|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
9-234 |
3.68e-124 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 351.27 E-value: 3.68e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSYGSGEGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAA 88
Cdd:COG1136 3 PLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 89 IRGRHLGFIFQFFNLIPVLSVFDNVFFPLVLNGhVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAH 168
Cdd:COG1136 83 LRRRHIGFVFQFFNLLPELTALENVALPLLLAG-VSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556463668 169 DPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQLKERARRVVEIKDGVLVHDSQ 234
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVSDER 227
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
11-229 |
1.65e-111 |
|
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: 318.67 E-value: 1.65e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSGEGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAAIR 90
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 91 GRHLGFIFQFFNLIPVLSVFDNVFFPLVLNGhVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHDP 170
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAG-VPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 556463668 171 QVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQLKERARRVVEIKDGVL 229
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
9-235 |
1.20e-95 |
|
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: 279.32 E-value: 1.20e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSYGSGEGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAA 88
Cdd:COG4181 7 PIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 89 IRGRHLGFIFQFFNLIPVLSVFDNVFFPLVLNGHvgkKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAH 168
Cdd:COG4181 87 LRARHVGFVFQSFQLLPTLTALENVMLPLELAGR---RDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFAT 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556463668 169 DPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQLKERARRVVEIKDGVLVHDSQT 235
Cdd:COG4181 164 EPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTAA 230
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
10-234 |
1.15e-89 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 263.45 E-value: 1.15e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 10 MISLNNIYKSYGSGegkVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAAI 89
Cdd:COG2884 1 MIRFENVSKRYPGG---REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 90 RgRHLGFIFQFFNLIPVLSVFDNVFFPLVLNGhVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHD 169
Cdd:COG2884 78 R-RRIGVVFQDFRLLPDRTVYENVALPLRVTG-KSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556463668 170 PQVVIADEPTGNLDLVTGEAILDLLLKINQeTRTTFIISTHSSQLKERAR-RVVEIKDGVLVHDSQ 234
Cdd:COG2884 156 PELLLADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPkRVLELEDGRLVRDEA 220
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
9-211 |
6.69e-81 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 242.69 E-value: 6.69e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSYGSGEGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVmflkkLLNHLPEEQLaa 88
Cdd:COG1116 6 PALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEV-----LVDGKPVTGP-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 89 irGRHLGFIFQFFNLIPVLSVFDNVFFPLVLNGhVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAH 168
Cdd:COG1116 79 --GPDRGVVFQEPALLPWLTVLDNVALGLELRG-VPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 556463668 169 DPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHS 211
Cdd:COG1116 156 DPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHD 198
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
9-232 |
6.91e-77 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 232.25 E-value: 6.91e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSYGSGegkVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAA 88
Cdd:COG3638 1 PMLELRNLSKRYPGG---TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 89 IRgRHLGFIFQFFNLIPVLSVFDNVffplvLNGHVGK------------KEARERALHFIESVGLAGFTERKPGQLSGGQ 156
Cdd:COG3638 78 LR-RRIGMIFQQFNLVPRLSVLTNV-----LAGRLGRtstwrsllglfpPEDRERALEALERVGLADKAYQRADQLSGGQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556463668 157 QQRVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQL-KERARRVVEIKDGVLVHD 232
Cdd:COG3638 152 QQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLaRRYADRIIGLRDGRVVFD 228
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
10-230 |
5.52e-75 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 230.35 E-value: 5.52e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 10 MISLNNIYKSYGSGEGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAAI 89
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 90 RgRHLGFIFQFFNLIPVLSVFDNVFFPLVLNGhVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHD 169
Cdd:COG1135 81 R-RKIGMIFQHFNLLSSRTVAENVALPLEIAG-VPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556463668 170 PQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQ-LKERARRVVEIKDGVLV 230
Cdd:COG1135 159 PKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDvVRRICDRVAVLENGRIV 220
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
11-211 |
6.54e-75 |
|
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: 226.20 E-value: 6.54e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSGEGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVmflkkLLNHLPEEQlaaiR 90
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEV-----LVDGEPVTG----P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 91 GRHLGFIFQFFNLIPVLSVFDNVFFPLVLNGhVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHDP 170
Cdd:cd03293 72 GPDRGYVFQQDALLPWLTVLDNVALGLELQG-VPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDP 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 556463668 171 QVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHS 211
Cdd:cd03293 151 DVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHD 191
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
9-210 |
2.74e-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: 221.51 E-value: 2.74e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSYGSgegkVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQlaa 88
Cdd:COG3842 4 PALELENVSKRYGD----VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 89 irgRHLGFIFQFFNLIPVLSVFDNVFFPLVLNGhVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAH 168
Cdd:COG3842 77 ---RNVGMVFQDYALFPHLTVAENVAFGLRMRG-VPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 556463668 169 DPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTH 210
Cdd:COG3842 153 EPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTH 194
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
10-230 |
2.26e-70 |
|
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: 215.14 E-value: 2.26e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 10 MISLNNIYKSYGSGEGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAAI 89
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 90 RgRHLGFIFQFFNLIPVLSVFDNVFFPLVLnGHVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHD 169
Cdd:cd03258 81 R-RRIGMIFQHFNLLSSRTVFENVALPLEI-AGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556463668 170 PQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQ-LKERARRVVEIKDGVLV 230
Cdd:cd03258 159 PKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEvVKRICDRVAVMEKGEVV 220
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
10-227 |
7.23e-70 |
|
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: 213.26 E-value: 7.23e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 10 MISLNNIYKSYGSGegkVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAAI 89
Cdd:TIGR02673 1 MIEFHNVSKAYPGG---VAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 90 RgRHLGFIFQFFNLIPVLSVFDNVFFPLVLNGhVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHD 169
Cdd:TIGR02673 78 R-RRIGVVFQDFRLLPDRTVYENVALPLEVRG-KKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 556463668 170 PQVVIADEPTGNLDLVTGEAILDLLLKINQETrTTFIISTHSSQLKER-ARRVVEIKDG 227
Cdd:TIGR02673 156 PPLLLADEPTGNLDPDLSERILDLLKRLNKRG-TTVIVATHDLSLVDRvAHRVIILDDG 213
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
10-232 |
7.79e-69 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 211.39 E-value: 7.79e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 10 MISLNNIYKSYGSGEgkvdALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLnHLPEEQLAAI 89
Cdd:COG1126 1 MIEIENLHKSFGDLE----VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 90 RgRHLGFIFQFFNLIPVLSVFDNVFFPLVLNGHVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHD 169
Cdd:COG1126 76 R-RKVGMVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556463668 170 PQVVIADEPTGNLD--LVtGEaILDLLLKINQEtRTTFIISTHS-SQLKERARRVVEIKDGVLVHD 232
Cdd:COG1126 155 PKVMLFDEPTSALDpeLV-GE-VLDVMRDLAKE-GMTMVVVTHEmGFAREVADRVVFMDGGRIVEE 217
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
7-232 |
1.01e-68 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 210.83 E-value: 1.01e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 7 ELPMISLNNIYKSYGSGEGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQL 86
Cdd:PRK11629 2 NKILLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 87 AAIRGRHLGFIFQFFNLIPVLSVFDNVFFPLVLnGHVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARAL 166
Cdd:PRK11629 82 AELRNQKLGFIYQFHHLLPDFTALENVAMPLLI-GKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556463668 167 AHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQLKERARRVVEIKDGVLVHD 232
Cdd:PRK11629 161 VNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAE 226
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
11-232 |
1.11e-68 |
|
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: 210.89 E-value: 1.11e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSGegkVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAAIR 90
Cdd:cd03256 1 IEVENLSKTYPNG---KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 91 gRHLGFIFQFFNLIPVLSVFDNVffplvLNGHVG------------KKEARERALHFIESVGLAGFTERKPGQLSGGQQQ 158
Cdd:cd03256 78 -RQIGMIFQQFNLIERLSVLENV-----LSGRLGrrstwrslfglfPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556463668 159 RVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQL-KERARRVVEIKDGVLVHD 232
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLaREYADRIVGLKDGRIVFD 226
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
11-229 |
1.28e-67 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 207.26 E-value: 1.28e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSGegkVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAAIR 90
Cdd:cd03292 1 IEFINVTKTYPNG---TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 91 gRHLGFIFQFFNLIPVLSVFDNVFFPLVLNGHvGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHDP 170
Cdd:cd03292 78 -RKIGVVFQDFRLLPDRNVYENVAFALEVTGV-PPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 171 QVVIADEPTGNLDLVTGEAILDLLLKINQETrTTFIISTHSSQLKERAR-RVVEIKDGVL 229
Cdd:cd03292 156 TILIADEPTGNLDPDTTWEIMNLLKKINKAG-TTVVVATHAKELVDTTRhRVIALERGKL 214
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
10-229 |
9.23e-67 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 205.34 E-value: 9.23e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 10 MISLNNIYKSYGSGEGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAAI 89
Cdd:NF038007 1 MLNMQNAEKCYITKTIKTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 90 RGRHLGFIFQFFNLIPVLSVFDNVFFPLVLNGhVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHD 169
Cdd:NF038007 81 RRELIGYIFQSFNLIPHLSIFDNVALPLKYRG-VAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSN 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 170 PQVVIADEPTGNLDLVTGEAILDLLLKINQeTRTTFIISTHSSQLKERARRVVEIKDGVL 229
Cdd:NF038007 160 PALLLADEPTGNLDSKNARAVLQQLKYINQ-KGTTIIMVTHSDEASTYGNRIINMKDGKL 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
9-230 |
1.06e-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: 214.00 E-value: 1.06e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSYGS-GEGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLA 87
Cdd:COG1123 259 PLLEVRNLSKRYPVrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 88 AIRgRHLGFIFQ--FFNLIPVLSVFDNVFFPLVLNGHVGKKEARERALHFIESVGL-AGFTERKPGQLSGGQQQRVAIAR 164
Cdd:COG1123 339 ELR-RRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556463668 165 ALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQLKER-ARRVVEIKDGVLV 230
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIV 484
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
9-232 |
1.56e-66 |
|
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: 205.60 E-value: 1.56e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSYGsgeGKVdALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAA 88
Cdd:COG1127 4 PMIEVRNLTKSFG---DRV-VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 89 IRgRHLGFIFQFFNLIPVLSVFDNVFFPLVLNGHVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAH 168
Cdd:COG1127 80 LR-RRIGMLFQGGALFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALAL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556463668 169 DPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHS-SQLKERARRVVEIKDGVLVHD 232
Cdd:COG1127 159 DPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDlDSAFAIADRVAVLADGKIIAE 223
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
9-233 |
3.31e-66 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 215.74 E-value: 3.31e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSYGSGEGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAA 88
Cdd:PRK10535 3 ALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 89 IRGRHLGFIFQFFNLIPVLSVFDNVFFPLVLNGhVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAH 168
Cdd:PRK10535 83 LRREHFGFIFQRYHLLSHLTAAQNVEVPAVYAG-LERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556463668 169 DPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTfIISTHSSQLKERARRVVEIKDGVLVHDS 233
