189 AILDLLLTINQQTGTTFVISTHS-SELKARARRVVEIQDG 227
Cdd:TIGR01277 166 EMLALVKQLCSERQRTLLMVTHHlSDARAIASQIAVVSQG 205
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
26-232 |
2.19e-29 |
|
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: 109.60 E-value: 2.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 26 KVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPeeqLAVIRgKHLGFIFQ----FF 101
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD---PADLR-RNIGYVPQdvtlFY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 102 NlmpvlNVFDNvyfpLVLNGQFSKkeaTERTLHYLDSVGLSGFGDRKP----------GQ-LSGGQQQRVAIARALAHEP 170
Cdd:cd03245 92 G-----TLRDN----ITLGAPLAD---DERILRAAELAGVTDFVNKHPngldlqigerGRgLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830546 171 MVVIADEPTGNLDLATGEAILDLLltinQQT--GTTFVISTHSSELKARARRVVEIQDGVLIHD 232
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERL----RQLlgDKTLIIITHRPSLLDLVDRIIVMDSGRIVAD 219
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
29-210 |
3.31e-29 |
|
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: 108.21 E-value: 3.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 29 ALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFlnkllNQLPEEQLAVIRGKHLGFIFQFFNLMPVLN 108
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRW-----NGTPLAEQRDEPHENILYLGHLPGLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 109 VFDNVYFPLVLNGqfskkeATERTLH-YLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNLDlATG 187
Cdd:TIGR01189 90 ALENLHFWAAIHG------GAQRTIEdALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD-KAG 162
|
170 180
....*....|....*....|...
gi 15830546 188 EAILDLLLTINQQTGTTFVISTH 210
Cdd:TIGR01189 163 VALLAGLLRAHLARGGIVLLTTH 185
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
29-210 |
6.52e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 110.21 E-value: 6.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 29 ALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAVIRGKHLGFIFQFfnlmPVLN 108
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQF----PESQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 109 VFDNVYFPLVLNGQ----FSKKEATERTLHYLDSVGLSG-FGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNLD 183
Cdd:PRK13643 97 LFEETVLKDVAFGPqnfgIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180
....*....|....*....|....*..
gi 15830546 184 LATGEAILDLLLTINqQTGTTFVISTH 210
Cdd:PRK13643 177 PKARIEMMQLFESIH-QSGQTVVLVTH 202
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
25-230 |
9.79e-29 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 108.71 E-value: 9.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 25 GKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDK-----PTSGTVIFLNKLLNQlPEEQLAVIRgKHLGFIFQ 99
Cdd:PRK14239 16 NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYS-PRTDTVDLR-KEIGMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 100 FFNLMPvLNVFDNVYFPLVLNGQFSKK---EATERTL-------HYLDSVGLSGFGdrkpgqLSGGQQQRVAIARALAHE 169
Cdd:PRK14239 94 QPNPFP-MSIYENVVYGLRLKGIKDKQvldEAVEKSLkgasiwdEVKDRLHDSALG------LSGGQQQRVCIARVLATS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830546 170 PMVVIADEPTGNLDLATGEAILDLLLTINQQtgTTFVISTHSSELKAR-ARRVVEIQDGVLI 230
Cdd:PRK14239 167 PKIILLDEPTSALDPISAGKIEETLLGLKDD--YTMLLVTRSMQQASRiSDRTGFFLDGDLI 226
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-221 |
1.43e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 108.39 E-value: 1.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 10 AISLSNIYKCYGAGagkvDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGI-----DKPTSGTVIFLNKllNQLPEE 84
Cdd:PRK14267 4 AIETVNLRVYYGSN----HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGR--NIYSPD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 85 QLAVIRGKHLGFIFQFFNLMPVLNVFDNVYFPLVLNGQF-SKKEATERTLHYLDSVGL-SGFGDR---KPGQLSGGQQQR 159
Cdd:PRK14267 78 VDPIEVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVkSKKELDERVEWALKKAALwDEVKDRlndYPSNLSGGQRQR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830546 160 VAIARALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQtgTTFVISTHSSelkARARRV 221
Cdd:PRK14267 158 LVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSP---AQAARV 214
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
7-229 |
1.50e-28 |
|
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: 112.44 E-value: 1.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 7 SLPA----ISLSNIYkcYGAGAGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLP 82
Cdd:TIGR01842 309 PLPEpeghLSVENVT--IVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWD 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 83 EEQLavirGKHLGFIFQFFNLMPVlNVFDNV-YFPLVLNGQFSKKEATERTLH---------YLDSVGLSGFGdrkpgqL 152
Cdd:TIGR01842 387 RETF----GKHIGYLPQDVELFPG-TVAENIaRFGENADPEKIIEAAKLAGVHelilrlpdgYDTVIGPGGAT------L 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830546 153 SGGQQQRVAIARALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVIsTHSSELKARARRVVEIQDGVL 229
Cdd:TIGR01842 456 SGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVI-THRPSLLGCVDKILVLQDGRI 531
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
33-210 |
2.13e-28 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 108.31 E-value: 2.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 33 INLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAVIRgKHLGFIFQFFNLMPVLNVFDN 112
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVR-KRMSMLFQSGALFTDMNVFDN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 113 VYFPLVLNGQFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNLDLATGEAILD 192
Cdd:PRK11831 105 VAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVK 184
|
170
....*....|....*...
gi 15830546 193 LLLTINQQTGTTFVISTH 210
Cdd:PRK11831 185 LISELNSALGVTCVVVSH 202
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
26-210 |
2.42e-28 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 112.26 E-value: 2.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 26 KVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAVIRgKHLGFIFQ--FFNL 103
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALR-RDIQFIFQdpYASL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 104 MPVLNVFDNVYFPLVLNGQFSKKEATERTLHYLDSVGL-SGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNL 182
Cdd:PRK10261 415 DPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180
....*....|....*....|....*...
gi 15830546 183 DLATGEAILDLLLTINQQTGTTFVISTH 210
Cdd:PRK10261 495 DVSIRGQIINLLLDLQRDFGIAYLFISH 522
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-210 |
2.67e-28 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 109.04 E-value: 2.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 1 MQSTIKSLPAISLSNIYKCYGAGAGKVDALKSINLDINKGEFLALCGPSGSGKS----TLLNILS--GIdkpTSGTVIFL 74
Cdd:PRK09473 3 PLAQQQADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAanGR---IGGSATFN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 75 NKLLNQLPEEQLAVIRGKHLGFIFQ--FFNLMPVLNVFDNVYFPLVLNGQFSKKEATERTLHYLDSVGLSGfgDRK---- 148
Cdd:PRK09473 80 GREILNLPEKELNKLRAEQISMIFQdpMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPE--ARKrmkm 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15830546 149 -PGQLSGGQQQRVAIARALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTH 210
Cdd:PRK09473 158 yPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITH 220
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
10-235 |
6.34e-28 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 106.32 E-value: 6.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 10 AISLSNIYKCY------------------GAGAGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTV 71
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 72 IflnkllnqlpeeqlavIRGKH-----LGFIFQffnlmPVLNVFDNVYFPLVLNGqFSKKEATERtlhyLDSV----GLS 142
Cdd:COG1134 84 E----------------VNGRVsalleLGAGFH-----PELTGRENIYLNGRLLG-LSRKEIDEK----FDEIvefaELG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 143 GFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPtgnldLATG---------EAILDLLltinqQTGTTFVISTHSSE 213
Cdd:COG1134 138 DFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEV-----LAVGdaafqkkclARIRELR-----ESGRTVIFVSHSMG 207
|
250 260
....*....|....*....|...
gi 15830546 214 -LKARARRVVEIQDGVLIHDSDA 235
Cdd:COG1134 208 aVRRLCDRAIWLEKGRLVMDGDP 230
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
30-214 |
6.81e-28 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 104.94 E-value: 6.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 30 LKSINLDINKGEFLALCGPSGSGKSTLLNILSG--IDKPTSGTViflnkLLNQLPEEQLAVirGKHLGFIFQFFNLMPVL 107
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEV-----LINGRPLDKRSF--RKIIGYVPQDDILHPTL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 108 NVFDNVYFplvlngqfskkeatertlhyldSVGLSGfgdrkpgqLSGGQQQRVAIARALAHEPMVVIADEPTGNLDLATG 187
Cdd:cd03213 98 TVRETLMF----------------------AAKLRG--------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180
....*....|....*....|....*....
gi 15830546 188 EAILDLLLTInQQTGTTFVISTH--SSEL 214
Cdd:cd03213 148 LQVMSLLRRL-ADTGRTIICSIHqpSSEI 175
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
25-208 |
8.46e-28 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 110.64 E-value: 8.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 25 GKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLaviRgKHLGFIFQ---FF 101
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESL---R-RQIGVVPQdtfLF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 102 NlmpvLNVFDNVyfplvlngQFSKKEAT-ERTLHYLDSVGLSGFGDRKPG-----------QLSGGQQQRVAIARALAHE 169
Cdd:COG1132 427 S----GTIRENI--------RYGRPDATdEEVEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARALLKD 494
|
170 180 190
....*....|....*....|....*....|....*....
gi 15830546 170 PMVVIADEPTGNLDLATGEAILDLLLTINQQTgTTFVIS 208
Cdd:COG1132 495 PPILILDEATSALDTETEALIQEALERLMKGR-TTIVIA 532
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
9-210 |
1.15e-27 |
|
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: 109.89 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 9 PAISLSNIYKCY-GAGAGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLnkllnqLPEEQLA 87
Cdd:TIGR03269 278 PIIKVRNVSKRYiSVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVR------VGDEWVD 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 88 VI------RG---KHLGFIFQFFNLMPVLNVFDNVYFPLVLngQFSKKEATERTLHYLDSVGLS-----GFGDRKPGQLS 153
Cdd:TIGR03269 352 MTkpgpdgRGrakRYIGILHQEYDLYPHRTVLDNLTEAIGL--ELPDELARMKAVITLKMVGFDeekaeEILDKYPDELS 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15830546 154 GGQQQRVAIARALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTH 210
Cdd:TIGR03269 430 EGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSH 486
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
29-231 |
8.16e-27 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 106.27 E-value: 8.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 29 ALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAVIRGKHLGFIFQFFNLMPVLN 108
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 109 VFDNVYFPLVLNGqFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNLDLATGE 188
Cdd:PRK10070 123 VLDNTAFGMELAG-INAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15830546 189 AILDLLLTINQQTGTTFVISTHSSELKAR-ARRVVEIQDGVLIH 231
Cdd:PRK10070 202 EMQDELVKLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQ 245
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
30-230 |
9.67e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 103.59 E-value: 9.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 30 LKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDK------PTSGTVIFLNKLLNQLPEEQLAvirgKHLGFIFQFFNL 103
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLR----KEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 104 MPVLNVFDNVYFPLVLNGQFSKKEATERTLHYLDSVGL-SGFGDR---KPGQLSGGQQQRVAIARALAHEPMVVIADEPT 179
Cdd:PRK14246 102 FPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwKEVYDRlnsPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15830546 180 GNLDLATGEAILDLLLTINQQtgTTFVISTHSSELKAR-ARRVVEIQDGVLI 230
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARvADYVAFLYNGELV 231
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
30-210 |
1.22e-26 |
|
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: 101.80 E-value: 1.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 30 LKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTViflnkLLNQLPEEQLAVIRGKHLGFIFQFFNLMPVLNV 109
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRV-----LLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 110 FDNVYFplvlngqFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNLDLAtGEA 189
Cdd:cd03231 91 LENLRF-------WHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA-GVA 162
|
170 180
....*....|....*....|.
gi 15830546 190 ILDLLLTINQQTGTTFVISTH 210
Cdd:cd03231 163 RFAEAMAGHCARGGMVVLTTH 183
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
25-230 |
1.41e-26 |
|
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: 102.30 E-value: 1.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 25 GKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAvirgKHLGFIFQffnlM 104
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLR----SMIGVVLQ----D 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 105 PVL---NVFDNvyfpLVLNGQFSKKEATERTlhyLDSVGLSGFGDRKP-----------GQLSGGQQQRVAIARALAHEP 170
Cdd:cd03254 86 TFLfsgTIMEN----IRLGRPNATDEEVIEA---AKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 171 MVVIADEPTGNLDLATGEAILDLLLTINQQTgTTFVISTHSSELKaRARRVVEIQDGVLI 230
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGR-TSIIIAHRLSTIK-NADKILVLDDGKII 216
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
29-230 |
1.96e-26 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 102.76 E-value: 1.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 29 ALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLA---VIRgkhlgfIFQFFNLMP 105
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIArmgVVR------TFQHVRLFR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 106 VLNVFDNVyfpLV----------LNGQF-------SKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAH 168
Cdd:PRK11300 94 EMTVIENL---LVaqhqqlktglFSGLLktpafrrAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830546 169 EPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSELkararrVVEIQDGVLI 230
Cdd:PRK11300 171 QPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKL------VMGISDRIYV 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
11-234 |
2.41e-26 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 106.04 E-value: 2.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGAgagkVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGID--KPTSGTVIF--------------- 73
Cdd:TIGR03269 1 IEVKNLTKKFDG----KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIYhvalcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 74 -----LNKLLNQLPEEQLAVIRG---------KHLGFIFQ-FFNLMPVLNVFDNVYFPLVLNGqFSKKEATERTLHYLDS 138
Cdd:TIGR03269 77 kvgepCPVCGGTLEPEEVDFWNLsdklrrrirKRIAIMLQrTFALYGDDTVLDNVLEALEEIG-YEGKEAVGRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 139 VGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSELKAR- 217
Cdd:TIGR03269 156 VQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDl 235
|
250
....*....|....*..
gi 15830546 218 ARRVVEIQDGVLIHDSD 234
Cdd:TIGR03269 236 SDKAIWLENGEIKEEGT 252
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
9-227 |
2.95e-26 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 102.31 E-value: 2.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 9 PAISLSNIYKCYGAGAGkvdaLKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNK-----LLNQLPE 83
Cdd:PRK11701 5 PLLSVRGLTKLYGPRKG----CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 84 EQLAVIRGKHLGFIFQffN----LMPVLNVFDNVYFPLVLNGQFSKKEATERTLHYLDSVGL-SGFGDRKPGQLSGGQQQ 158
Cdd:PRK11701 81 AERRRLLRTEWGFVHQ--HprdgLRMQVSAGGNIGERLMAVGARHYGDIRATAGDWLERVEIdAARIDDLPTTFSGGMQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830546 159 RVAIARALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHssELK-AR--ARRVVEIQDG 227
Cdd:PRK11701 159 RLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTH--DLAvARllAHRLLVMKQG 228
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
29-232 |
3.06e-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: 106.10 E-value: 3.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 29 ALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEeqlAVIRgKHLGFIFQffnlmpvln 108
Cdd:TIGR03375 480 ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDP---ADLR-RNIGYVPQ--------- 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 109 vfDNVYFPLVL--NGQFSKKEAT-ERTLHYLDSVGLSGFGDRKP-----------GQLSGGQQQRVAIARALAHEPMVVI 174
Cdd:TIGR03375 547 --DPRLFYGTLrdNIALGAPYADdEEILRAAELAGVTEFVRRHPdgldmqigergRSLSGGQRQAVALARALLRDPPILL 624
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 175 ADEPTGNLDLATGEAILDLLltinQQT--GTTFVISTHSSELKARARRVVEIQDGVLIHD 232
Cdd:TIGR03375 625 LDEPTSAMDNRSEERFKDRL----KRWlaGKTLVLVTHRTSLLDLVDRIIVMDNGRIVAD 680
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
26-230 |
3.10e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 102.57 E-value: 3.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 26 KVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAVIRGKhLGFIFQF-FNLM 104
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTVWDIREK-VGIVFQNpDNQF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 105 PVLNVFDNVYFPLVlNGQFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNLDL 184
Cdd:PRK13640 98 VGATVGDDVAFGLE-NRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDP 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15830546 185 ATGEAILDLLLTINQQTGTTFVISTHSSELKARARRVVEIQDGVLI 230
Cdd:PRK13640 177 AGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLL 222
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
13-216 |
3.39e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 102.57 E-value: 3.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 13 LSNIYKcygagaGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKllnQLPEEQLAVIRgK 92
Cdd:PRK13652 9 LCYSYS------GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGE---PITKENIREVR-K 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 93 HLGFIFQffnlmpvlNVFDNVYFPLV--------LNGQFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIAR 164
Cdd:PRK13652 79 FVGLVFQ--------NPDDQIFSPTVeqdiafgpINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAG 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15830546 165 ALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSELKA 216
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVP 202
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
33-227 |
3.87e-26 |
|
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: 103.65 E-value: 3.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 33 INLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLN------QLPEEQLAVirgkhlGFIFQFFNLMPV 106
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFdsrkgiFLPPEKRRI------GYVFQEARLFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 107 LNVFDNvyfplvLNGQFSKKEATERTLHY---LDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNLD 183
Cdd:TIGR02142 90 LSVRGN------LRYGMKRARPSERRISFervIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15830546 184 LATGEAILDLLLTINQQTGTTFVISTHS-SELKARARRVVEIQDG 227
Cdd:TIGR02142 164 DPRKYEILPYLERLHAEFGIPILYVSHSlQEVLRLADRVVVLEDG 208
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
29-211 |
5.13e-26 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 105.14 E-value: 5.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 29 ALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTViflnkLLNQLPeeqLAVIRGKHLGFIFQFFNLMPvlN 108
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEV-----TLDGVP---VSSLDQDEVRRRVSVCAQDA--H 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 109 VFDNVyfpLVLNGQFSKKEAT-ERTLHYLDSVGLSGFGDRKPG-----------QLSGGQQQRVAIARALAHEPMVVIAD 176
Cdd:TIGR02868 420 LFDTT---VRENLRLARPDATdEELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLD 496
|
170 180 190
....*....|....*....|....*....|....*
gi 15830546 177 EPTGNLDLATGEAILDLLLTINQqtGTTFVISTHS 211
Cdd:TIGR02868 497 EPTEHLDAETADELLEDLLAALS--GRTVVLITHH 529
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
29-230 |
5.38e-26 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 102.86 E-value: 5.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 29 ALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAVIRgKHLGFIFQ--FFNLMPV 106
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVR-SDIQMIFQdpLASLNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 107 LNVFDNVYFPL-VLNGQFSKKEATERTLHYLDSVGL-SGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNLDL 184
Cdd:PRK15079 115 MTIGEIIAEPLrTYHPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15830546 185 ATGEAILDLLLTINQQTGTTFVISTHSSELkararrVVEIQDGVLI 230
Cdd:PRK15079 195 SIQAQVVNLLQQLQREMGLSLIFIAHDLAV------VKHISDRVLV 234
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
33-227 |
5.77e-26 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 105.17 E-value: 5.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 33 INLDINKGEFLALCGPSGSGKS-TLLNILSGIDKP----TSGTVIFLNKLLNQLPEEQLAVIRGKHLGFIFQ--FFNLMP 105
Cdd:PRK15134 28 VSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGVRGNKIAMIFQepMVSLNP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 106 VLNVFDNVYFPLVLNGQFSKKEATERTLHYLDSVGLSGFGDR---KPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNL 182
Cdd:PRK15134 108 LHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRltdYPHQLSGGERQRVMIAMALLTRPELLIADEPTTAL 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15830546 183 DLATGEAILDLLLTINQQTGTTFVISTHS-SELKARARRVVEIQDG 227
Cdd:PRK15134 188 DVSVQAQILQLLRELQQELNMGLLFITHNlSIVRKLADRVAVMQNG 233
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
11-232 |
8.16e-26 |
|
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: 100.30 E-value: 8.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCY------------------GAGAGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVI 72
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 73 flnkllnqlpeeqlavIRGK-------HLGFifqffnlMPVLNVFDNVYFPLVLNGqFSKKEATERTLHYLDSVGLSGFG 145
Cdd:cd03220 81 ----------------VRGRvssllglGGGF-------NPELTGRENIYLNGRLLG-LSRKEIDEKIDEIIEFSELGDFI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 146 DRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQtGTTFVISTHS-SELKARARRVVEI 224
Cdd:cd03220 137 DLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDpSSIKRLCDRALVL 215
|
....*...