Cdd:PRK10535 162 GGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTV-IIVTHDPQVAAQAERVIEIRDGEIVRNP 225
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
11-211 |
5.82e-66 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 203.13 E-value: 5.82e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSgegkVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQlaair 90
Cdd:cd03259 1 LELKGLSKTYGS----VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 91 gRHLGFIFQFFNLIPVLSVFDNVFFPLVLNGhVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHDP 170
Cdd:cd03259 72 -RNIGMVFQDYALFPHLTVAENIAFGLKLRG-VPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 556463668 171 QVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHS 211
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHD 190
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
10-230 |
7.47e-66 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 207.23 E-value: 7.47e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 10 MISLNNIYKSYGsgegKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQlaai 89
Cdd:COG3839 3 SLELENVSKSYG----GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 90 rgRHLGFIFQFFNLIPVLSVFDNVFFPLVLNGhVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHD 169
Cdd:COG3839 75 --RNIAMVFQSYALYPHMTVYENIAFPLKLRK-VPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVRE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556463668 170 PQVVIADEPTGNLDlvtgeAIL-----DLLLKINQETRTTFIISTHsSQ-----LkerARRVVEIKDGVLV 230
Cdd:COG3839 152 PKVFLLDEPLSNLD-----AKLrvemrAEIKRLHRRLGTTTIYVTH-DQveamtL---ADRIAVMNDGRIQ 213
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
10-230 |
7.55e-65 |
|
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: 200.81 E-value: 7.55e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 10 MISLNNIYKSYGSGEGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAaI 89
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRK-I 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 90 RGRHLGFIFQ--FFNLIPVLSVFDNVFFPLVLNGHVGKKEARERALHFI-ESVGL-AGFTERKPGQLSGGQQQRVAIARA 165
Cdd:cd03257 80 RRKEIQMVFQdpMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLlVGVGLpEEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556463668 166 LAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHS-SQLKERARRVVEIKDGVLV 230
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDlGVVAKIADRVAVMYAGKIV 225
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
10-229 |
1.10e-64 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 200.39 E-value: 1.10e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 10 MISLNNIYKSYGSGEGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAAI 89
Cdd:PRK10584 6 IVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 90 RGRHLGFIFQFFNLIPVLSVFDNVFFPLVLNGHvGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHD 169
Cdd:PRK10584 86 RAKHVGFVFQSFMLIPTLNALENVELPALLRGE-SSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGR 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 170 PQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQLKERARRVVEIKDGVL 229
Cdd:PRK10584 165 PDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
10-232 |
4.38e-63 |
|
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: 196.75 E-value: 4.38e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 10 MISLNNIYKSYGSGegkVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAAI 89
Cdd:TIGR02315 1 MLEVENLSKVYPNG---KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 90 RgRHLGFIFQFFNLIPVLSVFDNVffplvLNGHVG------------KKEARERALHFIESVGLAGFTERKPGQLSGGQQ 157
Cdd:TIGR02315 78 R-RRIGMIFQHYNLIERLTVLENV-----LHGRLGykptwrsllgrfSEEDKERALSALERVGLADKAYQRADQLSGGQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556463668 158 QRVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQL-KERARRVVEIKDGVLVHD 232
Cdd:TIGR02315 152 QRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLaKKYADRIVGLKAGEIVFD 227
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
10-230 |
4.02e-62 |
|
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: 194.64 E-value: 4.02e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 10 MISLNNIYKSYGSGEGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHlpeEQLAAI 89
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTR---RRRKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 90 RgRHLGFIFQ--FFNLIPVLSVFDNVFFPLVLNGhvgKKEARERALHFIESVGL-AGFTERKPGQLSGGQQQRVAIARAL 166
Cdd:COG1124 78 R-RRVQMVFQdpYASLHPRHTVDRILAEPLRIHG---LPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556463668 167 AHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQLKER-ARRVVEIKDGVLV 230
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIV 218
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
10-230 |
1.20e-61 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 196.18 E-value: 1.20e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 10 MISLNNIYKSYGSGEGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAAI 89
Cdd:PRK11153 1 MIELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 90 RgRHLGFIFQFFNLIPVLSVFDNVFFPLVLNGhVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHD 169
Cdd:PRK11153 81 R-RQIGMIFQHFNLLSSRTVFDNVALPLELAG-TPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556463668 170 PQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQ-LKERARRVVEIKDGVLV 230
Cdd:PRK11153 159 PKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDvVKRICDRVAVIDAGRLV 220
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
11-232 |
6.06e-61 |
|
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: 191.01 E-value: 6.06e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYgsgEGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNhlpEEQLAAIR 90
Cdd:COG1122 1 IELENLSFSY---PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDIT---KKNLRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 91 gRHLGFIFQ-----FFNLipvlSVFDNVFFPLvLNGHVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARA 165
Cdd:COG1122 75 -RKVGLVFQnpddqLFAP----TVEEDVAFGP-ENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556463668 166 LAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQEtRTTFIISTHS-SQLKERARRVVEIKDGVLVHD 232
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDlDLVAELADRVIVLDDGRIVAD 215
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
12-227 |
9.29e-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: 189.60 E-value: 9.29e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 12 SLNNIYKSYGSGEGKvdALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAairg 91
Cdd:cd03225 1 ELKNLSFSYPDGARP--ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELR---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 92 RHLGFIFQ-----FFNLipvlSVFDNVFFPLvLNGHVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARAL 166
Cdd:cd03225 75 RKVGLVFQnpddqFFGP----TVEEEVAFGL-ENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556463668 167 AHDPQVVIADEPTGNLDLVTGEAILDLLLKINQEtRTTFIISTHS-SQLKERARRVVEIKDG 227
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDlDLLLELADRVIVLEDG 210
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
11-230 |
1.69e-60 |
|
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: 190.02 E-value: 1.69e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGsgEGKVdaLKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAAIR 90
Cdd:cd03261 1 IELRGLTKSFG--GRTV--LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 91 gRHLGFIFQFFNLIPVLSVFDNVFFPLVLNGHVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHDP 170
Cdd:cd03261 77 -RRMGMLFQSGALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556463668 171 QVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHS-SQLKERARRVVEIKDGVLV 230
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDlDTAFAIADRIAVLYDGKIV 216
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
9-211 |
2.38e-60 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 190.46 E-value: 2.38e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSYGSGEGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMflkklLNHLPEEQLAA 88
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEIT-----LDGVPVTGPGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 89 IRGrhlgFIFQFFNLIPVLSVFDNVFFPLVLNGhVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAH 168
Cdd:COG4525 77 DRG----VVFQKDALLPWLNVLDNVAFGLRLRG-VPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 556463668 169 DPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHS 211
Cdd:COG4525 152 DPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
11-229 |
2.49e-60 |
|
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: 188.89 E-value: 2.49e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSGEgkvdALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHlPEEQLAAIR 90
Cdd:cd03262 1 IEIKNLHKSFGDFH----VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 91 gRHLGFIFQFFNLIPVLSVFDNVFFPLVLNGHVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHDP 170
Cdd:cd03262 76 -QKVGMVFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556463668 171 QVVIADEPTGNLD--LVtGEaILDLLLKINQEtRTTFIISTHSSQL-KERARRVVEIKDGVL 229
Cdd:cd03262 155 KVMLFDEPTSALDpeLV-GE-VLDVMKDLAEE-GMTMVVVTHEMGFaREVADRVIFMDDGRI 213
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
11-230 |
3.08e-60 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 189.12 E-value: 3.08e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGsgegKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVmflkKLLNHLPEEQLAAIR 90
Cdd:COG1131 1 IEVRGLTKRYG----DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEV----RVLGEDVARDPAEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 91 gRHLGFIFQFFNLIPVLSVFDNVFFPLVLNGhVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHDP 170
Cdd:COG1131 73 -RRIGYVPQEPALYPDLTVRENLRFFARLYG-LPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556463668 171 QVVIADEPTGNLDLVTGEAILDLLLKINQEtRTTFIISTHS-SQLKERARRVVEIKDGVLV 230
Cdd:COG1131 151 ELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYlEEAERLCDRVAIIDKGRIV 210
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
10-210 |
9.13e-60 |
|
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: 190.65 E-value: 9.13e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 10 MISLNNIYKSYGSGEGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTV---GTVMFLKKLLNHLPEEQL 86
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 87 AAIRGRHLGFIFQ----FFNliPVLSVFDNVFFPLVLNGHVGKKEARERALHFIESVGLAGFTERK---PGQLSGGQQQR 159
Cdd:COG0444 81 RKIRGREIQMIFQdpmtSLN--PVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLdryPHELSGGMRQR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 556463668 160 VAIARALAHDPQVVIADEPTGNLDlVTGEA-ILDLLLKINQETRTTFIISTH 210
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALD-VTIQAqILNLLKDLQRELGLAILFITH 209
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
11-210 |
1.36e-58 |
|
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: 185.13 E-value: 1.36e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSGEgkvdALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQlaair 90
Cdd:cd03300 1 IELENVSKFYGGFV----ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 91 gRHLGFIFQFFNLIPVLSVFDNVFFPLVLNGhVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHDP 170
Cdd:cd03300 72 -RPVNTVFQNYALFPHLTVFENIAFGLRLKK-LPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 556463668 171 QVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTH 210
Cdd:cd03300 150 KVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTH 189
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
13-224 |
6.42e-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: 182.43 E-value: 6.42e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 13 LNNIYKSYGSGEgkvdALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAAIRGR 92
Cdd:TIGR03608 1 LKNISKKFGDKV----ILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 93 HLGFIFQFFNLIPVLSVFDNVFFPLVLNgHVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHDPQV 172
Cdd:TIGR03608 77 KLGYLFQNFALIENETVEENLDLGLKYK-KLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 556463668 173 VIADEPTGNLDLVTGEAILDLLLKINQETRtTFIISTHSSQLKERARRVVEI 224
Cdd:TIGR03608 156 ILADEPTGSLDPKNRDEVLDLLLELNDEGK-TIIIVTHDPEVAKQADRVIEL 206
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
9-230 |
2.17e-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: 184.72 E-value: 2.17e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSYGSGEgkVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTV---GTVMFLKKLLNHLPEeq 85
Cdd:COG1123 3 PLLEVRDLSVRYPGGD--VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 86 laAIRGRHLGFIFQFF--NLIPVlSVFDNVFFPLvLNGHVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIA 163
Cdd:COG1123 79 --ALRGRRIGMVFQDPmtQLNPV-TVGDQIAEAL-ENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556463668 164 RALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHS-SQLKERARRVVEIKDGVLV 230
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDlGVVAEIADRVVVMDDGRIV 222
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
11-230 |
2.19e-55 |
|
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: 177.84 E-value: 2.19e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGS-----------GEGKVD---------ALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGT 70
Cdd:cd03294 1 IKIKGLYKIFGKnpqkafkllakGKSKEEilkktgqtvGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 71 VMFLKKLLNHLPEEQLAAIRGRHLGFIFQFFNLIPVLSVFDNVFFPLVLNGhVGKKEARERALHFIESVGLAGFTERKPG 150
Cdd:cd03294 81 VLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVLENVAFGLEVQG-VPRAEREERAAEALELVGLEGWEHKYPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 151 QLSGGQQQRVAIARALAHDPQVVIADEPTGNLD-LVTGEaILDLLLKINQETRTTFIISTHSsqLKERAR---RVVEIKD 226
Cdd:cd03294 160 ELSGGMQQRVGLARALAVDPDILLMDEAFSALDpLIRRE-MQDELLRLQAELQKTIVFITHD--LDEALRlgdRIAIMKD 236
|
....