gi 15830546 225 QDGVLIHD 232
Cdd:cd03220 216 EKGKIRFD 223
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
29-227 |
9.23e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 101.37 E-value: 9.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 29 ALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQlpeEQLAVIRgKHLGFIFQFFNLMPVLN 108
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITD---DNFEKLR-KHIGIVFQNPDNQFVGS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 109 V--FDnVYFPLVlNGQFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNLDLAT 186
Cdd:PRK13648 100 IvkYD-VAFGLE-NHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15830546 187 GEAILDLLLTINQQTGTTFVISTHSSELKARARRVVEIQDG 227
Cdd:PRK13648 178 RQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKG 218
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
11-232 |
1.66e-25 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 100.16 E-value: 1.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGagaGKVdALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAvir 90
Cdd:COG4604 2 IEIKNVSKRYG---GKV-VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELA--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 gKHLGFIFQFFNLMPVLNVFDNVYFplvlnGQF--SK-------KEATERTLHYLDsvgLSGFGDRKPGQLSGGQQQRVA 161
Cdd:COG4604 75 -KRLAILRQENHINSRLTVRELVAF-----GRFpySKgrltaedREIIDEAIAYLD---LEDLADRYLDELSGGQRQRAF 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830546 162 IARALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSELKAR-ARRVVEIQDGVLIHD 232
Cdd:COG4604 146 IAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCyADHIVAMKDGRVVAQ 217
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
22-210 |
2.29e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 99.70 E-value: 2.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 22 AGAGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAvirgKHLGFIFQfF 101
Cdd:PRK11231 10 VGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA----RRLALLPQ-H 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 102 NLMPV-LNVFDNVYF---P-LVLNGQFSKKE------ATERTlhyldsvGLSGFGDRKPGQLSGGQQQRVAIARALAHEP 170
Cdd:PRK11231 85 HLTPEgITVRELVAYgrsPwLSLWGRLSAEDnarvnqAMEQT-------RINHLADRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15830546 171 MVVIADEPTGNLDLATGEAILDLLLTINQQtGTTFVISTH 210
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLH 196
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
29-227 |
2.42e-25 |
|
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: 99.23 E-value: 2.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 29 ALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNkllNQLPEEQLAVIRgKHLGFIFQ---FFNlmp 105
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDG---HDVRDYTLASLR-RQIGLVSQdvfLFN--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 106 vLNVFDNVyfplvlngQFSKKEAT-ERTLHYLDSVGLSGFGDRKPG-----------QLSGGQQQRVAIARALAHEPMVV 173
Cdd:cd03251 90 -DTVAENI--------AYGRPGATrEEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15830546 174 IADEPTGNLDLATGEAILDLL--LTINQqtgTTFVISTHSSELKaRARRVVEIQDG 227
Cdd:cd03251 161 ILDEATSALDTESERLVQAALerLMKNR---TTFVIAHRLSTIE-NADRIVVLEDG 212
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
9-207 |
2.65e-25 |
|
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: 99.29 E-value: 2.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 9 PAISLSNIYKCYGagagKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAv 88
Cdd:COG0410 2 PMLEVENLHAGYG----GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 89 irgkHLGF--------IFqffnlmPVLNVFDNvyfpLVLNGQFSKKEATERTLhyLDSVG-----LSGFGDRKPGQLSGG 155
Cdd:COG0410 77 ----RLGIgyvpegrrIF------PSLTVEEN----LLLGAYARRDRAEVRAD--LERVYelfprLKERRRQRAGTLSGG 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15830546 156 QQQRVAIARALAHEPMVVIADEPTgnLDLATG--EAILDLLLTINQQtGTTFVI 207
Cdd:COG0410 141 EQQMLAIGRALMSRPKLLLLDEPS--LGLAPLivEEIFEIIRRLNRE-GVTILL 191
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
7-227 |
3.56e-25 |
|
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: 102.90 E-value: 3.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 7 SLPA----ISLSNIYkcYGAGAGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLP 82
Cdd:COG4618 323 PLPRpkgrLSVENLT--VVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWD 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 83 EEQLavirGKHLGFIFQFFNLMP---VLNV--FDNVYFPLVLngqfskkEATERT-LH---------YLDSVGLSGFGdr 147
Cdd:COG4618 401 REEL----GRHIGYLPQDVELFDgtiAENIarFGDADPEKVV-------AAAKLAgVHemilrlpdgYDTRIGEGGAR-- 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 148 kpgqLSGGQQQRVAIARALAHEPMVVIADEPTGNLDlATGEAILDLLLTINQQTGTTFVISTHSSELKARARRVVEIQDG 227
Cdd:COG4618 468 ----LSGGQRQRIGLARALYGDPRLVVLDEPNSNLD-DEGEAALAAAIRALKARGATVVVITHRPSLLAAVDKLLVLRDG 542
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
11-227 |
7.94e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 98.91 E-value: 7.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGAGAgkvDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFlnKLLNQLPEEQLAVIR 90
Cdd:PRK13644 2 IRLENVSYSYPDGT---PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLV--SGIDTGDFSKLQGIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 gKHLGFIFQFFNLMPV-LNVFDNVYF-PLvlNGQFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAH 168
Cdd:PRK13644 77 -KLVGIVFQNPETQFVgRTVEEDLAFgPE--NLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTM 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15830546 169 EPMVVIADEPTGNLDLATGEAILDLLLTINQQtGTTFVISTHSSELKARARRVVEIQDG 227
Cdd:PRK13644 154 EPECLIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEELHDADRIIVMDRG 211
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
9-230 |
9.89e-25 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 97.98 E-value: 9.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 9 PAISLSNIYKCYGAGAGKVDalksINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNK-----LLNQLPE 83
Cdd:TIGR02323 2 PLLQVSGLSKSYGGGKGCRD----VSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRsgaelELYQLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 84 EQLAVIRGKHLGFIFQffnlmpvlNVFDNVYFPLVLNGQFSKKEATERTLHY----------LDSVGLS-GFGDRKPGQL 152
Cdd:TIGR02323 78 AERRRLMRTEWGFVHQ--------NPRDGLRMRVSAGANIGERLMAIGARHYgnirataqdwLEEVEIDpTRIDDLPRAF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 153 SGGQQQRVAIARALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSELkAR--ARRVVEIQDGVLI 230
Cdd:TIGR02323 150 SGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGV-ARllAQRLLVMQQGRVV 228
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
9-210 |
1.34e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 101.44 E-value: 1.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 9 PAISLSNIykCYGAGAGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLav 88
Cdd:PRK11160 337 VSLTLNNV--SFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAL-- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 89 iRgkhlgfifqffNLMPVLN----VFDNVyfpLVLNGQFSKKEAT-ERTLHYLDSVGLSGFGDRKPG----------QLS 153
Cdd:PRK11160 413 -R-----------QAISVVSqrvhLFSAT---LRDNLLLAAPNASdEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLS 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15830546 154 GGQQQRVAIARALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQqtGTTFVISTH 210
Cdd:PRK11160 478 GGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITH 532
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
30-227 |
3.48e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 100.27 E-value: 3.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 30 LKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTViflnkllnQLPEeqlavirGKHLGFIFQ--FfnlMPVL 107
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI--------ARPA-------GARVLFLPQrpY---LPLG 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 108 NVFDNVYFPLvLNGQFSKKEATErtlhYLDSVGLSGFGDR------KPGQLSGGQQQRVAIARALAHEPMVVIADEPTGN 181
Cdd:COG4178 441 TLREALLYPA-TAEAFSDAELRE----ALEAVGLGHLAERldeeadWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSA 515
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15830546 182 LDLATGEAILDLLLTinQQTGTTFVISTHSSELKARARRVVEIQDG 227
Cdd:COG4178 516 LDEENEAALYQLLRE--ELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
29-230 |
3.67e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 97.16 E-value: 3.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 29 ALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLN-KLLNQLPEEQLAVIRgKHLGFIFQFfnlmPVL 107
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDiTITHKTKDKYIRPVR-KRIGMVFQF----PES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 108 NVF-DNVYFPLVL---NGQFSKKEATERTLHYLDSVGLS-GFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNL 182
Cdd:PRK13646 97 QLFeDTVEREIIFgpkNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15830546 183 DLATGEAILDLLLTINQQTGTTFVISTHSSELKAR-ARRVVEIQDGVLI 230
Cdd:PRK13646 177 DPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARyADEVIVMKEGSIV 225
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
28-227 |
5.50e-24 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 94.42 E-value: 5.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 28 DALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQ-----LAVI---RGKHLgfifq 99
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDairagIAYVpedRKREG----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 100 ffnLMPVLNVFDNVYFPLvlngqfskkeatertlhyldsvglsgfgdrkpgQLSGGQQQRVAIARALAHEPMVVIADEPT 179
Cdd:cd03215 89 ---LVLDLSVAENIALSS---------------------------------LLSGGNQQKVVLARWLARDPRVLILDEPT 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15830546 180 GNLDLATGEAILDLLLTINQQTGTTFVISTHSSELKARARRVVEIQDG 227
Cdd:cd03215 133 RGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
29-218 |
5.57e-24 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 97.50 E-value: 5.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 29 ALKSINLDINKGEFLALCGPSGSGKS-TLLNILSGIDKPtsGTVI-----FLNKLLNQLPEEQLAVIRGKHLGFIFQffN 102
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVMaekleFNGQDLQRISEKERRNLVGAEVAMIFQ--D 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 103 LMPVLNVFDNVYFPL-----VLNGQfSKKEATERTLHYLDSVGLSGFGDR---KPGQLSGGQQQRVAIARALAHEPMVVI 174
Cdd:PRK11022 98 PMTSLNPCYTVGFQImeaikVHQGG-NKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15830546 175 ADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSELKARA 218
Cdd:PRK11022 177 ADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEA 220
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
11-211 |
7.21e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 95.92 E-value: 7.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGAG-AGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQlavi 89
Cdd:COG1101 2 LELKNLSKTFNPGtVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYK---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 90 RGKHLGFIFQffNLM----PVLNVFDNvyFPLVLN-GQF-------SKKEaTERTLHYLDSVGLsGFGDR---KPGQLSG 154
Cdd:COG1101 78 RAKYIGRVFQ--DPMmgtaPSMTIEEN--LALAYRrGKRrglrrglTKKR-RELFRELLATLGL-GLENRldtKVGLLSG 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15830546 155 GQQQRVAIARALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTG-TTFVIsTHS 211
Cdd:COG1101 152 GQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNlTTLMV-THN 208
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
25-217 |
1.12e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 95.62 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 25 GKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDK--PT---SGTVIFLNKLLNQLPEEQLAVIRgkHLGFIFQ 99
Cdd:PRK14243 21 GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNLYAPDVDPVEVRR--RIGMVFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 100 FFNLMPVlNVFDNVYFPLVLNG-QFSKKEATERTLHY----------LDSVGLSgfgdrkpgqLSGGQQQRVAIARALAH 168
Cdd:PRK14243 99 KPNPFPK-SIYDNIAYGARINGyKGDMDELVERSLRQaalwdevkdkLKQSGLS---------LSGGQQQRLCIARAIAV 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15830546 169 EPMVVIADEPTGNLDLATGEAILDLLLTINQQtgTTFVISTHSSELKAR 217
Cdd:PRK14243 169 QPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAAR 215
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
13-231 |
1.21e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 98.60 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 13 LSNIYKCYGagaGKVdALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIflnkllnqlpeeqlaVIRGK 92
Cdd:COG0488 1 LENLSKSFG---GRP-LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVS---------------IPKGL 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 93 HLGFIFQFFNLMPVLNVFDNV-------------YFPLVLNGQFSKKEATE--RTLHYLDSVG-----------LSGFG- 145
Cdd:COG0488 62 RIGYLPQEPPLDDDLTVLDTVldgdaelraleaeLEELEAKLAEPDEDLERlaELQEEFEALGgweaearaeeiLSGLGf 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 146 -----DRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNLDLatgEAIL---DLLltiNQQTGTTFVIStHSSE-LKA 216
Cdd:COG0488 142 peedlDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL---ESIEwleEFL---KNYPGTVLVVS-HDRYfLDR 214
|
250
....*....|....*
gi 15830546 217 RARRVVEIQDGVLIH 231
Cdd:COG0488 215 VATRILELDRGKLTL 229
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-231 |
1.37e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 98.21 E-value: 1.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 9 PAISLSNIYKCYGagaGKVdALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIflnkllnqlpeeqlav 88
Cdd:COG0488 314 KVLELEGLSKSYG---DKT-LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK---------------- 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 89 iRGKHL--GFIFQFF-NLMPVLNVFDNVyfplvlnGQFSKKEATERTLHYLDSVGLSGfgDR--KP-GQLSGGQQQRVAI 162
Cdd:COG0488 374 -LGETVkiGYFDQHQeELDPDKTVLDEL-------RDGAPGGTEQEVRGYLGRFLFSG--DDafKPvGVLSGGEKARLAL 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 163 ARALAHEPMVVIADEPTGNLDLATGEAILDLLLTINqqtGTTFVIStHSSELKAR-ARRVVEIQDGVLIH 231
Cdd:COG0488 444 AKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFP---GTVLLVS-HDRYFLDRvATRILEFEDGGVRE 509
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
11-230 |
1.67e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 98.39 E-value: 1.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGAGAGKVDALKSINLDINKGEFLALCGPSGSGKS-TLLNILSGIDKpTSGTV----IFLNKL------LN 79
Cdd:PRK10261 13 LAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-AGGLVqcdkMLLRRRsrqvieLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 80 QLPEEQLAVIRGKHLGFIFQ--FFNLMPVLNVFDNVYFPLVLNGQFSKKEATERTLHYLDSVGL---SGFGDRKPGQLSG 154
Cdd:PRK10261 92 EQSAAQMRHVRGADMAMIFQepMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIpeaQTILSRYPHQLSG 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15830546 155 GQQQRVAIARALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSELkararrVVEIQDGVLI 230
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGV------VAEIADRVLV 241
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
26-199 |
4.56e-23 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 93.10 E-value: 4.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 26 KVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGID---KPTSGTVIFLNKLLNqlPEEQLavirgKHLGFIFQFFN 102
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQPRK--PDQFQ-----KCVAYVRQDDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 103 LMPVLNVFDNVYFPLVL-------NGQFSKKEATERTLHyldsVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIA 175
Cdd:cd03234 92 LLPGLTVRETLTYTAILrlprkssDAIRKKRVEDVLLRD----LALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLIL 167
|
170 180 190
....*....|....*....|....*....|....*..
gi 15830546 176 DEPTGNLD-------------LATGEAIldLLLTINQ 199
Cdd:cd03234 168 DEPTSGLDsftalnlvstlsqLARRNRI--VILTIHQ 202
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
27-227 |
4.86e-23 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 94.09 E-value: 4.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 27 VDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIflnkllnqLPEEQLAV----IRGKHLGFIFQ--F 100
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELL--------IDDHPLHFgdysYRSQRIRMIFQdpS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 101 FNLMPVLNVFDNVYFPLVLNGQFSKKEATERTLHYLDSVGL-SGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPT 179
Cdd:PRK15112 98 TSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEAL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15830546 180 GNLDLATGEAILDLLLTINQQTGTTFVIST-HSSELKARARRVVEIQDG 227
Cdd:PRK15112 178 ASLDMSMRSQLINLMLELQEKQGISYIYVTqHLGMMKHISDQVLVMHQG 226
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
29-210 |
4.89e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 96.70 E-value: 4.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 29 ALKSINLDINKGEFLALCGPSGSGKST----LLNILsgidkPTSGTVIFLNKLLNQLPEEQLAVIRgKHLGFIFQFFN-- 102
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLLPVR-HRIQVVFQDPNss 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 103 LMPVLNVFDNVYFPL-VLNGQFSKKEATERTLHYLDSVGLSGFG-DRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTG 180
Cdd:PRK15134 375 LNPRLNVLQIIEEGLrVHQPTLSAAQREQQVIAVMEEVGLDPETrHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
|
170 180 190
....*....|....*....|....*....|
gi 15830546 181 NLDLATGEAILDLLLTINQQTGTTFVISTH 210
Cdd:PRK15134 455 SLDKTVQAQILALLKSLQQKHQLAYLFISH 484
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
11-183 |
1.34e-22 |
|
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: 91.84 E-value: 1.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGagagKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAvir 90
Cdd:cd03218 1 LRAENLSKRYG----KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 GKHLGFIFQFFNLMPVLNVFDNVYfpLVLNGQ-FSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHE 169
Cdd:cd03218 74 RLGIGYLPQEASIFRKLTVEENIL--AVLEIRgLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATN 151
|
170
....*....|....
gi 15830546 170 PMVVIADEPTGNLD 183
Cdd:cd03218 152 PKFLLLDEPFAGVD 165
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
20-225 |
1.44e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 91.70 E-value: 1.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 20 YGAGAGKVdaLKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAvirgKHLGFIFQ 99
Cdd:PRK10247 15 YLAGDAKI--LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYR----QQVSYCAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 100 ffnlMPVL---NVFDNVYFPLVLNGQFSKKEATERTLHYldsvglsgFG------DRKPGQLSGGQQQRVAIARALAHEP 170
Cdd:PRK10247 89 ----TPTLfgdTVYDNLIFPWQIRNQQPDPAIFLDDLER--------FAlpdtilTKNIAELSGGEKQRISLIRNLQFMP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15830546 171 MVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSELKARARRVVEIQ 225
Cdd:PRK10247 157 KVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQ 211
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
11-235 |
1.65e-22 |
|
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: 95.28 E-value: 1.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGAgagkVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGI--DKPTSGTVIFLNKllnQLPEEQLAV 88
Cdd:TIGR02633 2 LEMKGIVKTFGG----VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGS---PLKASNIRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 89 IRGKHLGFIFQFFNLMPVLNVFDNVYF--PLVLNGQFSKKEA-TERTLHYLDSVGLSGFGDRKP-GQLSGGQQQRVAIAR 164
Cdd:TIGR02633 75 TERAGIVIIHQELTLVPELSVAENIFLgnEITLPGGRMAYNAmYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830546 165 ALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSELKARARRVVEIQDGVLIHDSDA 235
Cdd:TIGR02633 155 ALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDM 225
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
11-227 |
4.40e-22 |
|
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: 88.27 E-value: 4.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGAGagkvDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIflnkllnqlpeeqlaviR 90
Cdd:cd03221 1 IELENLSKTYGGK----LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT-----------------W 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 GKHLGFifqffnlmpvlnvfdnVYFPlvlngqfskkeatertlhyldsvglsgfgdrkpgQLSGGQQQRVAIARALAHEP 170
Cdd:cd03221 60 GSTVKI----------------GYFE----------------------------------QLSGGEKMRLALAKLLLENP 89
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15830546 171 MVVIADEPTGNLDLATGEAILDLLLTINQqtgtTFVISTHSSE-LKARARRVVEIQDG 227
Cdd:cd03221 90 NLLLLDEPTNHLDLESIEALEEALKEYPG----TVILVSHDRYfLDQVATKIIELEDG 143
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
25-210 |
5.30e-22 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 92.28 E-value: 5.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 25 GKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPtSGTV----IFLN--KLLNQLPEEQLAVIrGKHLGFIF 98
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKD-NWHVtadrFRWNgiDLLKLSPRERRKII-GREIAMIF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 99 Q--FFNLMPVLNVFDNVYFPLvLNGQFS---------KKEATERTLHyldSVGLSgfgDRK------PGQLSGGQQQRVA 161
Cdd:COG4170 96 QepSSCLDPSAKIGDQLIEAI-PSWTFKgkwwqrfkwRKKRAIELLH---RVGIK---DHKdimnsyPHELTEGECQKVM 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15830546 162 IARALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTH 210
Cdd:COG4170 169 IAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISH 217
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
30-214 |
5.52e-22 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 93.96 E-value: 5.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 30 LKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPtsGTVIFLNKLLNQLP--EEQLAVIRgkhlGFIFQFFNLMPVL 107
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPK--GVKGSGSVLLNGMPidAKEMRAIS----AYVQQDDLFIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 108 NVFDNVYFP--LVLNGQFSKKEATERTLHYLDSVGLS-------GFGDRKPGqLSGGQQQRVAIARALAHEPMVVIADEP 178
Cdd:TIGR00955 115 TVREHLMFQahLRMPRRVTKKEKRERVDEVLQALGLRkcantriGVPGRVKG-LSGGERKRLAFASELLTDPPLLFCDEP 193
|
170 180 190
....*....|....*....|....*....|....*...
gi 15830546 179 TGNLDLATGEAILDLLLTINQQtGTTFVISTH--SSEL 214
Cdd:TIGR00955 194 TSGLDSFMAYSVVQVLKGLAQK-GKTIICTIHqpSSEL 230
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
33-225 |
5.80e-22 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 89.48 E-value: 5.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 33 INLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEE---QLAVIrGKHLGfifqffnLMPVLNV 109
Cdd:PRK13538 20 LSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEyhqDLLYL-GHQPG-------IKTELTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 110 FDNVYFPLVLNGQFSkkeaTERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNLDlATGEA 189
Cdd:PRK13538 92 LENLRFYQRLHGPGD----DEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID-KQGVA 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 15830546 190 ILDLLLTINQQTGTTFVISTHsSELKARARRVVEIQ 225
Cdd:PRK13538 167 RLEALLAQHAEQGGMVILTTH-QDLPVASDKVRKLR 201
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
15-227 |
7.48e-22 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 93.46 E-value: 7.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 15 NIYKCYGAgagkVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIdKPT---SGTVIFLNKLLnqlpeeQLAVIRG 91
Cdd:PRK13549 10 NITKTFGG----VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEEL------QASNIRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 92 ---KHLGFIFQFFNLMPVLNVFDNVYF--PLVLNGQFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARAL 166
Cdd:PRK13549 79 terAGIAIIHQELALVKELSVLENIFLgnEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKAL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830546 167 AHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSELKARARRVVEIQDG 227
Cdd:PRK13549 159 NKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDG 219
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
30-212 |
9.96e-22 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 89.16 E-value: 9.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 30 LKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNK-LLNQLPEEQLAVIrgKHLGFifqffnLMPVLN 108
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGdIDDPDVAEACHYL--GHRNA------MKPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 109 VFDNVYFPLVLNGQfskkeATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARAL-AHEPmVVIADEPTGNLDLATG 187
Cdd:PRK13539 90 VAENLEFWAAFLGG-----EELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLvSNRP-IWILDEPTAALDAAAV 163
|
170 180
....*....|....*....|....*
gi 15830546 188 EAILDLLLTiNQQTGTTFVISTHSS 212
Cdd:PRK13539 164 ALFAELIRA-HLAQGGIVIAATHIP 187
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
33-235 |
1.10e-21 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 90.14 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 33 INLDINKGEFLALCGPSGSGKS----TLLNILSGIDKPTSGTViflnkLLNQLPEEqLAVIRGKHLGFIFQ----FFNlm 104
Cdd:PRK10418 22 VSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRV-----LLDGKPVA-PCALRGRKIATIMQnprsAFN-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 105 PVLNVFDNVYFPLVLNGqfskKEATERTL-HYLDSVGLSGFG---DRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTG 180
Cdd:PRK10418 94 PLHTMHTHARETCLALG----KPADDATLtAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15830546 181 NLDLATGEAILDLLLTINQQTGTTFVISTHSSELKAR-ARRVVEIQDGVLIHDSDA 235
Cdd:PRK10418 170 DLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARlADDVAVMSHGRIVEQGDV 225
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
9-217 |
1.14e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 92.21 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 9 PAISLSNIYKCYGAgagkVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLA- 87
Cdd:PRK09536 2 PMIDVSDLSVEFGD----TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 88 ----VIRGKHLGFIFQffnlmpVLNVFDNVYFPLVlnGQFSKKEATERTL--HYLDSVGLSGFGDRKPGQLSGGQQQRVA 161
Cdd:PRK09536 78 rvasVPQDTSLSFEFD------VRQVVEMGRTPHR--SRFDTWTETDRAAveRAMERTGVAQFADRPVTSLSGGERQRVL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15830546 162 IARALAHEPMVVIADEPTGNLDLATGEAILDLLLTInQQTGTTFVISTHSSELKAR 217
Cdd:PRK09536 150 LARALAQATPVLLLDEPTASLDINHQVRTLELVRRL-VDDGKTAVAAIHDLDLAAR 204
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
30-230 |
2.00e-21 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 89.13 E-value: 2.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 30 LKSINLDINKGEFLALCGPSGSGKSTLLNILSGIdKPTSGTVIFLNKLLNQLPEEQLAVIRG------KHLGFI--FQFF 101
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAELARHRAylsqqqSPPFAMpvFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 102 NLmpvlnvfdnvYFPLVLNgqfskKEATERTLHYL-DSVGLSGFGDRKPGQLSGGQQQRVAIARALAH-------EPMVV 173
Cdd:COG4138 91 AL----------HQPAGAS-----SEAVEQLLAQLaEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15830546 174 IADEPTGNLDLATGEAILDLLLTINQQtGTTFVISTHSSELKAR-ARRVVEIQDGVLI 230
Cdd:COG4138 156 LLDEPMNSLDVAQQAALDRLLRELCQQ-GITVVMSSHDLNHTLRhADRVWLLKQGKLV 212
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
7-217 |
2.40e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 90.25 E-value: 2.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 7 SLPAISLSNIYKCYGAGAgKVDALksiNLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKllnqlPEEQL 86
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDKL-VVDGL---SFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGE-----PVPSR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 87 AVIRGKHLGFIFQFFNLMPVLNVFDNV-----YFPLvlngqfSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVA 161
Cdd:PRK13537 75 ARHARQRVGVVPQFDNLDPDFTVRENLlvfgrYFGL------SAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLT 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15830546 162 IARALAHEPMVVIADEPTGNLDLATGEAILDLLLTInQQTGTTFVISTHSSELKAR 217
Cdd:PRK13537 149 LARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSL-LARGKTILLTTHFMEEAER 203
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
30-229 |
3.12e-21 |
|
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: 88.30 E-value: 3.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 30 LKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEeqlavirgKHLGFIFQFFNLMPVL-- 107
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEH--------KYLHSKVSLVGQEPVLfa 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 108 -NVFDNVYFPLvlnGQFSKKEATE--RTLHYLDSVGLSGFG-----DRKPGQLSGGQQQRVAIARALAHEPMVVIADEPT 179
Cdd:cd03248 102 rSLQDNIAYGL---QSCSFECVKEaaQKAHAHSFISELASGydtevGEKGSQLSGGQKQRVAIARALIRNPQVLILDEAT 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15830546 180 GNLDLATGEAILDLLLTINQQTgTTFVISTHSSELKaRARRVVEIQDGVL 229
Cdd:cd03248 179 SALDAESEQQVQQALYDWPERR-TVLVIAHRLSTVE-RADQILVLDGGRI 226
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
27-227 |
3.14e-21 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 91.39 E-value: 3.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 27 VDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIdKPT---SGTVIFLNKllnqlpEEQLAVIRG-KHLGF--IFQF 100
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHgsyEGEILFDGE------VCRFKDIRDsEALGIviIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 101 FNLMPVLNVFDNVYF--PLVLNGQFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEP 178
Cdd:NF040905 87 LALIPYLSIAENIFLgnERAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEP 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15830546 179 TGNLDLATGEAILDLLLTINQQTGTTFVISTHSSELKARARRVVEIQDG 227
Cdd:NF040905 167 TAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDG 215
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
23-230 |
3.87e-21 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 88.89 E-value: 3.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 23 GAGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAvirgKHLGFIFQFFN 102
Cdd:PRK10253 16 GYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA----RRIGLLAQNAT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 103 LMPVLNVFDnvyfpLVLNGQFS--------KKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVI 174
Cdd:PRK10253 92 TPGDITVQE-----LVARGRYPhqplftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15830546 175 ADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSELKAR-ARRVVEIQDGVLI 230
Cdd:PRK10253 167 LDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRyASHLIALREGKIV 223
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
11-230 |
5.09e-21 |
|
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: 86.60 E-value: 5.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGAGAGKVdaLKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTvIFLNKLLNQLPEEQLAvir 90
Cdd:cd03247 1 LSINNVSFSYPEQEQQV--LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGE-ITLDGVPVSDLEKALS--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 gkhlgfifqffNLMPVLN----VFDNvyfplvlngqfskkeaterTLhyLDSVGLsgfgdrkpgQLSGGQQQRVAIARAL 166
Cdd:cd03247 75 -----------SLISVLNqrpyLFDT-------------------TL--RNNLGR---------RFSGGERQRLALARIL 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830546 167 AHEPMVVIADEPTGNLDLATGEAILDLLLtiNQQTGTTFVISTHSSELKARARRVVEIQDGVLI 230
Cdd:cd03247 114 LQDAPIVLLDEPTVGLDPITERQLLSLIF--EVLKDKTLIWITHHLTGIEHMDKILFLENGKII 175
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
28-214 |
6.13e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 90.46 E-value: 6.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 28 DALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQ-------------LPEEqlaviRgKHL 94
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIrsprdairagiayVPED-----R-KGE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 95 GfifqffnLMPVLNVFDNVYFP----LVLNGQFSKKEATERTLHYLDSVGLSGFGDRKP-GQLSGGQQQRVAIARALAHE 169
Cdd:COG1129 340 G-------LVLDLSIRENITLAsldrLSRGGLLDRRRERALAEEYIKRLRIKTPSPEQPvGNLSGGNQQKVVLAKWLATD 412
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15830546 170 PMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVIsthSSEL 214
Cdd:COG1129 413 PKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVI---SSEL 454
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
12-179 |
8.80e-21 |
|
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: 87.20 E-value: 8.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 12 SLSNIYKCYGAGagkvDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAViRG 91
Cdd:TIGR03410 2 EVSNLNVYYGQS----HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERAR-AG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 92 khLGFIFQFFNLMPVLNVFDNVYfpLVLNGQFSKKEATERTLHYLDSVgLSGFGDRKPGQLSGGQQQRVAIARALAHEPM 171
Cdd:TIGR03410 77 --IAYVPQGREIFPRLTVEENLL--TGLAALPRRSRKIPDEIYELFPV-LKEMLGRRGGDLSGGQQQQLAIARALVTRPK 151
|
....*...