gi 556463668 227 GVLV 230
Cdd:cd03294 237 GRLV 240
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
11-230 |
3.60e-54 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 177.26 E-value: 3.60e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSgegkVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLN-HLPeeqlaaI 89
Cdd:COG1118 3 IEVRNISKRFGS----FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtNLP------P 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 90 RGRHLGFIFQFFNLIPVLSVFDNV-FFPLVLNghVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAH 168
Cdd:COG1118 73 RERRVGFVFQHYALFPHMTVAENIaFGLRVRP--PSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556463668 169 DPQVVIADEPTGNLD-LVTGEaILDLLLKINQETRTTFIISTHsSQLK--ERARRVVEIKDGVLV 230
Cdd:COG1118 151 EPEVLLLDEPFGALDaKVRKE-LRRWLRRLHDELGGTTVFVTH-DQEEalELADRVVVMNQGRIE 213
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
11-230 |
3.21e-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: 170.51 E-value: 3.21e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGsgegKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQlaair 90
Cdd:cd03301 1 VELENVTKRFG----NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 91 gRHLGFIFQFFNLIPVLSVFDNVFFPLVLNgHVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHDP 170
Cdd:cd03301 72 -RDIAMVFQNYALYPHMTVYDNIAFGLKLR-KVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556463668 171 QVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSqlKER---ARRVVEIKDGVLV 230
Cdd:cd03301 150 KVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQ--VEAmtmADRIAVMNDGQIQ 210
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
11-227 |
1.04e-51 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 165.44 E-value: 1.04e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGsgegKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLpEEQLAAIR 90
Cdd:cd03229 1 LELKNVSKRYG----QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDL-EDELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 91 gRHLGFIFQFFNLIPVLSVFDNVFFPlvlnghvgkkeareralhfiesvglagfterkpgqLSGGQQQRVAIARALAHDP 170
Cdd:cd03229 76 -RRIGMVFQDFALFPHLTVLENIALG-----------------------------------LSGGQQQRVALARALAMDP 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 556463668 171 QVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHS-SQLKERARRVVEIKDG 227
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDlDEAARLADRVVVLRDG 177
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
9-233 |
1.72e-51 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 167.19 E-value: 1.72e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSYGsgegKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHlpeeqlaa 88
Cdd:COG1121 5 PAIELENLTVSYG----GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 89 iRGRHLGFIFQFFNL---IPVlSVFDnvffpLVLNGHVGK--------KEARERALHFIESVGLAGFTERKPGQLSGGQQ 157
Cdd:COG1121 73 -ARRRIGYVPQRAEVdwdFPI-TVRD-----VVLMGRYGRrglfrrpsRADREAVDEALERVGLEDLADRPIGELSGGQQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556463668 158 QRVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQEtRTTFIISTHS-SQLKERARRVVEIKDGVLVHDS 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 ... |
11-230 |
3.39e-51 |
|
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: 166.32 E-value: 3.39e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSGEgkvDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAair 90
Cdd:cd03295 1 IEFENVTKRYGGGK---KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELR--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 91 gRHLGFIFQFFNLIPVLSVFDNVFFPLVLNGhVGKKEARERALHFIESVGL--AGFTERKPGQLSGGQQQRVAIARALAH 168
Cdd:cd03295 75 -RKIGYVIQQIGLFPHMTVEENIALVPKLLK-WPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556463668 169 DPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQLKER-ARRVVEIKDGVLV 230
Cdd:cd03295 153 DPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRlADRIAIMKNGEIV 215
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
10-232 |
3.83e-51 |
|
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: 166.19 E-value: 3.83e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 10 MISLNNIYKSYGsgegKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLkkllNHLPEEQLAAI 89
Cdd:COG4555 1 MIEVENLSKKYG----KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILID----GEDVRKEPREA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 90 RgRHLGFIFQFFNLIPVLSVFDNVFFPLVLNGhVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHD 169
Cdd:COG4555 73 R-RQIGVLPDERGLYDRLTVRENIRYFAELYG-LFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556463668 170 PQVVIADEPTGNLDLVTGEAILDLLLKINQETRtTFIISTHSSQLKER-ARRVVEIKDGVLVHD 232
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLLREILRALKKEGK-TVLFSSHIMQEVEAlCDRVVILHKGKVVAQ 213
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
11-232 |
4.37e-51 |
|
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: 167.24 E-value: 4.37e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSG---EGKvdALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLA 87
Cdd:TIGR04521 1 IKLKNVSYIYQPGtpfEKK--ALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 88 AIRgRHLGFIFQF-----FNLipvlSVFDNVFF-PLVLNghVGKKEARERALHFIESVGL-AGFTERKPGQLSGGQQQRV 160
Cdd:TIGR04521 79 DLR-KKVGLVFQFpehqlFEE----TVYKDIAFgPKNLG--LSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556463668 161 AIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHS-SQLKERARRVVEIKDGVLVHD 232
Cdd:TIGR04521 152 AIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSmEDVAEYADRVIVMHKGKIVLD 224
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
10-210 |
5.59e-51 |
|
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: 165.99 E-value: 5.59e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 10 MISLNNIYKSYGSGEgkvdALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAai 89
Cdd:COG1120 1 MLEAENLSVGYGGRP----VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELA-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 90 rgRHLGFIFQFFNLIPVLSVFDnvffpLVLNG---HVG-----KKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVA 161
Cdd:COG1120 75 --RRIAYVPQEPPAPFGLTVRE-----LVALGrypHLGlfgrpSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 556463668 162 IARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTH 210
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLH 196
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
9-232 |
1.36e-50 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 168.59 E-value: 1.36e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSYGSGEgkvdALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQlaa 88
Cdd:PRK09452 13 PLVELRGISKSFDGKE----VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 89 irgRHLGFIFQFFNLIPVLSVFDNVFFPLVLNGhVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAH 168
Cdd:PRK09452 86 ---RHVNTVFQSYALFPHMTVFENVAFGLRMQK-TPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556463668 169 DPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSsqlKERA----RRVVEIKDGVLVHD 232
Cdd:PRK09452 162 KPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHD---QEEAltmsDRIVVMRDGRIEQD 226
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
11-235 |
7.05e-50 |
|
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: 162.35 E-value: 7.05e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSGEgkvdALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGI-----DKPTVGTVMFLKKLLNHLPEEQ 85
Cdd:cd03260 1 IELRDLNVYYGDKH----ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 86 LAaIRgRHLGFIFQFFNLIPvLSVFDNVFFPLVLNGHVGKKEARERALHFIESVGLAGFTERK--PGQLSGGQQQRVAIA 163
Cdd:cd03260 77 LE-LR-RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRlhALGLSGGQQQRLCLA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556463668 164 RALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQEtrTTFIISTHSSQLKER-ARRVVEIKDGVLVHDSQT 235
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPT 224
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
10-210 |
5.23e-49 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 162.57 E-value: 5.23e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 10 MISLNNIYKSYGsgEGKVdALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLaai 89
Cdd:COG1125 1 MIEFENVTKRYP--DGTV-AVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVEL--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 90 RgRHLGFIFQFFNLIPVLSVFDNVFFPLVLNGhVGKKEARERALHFIESVGL--AGFTERKPGQLSGGQQQRVAIARALA 167
Cdd:COG1125 75 R-RRIGYVIQQIGLFPHMTVAENIATVPRLLG-WDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 556463668 168 HDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTH 210
Cdd:COG1125 153 ADPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTH 195
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
11-229 |
2.62e-48 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 156.79 E-value: 2.62e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSGEgkvdALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVmflkKLLNHLPEEQLAAIR 90
Cdd:cd03230 1 IEVRNLSKRYGKKT----ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEI----KVLGKDIKKEPEEVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 91 gRHLGFIFQFFNLIPVLSVFDNVffplvlnghvgkkeareralhfiesvglagfterkpgQLSGGQQQRVAIARALAHDP 170
Cdd:cd03230 73 -RRIGYLPEEPSLYENLTVRENL-------------------------------------KLSGGMKQRLALAQALLHDP 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 171 QVVIADEPTGNLDLVTGEAILDLLLKINQEtRTTFIISTHS-SQLKERARRVVEIKDGVL 229
Cdd:cd03230 115 ELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHIlEEAERLCDRVAILNNGRI 173
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
11-227 |
8.37e-48 |
|
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: 157.50 E-value: 8.37e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSgegkVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPeeqlaaIR 90
Cdd:cd03296 3 IEVRNVSKRFGD----FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP------VQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 91 GRHLGFIFQFFNLIPVLSVFDNVFFPLVL---NGHVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALA 167
Cdd:cd03296 73 ERNVGFVFQHYALFRHMTVFDNVAFGLRVkprSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556463668 168 HDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTH-SSQLKERARRVVEIKDG 227
Cdd:cd03296 153 VEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHdQEEALEVADRVVVMNKG 213
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
11-230 |
8.55e-48 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 157.87 E-value: 8.55e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSgegkVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKK---LLNHLPEEQLA 87
Cdd:COG4161 3 IQLKNINCFYGS----HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdFSQKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 88 AIRgRHLGFIFQFFNLIPVLSVFDNVF-FPLVLNGhVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARAL 166
Cdd:COG4161 79 LLR-QKVGMVFQQYNLWPHLTVMENLIeAPCKVLG-LSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556463668 167 AHDPQVVIADEPTGNLDLVTGEAILDLLLKInQETRTTFIISTHSSQL-KERARRVVEIKDGVLV 230
Cdd:COG4161 157 MMEPQVLLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVEFaRKVASQVVYMEKGRII 220
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
11-230 |
1.29e-47 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 157.10 E-value: 1.29e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSGEgkvdALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKK---LLNHLPEEQLA 87
Cdd:PRK11124 3 IQLNGINCFYGAHQ----ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfdFSKTPSDKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 88 AIRgRHLGFIFQFFNLIPVLSVFDNVF-FPLVLNGhVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARAL 166
Cdd:PRK11124 79 ELR-RNVGMVFQQYNLWPHLTVQQNLIeAPCRVLG-LSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556463668 167 AHDPQVVIADEPTGNLDLVTGEAILDLLLKInQETRTTFIISTHSSQL-KERARRVVEIKDGVLV 230