gi 15830546 172 VVIADEPT 179
Cdd:TIGR03410 152 LLLLDEPT 159
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-230 |
9.86e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 88.73 E-value: 9.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 2 QSTIKSLPAISLSNIYKCYGaGAGKVDALksiNLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNkllnqL 81
Cdd:PRK13536 33 IPGSMSTVAIDLAGVSKSYG-DKAVVNGL---SFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG-----V 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 82 PEEQLAVIRGKHLGFIFQFFNLMPVLNVFDNvyfpLVLNGQF---SKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQ 158
Cdd:PRK13536 104 PVPARARLARARIGVVPQFDNLDLEFTVREN----LLVFGRYfgmSTREIEAVIPSLLEFARLESKADARVSDLSGGMKR 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15830546 159 RVAIARALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQtGTTFVISTHSSELKAR-ARRVVEIQDGVLI 230
Cdd:PRK13536 180 RLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERlCDRLCVLEAGRKI 251
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
8-229 |
1.09e-20 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 90.46 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 8 LPAISLSNIYKCYG-AGAGKVDALksiNLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLnqlpEEQL 86
Cdd:TIGR01257 926 VPGVCVKNLVKIFEpSGRPAVDRL---NITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNL 998
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 87 AVIRgKHLGFIFQFFNLMPVLNVFDNVYFPLVLNGQfSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARAL 166
Cdd:TIGR01257 999 DAVR-QSLGMCPQHNILFHHLTVAEHILFYAQLKGR-SWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAF 1076
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830546 167 AHEPMVVIADEPTGNLDLATGEAILDLLLtiNQQTGTTFVISTHS-SELKARARRVVEIQDGVL 229
Cdd:TIGR01257 1077 VGDAKVVVLDEPTSGVDPYSRRSIWDLLL--KYRSGRTIIMSTHHmDEADLLGDRIAIISQGRL 1138
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
10-179 |
2.87e-20 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 89.03 E-value: 2.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 10 AISLSNIYKCYGagagKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAVI 89
Cdd:NF033858 1 VARLEGVSHRYG----KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 90 R--------GKhlgfifqffNLMPVLNVFDNVYFPLVLNGQfSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVA 161
Cdd:NF033858 77 RiaympqglGK---------NLYPTLSVFENLDFFGRLFGQ-DAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLG 146
|
170
....*....|....*...
gi 15830546 162 IARALAHEPMVVIADEPT 179
Cdd:NF033858 147 LCCALIHDPDLLILDEPT 164
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
11-178 |
3.27e-20 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 85.85 E-value: 3.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGagagKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAvIR 90
Cdd:COG1137 4 LEAENLVKSYG----KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRA-RL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 GkhLGF------IFQffnlmpVLNVFDNVYfpLVLNGQ-FSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIA 163
Cdd:COG1137 79 G--IGYlpqeasIFR------KLTVEDNIL--AVLELRkLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIA 148
|
170
....*....|....*
gi 15830546 164 RALAHEPMVVIADEP 178
Cdd:COG1137 149 RALATNPKFILLDEP 163
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
29-227 |
4.13e-20 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 84.44 E-value: 4.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 29 ALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKL--LNQLPEEQLAVIRGKHLGFifqffnlmpv 106
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIayVSQEPWIQNGTIRENILFG---------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 107 lNVFDNVYFPLVLNG--------QFSKKEATErtlhyldsVGLSGFGdrkpgqLSGGQQQRVAIARALAHEPMVVIADEP 178
Cdd:cd03250 90 -KPFDEERYEKVIKAcalepdleILPDGDLTE--------IGEKGIN------LSGGQKQRISLARAVYSDADIYLLDDP 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15830546 179 TGNLDLATGEAILDLLLTINQQTGTTFVISTHSSELKARARRVVEIQDG 227
Cdd:cd03250 155 LSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-211 |
5.63e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 85.47 E-value: 5.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 6 KSLPAISLSNIYKCYGAGagkvDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTS-----GTVIFLNKllnQ 80
Cdd:PRK14258 3 KLIPAIKVNNLSFYYDTQ----KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQ---N 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 81 LPEEQLAVIR-GKHLGFIFQFFNLMPvLNVFDNVYFPLVLNGQFSKKEatertlhyLDSVGLSGFGD------------R 147
Cdd:PRK14258 76 IYERRVNLNRlRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKLE--------IDDIVESALKDadlwdeikhkihK 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830546 148 KPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHS 211
Cdd:PRK14258 147 SALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHN 210
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
27-230 |
8.11e-20 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 87.46 E-value: 8.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 27 VDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNkllNQLPEEQLAVIRgKHLGFIFQ---FFNL 103
Cdd:TIGR02203 345 RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDG---HDLADYTLASLR-RQVALVSQdvvLFND 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 104 mpvlNVFDNVYFPLVlnGQFSKkeatERTLHYLDSVGLSGFGDRKP-----------GQLSGGQQQRVAIARALAHEPMV 172
Cdd:TIGR02203 421 ----TIANNIAYGRT--EQADR----AEIERALAAAYAQDFVDKLPlgldtpigengVLLSGGQRQRLAIARALLKDAPI 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15830546 173 VIADEPTGNLDLATGEAILDLLLTInQQTGTTFVISTHSSELKaRARRVVEIQDGVLI 230
Cdd:TIGR02203 491 LILDEATSALDNESERLVQAALERL-MQGRTTLVIAHRLSTIE-KADRIVVMDDGRIV 546
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
9-235 |
9.60e-20 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 84.55 E-value: 9.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 9 PAISLSNIYKCYGagagKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLpeeQLAV 88
Cdd:PRK11614 4 VMLSFDKVSAHYG----KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDW---QTAK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 89 IRGKHLGFIFQFFNLMPVLNVFDNvyfpLVLNGQFSKKEATERTLHYLDSVGLSGFGDR--KPGQLSGGQQQRVAIARAL 166
Cdd:PRK11614 77 IMREAVAIVPEGRRVFSRMTVEEN----LAMGGFFAERDQFQERIKWVYELFPRLHERRiqRAGTMSGGEQQMLAIGRAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 167 AHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSELKARARRVVEIQDG-VLIHDSDA 235
Cdd:PRK11614 153 MSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGhVVLEDTGD 222
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
29-230 |
1.04e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 85.44 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 29 ALKSINLDINKGEFLALCGPSGSGKSTLLNILSG-IDKPTSGTVIFLNKLLNQLPE-EQLAVIRgKHLGFIFQFfnlmPV 106
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGlIISETGQTIVGDYAIPANLKKiKEVKRLR-KEIGLVFQF----PE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 107 LNVF------DNVYFPLVLNGqfSKKEATERTLHYLDSVGL-SGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPT 179
Cdd:PRK13645 101 YQLFqetiekDIAFGPVNLGE--NKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPT 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15830546 180 GNLDLATGEAILDLLLTINQQTGTTFVISTHSSElkararRVVEIQDGVLI 230
Cdd:PRK13645 179 GGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMD------QVLRIADEVIV 223
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
27-233 |
1.10e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 85.14 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 27 VDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKllnQLPEEQLAVIRGKhLGFIFQF-FNLMP 105
Cdd:PRK13642 20 VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE---LLTAENVWNLRRK-IGMVFQNpDNQFV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 106 VLNVFDNVYFPLVLNGqFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNLDLA 185
Cdd:PRK13642 96 GATVEDDVAFGMENQG-IPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPT 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15830546 186 TGEAILDLLLTINQQTGTTFVISTHSSELKARARRVVEIQDGVLIHDS 233
Cdd:PRK13642 175 GRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEA 222
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
30-230 |
1.28e-19 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 84.21 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 30 LKSINLDINKGEFLALCGPSGSGKSTLLNILSGIdKPTSGTVIFLNKLLNQLPEEQLAVIRgkhlGFIFQFFN---LMPV 106
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHR----AYLSQQQTppfAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 107 LNvfdnvYFPLVLNGQfSKKEATERTLHYL-DSVGLSGFGDRKPGQLSGGQQQRVAIA-------RALAHEPMVVIADEP 178
Cdd:PRK03695 87 FQ-----YLTLHQPDK-TRTEAVASALNEVaEALGLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15830546 179 TGNLDLATgEAILDLLLTINQQTGTTFVISTHSSELKAR-ARRVVEIQDGVLI 230
Cdd:PRK03695 161 MNSLDVAQ-QAALDRLLSELCQQGIAVVMSSHDLNHTLRhADRVWLLKQGKLL 212
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
7-182 |
1.34e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 86.89 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 7 SLPAISLSNIYKCYGAgagkVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTViflnkllnqlpeeql 86
Cdd:PRK11288 1 SSPYLSFDGIGKTFPG----VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSI--------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 87 aVIRGKHLGF-------------IFQFFNLMPVLNVFDNVYFplvlnGQF-------SKKEATERTLHYLDSVGLSGFGD 146
Cdd:PRK11288 62 -LIDGQEMRFasttaalaagvaiIYQELHLVPEMTVAENLYL-----GQLphkggivNRRLLNYEAREQLEHLGVDIDPD 135
|
170 180 190
....*....|....*....|....*....|....*.
gi 15830546 147 RKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNL 182
Cdd:PRK11288 136 TPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSL 171
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1-232 |
4.17e-19 |
|
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: 85.56 E-value: 4.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 1 MQSTIKSLPAISLSNIYKCYGAGAgkvDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQ 80
Cdd:TIGR01193 464 RTELNNLNGDIVINDVSYSYGYGS---NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKD 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 81 LPEEQLAvirgkhlgfifQFFNLMPVLNV-FDNVYFPLVLNGqfSKKEATERTLhyLDSVGLS-----------GFGDR- 147
Cdd:TIGR01193 541 IDRHTLR-----------QFINYLPQEPYiFSGSILENLLLG--AKENVSQDEI--WAACEIAeikddienmplGYQTEl 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 148 --KPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTgTTFVisTHSSELKARARRVVEIQ 225
Cdd:TIGR01193 606 seEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDKT-IIFV--AHRLSVAKQSDKIIVLD 682
|
....*..
gi 15830546 226 DGVLIHD 232
Cdd:TIGR01193 683 HGKIIEQ 689
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
27-230 |
4.27e-19 |
|
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: 82.59 E-value: 4.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 27 VDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLaviRgKHLGFIFQffnlMPV 106
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWL---R-SQIGLVSQ----EPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 107 LnvFDN-VYFplvlNGQFSKKEATERT---------LH---------YLDSVGLSGFgdrkpgQLSGGQQQRVAIARALA 167
Cdd:cd03249 88 L--FDGtIAE----NIRYGKPDATDEEveeaakkanIHdfimslpdgYDTLVGERGS------QLSGGQKQRIAIARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830546 168 HEPMVVIADEPTGNLDLATGEAI---LDLLLtinqqTGTTFVISTHS-SELKaRARRVVEIQDGVLI 230
Cdd:cd03249 156 RNPKILLLDEATSALDAESEKLVqeaLDRAM-----KGRTTIVIAHRlSTIR-NADLIAVLQNGQVV 216
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
33-227 |
5.36e-19 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 84.16 E-value: 5.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 33 INLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQ------LPEEQlavirgKHLGFIFQFFNLMPV 106
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDaekgicLPPEK------RRIGYVFQDARLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 107 LNVFDNVYFPLvlngqfskkeATERTLHYLDSVGLSGFG---DRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNLD 183
Cdd:PRK11144 91 YKVRGNLRYGM----------AKSMVAQFDKIVALLGIEpllDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15830546 184 LATGEAILDLLLTINQQTGTTFVISTHS-SELKARARRVVEIQDG 227
Cdd:PRK11144 161 LPRKRELLPYLERLAREINIPILYVSHSlDEILRLADRVVVLEQG 205
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
11-210 |
6.28e-19 |
|
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: 82.28 E-value: 6.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGAGagkVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLpeeQLAVIR 90
Cdd:cd03253 1 IEFENVTFAYDPG---RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREV---TLDSLR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 gKHLGFIFQ---FFNlmpvlnvfDNVYFplvlNGQFSKKEATE-------RTLHYLDSVGLSGFG-DRKPGQ----LSGG 155
Cdd:cd03253 75 -RAIGVVPQdtvLFN--------DTIGY----NIRYGRPDATDeevieaaKAAQIHDKIMRFPDGyDTIVGErglkLSGG 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15830546 156 QQQRVAIARALAHEPMVVIADEPTGNLDLATGEAILDLLLTInqQTGTTFVISTH 210
Cdd:cd03253 142 EKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDV--SKGRTTIVIAH 194
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
30-216 |
9.90e-19 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 81.54 E-value: 9.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 30 LKSINLDINKGEFLALCGPSGSGKSTLLNILSGI--DKPTSGTVIFLNkllNQLPEEqlavirgkhlgfifqffnlmpvL 107
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAlkGTPVAGCVDVPD---NQFGRE----------------------A 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 108 NVFDNVYfplvLNGqfSKKEATErtlhYLDSVGLSgfgD-----RKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNL 182
Cdd:COG2401 101 SLIDAIG----RKG--DFKDAVE----LLNAVGLS---DavlwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHL 167
|
170 180 190
....*....|....*....|....*....|....
gi 15830546 183 DLATGEAILDLLLTINQQTGTTFVISTHSSELKA 216
Cdd:COG2401 168 DRQTAKRVARNLQKLARRAGITLVVATHHYDVID 201
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
11-232 |
1.75e-18 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 80.99 E-value: 1.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGAGAGkvDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNkllNQLPEEQLAVIR 90
Cdd:cd03252 1 ITFEHVRFRYKPDGP--VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDG---HDLALADPAWLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 gKHLGFIFQFfNLMPVLNVFDNVYF----PLVLNGQFSKKEA------TERTLHYLDSVGLSGFGdrkpgqLSGGQQQRV 160
Cdd:cd03252 76 -RQVGVVLQE-NVLFNRSIRDNIALadpgMSMERVIEAAKLAgahdfiSELPEGYDTIVGEQGAG------LSGGQRQRI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830546 161 AIARALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQqtGTTFVISTHSSELKARARRVVEIQDGVLIHD 232
Cdd:cd03252 148 AIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKNADRIIVMEKGRIVEQ 217
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
22-195 |
2.48e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 83.15 E-value: 2.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 22 AGAGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNK-LLNQLPEEqlavIRGKHLGFI--- 97
Cdd:COG3845 266 RDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEdITGLSPRE----RRRLGVAYIped 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 98 FQFFNLMPVLNVFDNVYF------PLVLNGQFSKKEATERTLHYLDSvglsgFGDRKPG------QLSGGQQQRVAIARA 165
Cdd:COG3845 342 RLGRGLVPDMSVAENLILgryrrpPFSRGGFLDRKAIRAFAEELIEE-----FDVRTPGpdtparSLSGGNQQKVILARE 416
|
170 180 190
....*....|....*....|....*....|
gi 15830546 166 LAHEPMVVIADEPTGNLDLATGEAILDLLL 195
Cdd:COG3845 417 LSRDPKLLIAAQPTRGLDVGAIEFIHQRLL 446
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
30-226 |
2.60e-18 |
|
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: 78.73 E-value: 2.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 30 LKSINLDINKGEFLALCGPSGSGKSTLLNILSG--------IDKPTSGTVIFLNkllnQLPeeqlavirgkhlgfifqff 101
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGlwpwgsgrIGMPEGEDLLFLP----QRP------------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 102 nlmpvlnvfdnvYFPLVlngqfSKKEAtertLHY-LDSVglsgfgdrkpgqLSGGQQQRVAIARALAHEPMVVIADEPTG 180
Cdd:cd03223 74 ------------YLPLG-----TLREQ----LIYpWDDV------------LSGGEQQRLAFARLLLHKPKFVFLDEATS 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15830546 181 NLDLATGEAILDLLltinQQTGTTFVISTHSSELKARARRVVEIQD 226
Cdd:cd03223 121 ALDEESEDRLYQLL----KELGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
30-214 |
5.48e-18 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 78.72 E-value: 5.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 30 LKSINLDINKGEFLALCGPSGSGKSTLLNILSGID--KPTSGTVIFLNKLLNQLPEEQLAvirGKHLGFIFQffnlMPvl 107
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERA---RLGIFLAFQ----YP-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 108 nvfdnVYFPLVLNGQFskkeatertLHYLDsVGLSGfGDRKpgqlsggqqqRVAIARALAHEPMVVIADEPTGNLDLATG 187
Cdd:cd03217 87 -----PEIPGVKNADF---------LRYVN-EGFSG-GEKK----------RNEILQLLLLEPDLAILDEPDSGLDIDAL 140
|
170 180
....*....|....*....|....*..
gi 15830546 188 EAILDLLLTINQQtGTTFVISTHSSEL 214
Cdd:cd03217 141 RLVAEVINKLREE-GKSVLIITHYQRL 166
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
30-183 |
2.06e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 78.40 E-value: 2.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 30 LKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAvIRGkhLGFIFQFFNLMPVLNV 109
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARA-RRG--IGYLPQEASIFRRLSV 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830546 110 FDNVYFPLVLNGQFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNLD 183
Cdd:PRK10895 96 YDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
9-224 |
2.09e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 80.43 E-value: 2.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 9 PAISLSNIYKCYGAgagkVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNK--LLNQLPEEQL 86
Cdd:PRK10762 3 ALLQLKGIDKAFPG----VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKevTFNGPKSSQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 87 AVIrgkhlGFIFQFFNLMPVLNVFDNVYFPLVLNGQFSK---KEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIA 163
Cdd:PRK10762 79 AGI-----GIIHQELNLIPQLTIAENIFLGREFVNRFGRidwKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830546 164 RALAHEPMVVIADEPTgnldlatgEAILDllltinQQTGTTF-VIsthsSELKARARRVVEI 224
Cdd:PRK10762 154 KVLSFESKVIIMDEPT--------DALTD------TETESLFrVI----RELKSQGRGIVYI 197
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-229 |
2.45e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.09 E-value: 2.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 1 MQSTIKS-LPAISLSNIYKCYGAgagkVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTViflnkLLN 79
Cdd:PRK15439 1 MQTSDTTaPPLLCARSISKQYSG----VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTL-----EIG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 80 QLPEEQLAVIRGKHLG--FIFQFFNLMPVLNVFDNVYFPLvlngqfSKKEATERTL-HYLDSVGLSGFGDRKPGQLSGGQ 156
Cdd:PRK15439 72 GNPCARLTPAKAHQLGiyLVPQEPLLFPNLSVKENILFGL------PKRQASMQKMkQLLAALGCQLDLDSSAGSLEVAD 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15830546 157 QQRVAIARALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSELKARARRVVEIQDGVL 229
Cdd:PRK15439 146 RQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
29-211 |
2.66e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 78.39 E-value: 2.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 29 ALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLA--VIRGKHLGFIFqffnlmPV 106
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVayVPQSEEVDWSF------PV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 107 LnVFDnvyfpLVLNGQF--------SKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEP 178
Cdd:PRK15056 96 L-VED-----VVMMGRYghmgwlrrAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEP 169
|
170 180 190
....*....|....*....|....*....|...
gi 15830546 179 TGNLDLATGEAILDLLLTINQQtGTTFVISTHS 211
Cdd:PRK15056 170 FTGVDVKTEARIISLLRELRDE-GKTMLVSTHN 201
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
30-229 |
3.14e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 80.15 E-value: 3.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 30 LKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAvirgKHLGFIFQffnlMPVL-- 107
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLH----RQVALVGQ----EPVLfs 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 108 -NVFDNVYFPL-------VLNgqfSKKEA------TERTLHYLDSVGLSGfgdrkpGQLSGGQQQRVAIARALAHEPMVV 173
Cdd:TIGR00958 569 gSVRENIAYGLtdtpdeeIMA---AAKAAnahdfiMEFPNGYDTEVGEKG------SQLSGGQKQRIAIARALVRKPRVL 639
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15830546 174 IADEPTGNLDLatgeAILDLLLTINQQTGTTFVISTHSSELKARARRVVEIQDGVL 229
Cdd:TIGR00958 640 ILDEATSALDA----ECEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSV 691
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
30-230 |
3.16e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 78.13 E-value: 3.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 30 LKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAVirGKHLGFIFQffnlMPVLNV 109
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLAL--RQQVATVFQ----DPEQQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 110 F-----DNVYFPLvLNGQFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNLDL 184
Cdd:PRK13638 91 FytdidSDIAFSL-RNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15830546 185 ATGEAILDLLLTINQQtGTTFVISTHSSELkararrVVEIQDGVLI 230
Cdd:PRK13638 170 AGRTQMIAIIRRIVAQ-GNHVIISSHDIDL------IYEISDAVYV 208
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
25-230 |
4.23e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 79.50 E-value: 4.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 25 GKVdALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIdKPTSGTVIFLNKLLNQLPEEQLAvirgKHLGFIFQffN-L 103
Cdd:PRK11174 362 GKT-LAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDPESWR----KHLSWVGQ--NpQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 104 MPVLNVFDNVyfplvlngQFSKKEATERTLHY-LDSVGLSGFGDRKP-----------GQLSGGQQQRVAIARALAHEPM 171
Cdd:PRK11174 434 LPHGTLRDNV--------LLGNPDASDEQLQQaLENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQ 505
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15830546 172 VVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVisTHSSELKARARRVVEIQDGVLI 230
Cdd:PRK11174 506 LLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMV--THQLEDLAQWDQIWVMQDGQIV 562
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
37-230 |
5.76e-17 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 79.54 E-value: 5.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 37 INKGEFLALCGPSGSGKSTLLNILSGIDKPTSGT-VIFLNkllNQLPEEQLAvirgKHLGFIFQFFNLMPVLNVFDNVYF 115
Cdd:PLN03211 91 ASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTgTILAN---NRKPTKQIL----KRTGFVTQDDILYPHLTVRETLVF 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 116 P--LVLNGQFSKKEATERTLHYLDSVGLSGFGDRKPGQ-----LSGGQQQRVAIARALAHEPMVVIADEPTGNLDlATGE 188
Cdd:PLN03211 164 CslLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLD-ATAA 242
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15830546 189 AILDLLLTINQQTGTTFVISTHSSelkarARRVVEIQDGVLI 230
Cdd:PLN03211 243 YRLVLTLGSLAQKGKTIVTSMHQP-----SSRVYQMFDSVLV 279
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
29-194 |
1.26e-16 |
|
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: 75.61 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 29 ALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLaviRgKHLGFIFQffnlMPVLn 108
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDL---R-SRISIIPQ----DPVL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 109 vFD-NVYFPLVLNGQFSKkeatERTLHYLDSVGLSGFGDRKPGQL-----------SGGQQQRVAIARALAHEPMVVIAD 176
Cdd:cd03244 90 -FSgTIRSNLDPFGEYSD----EELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALLRKSKILVLD 164
|
170
....*....|....*...
gi 15830546 177 EPTGNLDLATGEAILDLL 194
Cdd:cd03244 165 EATASVDPETDALIQKTI 182
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
30-210 |
1.35e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 78.22 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 30 LKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEeqlAVIRgKHLGFIFQffnlMPVL-- 107
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSH---SVLR-QGVAMVQQ----DPVVla 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 108 -NVFDNVyfplVLNGQFSKkeatERTLHYLDSVGLSGFGDRKPG-----------QLSGGQQQRVAIARALAHEPMVVIA 175
Cdd:PRK10790 429 dTFLANV----TLGRDISE----EQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALARVLVQTPQILIL 500
|
170 180 190
....*....|....*....|....*....|....*
gi 15830546 176 DEPTGNLDLATGEAILDLLLTINQQtgTTFVISTH 210
Cdd:PRK10790 501 DEATANIDSGTEQAIQQALAAVREH--TTLVVIAH 533
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
24-207 |
1.49e-16 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 78.08 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 24 AGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTV----IFLNKLlnqlpeeQLAVIRgKHLGFIFQ 99
Cdd:PRK13657 345 DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRIlidgTDIRTV-------TRASLR-RNIAVVFQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 100 ---FFNLmpvlNVFDNVyfplvlngQFSKKEATERTLH-YLDSVGLSGFGDRKPG-----------QLSGGQQQRVAIAR 164
Cdd:PRK13657 417 dagLFNR----SIEDNI--------RVGRPDATDEEMRaAAERAQAHDFIERKPDgydtvvgergrQLSGGERQRLAIAR 484
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15830546 165 ALAHEPMVVIADEPTGNLDLATgEAILDLLLTINQQTGTTFVI 207
Cdd:PRK13657 485 ALLKDPPILILDEATSALDVET-EAKVKAALDELMKGRTTFII 526
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
33-210 |
2.90e-16 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 74.50 E-value: 2.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 33 INLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTvIFLNKLLNQLPEeqlaviRGKHLGFIFQFFNLMPVLNVFDN 112
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQ-IQIDGKTATRGD------RSRFMAYLGHLPGLKADLSTLEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 113 VYFPLVLNGQFSKKEATERtlhyLDSVGLSGFGDRKPGQLSGGQQQRVAIARA-LAHEPMVVIaDEPTGNLDLaTGEAIL 191
Cdd:PRK13543 103 LHFLCGLHGRRAKQMPGSA----LAIVGLAGYEDTLVRQLSAGQKKRLALARLwLSPAPLWLL-DEPYANLDL-EGITLV 176
|
170
....*....|....*....
gi 15830546 192 DLLLTINQQTGTTFVISTH 210
Cdd:PRK13543 177 NRMISAHLRGGGAALVTTH 195
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
29-230 |
1.00e-15 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 75.83 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 29 ALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTvIFLNKLlnQLPEEQLAVIRgKHLGFIFQ---FFNLmp 105
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGE-ILLDGH--DLRDYTLASLR-NQVALVSQnvhLFND-- 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 106 vlNVFDNVYFPLvlNGQFSKK--EATERTLHYLDSV-----GLsgfgDRKPGQ----LSGGQQQRVAIARALAHEPMVVI 174
Cdd:PRK11176 432 --TIANNIAYAR--TEQYSREqiEEAARMAYAMDFInkmdnGL----DTVIGEngvlLSGGQRQRIAIARALLRDSPILI 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15830546 175 ADEPTGNLDLATGEAI---LDLLltinQQTGTTFVISTHSSELKaRARRVVEIQDGVLI 230
Cdd:PRK11176 504 LDEATSALDTESERAIqaaLDEL----QKNRTSLVIAHRLSTIE-KADEILVVEDGEIV 557
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-232 |
1.98e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 73.59 E-value: 1.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 9 PAISLSNIYKCYgagAGKVdALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLN--QLPEEQL 86
Cdd:PRK14271 20 PAMAAVNLTLGF---AGKT-VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGgrSIFNYRD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 87 AVIRGKHLGFIFQFFNLMPvLNVFDNVYFPLVLNGQFSKKEATERTLHYLDSVGL-SGFGDR---KPGQLSGGQQQRVAI 162
Cdd:PRK14271 96 VLEFRRRVGMLFQRPNPFP-MSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwDAVKDRlsdSPFRLSGGQQQLLCL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830546 163 ARALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQtgTTFVISTHSSELKAR-ARRVVEIQDGVLIHD 232
Cdd:PRK14271 175 ARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARiSDRAALFFDGRLVEE 243
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
8-210 |
4.59e-15 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 72.91 E-value: 4.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 8 LPAISLSNIYKCYGAGAGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKP----TSGTVIFLN-KLLNQLP 82
Cdd:PRK15093 1 MPLLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDiDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 83 EEQLAVIrGKHLGFIFQffNLMPVLNVFDNVYFPLVLN-------GQFSKKEA--TERTLHYLDSVGLSGFGD---RKPG 150
Cdd:PRK15093 81 RERRKLV-GHNVSMIFQ--EPQSCLDPSERVGRQLMQNipgwtykGRWWQRFGwrKRRAIELLHRVGIKDHKDamrSFPY 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 151 QLSGGQQQRVAIARALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTH 210
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISH 217
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
31-231 |
5.31e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.55 E-value: 5.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 31 KSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQL-PEEQLAvirgkhLGFIF-----QFFNLM 104
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALsTAQRLA------RGLVYlpedrQSSGLY 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 105 PVLNVFDNVYFPLVLNGQFSKKEATERTL--HYLDSVGLSGFGDRKP-GQLSGGQQQRVAIARALAHEPMVVIADEPTGN 181
Cdd:PRK15439 354 LDAPLAWNVCALTHNRRGFWIKPARENAVleRYRRALNIKFNHAEQAaRTLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15830546 182 LDLATGEAILDLLLTINQQTGTTFVISTHSSELKARARRVVEIQDGVLIH 231
Cdd:PRK15439 434 VDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEISG 483
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
11-214 |
1.18e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 70.91 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGAGAgkvdALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLlnqlpeeqlavir 90
Cdd:PRK09544 5 VSLENVSVSFGQRR----VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKL------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 gkHLGFIFQFFNLMPVLnvfdnvyfPLVLNGQFSKKEATERT--LHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAH 168
Cdd:PRK09544 68 --RIGYVPQKLYLDTTL--------PLTVNRFLRLRPGTKKEdiLPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLN 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15830546 169 EPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSEL 214
Cdd:PRK09544 138 RPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHL 183
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
28-231 |
5.39e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 70.51 E-value: 5.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 28 DALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLpeeQLAVIRGKhlgfiFQFFNLMPVL 107
Cdd:PRK10789 329 PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---QLDSWRSR-----LAVVSQTPFL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 108 nvF-DNVYFPLVLNGQFSKKEATER-----TLH---------YLDSVGLSGFgdrkpgQLSGGQQQRVAIARALAHEPMV 172
Cdd:PRK10789 401 --FsDTVANNIALGRPDATQQEIEHvarlaSVHddilrlpqgYDTEVGERGV------MLSGGQKQRISIARALLLNAEI 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15830546 173 VIADEPTGNLDLATGEAILDLLLTINQqtGTTFVISTHSSELKARARRVVEIQDGVLIH 231
Cdd:PRK10789 473 LILDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLSALTEASEILVMQHGHIAQ 529
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
7-195 |
7.02e-14 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 70.27 E-value: 7.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 7 SLPAISLSNiyKCYGAGAGKVdALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIflnkllnQLPEEQL 86
Cdd:PLN03073 505 GPPIISFSD--ASFGYPGGPL-LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF-------RSAKVRM 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 87 AVIRGKHL-GFIFQFFNLMPVLNVFDNVyfplvlngqfskkeATERTLHYLDSVGLSGFGDRKPG-QLSGGQQQRVAIAR 164
Cdd:PLN03073 575 AVFSQHHVdGLDLSSNPLLYMMRCFPGV--------------PEQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAK 640
|
170 180 190
....*....|....*....|....*....|.
gi 15830546 165 ALAHEPMVVIADEPTGNLDLATGEAILDLLL 195
Cdd:PLN03073 641 ITFKKPHILLLDEPSNHLDLDAVEALIQGLV 671
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
30-217 |
7.64e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 68.66 E-value: 7.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 30 LKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAvirgKHLGFIFQFFNLMPVLNV 109
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFA----RKVAYLPQQLPAAEGMTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 110 FDnvyfpLVLNGQFS--------KKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGN 181
Cdd:PRK10575 103 RE-----LVAIGRYPwhgalgrfGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSA 177
|
170 180 190
....*....|....*....|....*....|....*.