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVaRKTASRVVYMENGHIV 220
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
9-210 |
2.07e-47 |
|
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: 159.82 E-value: 2.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSYGSgegkVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQlaa 88
Cdd:TIGR03265 3 PYLSIDNIRKRFGA----FTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQK--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 89 irgRHLGFIFQFFNLIPVLSVFDNVFFPLVlNGHVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAH 168
Cdd:TIGR03265 76 ---RDYGIVFQSYALFPNLTVADNIAYGLK-NRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALAT 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 556463668 169 DPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTH 210
Cdd:TIGR03265 152 SPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTH 193
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
9-210 |
4.99e-47 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 156.11 E-value: 4.99e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSYGSGEgkvdALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMF------LKKLLNHLP 82
Cdd:COG4598 7 PALEVRDLHKSFGDLE----VLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVggeeirLKPDRDGEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 83 E----EQLAAIRGRhLGFIFQFFNLIPVLSVFDNVFF-PL-VLNghVGKKEARERALHFIESVGLAGFTERKPGQLSGGQ 156
Cdd:COG4598 83 VpadrRQLQRIRTR-LGMVFQSFNLWSHMTVLENVIEaPVhVLG--RPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 556463668 157 QQRVAIARALAHDPQVVIADEPTGNLD--LVtGEaILDLLLKINQETRtTFIISTH 210
Cdd:COG4598 160 QQRAAIARALAMEPEVMLFDEPTSALDpeLV-GE-VLKVMRDLAEEGR-TMLVVTH 212
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
10-210 |
6.43e-47 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 156.01 E-value: 6.43e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 10 MISLNNIYKSYGsgeGKvDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMflkklLNHLPEEQLAAI 89
Cdd:PRK11248 1 MLQISHLYADYG---GK-PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSIT-----LDGKPVEGPGAE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 90 RGrhlgFIFQFFNLIPVLSVFDNVFFPLVLNGhVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHD 169
Cdd:PRK11248 72 RG----VVFQNEGLLPWRNVQDNVAFGLQLAG-VEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAAN 146
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 556463668 170 PQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTH 210
Cdd:PRK11248 147 PQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITH 187
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
12-232 |
8.75e-47 |
|
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: 154.23 E-value: 8.75e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 12 SLNNIYKSYGSGEgkvdALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKllnhlpeeQLAAIRG 91
Cdd:cd03235 1 EVEDLTVSYGGHP----VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK--------PLEKERK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 92 RhLGFIFQFFNL---IPVlSVFDNVFfpLVLNGHVG-----KKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIA 163
Cdd:cd03235 69 R-IGYVPQRRSIdrdFPI-SVRDVVL--MGLYGHKGlfrrlSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 164 RALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRtTFIISTHS-SQLKERARRVVEIKDGVLVHD 232
Cdd:cd03235 145 RALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGM-TILVVTHDlGLVLEYFDRVLLLNRTVVASG 213
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
11-229 |
1.10e-46 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 153.82 E-value: 1.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIykSYGSGEGKVdaLKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLaaiR 90
Cdd:COG4619 1 LELEGL--SFRVGGKPI--LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEW---R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 91 gRHLGFIFQffnlIPVL---SVFDNVFFPLVLNGhvgKKEARERALHFIESVGL-AGFTERKPGQLSGGQQQRVAIARAL 166
Cdd:COG4619 74 -RQVAYVPQ----EPALwggTVRDNLPFPFQLRE---RKFDRERALELLERLGLpPDILDKPVERLSGGERQRLALIRAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556463668 167 AHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQLKER-ARRVVEIKDGVL 229
Cdd:COG4619 146 LLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
10-235 |
1.32e-46 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 154.14 E-value: 1.32e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 10 MISLNNIYKSYGsgegkvDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQlaai 89
Cdd:COG3840 1 MLRLDDLTYRYG------DFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 90 rgRHLGFIFQFFNLIPVLSVFDNVFF---P-LVLNghvgkKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARA 165
Cdd:COG3840 71 --RPVSMLFQENNLFPHLTVAQNIGLglrPgLKLT-----AEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARC 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556463668 166 LAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQLKER-ARRVVEIKDGVLVHDSQT 235
Cdd:COG3840 144 LVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPT 214
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
30-179 |
1.38e-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: 1.38e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 30 LKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLaairGRHLGFIFQFFNLIPVLSV 109
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSL----RKEIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556463668 110 FDNVFFPLVLnGHVGKKEARERALHFIESVGLAGFTERK----PGQLSGGQQQRVAIARALAHDPQVVIADEPT 179
Cdd:pfam00005 77 RENLRLGLLL-KGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
9-230 |
9.07e-46 |
|
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: 159.46 E-value: 9.07e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSYGSGEGKVDALKNINLEIEKGEFLALCGPSGSGKS-TLLNIL----SGIDKPTvGTVMFLKKLLNHLPE 83
Cdd:COG4172 5 PLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILrllpDPAAHPS-GSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 84 EQLAAIRGRHLGFIFQ--FFNLIPVLSVFDNVFFPLVLNGHVGKKEARERALHFIESVGLAGfTERK----PGQLSGGQQ 157
Cdd:COG4172 84 RELRRIRGNRIAMIFQepMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPD-PERRldayPHQLSGGQR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556463668 158 QRVAIARALAHDPQVVIADEPTGNLDlVTGEA-ILDLLLKINQETRTTFIISTHSSQLKER-ARRVVEIKDGVLV 230
Cdd:COG4172 163 QRVMIAMALANEPDLLIADEPTTALD-VTVQAqILDLLKDLQRELGMALLLITHDLGVVRRfADRVAVMRQGEIV 236
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
9-207 |
1.91e-45 |
|
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: 152.12 E-value: 1.91e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSYGSgegkVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAA 88
Cdd:COG0411 3 PLLEVRGLTKRFGG----LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 89 iRGrhLGFIFQFFNLIPVLSVFDNV-----------FFPLVLNGHVGKK---EARERALHFIESVGLAGFTERKPGQLSG 154
Cdd:COG0411 79 -LG--IARTFQNPRLFPELTVLENVlvaaharlgrgLLAALLRLPRARReerEARERAEELLERVGLADRADEPAGNLSY 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 556463668 155 GQQQRVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFII 207
Cdd:COG0411 156 GQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILL 208
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
11-227 |
2.01e-45 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 149.07 E-value: 2.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSGEGKVdaLKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAair 90
Cdd:cd03228 1 IEFKNVSFSYPGRPKPV--LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLR--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 91 gRHLGFIFQFfnliPVL---SVFDNVffplvlnghvgkkeareralhfiesvglagfterkpgqLSGGQQQRVAIARALA 167
Cdd:cd03228 76 -KNIAYVPQD----PFLfsgTIRENI--------------------------------------LSGGQRQRIAIARALL 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 168 HDPQVVIADEPTGNLDLVTGEAILDLLLKINQEtRTTFIIsTHSSQLKERARRVVEIKDG 227
Cdd:cd03228 113 RDPPILILDEATSALDPETEALILEALRALAKG-KTVIVI-AHRLSTIRDADRIIVLDDG 170
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
11-207 |
9.48e-45 |
|
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: 9.48e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSgegkVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAAiR 90
Cdd:cd03219 1 LEVRGLTKRFGG----LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIAR-L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 91 GrhLGFIFQFFNLIPVLSVFDNV---------FFPLVLNGHVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVA 161
Cdd:cd03219 76 G--IGRTFQIPRLFPELTVLENVmvaaqartgSGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 556463668 162 IARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFII 207
Cdd:cd03219 154 IARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLV 199
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
11-231 |
2.40e-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: 148.64 E-value: 2.40e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSGEgkvdaLKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQlaair 90
Cdd:cd03299 1 LKVENLSKDWKEFK-----LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 91 gRHLGFIFQFFNLIPVLSVFDNVFFPLVLNgHVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHDP 170
Cdd:cd03299 71 -RDISYVPQNYALFPHMTVYKNIAYGLKKR-KVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556463668 171 QVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHS-SQLKERARRVVEIKDGVLVH 231
Cdd:cd03299 149 KILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDfEEAWALADKVAIMLNGKLIQ 210
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
11-229 |
2.78e-44 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 151.77 E-value: 2.78e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGsgegKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLpeeqlaAIR 90
Cdd:PRK10851 3 IEIANIKKSFG----RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL------HAR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 91 GRHLGFIFQFFNLIPVLSVFDNVFFPL-VLNGH--VGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALA 167
Cdd:PRK10851 73 DRKVGFVFQHYALFRHMTVFDNIAFGLtVLPRRerPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556463668 168 HDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQ-LKERARRVVEIKDGVL 229
Cdd:PRK10851 153 VEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEeAMEVADRVVVMSQGNI 215
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
10-232 |
2.97e-44 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 148.70 E-value: 2.97e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 10 MISLNNIYKSYGsgegKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHlPEEQLAAI 89
Cdd:PRK09493 1 MIEFKNVSKHFG----PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVND-PKVDERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 90 RgRHLGFIFQFFNLIPVLSVFDNVFF-PLVLNGhVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAH 168
Cdd:PRK09493 76 R-QEAGMVFQQFYLFPHLTALENVMFgPLRVRG-ASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556463668 169 DPQVVIADEPTGNLDLVTGEAILDLLLKINQETrTTFIISTHSSQLKER-ARRVVEIKDGVLVHD 232
Cdd:PRK09493 154 KPKLMLFDEPTSALDPELRHEVLKVMQDLAEEG-MTMVIVTHEIGFAEKvASRLIFIDKGRIAED 217
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
30-210 |
6.59e-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: 147.23 E-value: 6.59e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 30 LKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAairgrhlgfIFQFFNLIPVLSV 109
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV---------VFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 110 FDNVFFPL-VLNGHVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHDPQVVIADEPTGNLDLVTGE 188
Cdd:TIGR01184 72 RENIALAVdRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180
....*....|....*....|..