gi 15830546 182 LDLATGEAILDLLLTINQQTGTTFVISTHSSELKAR 217
Cdd:PRK10575 178 LDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAAR 213
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
8-229 |
2.46e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 69.00 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 8 LPAISLSNIYKCYGAGAGKvDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIflnkllnqlpeeqla 87
Cdd:PLN03130 612 LPAISIKNGYFSWDSKAER-PTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASV--------------- 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 88 VIRGKhLGFIFQ---FFNLmpvlNVFDNVYFPLVLNGQFSKK----EATERTLHYLDSVGLSGFGDRKPgQLSGGQQQRV 160
Cdd:PLN03130 676 VIRGT-VAYVPQvswIFNA----TVRDNILFGSPFDPERYERaidvTALQHDLDLLPGGDLTEIGERGV-NISGGQKQRV 749
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15830546 161 AIARALAHEPMVVIADEPTGNLDLATGEAILDLLLTiNQQTGTTFVISTHSSELKARARRVVEIQDGVL 229
Cdd:PLN03130 750 SMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIK-DELRGKTRVLVTNQLHFLSQVDRIILVHEGMI 817
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
11-208 |
2.53e-13 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 66.13 E-value: 2.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGAGAGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPT---SGTVIFlnkllNQLPEEQLA 87
Cdd:cd03233 4 LSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHY-----NGIPYKEFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 88 VIRGKHLGFIFQFFNLMPVLNVFDNVYFPLVLNG-QFSKKeatertlhyldsvglsgfgdrkpgqLSGGQQQRVAIARAL 166
Cdd:cd03233 79 EKYPGEIIYVSEEDVHFPTLTVRETLDFALRCKGnEFVRG-------------------------ISGGERKRVSIAEAL 133
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15830546 167 AHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVIS 208
Cdd:cd03233 134 VSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVS 175
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
11-213 |
3.19e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 68.50 E-value: 3.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCY-GAGAGKVDALksiNLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNK-LLNQLPEEQlav 88
Cdd:TIGR01257 1938 LRLNELTKVYsGTSSPAVDRL---CVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKsILTNISDVH--- 2011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 89 irgKHLGFIFQFFNLMPVLNVFDNVYFPLVLNGQFSKKeaTERTLHY-LDSVGLSGFGDRKPGQLSGGQQQRVAIARALA 167
Cdd:TIGR01257 2012 ---QNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEE--IEKVANWsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALI 2086
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15830546 168 HEPMVVIADEPTGNLDLATGEAILDLLLTINQQtGTTFVISTHSSE 213
Cdd:TIGR01257 2087 GCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSME 2131
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
27-182 |
4.16e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.83 E-value: 4.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 27 VDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNqLPEEQLAVIRGkhLGFIFQFFNLMPV 106
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEID-FKSSKEALENG--ISMVHQELNLVLQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 107 LNVFDNVY---FPlvLNGQF-SKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNL 182
Cdd:PRK10982 88 RSVMDNMWlgrYP--TKGMFvDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
11-230 |
6.16e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 67.28 E-value: 6.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGagagkvDA--LKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKL----LNQLP-- 82
Cdd:PRK11147 4 ISIHGAWLSFS------DAplLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLivarLQQDPpr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 83 --------------EEQLAVIRGKHlgfifQFFNLM------PVLNVFDNVYFPL-VLNG-QFSKkeateRTLHYLDSVG 140
Cdd:PRK11147 78 nvegtvydfvaegiEEQAEYLKRYH-----DISHLVetdpseKNLNELAKLQEQLdHHNLwQLEN-----RINEVLAQLG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 141 LSGfgDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNLDLATGEAILDLLLTINqqtGTTFVISTHSSELKARARR 220
Cdd:PRK11147 148 LDP--DAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQ---GSIIFISHDRSFIRNMATR 222
|
250
....*....|
gi 15830546 221 VVEIQDGVLI 230
Cdd:PRK11147 223 IVDLDRGKLV 232
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
30-209 |
6.82e-13 |
|
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: 67.15 E-value: 6.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 30 LKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLaviRgKHLGFIFQ---FFNlmpv 106
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASL---R-AAIGIVPQdtvLFN---- 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 107 lnvfDNVYFplvlNGQFSKKEATE-------RTLHyldsvgLSGF------------GDR--KpgqLSGGQQQRVAIARA 165
Cdd:COG5265 446 ----DTIAY----NIAYGRPDASEeeveaaaRAAQ------IHDFieslpdgydtrvGERglK---LSGGEKQRVAIART 508
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15830546 166 LAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTgTTFVI----ST 209
Cdd:COG5265 509 LLKNPPILIFDEATSALDSRTERAIQAALREVARGR-TTLVIahrlST 555
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
31-229 |
8.18e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.12 E-value: 8.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 31 KSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNqlPEEQLAVIRgKHLGFIFQffnlmpvlNVF 110
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS--PRSPLDAVK-KGMAYITE--------SRR 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 111 DNVYFPlvlngQFSKKE--ATERTLH---YLDSVGLsgFGDRKP----------------------GQLSGGQQQRVAIA 163
Cdd:PRK09700 349 DNGFFP-----NFSIAQnmAISRSLKdggYKGAMGL--FHEVDEqrtaenqrellalkchsvnqniTELSGGNQQKVLIS 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15830546 164 RALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSELKARARRVVEIQDGVL 229
Cdd:PRK09700 422 KWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
29-229 |
1.02e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 66.92 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 29 ALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNqlpEEQLAVIRgKHLGFIFQFFNLmpvln 108
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT---AEQPEDYR-KLFSAVFTDFHL----- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 109 vFDNVYFPlvlNGQFSKKEATERTLHYL---DSVGLSGFGDRKPgQLSGGQQQRVAIARALAHEPMVVIADEPTGNLDLA 185
Cdd:PRK10522 409 -FDQLLGP---EGKPANPALVEKWLERLkmaHKLELEDGRISNL-KLSKGQKKRLALLLALAEERDILLLDEWAADQDPH 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15830546 186 TGEAILDLLLTINQQTGTTFVISTHSSELKARARRVVEIQDGVL 229
Cdd:PRK10522 484 FRREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQL 527
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
11-227 |
1.20e-12 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 64.66 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGAGagkVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAVIR 90
Cdd:cd03290 1 VQVTNGYFSWGSG---LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 GKHLGFIFQFFNLMPVlNVFDNVYFPLVLNGQFSKKEATERTLHylDSVGLSGFGDR-----KPGQLSGGQQQRVAIARA 165
Cdd:cd03290 78 RYSVAYAAQKPWLLNA-TVEENITFGSPFNKQRYKAVTDACSLQ--PDIDLLPFGDQteigeRGINLSGGQRQRICVARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830546 166 LAHEPMVVIADEPTGNLDLATG-----EAILDLLltinQQTGTTFVISTHSSELKARARRVVEIQDG 227
Cdd:cd03290 155 LYQNTNIVFLDDPFSALDIHLSdhlmqEGILKFL----QDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
36-183 |
1.21e-12 |
|
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: 65.12 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 36 DINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEqlavIRGKHLGFIFQFfnLMPVLNVFdnvyf 115
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQY----IKADYEGTVRDL--LSSITKDF----- 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15830546 116 plvLNGQFSKKEAtertlhyLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNLD 183
Cdd:cd03237 90 ---YTHPYFKTEI-------AKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
40-184 |
2.02e-12 |
|
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: 64.70 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 40 GEFLALCGPSGSGKSTLLNILSGIDKPTSG---------TVI--F----LNKLLNQLPEEQLAVIRGKhlgfifQFFNLM 104
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGkfddppdwdEILdeFrgseLQNYFTKLLEGDVKVIVKP------QYVDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 105 PvlNVFDNVYFPLVlngqfSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNLDL 184
Cdd:cd03236 100 P--KAVKGKVGELL-----KKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
33-210 |
2.21e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 65.92 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 33 INLDINKGE---FLalcGPSGSGKSTLLNILSGIDKPTSGTViflnKLLNQLPEEQLAVIRgKHLGFIFQFFNLMPVLNV 109
Cdd:NF033858 285 VSFRIRRGEifgFL---GSNGCGKSTTMKMLTGLLPASEGEA----WLFGQPVDAGDIATR-RRVGYMSQAFSLYGELTV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 110 FDNvyfpLVLNGQ-F--SKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNLDLAT 186
Cdd:NF033858 357 RQN----LELHARlFhlPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVA 432
|
170 180
....*....|....*....|....
gi 15830546 187 GEAILDLLLTINQQTGTTFVISTH 210
Cdd:NF033858 433 RDMFWRLLIELSREDGVTIFISTH 456
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
11-208 |
2.23e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 65.73 E-value: 2.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGagaGKVdALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFlnkllnqlpeeqlavir 90
Cdd:TIGR03719 323 IEAENLTKAFG---DKL-LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI----------------- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 GK--HLGFIFQFF-NLMPVLNVFDNVYfplvlNG----QFSKKEATERTlhYLDSVGLSGfGD--RKPGQLSGGQQQRVA 161
Cdd:TIGR03719 382 GEtvKLAYVDQSRdALDPNKTVWEEIS-----GGldiiKLGKREIPSRA--YVGRFNFKG-SDqqKKVGQLSGGERNRVH 453
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15830546 162 IARALAHEPMVVIADEPTGNLDLATGEAILDLLLTInqqTGTTFVIS 208
Cdd:TIGR03719 454 LAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNF---AGCAVVIS 497
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
29-211 |
4.38e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 62.97 E-value: 4.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 29 ALKSINLDINKGEFLALC------------GPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAVIrGKHLGF 96
Cdd:PRK13541 3 SLHQLQFNIEQKNLFDLSitflpsaityikGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYI-GHNLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 97 IFQffnlmpvLNVFDNVYFplvLNGQFSKKEATERTLHYLDsvgLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIAD 176
Cdd:PRK13541 82 KLE-------MTVFENLKF---WSEIYNSAETLYAAIHYFK---LHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLD 148
|
170 180 190
....*....|....*....|....*....|....*
gi 15830546 177 EPTGNLDlATGEAILDLLLTINQQTGTTFVISTHS 211
Cdd:PRK13541 149 EVETNLS-KENRDLLNNLIVMKANSGGIVLLSSHL 182
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
30-232 |
5.05e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 63.69 E-value: 5.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 30 LKSINLDINKGEFLALCGPSGSGKSTLLNILSGiDKPTS---------GTVIFLNKLLNQLPEEQLAVIRGkhlgfifqf 100
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG-DLTGGgaprgarvtGDVTLNGEPLAAIDAPRLARLRA--------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 101 fnlmpVLNVFDNVYFP-----LVLNGQFSKKEATERTLHY--------LDSVGLSGFGDRKPGQLSGGQQQRVAIARALA 167
Cdd:PRK13547 87 -----VLPQAAQPAFAfsareIVLLGRYPHARRAGALTHRdgeiawqaLALAGATALVGRDVTTLSGGELARVQFARVLA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15830546 168 H---------EPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSELKAR-ARRVVEIQDGVLIHD 232
Cdd:PRK13547 162 QlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARhADRIAMLADGAIVAH 236
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
37-190 |
1.13e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 63.67 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 37 INKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTViflnkllnqLPEEQLAV----IRGKHLGFIFQFfnLMPVLNVFDN 112
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV---------DPELKISYkpqyIKPDYDGTVEDL--LRSITDDLGS 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 113 VYFplvlNGQFSKKEATERTLhyldsvglsgfgDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNLD----LATGE 188
Cdd:PRK13409 431 SYY----KSEIIKPLQLERLL------------DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrLAVAK 494
|
..
gi 15830546 189 AI 190
Cdd:PRK13409 495 AI 496
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
12-229 |
1.32e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.39 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 12 SLSNIY----KCYGAGAGKVDALKS------INLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNqL 81
Cdd:PRK11288 241 EIGDIYgyrpRPLGEVRLRLDGLKGpglrepISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID-I 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 82 PEEQLAVIRG--------KHLGFIfqffnlmPVLNVFDNV---------YFPLVLNGqfsKKEAtERTLHYLDSVGLSGF 144
Cdd:PRK11288 320 RSPRDAIRAGimlcpedrKAEGII-------PVHSVADNInisarrhhlRAGCLINN---RWEA-ENADRFIRSLNIKTP 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 145 GDRKP-GQLSGGQQQRVAIARALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSELKARARRVVE 223
Cdd:PRK11288 389 SREQLiMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVV 468
|
....*.
gi 15830546 224 IQDGVL 229
Cdd:PRK11288 469 MREGRI 474
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
30-227 |
1.44e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 63.64 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 30 LKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTViFLNKLLNQLPEEQL---AVIRGKHLgfifqFFNLMPV 106
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-WAERSIAYVPQQAWimnATVRGNIL-----FFDEEDA 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 107 LNVFDNVyfplvlngQFSKKEATERTLhyldSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNLDLAT 186
Cdd:PTZ00243 750 ARLADAV--------RVSQLEADLAQL----GGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHV 817
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15830546 187 GEAIL-DLLLtiNQQTGTTFVISTHSSELKARARRVVEIQDG 227
Cdd:PTZ00243 818 GERVVeECFL--GALAGKTRVLATHQVHVVPRADYVVALGDG 857
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
30-227 |
1.93e-11 |
|
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: 62.18 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 30 LKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTViflnkllnqlpeeqlavirgKHLG---FIFQFFNLMPV 106
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI--------------------KHSGrisFSSQFSWIMPG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 107 lNVFDNVYFPLVLNgQFSKKEATERTLHYLDsvgLSGFGDRKPG-------QLSGGQQQRVAIARALAHEPMVVIADEPT 179
Cdd:cd03291 113 -TIKENIIFGVSYD-EYRYKSVVKACQLEED---ITKFPEKDNTvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPF 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15830546 180 GNLDLATGEAILDLLLTINQQTGTTFVISTHSSELKaRARRVVEIQDG 227
Cdd:cd03291 188 GYLDVFTEKEIFESCVCKLMANKTRILVTSKMEHLK-KADKILILHEG 234
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
39-183 |
3.25e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.52 E-value: 3.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 39 KGEFLALCGPSGSGKSTLLNILSGIDKPTsgtvifLNKLLNQL-PEEQLAVIRGKHLGfifqffnlmpvlNVFDNVY--- 114
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPN------LGDYEEEPsWDEVLKRFRGTELQ------------NYFKKLYnge 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 115 ------------FPLVLNGQFSK--KEATER--TLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEP 178
Cdd:PRK13409 160 ikvvhkpqyvdlIPKVFKGKVREllKKVDERgkLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
....*
gi 15830546 179 TGNLD 183
Cdd:PRK13409 240 TSYLD 244
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
30-228 |
3.46e-11 |
|
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: 62.62 E-value: 3.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 30 LKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTViflnkllnqlpeeqlavirgKHLG---FIFQFFNLMPV 106
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI--------------------KHSGrisFSPQTSWIMPG 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 107 lNVFDNVYFPL---------VLNG--------QFSKKEATertlhYLDSVGLSgfgdrkpgqLSGGQQQRVAIARALAHE 169
Cdd:TIGR01271 502 -TIKDNIIFGLsydeyrytsVIKAcqleediaLFPEKDKT-----VLGEGGIT---------LSGGQRARISLARAVYKD 566
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15830546 170 PMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSELKaRARRVVEIQDGV 228
Cdd:TIGR01271 567 ADLYLLDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLK-KADKILLLHEGV 624
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
39-193 |
4.46e-11 |
|
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: 62.11 E-value: 4.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 39 KGEFLALCGPSGSGKSTLLNILSGIDKPTSGtvIFLNKllnqlP--EEQLAVIRGKHLGFIFQffnlmpvlNVFDN---- 112
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLG--DYDEE-----PswDEVLKRFRGTELQDYFK--------KLANGeikv 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 113 ------VYF-PLVLNGQFSK--KEATER--TLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGN 181
Cdd:COG1245 163 ahkpqyVDLiPKVFKGTVREllEKVDERgkLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSY 242
|
170
....*....|....*.
gi 15830546 182 LD----LATGEAILDL 193
Cdd:COG1245 243 LDiyqrLNVARLIREL 258
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
30-199 |
5.58e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.56 E-value: 5.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 30 LKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNK-LLNQLPEEQLAviRG--------KHLGFIFQf 100
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHeVVTRSPQDGLA--NGivyisedrKRDGLVLG- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 101 fnlmpvLNVFDNVyfPLVLNGQFSK-----KEATERTLhYLDSVGLsgFGDRKP------GQLSGGQQQRVAIARALAHE 169
Cdd:PRK10762 345 ------MSVKENM--SLTALRYFSRaggslKHADEQQA-VSDFIRL--FNIKTPsmeqaiGLLSGGNQQKVAIARGLMTR 413
|
170 180 190
....*....|....*....|....*....|
gi 15830546 170 PMVVIADEPTGNLDLATGEAILDLlltINQ 199
Cdd:PRK10762 414 PKVLILDEPTRGVDVGAKKEIYQL---INQ 440
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
39-227 |
1.57e-10 |
|
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: 57.77 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 39 KGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNkllnqlpeeqlavirgkhlgfifqffnlmpvlnvfdnvyfplv 118
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYID------------------------------------------- 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 119 lngqfskkeaTERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNLDLATGEAILDL----- 193
Cdd:smart00382 38 ----------GEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrl 107
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15830546 194 LLTINQQTGTTFVISTH------SSELKARARRVVEIQDG 227
Cdd:smart00382 108 LLLLKSEKNLTVILTTNdekdlgPALLRRRFDRRIVLLLI 147
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
22-184 |
1.82e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 59.27 E-value: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 22 AGAGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGID--KPTSGTVIFLNKLLNQLPEEQLAvirgkHLGFIFQ 99
Cdd:CHL00131 15 ASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEERA-----HLGIFLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 100 FFNLMPVLNVFDNVYFPLVLNG--QFSKKEATERTLHY------LDSVGLS-GFGDRKPGQ-LSGGQQQRVAIARALAHE 169
Cdd:CHL00131 90 FQYPIEIPGVSNADFLRLAYNSkrKFQGLPELDPLEFLeiinekLKLVGMDpSFLSRNVNEgFSGGEKKRNEILQMALLD 169
|
170
....*....|....*
gi 15830546 170 PMVVIADEPTGNLDL 184
Cdd:CHL00131 170 SELAILDETDSGLDI 184
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
30-183 |
3.15e-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: 59.56 E-value: 3.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 30 LKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSG--------TVIFL--------NKLLNQLPEEQLAVIRGkh 93
Cdd:TIGR03719 21 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGearpqpgiKVGYLpqepqldpTKTVRENVEEGVAEIKD-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 94 lgfifqffnlmpVLNVFDNVYFPLVLNGQFSKKEATERT----------LHYLDS---VGLSGF----GDRKPGQLSGGQ 156
Cdd:TIGR03719 99 ------------ALDRFNEISAKYAEPDADFDKLAAEQAelqeiidaadAWDLDSqleIAMDALrcppWDADVTKLSGGE 166
|
170 180
....*....|....*....|....*..
gi 15830546 157 QQRVAIARALAHEPMVVIADEPTGNLD 183
Cdd:TIGR03719 167 RRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
9-229 |
3.53e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.60 E-value: 3.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 9 PAISLSNIYKCYGAGAGKvDALKSINLDINKGEFLALCGPSGSGKSTLLNilsgidkptsgtviflnKLLNQLP--EEQL 86
Cdd:PLN03232 613 PAISIKNGYFSWDSKTSK-PTLSDINLEIPVGSLVAIVGGTGEGKTSLIS-----------------AMLGELShaETSS 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 87 AVIRGKhLGFIFQ---FFNLmpvlNVFDNVYFplvlngqfSKKEATERTLHYLDSVGLSGFGDRKPGQ-----------L 152
Cdd:PLN03232 675 VVIRGS-VAYVPQvswIFNA----TVRENILF--------GSDFESERYWRAIDVTALQHDLDLLPGRdlteigergvnI 741
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830546 153 SGGQQQRVAIARALAHEPMVVIADEPTGNLDLATGEAILDLLLTiNQQTGTTFVISTHSSELKARARRVVEIQDGVL 229
Cdd:PLN03232 742 SGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMK-DELKGKTRVLVTNQLHFLPLMDRIILVSEGMI 817
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
30-231 |
5.51e-10 |
|
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: 57.27 E-value: 5.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 30 LKSINLDINKGEFLALCGPSGSGKSTLL---------------------NILSGIDKPT-------SGTVIFLNKLLNQL 81
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKPDvdsieglSPAIAIDQKTTSRN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 82 PEEQLAVIRGkhlgfIFQFFNLMpvlnvfdnvyfplvlngqFSKKEATERtLHYLDSVGLSGFG-DRKPGQLSGGQQQRV 160
Cdd:cd03270 91 PRSTVGTVTE-----IYDYLRLL------------------FARVGIRER-LGFLVDVGLGYLTlSRSAPTLSGGEAQRI 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15830546 161 AIARALAHEPMVV--IADEPTGNLDLATGEAILDLLLTInQQTGTTFVISTHSSELKARARRVVEIQDGVLIH 231
Cdd:cd03270 147 RLATQIGSGLTGVlyVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDTIRAADHVIDIGPGAGVH 218
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
3-183 |
9.88e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 57.87 E-value: 9.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 3 STIKSLPAISLSNIYKCYGAGAGKVDALKsinldINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTViflnkllnqlp 82
Cdd:COG1245 334 REKEEETLVEYPDLTKSYGGFSLEVEGGE-----IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV----------- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 83 EEQLAV------IRGKHLGFIFQFfnLMPVLNV-FDNVYFplvlNGQFSKKEATERTLhyldsvglsgfgDRKPGQLSGG 155
Cdd:COG1245 398 DEDLKIsykpqyISPDYDGTVEEF--LRSANTDdFGSSYY----KTEIIKPLGLEKLL------------DKNVKDLSGG 459
|
170 180
....*....|....*....|....*...
gi 15830546 156 QQQRVAIARALAHEPMVVIADEPTGNLD 183
Cdd:COG1245 460 ELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
30-210 |
2.38e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 55.95 E-value: 2.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 30 LKSINLDINKGEFLALCGPSGSGKSTLLNILSGID--KPTSGTVIFLNKLLNQLPEEQLAvirGKHLGFIFQFfnlmpvl 107
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRA---GEGIFMAFQY------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 108 nvfdNVYFPLVLNgQFSKKEATERTLHY-----LDSVGLSGFGDRKPGQL---------------SGGQQQRVAIARALA 167
Cdd:PRK09580 87 ----PVEIPGVSN-QFFLQTALNAVRSYrgqepLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGEKKRNDILQMAV 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15830546 168 HEPMVVIADEPTGNLDLATGEAILDLLLTInQQTGTTFVISTH 210
Cdd:PRK09580 162 LEPELCILDESDSGLDIDALKIVADGVNSL-RDGKRSFIIVTH 203
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
26-208 |
2.80e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 56.66 E-value: 2.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 26 KVDALKSINLDINKGEFLALCGPSGSGKSTLLNILS----GIDKPTSGTV----IFLNKLLNQLPEEQLavirgkhlgFI 97
Cdd:TIGR00956 73 TFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVItydgITPEEIKKHYRGDVV---------YN 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 98 FQFFNLMPVLNVFDNVYFPLVLNG------QFSKKE-ATERTLHYLDSVGLSGFGDRKPGQ-----LSGGQQQRVAIARA 165
Cdd:TIGR00956 144 AETDVHFPHLTVGETLDFAARCKTpqnrpdGVSREEyAKHIADVYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEA 223
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15830546 166 LAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVIS 208
Cdd:TIGR00956 224 SLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVA 266
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
44-222 |
5.02e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 56.19 E-value: 5.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 44 ALCGPSGSGKSTLLNILSGI-DKPTSGTVIFLNKLLNQLPEEQL-----------------------------AVIR--G 91
Cdd:PTZ00265 1198 AIVGETGSGKSTVMSLLMRFyDLKNDHHIVFKNEHTNDMTNEQDyqgdeeqnvgmknvnefsltkeggsgedsTVFKnsG 1277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 92 KHL--GFIFQFFNLMPVLNVFDNV-YFPLVLNG------QFSKKEAT-ERTLHYLDSVGLSGFGDRKPGQ---------- 151
Cdd:PTZ00265 1278 KILldGVDICDYNLKDLRNLFSIVsQEPMLFNMsiyeniKFGKEDATrEDVKRACKFAAIDEFIESLPNKydtnvgpygk 1357
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830546 152 -LSGGQQQRVAIARALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSELKARARRVV 222
Cdd:PTZ00265 1358 sLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIV 1429
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
30-208 |
5.05e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.19 E-value: 5.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 30 LKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFlnklLNQLPEEQLAVIRgKHLGFIFQFFNLMPVLNV 109
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILF----ERQSIKKDLCTYQ-KQLCFVGHRSGINPYLTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 110 FDNVYFPLvlngQFSKKEATERTLHYLDSVGlsGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNLDLATGEA 189
Cdd:PRK13540 92 RENCLYDI----HFSPGAVGITELCRLFSLE--HLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLT 165
|
170
....*....|....*....
gi 15830546 190 ILDLLLTINQQTGTTFVIS 208
Cdd:PRK13540 166 IITKIQEHRAKGGAVLLTS 184
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
10-231 |
7.99e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 55.28 E-value: 7.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 10 AISLSNIYKCYGAGagkvDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKllnqlpeeqlavi 89
Cdd:PRK15064 319 ALEVENLTKGFDNG----PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSEN------------- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 90 rgKHLGFIFQ-----FFNLMpvlNVFDNVyfplvlnGQFSKKEATE--------RTLHYLDSVGlsgfgdRKPGQLSGGQ 156
Cdd:PRK15064 382 --ANIGYYAQdhaydFENDL---TLFDWM-------SQWRQEGDDEqavrgtlgRLLFSQDDIK------KSVKVLSGGE 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15830546 157 QQRVAIARALAHEPMVVIADEPTGNLDLatgEAILDLLLTINQQTGTTFVIStHSSEL-KARARRVVEIQDGVLIH 231
Cdd:PRK15064 444 KGRMLFGKLMMQKPNVLVMDEPTNHMDM---ESIESLNMALEKYEGTLIFVS-HDREFvSSLATRIIEITPDGVVD 515
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
22-192 |
8.35e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.18 E-value: 8.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 22 AGAGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTViflnkllnqlpeeqlAVIRGKHLGFIFQff 101
Cdd:PRK10636 320 AGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI---------------GLAKGIKLGYFAQ-- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 102 NLMPVLNVFDNvyfPLVLNGQFSKKEATERTLHYLDSVGLSGFGDRKP-GQLSGGQQQRVAIARALAHEPMVVIADEPTG 180
Cdd:PRK10636 383 HQLEFLRADES---PLQHLARLAPQELEQKLRDYLGGFGFQGDKVTEEtRRFSGGEKARLVLALIVWQRPNLLLLDEPTN 459
|
170
....*....|....*.
gi 15830546 181 NLDL----ATGEAILD 192
Cdd:PRK10636 460 HLDLdmrqALTEALID 475
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
30-205 |
1.23e-08 |
|
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: 53.02 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 30 LKSINLDINKGEFLALCGPSGSGKSTLLNILSGidKPTSGTV---IFLNKLlnQLPEEQLAVIrgkhlGFIFQFFNLMPV 106
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVItgeILINGR--PLDKNFQRST-----GYVEQQDVHSPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 107 LNVFDNVYFPLVLNGqfskkeatertlhyldsvglsgfgdrkpgqLSGGQQQRVAIARALAHEPMVVIADEPTGNLD--- 183
Cdd:cd03232 94 LTVREALRFSALLRG------------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDsqa 143
|
170 180 190
....*....|....*....|....*....|...
gi 15830546 184 ----------LA-TGEAIldlLLTINQQTGTTF 205
Cdd:cd03232 144 aynivrflkkLAdSGQAI---LCTIHQPSASIF 173
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
32-179 |
1.44e-08 |
|
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: 54.37 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 32 SINLDINKGEFLALCGPSGSGKSTLLNILSGI--------DKPTSGTVIFLNkllnQLPEEQLAVIRgkhlgfifqffnl 103
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFRILGELwpvyggrlTKPAKGKLFYVP----QRPYMTLGTLR------------- 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 104 mpvlnvfDNVYFPLVLNgQFSKKEATERTL-HYLDSVGLSGFGDRKPG---------QLSGGQQQRVAIARALAHEPMVV 173
Cdd:TIGR00954 533 -------DQIIYPDSSE-DMKRRGLSDKDLeQILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFA 604
|
....*.
gi 15830546 174 IADEPT 179
Cdd:TIGR00954 605 ILDECT 610
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
47-208 |
2.05e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.97 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 47 GPSGSGKSTLLNILSGIDKPTSGTVIFlnkllnqlpeeqlavirGK--HLGFIFQFF-NLMPVLNVFDNVYfplvlNGQ- 122
Cdd:PRK11819 357 GPNGAGKSTLFKMITGQEQPDSGTIKI-----------------GEtvKLAYVDQSRdALDPNKTVWEEIS-----GGLd 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 123 ---FSKKEATERTlhYLDSVGLSGfGD--RKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNLDLATGEAILDLLLTI 197
Cdd:PRK11819 415 iikVGNREIPSRA--YVGRFNFKG-GDqqKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEF 491
|
170
....*....|.
gi 15830546 198 nqqTGTTFVIS 208
Cdd:PRK11819 492 ---PGCAVVIS 499
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
30-183 |
4.14e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.09 E-value: 4.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 30 LKSINLDINKGEFLALCGPSGSGKSTLLNILSGiDKPTSgtviFLNKLLnqLPEEQlaviRG---------KHLGFIFQF 100
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQG----YSNDLT--LFGRR----RGsgetiwdikKHIGYVSSS 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 101 FNL-----MPVLNVFDNVYFPLVlnGQFSKKEATERTL--HYLDSVGLSGFGDRKPGQ-LSGGQQQRVAIARALAHEPMV 172
Cdd:PRK10938 345 LHLdyrvsTSVRNVILSGFFDSI--GIYQAVSDRQQKLaqQWLDILGIDKRTADAPFHsLSWGQQRLALIVRALVKHPTL 422
|
170
....*....|.
gi 15830546 173 VIADEPTGNLD 183
Cdd:PRK10938 423 LILDEPLQGLD 433
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
151-224 |
4.83e-08 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 50.82 E-value: 4.83e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15830546 151 QLSGGQQQRVAIARALAHE-----PMVVIaDEPTGNLDLATGEAILDLLLTINQQTGTTFVIsTHSSELKARARRVVEI 224
Cdd:cd03227 77 QLSGGEKELSALALILALAslkprPLYIL-DEIDRGLDPRDGQALAEAILEHLVKGAQVIVI-THLPELAELADKLIHI 153
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
30-208 |
5.18e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 52.65 E-value: 5.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 30 LKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKL----LNQLPEEqlavirgkhlgfifqffnLMP 105
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLevayFDQHRAE------------------LDP 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 106 VLNVFDNvyfplVLNGqfsKKEAT----ER-TLHYLDSVGLSGFGDRKPGQ-LSGGQQQRVAIARALAHEPMVVIADEPT 179
Cdd:PRK11147 397 EKTVMDN-----LAEG---KQEVMvngrPRhVLGYLQDFLFHPKRAMTPVKaLSGGERNRLLLARLFLKPSNLLILDEPT 468
|
170 180
....*....|....*....|....*....
gi 15830546 180 GNLDLATGEaILDLLLTINQqtGTTFVIS 208
Cdd:PRK11147 469 NDLDVETLE-LLEELLDSYQ--GTVLLVS 494
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
30-183 |
1.06e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 51.66 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 30 LKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKL----LNQLP------------EEQLAVIRGKh 93
Cdd:PRK11819 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIkvgyLPQEPqldpektvrenvEEGVAEVKAA- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 94 lgfifqffnlmpvLNVFDNVYFPLVLNGQFSKKEATERT----------LHYLDS---VGLSGF----GDRKPGQLSGGQ 156
Cdd:PRK11819 102 -------------LDRFNEIYAAYAEPDADFDALAAEQGelqeiidaadAWDLDSqleIAMDALrcppWDAKVTKLSGGE 168
|
170 180
....*....|....*....|....*..
gi 15830546 157 QQRVAIARALAHEPMVVIADEPTGNLD 183
Cdd:PRK11819 169 RRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
25-232 |
1.28e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 51.27 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 25 GKVDALKSINLDINKGEFLALCGPSGSG--KSTLLNILSGID---KPTSGTVIFLNK-LLNQLPEEQLAVIRGKHLGFIF 98
Cdd:NF000106 24 GEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDagrRPWRF*TWCANRrALRRTIG*HRPVR*GRRESFSG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 99 QFfNLMPVLNVFDnvyfplvlngqFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEP 178
Cdd:NF000106 104 RE-NLYMIGR*LD-----------LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15830546 179 TGNLDLATGEAILDLLLTINQQTGTTFVISTHSSELKARARRVVEIQDGVLIHD 232
Cdd:NF000106 172 TTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIAD 225
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
150-229 |
1.58e-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: 51.36 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 150 GQLSGGQQQRVAIARALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSELKARARRVVEIQDGVL 229
Cdd:TIGR02633 402 GRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
34-231 |
1.82e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.17 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 34 NLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLAvirgKHLGFIFQFFN---LMPVLNVF 110
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQ----KLVSDEWQRNNtdmLSPGEDDT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 111 DNVYFPLVLNGqfSKKEAteRTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNLDLATGEAI 190
Cdd:PRK10938 99 GRTTAEIIQDE--VKDPA--RCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15830546 191 LDLLLTINQQTGTTFVISTHSSELKARARRVVEIQDGVLIH 231
Cdd:PRK10938 175 AELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAE 215
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
29-227 |
2.14e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.88 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 29 ALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLL-NQLPEEQLA-----VIRGKHLGFIFQF-- 100
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKInNHNANEAINhgfalVTEERRSTGIYAYld 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 101 --FN-LMPVLNVFDNVYfplvlnGQFSKKEATERTLHYLDSVGLSGFGDRKP-GQLSGGQQQRVAIARALAHEPMVVIAD 176
Cdd:PRK10982 343 igFNsLISNIRNYKNKV------GLLDNSRMKSDTQWVIDSMRVKTPGHRTQiGSLSGGNQQKVIIGRWLLTQPEILMLD 416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15830546 177 EPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSELKARARRVVEIQDG 227
Cdd:PRK10982 417 EPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG 467
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
30-211 |
3.85e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 50.33 E-value: 3.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 30 LKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIfLNKLLNQLPeeQLAVIRGKHLGfifqffnlmpvlnv 109
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVH-MKGSVAYVP--QQAWIQNDSLR-------------- 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 110 fDNVYFPLVLNGQFSKkeATERTLHYLDSVGLSGFGDR-----KPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNLDL 184
Cdd:TIGR00957 717 -ENILFGKALNEKYYQ--QVLEACALLPDLEILPSGDRteigeKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDA 793
|
170 180
....*....|....*....|....*...
gi 15830546 185 ATGEAILDLLL-TINQQTGTTFVISTHS 211
Cdd:TIGR00957 794 HVGKHIFEHVIgPEGVLKNKTRILVTHG 821
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-183 |
3.90e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.41 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 4 TIKSLPAISLSNIYKCYGAgAGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIfLNKLLNqLPE 83
Cdd:PTZ00265 376 KLKDIKKIQFKNVRFHYDT-RKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDII-INDSHN-LKD 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 84 EQLAVIRGKhLGFIFQffnlMPVL---NVFDNVYFPLVL-------------NGQFSKKEATERT-------------LH 134
Cdd:PTZ00265 453 INLKWWRSK-IGVVSQ----DPLLfsnSIKNNIKYSLYSlkdlealsnyyneDGNDSQENKNKRNscrakcagdlndmSN 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 135 YLDSVGL----------------------------SGFGDR-------KPGQLSGGQQQRVAIARALAHEPMVVIADEPT 179
Cdd:PTZ00265 528 TTDSNELiemrknyqtikdsevvdvskkvlihdfvSALPDKyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEAT 607
|
....
gi 15830546 180 GNLD 183
Cdd:PTZ00265 608 SSLD 611
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
11-227 |
6.77e-07 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 48.18 E-value: 6.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNIYKCYGAGAGKVdaLKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTVIFLNKLLNQLPEEQLaviR 90
Cdd:cd03369 7 IEVENLSVRYAPDLPPV--LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL---R 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 91 GKhLGFIFQffnlMPVLnvFD-NVYFPLVLNGQFSKKEATErtlhyldSVGLSGFGDrkpgQLSGGQQQRVAIARALAHE 169
Cdd:cd03369 82 SS-LTIIPQ----DPTL--FSgTIRSNLDPFDEYSDEEIYG-------ALRVSEGGL----NLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15830546 170 PMVVIADEPTGNLDLATGEAILDlllTINQQ-TGTTFVISTHSSELKARARRVVEIQDG 227
Cdd:cd03369 144 PRVLVLDEATASIDYATDALIQK---TIREEfTNSTILTIAHRLRTIIDYDKILVMDAG 199
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
29-229 |
1.29e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 47.89 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 29 ALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSG--------TVIFLNKLLNQlpeeQLAVIrgkhlgfifqf 100
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGkvdrngevSVIAISAGLSG----QLTGI----------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 101 fnlmpvlnvfDNVYFPLVLNGqFSKKEATERTLHYLDSVGLSGFGDRKPGQLSGGQQQRVAIARALAHEPMVVIADEPTG 180
Cdd:PRK13546 104 ----------ENIEFKMLCMG-FKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALS 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15830546 181 NLDLATGEAILDLLLTINQQTGTTFVISTHSSELKARARRVVEIQDGVL 229
Cdd:PRK13546 173 VGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
11-177 |
1.30e-06 |
|
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: 48.64 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 11 ISLSNI-YKCYGAGAGKVDALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTViflnkLLN--QLPEEQLA 87
Cdd:COG4615 328 LELRGVtYRYPGEDGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEI-----LLDgqPVTADNRE 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 88 VIRgKHLGFIFQFFNLmpvlnvFDNVYfplvlngQFSKKEATERTLHYLDSVGLSG--------FGDRKpgqLSGGQQQR 159
Cdd:COG4615 403 AYR-QLFSAVFSDFHL------FDRLL-------GLDGEADPARARELLERLELDHkvsvedgrFSTTD---LSQGQRKR 465
|
170
....*....|....*...