gi 556463668 189 AILDLLLKINQETRTTFIISTH 210
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTH 173
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
11-210 |
7.93e-44 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 150.95 E-value: 7.93e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSgegkVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQlaair 90
Cdd:PRK11000 4 VTLRNVTKAYGD----VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 91 gRHLGFIFQFFNLIPVLSVFDNVFFPLVLNGhVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHDP 170
Cdd:PRK11000 75 -RGVGMVFQSYALYPHLSVAENMSFGLKLAG-AKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 556463668 171 QVVIADEPTGNLDlvtgeAILDLLLKI-----NQETRTTFIISTH 210
Cdd:PRK11000 153 SVFLLDEPLSNLD-----AALRVQMRIeisrlHKRLGRTMIYVTH 192
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
11-232 |
1.24e-43 |
|
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: 146.18 E-value: 1.24e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSGegkvDALKNINLEIEKGeFLALCGPSGSGKSTLLNILSGIDKPTVGTVmflkKLLNHLPEEQLAAIR 90
Cdd:cd03264 1 LQLENLTKRYGKK----RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTI----RIDGQDVLKQPQKLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 91 gRHLGFIFQFFNLIPVLSVFDNVFFPLVLNGhVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHDP 170
Cdd:cd03264 72 -RRIGYLPQEFGVYPNFTVREFLDYIAWLKG-IPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556463668 171 QVVIADEPTGNLDLVTGEAILDLLLKINQEtrTTFIISTH-SSQLKERARRVVEIKDGVLVHD 232
Cdd:cd03264 150 SILIVDEPTAGLDPEERIRFRNLLSELGED--RIVILSTHiVEDVESLCNQVAVLNKGKLVFE 210
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
9-210 |
1.68e-43 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 149.11 E-value: 1.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSY-------GSGEGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHL 81
Cdd:COG4608 6 PLLEVRDLKKHFpvrgglfGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 82 PEEQLAAIRgRHLGFIFQ--FFNLIPVLSVFDNVFFPLVLNGHVGKKEARERALHFIESVGL-AGFTERKPGQLSGGQQQ 158
Cdd:COG4608 86 SGRELRPLR-RRMQMVFQdpYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQ 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 556463668 159 RVAIARALAHDPQVVIADEPTGNLDlVTGEA-ILDLLLKINQETRTTFIISTH 210
Cdd:COG4608 165 RIGIARALALNPKLIVCDEPVSALD-VSIQAqVLNLLEDLQDELGLTYLFISH 216
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
8-230 |
2.86e-43 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 146.43 E-value: 2.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 8 LPMISLNNIYKSYgsgEGKVdALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLN---HLPEE 84
Cdd:PRK11264 1 MSAIEVKNLVKKF---HGQT-VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDtarSLSQQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 85 QlAAIRG--RHLGFIFQFFNLIPVLSVFDNVF-FPLVLNGHVgKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVA 161
Cdd:PRK11264 77 K-GLIRQlrQHVGFVFQNFNLFPHRTVLENIIeGPVIVKGEP-KEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556463668 162 IARALAHDPQVVIADEPTGNLD--LVtGEaILDLLLKINQETRTTFIISTHSSQLKERARRVVEIKDGVLV 230
Cdd:PRK11264 155 IARALAMRPEVILFDEPTSALDpeLV-GE-VLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
11-232 |
3.33e-43 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 146.42 E-value: 3.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGsgEGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKklLNHLPEEQLAAIR 90
Cdd:TIGR04520 1 IEVENVSFSYP--ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENLWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 91 gRHLGFIF-----QFFNLIpvlsVFDNVFFPLVLNGhVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARA 165
Cdd:TIGR04520 77 -KKVGMVFqnpdnQFVGAT----VEDDVAFGLENLG-VPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556463668 166 LAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHssQLKE--RARRVVEIKDGVLVHD 232
Cdd:TIGR04520 151 LAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITH--DMEEavLADRVIVMNKGKIVAE 217
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
9-230 |
6.21e-43 |
|
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: 152.22 E-value: 6.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIykSYGSGEGKVdALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAa 88
Cdd:COG4988 335 PSIELEDV--SFSYPGGRP-ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWR- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 89 irgRHLGFIFQFfnliPVL---SVFDNVFFplvlnghvGKKEARERALH-FIESVGLAGFTERKPG-----------QLS 153
Cdd:COG4988 411 ---RQIAWVPQN----PYLfagTIRENLRL--------GRPDASDEELEaALEAAGLDEFVAALPDgldtplgeggrGLS 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556463668 154 GGQQQRVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQEtRTTFIIsTHSSQLKERARRVVEIKDGVLV 230
Cdd:COG4988 476 GGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKG-RTVILI-THRLALLAQADRILVLDDGRIV 550
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
9-221 |
6.86e-43 |
|
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: 143.77 E-value: 6.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSYGsgegKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVmflkkLLNHLPEEQLAA 88
Cdd:COG4133 1 MMLEAENLSCRRG----ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEV-----LWNGEPIRDARE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 89 IRGRHLGFIFQFFNLIPVLSVFDNVFFPLVLNGHVGKKEARERALhfiESVGLAGFTERKPGQLSGGQQQRVAIARALAH 168
Cdd:COG4133 72 DYRRRLAYLGHADGLKPELTVRENLRFWAALYGLRADREAIDEAL---EAVGLAGLADLPVRQLSAGQKRRVALARLLLS 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 556463668 169 DPQVVIADEPTGNLDlVTGEAILDLLLKINQETRTTFIISTHSSQLKERARRV 221
Cdd:COG4133 149 PAPLWLLDEPFTALD-AAGVALLAELIAAHLARGGAVLLTTHQPLELAAARVL 200
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
9-230 |
1.21e-42 |
|
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: 151.46 E-value: 1.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSYGsgEGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAa 88
Cdd:COG4987 332 PSLELEDVSFRYP--GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLR- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 89 irgRHLGFIFQ---FFNLipvlSVFDNVffplvlngHVGKKEARERALHF-IESVGLAGFTERKPG-----------QLS 153
Cdd:COG4987 409 ---RRIAVVPQrphLFDT----TLRENL--------RLARPDATDEELWAaLERVGLGDWLAALPDgldtwlgeggrRLS 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556463668 154 GGQQQRVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQEtRTTFIIsTHSSQLKERARRVVEIKDGVLV 230
Cdd:COG4987 474 GGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAG-RTVLLI-THRLAGLERMDRILVLEDGRIV 548
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
12-232 |
1.10e-41 |
|
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: 139.88 E-value: 1.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 12 SLNNIYKSYGsgegKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAairg 91
Cdd:cd03214 1 EVENLSVGYG----GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELA---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 92 RHLGFIFQFfnlipvlsvfdnvffplvlnghvgkkeareralhfIESVGLAGFTERKPGQLSGGQQQRVAIARALAHDPQ 171
Cdd:cd03214 73 RKIAYVPQA-----------------------------------LELLGLAHLADRPFNELSGGERQRVLLARALAQEPP 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556463668 172 VVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQLKER-ARRVVEIKDGVLVHD 232
Cdd:cd03214 118 ILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARyADRVILLKDGRIVAQ 179
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
11-232 |
1.49e-41 |
|
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: 149.98 E-value: 1.49e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIykSYGSGEGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPeeqLAAIR 90
Cdd:COG2274 474 IELENV--SFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID---PASLR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 91 gRHLGFIFQ---FFNlipvLSVFDNVffplvlngHVGKKEA-RERALHFIESVGLAGFTERKP-----------GQLSGG 155
Cdd:COG2274 549 -RQIGVVLQdvfLFS----GTIRENI--------TLGDPDAtDEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGG 615
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556463668 156 QQQRVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQEtRTTFIIsTHSSQLKERARRVVEIKDGVLVHD 232
Cdd:COG2274 616 QRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKG-RTVIII-AHRLSTIRLADRIIVLDKGRIVED 690
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
11-232 |
1.93e-41 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 140.32 E-value: 1.93e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSGEGKVDalkninLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQlaair 90
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFD------LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 91 gRHLGFIFQFFNLIPVLSVFDNVFFPLVLNGHVgKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHDP 170
Cdd:cd03298 70 -RPVSMLFQENNLFAHLTVEQNVGLGLSPGLKL-TAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556463668 171 QVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQLKER-ARRVVEIKDGVLVHD 232
Cdd:cd03298 148 PVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQ 210
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
30-233 |
1.02e-40 |
|
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: 138.58 E-value: 1.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 30 LKNINLEIE---KGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLN------HLPEEQlaairgRHLGFIFQF 100
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFdsrkkiNLPPQQ------RKIGLVFQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 101 FNLIPVLSVFDNVFFplVLNGHvGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHDPQVVIADEPTG 180
Cdd:cd03297 84 YALFPHLNVRENLAF--GLKRK-RNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 556463668 181 NLDLVTGEAILDLLLKINQETRTTFIISTHS-SQLKERARRVVEIKDGVLVHDS 233
Cdd:cd03297 161 ALDRALRLQLLPELKQIKKNLNIPVIFVTHDlSEAEYLADRIVVMEDGRLQYIG 214
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
8-232 |
1.30e-40 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 139.82 E-value: 1.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 8 LPMISLNNIYKSYGSG-----EGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLP 82
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 83 EEQLAAIRgRHLGFIFQ----FFNliPVLSVFDNVFFPLVLNGHVGKKEARERALHFIESVGLA-GFTERKPGQLSGGQQ 157
Cdd:PRK10419 81 RAQRKAFR-RDIQMVFQdsisAVN--PRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556463668 158 QRVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQLKER-ARRVVEIKDGVLVHD 232
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIVET 233
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
12-227 |
1.57e-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: 136.22 E-value: 1.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 12 SLNNIYKSYGSGEgkvdALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAairg 91
Cdd:cd00267 1 EIENLSFRYGGRT----ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELR---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 92 RHLGFIFQffnlipvlsvfdnvffplvlnghvgkkeareralhfiesvglagfterkpgqLSGGQQQRVAIARALAHDPQ 171
Cdd:cd00267 73 RRIGYVPQ----------------------------------------------------LSGGQRQRVALARALLLNPD 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 556463668 172 VVIADEPTGNLDLVTGEAILDLLLKINQETRtTFIISTHSSQLKERAR-RVVEIKDG 227
Cdd:cd00267 101 LLLLDEPTSGLDPASRERLLELLRELAEEGR-TVIIVTHDPELAELAAdRVIVLKDG 156
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
10-230 |
1.64e-40 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 138.47 E-value: 1.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 10 MISLNNIYKSYGSGEgkvDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAAI 89
Cdd:PRK10908 1 MIRFEHVSKAYLGGR---QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 90 RgRHLGFIFQFFNLIPVLSVFDNVFFPLVLNGHVGKkEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHD 169
Cdd:PRK10908 78 R-RQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGD-DIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556463668 170 PQVVIADEPTGNLDLVTGEAILDLLLKINQeTRTTFIISTHSSQL-KERARRVVEIKDGVLV 230
Cdd:PRK10908 156 PAVLLADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLiSRRSYRMLTLSDGHLH 216
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
11-231 |
1.69e-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: 138.02 E-value: 1.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSGEgkVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNhlpeEQLAAIR 90
Cdd:cd03263 1 LQIRNLTKTYKKGT--KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR----TDRKAAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 91 gRHLGFIFQFFNLIPVLSVFDNVFFPLVLNGHvGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHDP 170
Cdd:cd03263 75 -QSLGYCPQFDALFDELTVREHLRFYARLKGL-PKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556463668 171 QVVIADEPTGNLDLVTGEAILDLLLKINQEtrTTFIISTHSSQLKER-ARRVVEIKDGVLVH 231
Cdd:cd03263 153 SVLLLDEPTSGLDPASRRAIWDLILEVRKG--RSIILTTHSMDEAEAlCDRIAIMSDGKLRC 212
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
11-231 |
2.33e-40 |
|
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: 137.41 E-value: 2.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSgegkVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKK--------LLNHLP 82
Cdd:cd03269 1 LEVENVTKRFGR----VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKpldiaarnRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 83 EEqlaaiRGrhlgfifqffnLIPVLSVFDNVFFPLVLNGhVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAI 162
Cdd:cd03269 77 EE-----RG-----------LYPKMKVIDQLVYLAQLKG-LKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQF 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 163 ARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKInQETRTTFIISTHSSQLKER-ARRVVEIKDGVLVH 231
Cdd:cd03269 140 IAAVIHDPELLILDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEElCDRVLLLNKGRAVL 208
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
11-235 |
3.09e-40 |
|
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: 138.20 E-value: 3.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSGEgkvdALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDK-----PTVGTVMFLKKLLNHlPEEQ 85
Cdd:TIGR00972 2 IEIENLNLFYGEKE----ALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDlvpgvRIEGKVLFDGQDIYD-KKID 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 86 LAAIRgRHLGFIFQFFNLIPvLSVFDNVFFPLVLNGHVGKKEARERALHFIESVGLagFTERK------PGQLSGGQQQR 159
Cdd:TIGR00972 77 VVELR-RRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIKDKKELDEIVEESLKKAAL--WDEVKdrlhdsALGLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556463668 160 VAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLlkinQETRT--TFIISTHSSQLKER-ARRVVEIKDGVLVHDSQT 235
Cdd:TIGR00972 153 LCIARALAVEPEVLLLDEPTSALDPIATGKIEELI----QELKKkyTIVIVTHNMQQAARiSDRTAFFYDGELVEYGPT 227
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
11-235 |
4.40e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 139.45 E-value: 4.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSGEG-KVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFL--KKLLNHLPEE--- 84
Cdd:PRK13651 3 IKVKNIVKIFNKKLPtELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIfkDEKNKKKTKEkek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 85 ----------------QLAAIRgRHLGFIFQF--FNLIPVLSVFDNVFFPLVLNghVGKKEARERALHFIESVGL-AGFT 145
Cdd:PRK13651 83 vleklviqktrfkkikKIKEIR-RRVGVVFQFaeYQLFEQTIEKDIIFGPVSMG--VSKEEAKKRAAKYIELVGLdESYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 146 ERKPGQLSGGQQQRVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRtTFIISTHS-SQLKERARRVVEI 224
Cdd:PRK13651 160 QRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDlDNVLEWTKRTIFF 238
|
250
....*....|.
gi 556463668 225 KDGVLVHDSQT 235
Cdd:PRK13651 239 KDGKIIKDGDT 249
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
11-227 |
1.69e-39 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 136.73 E-value: 1.69e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSGEgkvdALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEqlaaIR 90
Cdd:PRK11247 13 LLLNAVSKRYGERT----VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARED----TR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 91 grhlgFIFQFFNLIPVLSVFDNVffPLVLNGHvgkkeARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHDP 170
Cdd:PRK11247 85 -----LMFQDARLLPWKKVIDNV--GLGLKGQ-----WRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 556463668 171 QVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHS-SQLKERARRVVEIKDG 227
Cdd:PRK11247 153 GLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDvSEAVAMADRVLLIEEG 210
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
29-232 |
4.99e-39 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 135.91 E-value: 4.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 29 ALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGI---DKPTVGTVMFLKKLLNHlpEEQLAA-IRGR--HLGFIFQFFN 102
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQR--EGRLARdIRKSraNTGYIFQQFN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 103 LIPVLSVFDNVffplvLNGHVG------------KKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHDP 170
Cdd:PRK09984 97 LVNRLSVLENV-----LIGALGstpfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556463668 171 QVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQLKER-ARRVVEIKDGVLVHD 232
Cdd:PRK09984 172 KVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRyCERIVALRQGHVFYD 234
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
10-230 |
6.48e-39 |
|
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: 135.70 E-value: 6.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 10 MISLNNIYKSYGSG-----EGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEE 84
Cdd:TIGR02769 2 LLEVRDVTHTYRTGglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 85 QLAAIRgRHLGFIFQ----FFNliPVLSVFDNVFFPLVLNGHVGKKEARERALHFIESVGL-AGFTERKPGQLSGGQQQR 159
Cdd:TIGR02769 82 QRRAFR-RDVQLVFQdspsAVN--PRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556463668 160 VAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQLKER-ARRVVEIKDGVLV 230
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIV 230
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
25-221 |
7.89e-39 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 135.16 E-value: 7.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 25 GKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSG----IDKPTV-GTVMFLKKLLNHlPEEQLAAIRgRHLGFIFQ 99
Cdd:COG1117 22 GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRmndlIPGARVeGEILLDGEDIYD-PDVDVVELR-RRVGMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 100 FFNLIPvLSVFDNVFFPLVLNGHVGKKEARERALHFIESVGLagFTE-----RKPGQ-LSGGQQQRVAIARALAHDPQVV 173
Cdd:COG1117 100 KPNPFP-KSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAAL--WDEvkdrlKKSALgLSGGQQQRLCIARALAVEPEVL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 556463668 174 IADEPTGNLDLVTGEAILDLLLKINQEtrTTFIISTHSSQlkeRARRV 221
Cdd:COG1117 177 LMDEPTSALDPISTAKIEELILELKKD--YTIVIVTHNMQ---QAARV 219
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
45-232 |
1.01e-38 |
|
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: 136.47 E-value: 1.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 45 LCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQlaairgRHLGFIFQFFNLIPVLSVFDNVFFPLVLNGhVG 124
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHL------RHINMVFQSYALFPHMTVEENVAFGLKMRK-VP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 125 KKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTT 204
Cdd:TIGR01187 74 RAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGIT 153
|
170 180
....*....|....*....|....*....
gi 556463668 205 FIISTH-SSQLKERARRVVEIKDGVLVHD 232
Cdd:TIGR01187 154 FVFVTHdQEEAMTMSDRIAIMRKGKIAQI 182
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
30-183 |
1.89e-38 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 132.61 E-value: 1.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 30 LKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTV---GTVMFLKKLLNHLPEEQlaairgRHLGFIFQFFNLIPV 106
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFsasGEVLLNGRRLTALPAEQ------RRIGILFQDDLLFPH 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556463668 107 LSVFDNVFFPLVlnGHVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHDPQVVIADEPTGNLD 183
Cdd:COG4136 91 LSVGENLAFALP--PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
9-230 |
2.41e-38 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 139.00 E-value: 2.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSYGSgegkVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVmflkkLLNHLPEEQLAA 88
Cdd:COG1129 3 PLLEMRGISKSFGG----VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEI-----LLDGEPVRFRSP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 89 IRGRHLG--FIFQFFNLIPVLSVFDNVFF--PLVLNGHVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIAR 164
Cdd:COG1129 74 RDAQAAGiaIIHQELNLVPNLSVAENIFLgrEPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556463668 165 ALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQLKERARRVVEIKDGVLV 230
Cdd:COG1129 154 ALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLV 219
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
13-183 |
3.34e-38 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 136.00 E-value: 3.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 13 LNNIYKSYGsgegKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHlpeeqlAAIRGR 92
Cdd:PRK11432 9 LKNITKRFG----SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH------RSIQQR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 93 HLGFIFQFFNLIPVLSVFDNVFFPLVLNGhVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHDPQV 172
Cdd:PRK11432 79 DICMVFQSYALFPHMSLGENVGYGLKMLG-VPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKV 157
|
170
....*....|.