gi 15830546 160 VAIARALAHEPMVVIADE 177
Cdd:COG4615 466 LALLVALLEDRPILVFDE 483
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
30-227 |
1.43e-06 |
|
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: 47.93 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 30 LKSINLDINKGEFLALCGPSGSGKSTLLNI---LSGIDKPTSGTVIFLNKLLNQLPEEQLAVIRGKHLGFIFQF-FNLMP 105
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAflrLLNTEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFrKNLDP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 106 vlnvfdnvyfplvlNGQFSKKEaterTLHYLDSVGLSGFGDRKPGQL-----------SGGQQQRVAIARALAHEPMVVI 174
Cdd:cd03289 100 --------------YGKWSDEE----IWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15830546 175 ADEPTGNLDLATGEAILDlllTINQQ-TGTTFVISTHSSELKARARRVVEIQDG 227
Cdd:cd03289 162 LDEPSAHLDPITYQVIRK---TLKQAfADCTVILSEHRIEAMLECQRFLVIEEN 212
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
26-224 |
1.75e-06 |
|
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: 46.55 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 26 KVDALKSINLDINKGEFLALCGPSGSGKSTLLNilSGIDKPTSGTvifLNKLLnQLPEEQLAVirgkhlgFIFQFFNLMP 105
Cdd:cd03238 7 NVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLYASGKAR---LISFL-PKFSRNKLI-------FIDQLQFLID 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 106 V-LNvfdnvYFPLvlngqfskkeatertlhyldsvglsgfgDRKPGQLSGGQQQRVAIARALAHEP--MVVIADEPTGNL 182
Cdd:cd03238 74 VgLG-----YLTL----------------------------GQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGL 120
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15830546 183 DLATGEAILDLLLTINQQtGTTFVISTHSSELKARARRVVEI 224
Cdd:cd03238 121 HQQDINQLLEVIKGLIDL-GNTVILIEHNLDVLSSADWIIDF 161
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
47-224 |
2.98e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 46.45 E-value: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 47 GPSGSGKSTLLN----ILSGIDKPTSGTVIFLNKLLNQlpEEQLAVIrgkHLGFIFQFFNLMPV---LNVFDNVYFplVL 119
Cdd:cd03240 29 GQNGAGKTTIIEalkyALTGELPPNSKGGAHDPKLIRE--GEVRAQV---KLAFENANGKKYTItrsLAILENVIF--CH 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 120 NGQFSKKEATERtlhyldsvglsgfgdrkpGQLSGGQQQ------RVAIARALAHEPMVVIADEPTGNLDLATGE-AILD 192
Cdd:cd03240 102 QGESNWPLLDMR------------------GRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEeSLAE 163
|
170 180 190
....*....|....*....|....*....|..
gi 15830546 193 LLLTINQQTGTTFVISTHSSELKARARRVVEI 224
Cdd:cd03240 164 IIEERKSQKNFQLIVITHDEELVDAADHIYRV 195
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
30-224 |
3.02e-06 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 46.84 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 30 LKSINLDINKGEFLALCGPSGSGKSTLLN-ILSgidkPTSGTVIFLNKllnQLPEEQLAVIRGKHLGFIFQfFNLMPV-- 106
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINdTLY----PALARRLHLKK---EQPGNHDRIEGLEHIDKVIV-IDQSPIgr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 107 ---------LNVFDNV------------YFPLVLNGQFSKK-----------EATE---------RTLHYLDSVGLsgfG 145
Cdd:cd03271 83 tprsnpatyTGVFDEIrelfcevckgkrYNRETLEVRYKGKsiadvldmtveEALEffenipkiaRKLQTLCDVGL---G 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 146 DRKPGQ----LSGGQQQRVAIARALAHE---PMVVIADEPTGNLDLATGEAILDLLLTINQQtGTTFVISTHSSELKARA 218
Cdd:cd03271 160 YIKLGQpattLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDK-GNTVVVIEHNLDVIKCA 238
|
....*.
gi 15830546 219 RRVVEI 224
Cdd:cd03271 239 DWIIDL 244
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
150-229 |
4.06e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 46.85 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 150 GQLSGGQQQRVAIARALAHEPMVVIADEPTGNLDLATGEAILDLLLTINQQTGTTFVISTHSSELKARARRVVEIQDGVL 229
Cdd:PRK13549 404 ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
30-56 |
5.26e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 46.94 E-value: 5.26e-06
10 20
....*....|....*....|....*..
gi 15830546 30 LKSINLDINKGEFLALCGPSGSGKSTL 56
Cdd:COG0178 16 LKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
29-71 |
1.56e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 45.27 E-value: 1.56e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 15830546 29 ALKSINLDINKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTV 71
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV 81
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
147-213 |
1.60e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.24 E-value: 1.60e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830546 147 RKPGQLSGGQQQRVAIARALAHEPMVVIADEPTGNLDLatgEAILdLLLTINQQTGTTFVISTHSSE 213
Cdd:PLN03073 340 KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL---HAVL-WLETYLLKWPKTFIVVSHARE 402
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
45-208 |
8.18e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.96 E-value: 8.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 45 LCGPSGSGKSTLLNILSGIDKPTSGTV-IFLNKLLNQLPEEQLA---------VIRGKHlgfifqffNLMPVLNVFDNVY 114
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEPSAGNVsLDPNERLGKLRQDQFAfeeftvldtVIMGHT--------ELWEVKQERDRIY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 115 fplvlngqfSKKEATE-----------------------RTLHYLDSVGLS---GFGDRKpgQLSGGQQQRVAIARALAH 168
Cdd:PRK15064 104 ---------ALPEMSEedgmkvadlevkfaemdgytaeaRAGELLLGVGIPeeqHYGLMS--EVAPGWKLRVLLAQALFS 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15830546 169 EPMVVIADEPTGNLDLATgeaILDLLLTINQQTGTTFVIS 208
Cdd:PRK15064 173 NPDILLLDEPTNNLDINT---IRWLEDVLNERNSTMIIIS 209
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
27-71 |
1.09e-04 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 42.61 E-value: 1.09e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 15830546 27 VDALKSINLD-----INKGEFLALCGPSGSGKSTLLNILSGIDKPTSGTV 71
Cdd:PRK01889 177 VSALDGEGLDvlaawLSGGKTVALLGSSGVGKSTLVNALLGEEVQKTGAV 226
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
30-60 |
2.45e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.94 E-value: 2.45e-04
10 20 30
....*....|....*....|....*....|..
gi 15830546 30 LKSINLDINKGEFLALCGPSGSGKSTLLN-IL 60
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKSTLVNdIL 652
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
30-58 |
2.53e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.60 E-value: 2.53e-04
10 20
....*....|....*....|....*....
gi 15830546 30 LKSINLDINKGEFLALCGPSGSGKSTLLN 58
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLIN 653
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
29-211 |
2.59e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 41.11 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 29 ALKSINLDINKgeFLALCGPSGSGKSTLLNILSGIdkpTSGTVIFLN-------KLLNQLPEEQLAV-IRGKHLGFIFQF 100
Cdd:COG4938 11 PFKEAELELKP--LTLLIGPNGSGKSTLIQALLLL---LQSNFIYLPaersgpaRLYPSLVRELSDLgSRGEYTADFLAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 101 FNLMPVLNVFDNVYFPLVLN--GQFSKKEATERTLHYLDSVGLSGFGDRK---PGQLSGGQQQR----VAIARALAHEPM 171
Cdd:COG4938 86 LENLEILDDKSKELLEQVEEwlEKIFPGKVEVDASSDLVRLVFRPSGNGKripLSNVGSGVSELlpilLALLSAAKPGSL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15830546 172 VVIaDEPTGNLDLATGEAILDLLLTInQQTGTTFVISTHS 211
Cdd:COG4938 166 LII-EEPEAHLHPKAQSALAELLAEL-ANSGVQVIIETHS 203
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
30-58 |
2.66e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.54 E-value: 2.66e-04
10 20
....*....|....*....|....*....
gi 15830546 30 LKSINLDINKGEFLALCGPSGSGKSTLLN 58
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLIN 652
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
27-93 |
3.36e-04 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 40.46 E-value: 3.36e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830546 27 VDALKSInLdinKGEFLALCGPSGSGKSTLLNILsgidkptsgtviflnkllnqLPEEQLAVI-------RGKH 93
Cdd:cd01854 76 LDELREL-L---KGKTSVLVGQSGVGKSTLLNAL--------------------LPELVLATGeiseklgRGRH 125
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
30-56 |
5.01e-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: 40.77 E-value: 5.01e-04
10 20
....*....|....*....|....*..
gi 15830546 30 LKSINLDINKGEFLALCGPSGSGKSTL 56
Cdd:TIGR00630 12 LKNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
133-230 |
7.33e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.58 E-value: 7.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 133 LHYLDSVGLSGFG-DRKPGQLSGGQQQRVAIARALAHEPMVV--IADEPTGNLDLATGEAILDLLLTINQQtGTTFVIST 209
Cdd:PRK00635 457 LSILIDLGLPYLTpERALATLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQ-GNTVLLVE 535
|
90 100
....*....|....*....|.
gi 15830546 210 HSSELKARARRVVEIQDGVLI 230
Cdd:PRK00635 536 HDEQMISLADRIIDIGPGAGI 556
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
146-179 |
9.56e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.77 E-value: 9.56e-04
10 20 30
....*....|....*....|....*....|....
gi 15830546 146 DRKPGQLSGGQQQRVAIARALAHEPMVVIADEPT 179
Cdd:NF040905 399 FQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPT 432
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
36-190 |
1.13e-03 |
|
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: 38.71 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 36 DINKGEFLALCGPSGSGKSTLLNILSGIDKPTSgtviflnkllnqlpeeqlavirgkhlgfifqffnlmpvlnvfDNVYF 115
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNG------------------------------------------DNDEW 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 116 PLVlngqfskkeaterTLHYldsvglsgfgdrKPG--QLSGGQQQRVAIARALAHEPMVVIADEPTGNLD----LATGEA 189
Cdd:cd03222 59 DGI-------------TPVY------------KPQyiDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDieqrLNAARA 113
|
.
gi 15830546 190 I 190
Cdd:cd03222 114 I 114
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
36-224 |
1.26e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 38.79 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 36 DINKGEFLALCGPSGSGKSTLL---------------------NILSGIDKPTSGTVIFlnkllnQLPEEQLAVIRGKHL 94
Cdd:cd03279 24 GLDNNGLFLICGPTGAGKSTILdaityalygktprygrqenlrSVFAPGEDTAEVSFTF------QLGGKKYRVERSRGL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 95 GFIfQFFNLmpvlnvfdnVYFPlvlNGQFSKkeatertlhyldsvglsgFGDRKPGQLSGGQQQRVAIARALAHEPMV-- 172
Cdd:cd03279 98 DYD-QFTRI---------VLLP---QGEFDR------------------FLARPVSTLSGGETFLASLSLALALSEVLqn 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 173 --------VIADEPTGNLDLATGEAILDLLLTINQQTGTTFVIStHSSELKARARRVVEI 224
Cdd:cd03279 147 rggarleaLFIDEGFGTLDPEALEAVATALELIRTENRMVGVIS-HVEELKERIPQRLEV 205
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
114-221 |
1.36e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 114 YFPLVLNGQFSKKEATERT-LHYLDSVGLSgfgdRKPGQLSGG-QQQ-----RVAIARALAHEPMVVIADEPTGNLDLAT 186
Cdd:COG4717 524 YFSRLTDGRYRLIRIDEDLsLKVDTEDGRT----RPVEELSRGtREQlylalRLALAELLAGEPLPLILDDAFVNFDDER 599
|
90 100 110
....*....|....*....|....*....|....*...
gi 15830546 187 GEAILDLLLTI--NQQtgttfVIS-THSSELKARARRV 221
Cdd:COG4717 600 LRAALELLAELakGRQ-----VIYfTCHEELVELFQEE 632
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
81-231 |
1.65e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.23 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 81 LPEEQLAV-IRGKHlgfiFQFFNLMPVLNVFDnVYFPLVLNGQFSK------KEATERtLHYLDSVGLSGFG-DRKPGQL 152
Cdd:TIGR00630 416 LKPEALAVtVGGKS----IADVSELSIREAHE-FFNQLTLTPEEKKiaeevlKEIRER-LGFLIDVGLDYLSlSRAAGTL 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 153 SGGQQQRVAIARALAHEPMVV--IADEPTGNLDLATGEAILDLLLTINQQtGTTFVISTHSSELKARARRVVEIQDGVLI 230
Cdd:TIGR00630 490 SGGEAQRIRLATQIGSGLTGVlyVLDEPSIGLHQRDNRRLINTLKRLRDL-GNTLIVVEHDEDTIRAADYVIDIGPGAGE 568
|
.
gi 15830546 231 H 231
Cdd:TIGR00630 569 H 569
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
30-56 |
2.11e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 38.90 E-value: 2.11e-03
10 20
....*....|....*....|....*..
gi 15830546 30 LKSINLDINKGEFLALCGPSGSGKSTL 56
Cdd:PRK00349 16 LKNIDLDIPRDKLVVFTGLSGSGKSSL 42
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
39-93 |
3.24e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 37.14 E-value: 3.24e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 15830546 39 KGEFLALCGPSGSGKSTLLN-ILSGIDKPTSGTVIFLNkllnqlpeeqlaviRGKH 93
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTLLNaLLPELDLRTGEISEKLG--------------RGRH 146
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
43-141 |
5.24e-03 |
|
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.
Pssm-ID: 206733 [Multi-domain] Cd Length: 268 Bit Score: 37.19 E-value: 5.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 43 LALCGPSGSGKSTLLNIL---SG-IDKPtsGTVIFLNKLLNQLPEE-------QLAVI----RGKHLGFI-------FQF 100
Cdd:cd04170 2 IALVGHSGSGKTTLAEALlyaTGaIDRL--GRVEDGNTVSDYDPEEkkrkmsiETSVAplewNGHKINLIdtpgyadFVG 79
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 15830546 101 FnLMPVLNVFDNVYFplVLNGQFSKKEATERTLHYLDSVGL 141
Cdd:cd04170 80 E-TLSALRAVDAALI--VVEAQSGVEVGTEKVWEFLDDAKL 117
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
81-179 |
5.64e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 37.70 E-value: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 81 LPEEQLAV-IRGKHlgfIFQFfNLMPV---LNVFDNvyfpLVLNGQFSK------KEATERtLHYLDSVGLsgfG----D 146
Cdd:COG0178 413 LKPEALAVkIGGKN---IAEL-TALSIdeaLEFFEN----LELTEREAEiaerilKEIRSR-LGFLVDVGL---DyltlD 480
|
90 100 110
....*....|....*....|....*....|....*
gi 15830546 147 RKPGQLSGGQQQRVAIARALAHEPMVV--IADEPT 179
Cdd:COG0178 481 RSAGTLSGGEAQRIRLATQIGSGLVGVlyVLDEPS 515
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
133-229 |
6.97e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 37.50 E-value: 6.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 133 LHYLDSVGLSGFGDRKP-GQLSGGQQQRVAIARAL---AHEPMVVIADEPTGNLDLATGEAILDLLLTINQQtGTTFVIS 208
Cdd:PRK00635 790 IHALCSLGLDYLPLGRPlSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQ-GHTVVII 868
|
90 100
....*....|....*....|.
gi 15830546 209 THSSElkararrVVEIQDGVL 229
Cdd:PRK00635 869 EHNMH-------VVKVADYVL 882
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
153-229 |
7.07e-03 |
|
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that maintains replication in the presence of DNA damage. When replication is prematurely disrupted by DNA damage, several recF pathway gene products play critical roles processing the arrested replication fork, allowing it to resume and complete its task. This CD represents the nucleotide binding domain of RecF. RecF belongs to a large superfamily of ABC transporters 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 with 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: 213209 [Multi-domain] Cd Length: 270 Bit Score: 36.89 E-value: 7.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830546 153 SGGQQQRVAIARALAH---------EPMVVIADEPTGNLDLATGEAILDLLLTINQqtgtTFVISTHSSELKARARR--- 220
Cdd:cd03242 185 SQGQQRTLALALKLAEiqlikevsgEYPVLLLDDVLAELDLGRQAALLDAIEGRVQ----TFVTTTDLADFDALWLRraq 260
|
....*....
gi 15830546 221 VVEIQDGVL 229
Cdd:cd03242 261 IFRVDAGTL 269
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
17-62 |
8.78e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 36.72 E-value: 8.78e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 15830546 17 YKCYG--AGAGK-VDALKSInLdinKGEFLALCGPSGSGKSTLLNILSG 62
Cdd:PRK00098 142 YDVLElsAKEGEgLDELKPL-L---AGKVTVLAGQSGVGKSTLLNALAP 186
|
|
| |