gi 556463668 173 VIADEPTGNLD 183
Cdd:PRK11432 158 LLFDEPLSNLD 168
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
10-183 |
1.16e-37 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 134.59 E-value: 1.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 10 MISLNNIYKSYgsgEGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHL-PEEqlaa 88
Cdd:PRK11650 3 GLKLQAVRKSY---DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELePAD---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 89 irgRHLGFIFQFFNLIPVLSVFDNVFFPLVLNGhVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAH 168
Cdd:PRK11650 76 ---RDIAMVFQNYALYPHMSVRENMAYGLKIRG-MPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVR 151
|
170
....*....|....*
gi 556463668 169 DPQVVIADEPTGNLD 183
Cdd:PRK11650 152 EPAVFLFDEPLSNLD 166
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
9-210 |
2.06e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 131.65 E-value: 2.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSYGSGEGkvDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNhlpEEQLAA 88
Cdd:PRK13632 6 VMIKVENVSFSYPNSEN--NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIS---KENLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 89 IRGrHLGFIFQ-----FFNLipvlSVFDNVFFPLVlNGHVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIA 163
Cdd:PRK13632 81 IRK-KIGIIFQnpdnqFIGA----TVEDDIAFGLE-NKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 556463668 164 RALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTH 210
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITH 201
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
9-183 |
6.15e-37 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 133.04 E-value: 6.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSYgSGEGKVDalkNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQlaa 88
Cdd:PRK11607 18 PLLEIRNLTKSF-DGQHAVD---DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 89 irgRHLGFIFQFFNLIPVLSVFDNVFFPLVLNgHVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAH 168
Cdd:PRK11607 91 ---RPINMMFQSYALFPHMTVEQNIAFGLKQD-KLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAK 166
|
170
....*....|....*
gi 556463668 169 DPQVVIADEPTGNLD 183
Cdd:PRK11607 167 RPKLLLLDEPMGALD 181
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
10-232 |
9.50e-37 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 130.61 E-value: 9.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 10 MISLNNIYKSYGSgegkVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNH--------L 81
Cdd:COG4152 1 MLELKGLTKRFGD----KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPedrrrigyL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 82 PEEqlaaiRGrhlgfifqffnLIPVLSVFDNVFFPLVLNGhVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVA 161
Cdd:COG4152 77 PEE-----RG-----------LYPKMKVGEQLVYLARLKG-LSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556463668 162 IARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETrTTFIISTHSSQLKER-ARRVVEIKDGVLVHD 232
Cdd:COG4152 140 LIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKG-TTVIFSSHQMELVEElCDRIVIINKGRKVLS 210
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
22-230 |
2.61e-36 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 130.47 E-value: 2.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 22 SGEGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAAIRgRHLGFIFQ-- 99
Cdd:PRK11308 23 KPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLR-QKIQIVFQnp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 100 FFNLIPVLSVFDNVFFPLVLNGHVGKKEARERALHFIESVGL-AGFTERKPGQLSGGQQQRVAIARALAHDPQVVIADEP 178
Cdd:PRK11308 102 YGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEP 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 556463668 179 TGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQlkerarrVVE-IKDGVLV 230
Cdd:PRK11308 182 VSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLS-------VVEhIADEVMV 227
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
10-232 |
3.67e-36 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 129.82 E-value: 3.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 10 MISLNNIYKSY----------GSGEG-------KVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVm 72
Cdd:COG4586 1 IIEVENLSKTYrvyekepglkGALKGlfrreyrEVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 73 flkKLLNHLPEEQLAAIRgRHLGFIF-QFFNLIPVLSVFDNvffpLVLNGH---VGKKEARERALHFIESVGLAGFTERK 148
Cdd:COG4586 80 ---RVLGYVPFKRRKEFA-RRIGVVFgQRSQLWWDLPAIDS----FRLLKAiyrIPDAEYKKRLDELVELLDLGELLDTP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 149 PGQLSGGQQQRVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQLKER-ARRVVEIKDG 227
Cdd:COG4586 152 VRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEAlCDRVIVIDHG 231
|
....*
gi 556463668 228 VLVHD 232
Cdd:COG4586 232 RIIYD 236
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
28-211 |
3.93e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 128.98 E-value: 3.93e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 28 DALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLL-NHLPEEQLAAIRgRHLGFIFQFfnliPV 106
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItAGKKNKKLKPLR-KKVGIVFQF----PE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 107 LSVF------DNVFFPLvlNGHVGKKEARERALHFIESVGL-AGFTERKPGQLSGGQQQRVAIARALAHDPQVVIADEPT 179
Cdd:PRK13634 96 HQLFeetvekDICFGPM--NFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPT 173
|
170 180 190
....*....|....*....|....*....|..
gi 556463668 180 GNLDLVTGEAILDLLLKINQETRTTFIISTHS 211
Cdd:PRK13634 174 AGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHS 205
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
10-232 |
7.83e-36 |
|
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: 126.33 E-value: 7.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 10 MISLNNIYKSYGSGEGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLaai 89
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEAR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 90 rgRHLGFIFQFFNLIPVLSVFDNVFFPLVLNGhVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHD 169
Cdd:cd03266 78 --RRLGFVSDSTGLYDRLTARENLEYFAGLYG-LKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556463668 170 PQVVIADEPTGNLDLVTGEAILDLLLKInQETRTTFIISTHSSQLKER-ARRVVEIKDGVLVHD 232
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYE 217
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
11-230 |
1.11e-35 |
|
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: 125.41 E-value: 1.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSGEgkvdALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQlaair 90
Cdd:cd03268 1 LKTNDLTKTYGKKR----VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 91 gRHLGFIFQFFNLIPVLSVFDNvfFPLVLNGHVGKKEARERALhfiESVGLAGFTERKPGQLSGGQQQRVAIARALAHDP 170
Cdd:cd03268 72 -RRIGALIEAPGFYPNLTAREN--LRLLARLLGIRKKRIDEVL---DVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNP 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556463668 171 QVVIADEPTGNLDLVTGEAILDLLLKINQETRtTFIISTHS-SQLKERARRVVEIKDGVLV 230
Cdd:cd03268 146 DLLILDEPTNGLDPDGIKELRELILSLRDQGI-TVLISSHLlSEIQKVADRIGIINKGKLI 205
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
9-232 |
3.38e-35 |
|
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: 125.20 E-value: 3.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSYGsgeGKVdALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMflkKLLNH-LPEEQLA 87
Cdd:COG1119 2 PLLELRNVTVRRG---GKT-ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDV---RLFGErRGGEDVW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 88 AIRgRHLGFI-FQFFNLIPV-LSVFDNV---FFP-LVLNGHVGKkEARERALHFIESVGLAGFTERKPGQLSGGQQQRVA 161
Cdd:COG1119 75 ELR-KRIGLVsPALQLRFPRdETVLDVVlsgFFDsIGLYREPTD-EQRERARELLELLGLAHLADRPFGTLSQGEQRRVL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556463668 162 IARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHssQLKERAR---RVVEIKDGVLVHD 232
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTH--HVEEIPPgitHVLLLKDGRVVAA 224
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
11-230 |
5.29e-35 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 130.67 E-value: 5.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSGEgkvDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVmflkkLLNHLP--EEQLAA 88
Cdd:COG1132 340 IEFENVSFSYPGDR---PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRI-----LIDGVDirDLTLES 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 89 IRgRHLGFIFQ---FFNlipvLSVFDNVFFplvlnghvGKKEA-RERALHFIESVGLAGFTERKPG-----------QLS 153
Cdd:COG1132 412 LR-RQIGVVPQdtfLFS----GTIRENIRY--------GRPDAtDEEVEEAAKAAQAHEFIEALPDgydtvvgergvNLS 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556463668 154 GGQQQRVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQEtRTTFIIStHS-SQLKeRARRVVEIKDGVLV 230
Cdd:COG1132 479 GGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKG-RTTIVIA-HRlSTIR-NADRILVLDDGRIV 553
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
22-232 |
6.63e-35 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 123.70 E-value: 6.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 22 SGEGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAAiRGrhLGFIFQFF 101
Cdd:cd03224 8 AGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERAR-AG--IGYVPEGR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 102 NLIPVLSVFDNvffpLVLNGHVGKKEARERALHFIESV--GLAGFTERKPGQLSGGQQQRVAIARALAHDPQVVIADEPT 179
Cdd:cd03224 85 RIFPELTVEEN----LLLGAYARRRAKRKARLERVYELfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 556463668 180 GNLDLVTGEAILDLLLKINQETRTTFIISTHSSQLKERARRVVEIKDGVLVHD 232
Cdd:cd03224 161 EGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLE 213
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
32-227 |
7.04e-35 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 127.14 E-value: 7.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 32 NINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNH------LPEEQlaairgRHLGFIFQFFNLIP 105
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDsargifLPPHR------RRIGYVFQEARLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 106 VLSVFDNVFFplvlnghvGKK--EARERALHF---IESVGLAGFTERKPGQLSGGQQQRVAIARALAHDPQVVIADEPTG 180
Cdd:COG4148 91 HLSVRGNLLY--------GRKraPRAERRISFdevVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 556463668 181 NLDLVTGEAILDLLLKINQETRTTFIISTHSsqLKERAR---RVVEIKDG 227
Cdd:COG4148 163 ALDLARKAEILPYLERLRDELDIPILYVSHS--LDEVARladHVVLLEQG 210
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
10-230 |
7.22e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 125.19 E-value: 7.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 10 MISLNNIYKSYGSGegkVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHlPEEQLAAI 89
Cdd:PRK13639 1 ILETRDLKYSYPDG---TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKY-DKKSLLEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 90 RgRHLGFIFQffnlipvlSVFDNVFFPLV--------LNGHVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVA 161
Cdd:PRK13639 77 R-KTVGIVFQ--------NPDDQLFAPTVeedvafgpLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 162 IARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETrTTFIISTHSSQLKER-ARRVVEIKDGVLV 230
Cdd:PRK13639 148 IAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEG-ITIIISTHDVDLVPVyADKVYVMSDGKII 216
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
9-196 |
8.56e-35 |
|
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: 123.70 E-value: 8.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKS---YGSGEGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKL----LNHL 81
Cdd:COG4778 3 TLLEVENLSKTftlHLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdLAQA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 82 PEEQLAAIRGRHLGFIFQFFNLIPVLSVFDNVFFPLVLNGhVGKKEARERALHFIESVGLAgftER----KPGQLSGGQQ 157
Cdd:COG4778 83 SPREILALRRRTIGYVSQFLRVIPRVSALDVVAEPLLERG-VDREEARARARELLARLNLP---ERlwdlPPATFSGGEQ 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 556463668 158 QRVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLK 196
Cdd:COG4778 159 QRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEE 197
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
9-227 |
2.41e-34 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 123.97 E-value: 2.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSYGsgEGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNhlpEEQLAA 88
Cdd:PRK13635 4 EIIRVEHISFRYP--DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLS---EETVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 89 IRgRHLGFIFQ-----FFNLipvlSVFDNVFFPLVLNGhVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIA 163
Cdd:PRK13635 79 VR-RQVGMVFQnpdnqFVGA----TVQDDVAFGLENIG-VPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556463668 164 RALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQLKERARRVVEIKDG 227
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKG 216
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
10-184 |
3.14e-34 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 122.92 E-value: 3.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 10 MISLNNIykSYGSGEGKVdaLKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAAI 89
Cdd:COG4559 1 MLEAENL--SVRLGGRTL--LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 90 RG-----RHLGFIFqffnliPVLSVfdnvffplV----LNGHVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRV 160
Cdd:COG4559 77 RAvlpqhSSLAFPF------TVEEV--------ValgrAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRV 142
|
170 180 190
....*....|....*....|....*....|.
gi 556463668 161 AIARALA-------HDPQVVIADEPTGNLDL 184
Cdd:COG4559 143 QLARVLAqlwepvdGGPRWLFLDEPTSALDL 173
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
27-233 |
4.64e-34 |
|
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: 122.06 E-value: 4.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 27 VDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVmflkKLLNHLPEEQLAAIRGRhLGFIF-QFFNLIP 105
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV----RVAGLVPWKRRKKFLRR-IGVVFgQKTQLWW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 106 VLSVFDNvffpLVLNGH---VGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHDPQVVIADEPTGNL 182
Cdd:cd03267 109 DLPVIDS----FYLLAAiydLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 556463668 183 DLVTGEAILDLLLKINQETRTTFIISTHSSQLKER-ARRVVEIKDGVLVHDS 233
Cdd:cd03267 185 DVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEAlARRVLVIDKGRLLYDG 236
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
11-221 |
1.21e-33 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 121.61 E-value: 1.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSGEgkvdALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPE------- 83
Cdd:PRK10619 6 LNVIDLHKRYGEHE----VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDkdgqlkv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 84 ---EQLAAIRGRhLGFIFQFFNLIPVLSVFDNVFFPLVLNGHVGKKEARERALHFIESVGLAGFTERK-PGQLSGGQQQR 159
Cdd:PRK10619 82 adkNQLRLLRTR-LTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556463668 160 VAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIIsTHSsqlKERARRV 221
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVV-THE---MGFARHV 218
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
21-230 |
1.24e-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: 126.34 E-value: 1.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 21 GSGEGKVDALKNINLEIEKGEFLALCGPSGSGKSTL-LNILSGIdkPTVGTVMFLKKLLNHLPEEQLAAIRgRHLGFIFQ 99
Cdd:COG4172 293 RRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALLRLI--PSEGEIRFDGQDLDGLSRRALRPLR-RRMQVVFQ 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 100 --FFNLIPVLSVFDNVFFPLVLNG-HVGKKEARERALHFIESVGL-AGFTERKPGQLSGGQQQRVAIARALAHDPQVVIA 175
Cdd:COG4172 370 dpFGSLSPRMTVGQIIAEGLRVHGpGLSAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVL 449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 556463668 176 DEPTGNLDlVTGEA-ILDLLLKINQETRTTFIISTHS-SQLKERARRVVEIKDGVLV 230
Cdd:COG4172 450 DEPTSALD-VSVQAqILDLLRDLQREHGLAYLFISHDlAVVRALAHRVMVMKDGKVV 505
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
9-230 |
1.31e-33 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 121.48 E-value: 1.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSYGSGEG-----KVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHlpe 83
Cdd:COG4167 3 ALLEVRNLSKTFKYRTGlfrrqQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEY--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 84 eQLAAIRGRHLGFIFQFFN--LIPVLSVFDNVFFPLVLNGHVGKKEARERALHFIESVGL----AGFterKPGQLSGGQQ 157
Cdd:COG4167 80 -GDYKYRCKHIRMIFQDPNtsLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLlpehANF---YPHMLSSGQK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556463668 158 QRVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQLkerarrVVEIKDGVLV 230
Cdd:COG4167 156 QRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGI------VKHISDKVLV 222
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
11-230 |
1.32e-33 |
|
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: 120.55 E-value: 1.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSGEgkvdALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMflkkLLNHLPEEQLAAIR 90
Cdd:cd03265 1 IEVENLVKKYGDFE----AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRAT----VAGHDVVREPREVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 91 gRHLGFIFQFFNLIPVLSVFDNVFFPLVLNGhVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHDP 170
Cdd:cd03265 73 -RRIGIVFQDLSVDDELTGWENLYIHARLYG-VPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556463668 171 QVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQLKER-ARRVVEIKDGVLV 230
Cdd:cd03265 151 EVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRII 211
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-217 |
5.99e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 119.63 E-value: 5.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 25 GKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGI----DKPTV-GTVMFLKKLLNHLPEEQLAairgRHLGFIFQ 99
Cdd:PRK14247 14 GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielyPEARVsGEVYLDGQDIFKMDVIELR----RRVQMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 100 FFNLIPVLSVFDNVFFPLVLNGHV-GKKEARERALHFIESVGLagFTERK------PGQLSGGQQQRVAIARALAHDPQV 172
Cdd:PRK14247 90 IPNPIPNLSIFENVALGLKLNRLVkSKKELQERVRWALEKAQL--WDEVKdrldapAGKLSGGQQQRLCIARALAFQPEV 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 556463668 173 VIADEPTGNLDLVTGEAILDLLLKINQEtrTTFIISTHSSQLKER 217
Cdd:PRK14247 168 LLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAAR 210
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
9-182 |
7.50e-33 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 123.98 E-value: 7.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSYGSgegkVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNhlPEEQLAA 88
Cdd:COG3845 4 PALELRGITKRFGG----VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVR--IRSPRDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 89 IRgRHLGFIFQFFNLIPVLSVFDNVffplVL------NGHVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAI 162
Cdd:COG3845 78 IA-LGIGMVHQHFMLVPNLTVAENI----VLgleptkGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEI 152
|
170 180
....*....|....*....|
gi 556463668 163 ARALAHDPQVVIADEPTGNL 182
Cdd:COG3845 153 LKALYRGARILILDEPTAVL 172
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
29-230 |
4.61e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 117.91 E-value: 4.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 29 ALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNhlpEEQLAAIRGRhLGFIFQ-----FFNL 103
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN---AENEKWVRSK-VGLVFQdpddqVFSS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 104 ipvlSVFDNVFF-PLvlNGHVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHDPQVVIADEPTGNL 182
Cdd:PRK13647 96 ----TVWDDVAFgPV--NMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 556463668 183 DLVTGEAILDLLLKINQETrTTFIISTHSSQLK-ERARRVVEIKDGVLV 230
Cdd:PRK13647 170 DPRGQETLMEILDRLHNQG-KTVIVATHDVDLAaEWADQVIVLKEGRVL 217
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
7-222 |
5.42e-32 |
|
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: 122.01 E-value: 5.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 7 ELPMISLNNIYKSYgsgEGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVmflkkLLNHLPEEQL 86
Cdd:TIGR02857 318 PASSLEFSGVSVAY---PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSI-----AVNGVPLADA 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 87 -AAIRGRHLGFIFQffnlIPVL---SVFDNVFFplvlnghvGKKEARERAL-HFIESVGLAGFTERKPGQ---------- 151
Cdd:TIGR02857 390 dADSWRDQIAWVPQ----HPFLfagTIAENIRL--------ARPDASDAEIrEALERAGLDEFVAALPQGldtpigegga 457
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556463668 152 -LSGGQQQRVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQeTRTTFIIsTHSSQLKERARRVV 222
Cdd:TIGR02857 458 gLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLV-THRLALAALADRIV 527
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
9-194 |
5.88e-32 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 117.18 E-value: 5.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSYGsgeGKVdALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAA 88
Cdd:PRK13548 1 AMLEARNLSVRLG---GRT-LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 89 IRG-----RHLGFIFqffnlipvlSVFDNVFFPLVLNGHvGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIA 163
Cdd:PRK13548 77 RRAvlpqhSSLSFPF---------TVEEVVAMGRAPHGL-SRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLA 146
|
170 180 190
....*....|....*....|....*....|....*..
gi 556463668 164 RALA------HDPQVVIADEPTGNLDLVTGEAILDLL 194
Cdd:PRK13548 147 RVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLA 183
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
11-229 |
7.34e-32 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 114.62 E-value: 7.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSGEGKVdaLKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVmflkkLLNHLPEEQLA-AI 89
Cdd:cd03246 1 LEVENVSFRYPGAEPPV--LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRV-----RLDGADISQWDpNE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 90 RGRHLGFIFQFFNLIPVlSVFDNVffplvlnghvgkkeareralhfiesvglagfterkpgqLSGGQQQRVAIARALAHD 169
Cdd:cd03246 74 LGDHVGYLPQDDELFSG-SIAENI--------------------------------------LSGGQRQRLGLARALYGN 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 170 PQVVIADEPTGNLDlVTGEAILDLLLKINQETRTTFIISTHSSQLKERARRVVEIKDGVL 229
Cdd:cd03246 115 PRILVLDEPNSHLD-VEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
10-232 |
9.22e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 117.11 E-value: 9.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 10 MISLNNI---YKSYGSGEGKVdALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFlkKLLNHLPEEQL 86
Cdd:PRK13633 4 MIKCKNVsykYESNEESTEKL-ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYV--DGLDTSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 87 AAIRGRhLGFIFQF-FNLIPVLSVFDNVFF-PLVLNghVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIAR 164
Cdd:PRK13633 81 WDIRNK-AGMVFQNpDNQIVATIVEEDVAFgPENLG--IPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556463668 165 ALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQLKERARRVVEIKDGVLVHD 232
Cdd:PRK13633 158 ILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVME 225
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
9-230 |
9.88e-32 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 121.04 E-value: 9.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSYGSgegkVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLpEEQLAA 88
Cdd:PRK09700 4 PYISMAGIGKSFGP----VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKL-DHKLAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 89 IRGrhLGFIFQFFNLIPVLSVFDNVFFPLVLNGHV------GKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAI 162
Cdd:PRK09700 79 QLG--IGIIYQELSVIDELTVLENLYIGRHLTKKVcgvniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556463668 163 ARALAHDPQVVIADEPTGNLdlvTGEAILDLLLKINQ---ETRTTFIISTHSSQLKERARRVVEIKDGVLV 230
Cdd:PRK09700 157 AKTLMLDAKVIIMDEPTSSL---TNKEVDYLFLIMNQlrkEGTAIVYISHKLAEIRRICDRYTVMKDGSSV 224
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
11-230 |
1.85e-31 |
|
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: 115.41 E-value: 1.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSGEGKVdaLKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVmflkKLLNH-LPEEQLAAI 89
Cdd:cd03251 1 VEFKNVTFRYPGDGPPV--LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRI----LIDGHdVRDYTLASL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 90 RgRHLGFIFQ---FFNLipvlSVFDNVFFplvlnghvGKKEA-RERALHFIESVGLAGFTERKPG-----------QLSG 154
Cdd:cd03251 75 R-RQIGLVSQdvfLFND----TVAENIAY--------GRPGAtREEVEEAARAANAHEFIMELPEgydtvigergvKLSG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556463668 155 GQQQRVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKInQETRTTFIIStHSSQLKERARRVVEIKDGVLV 230
Cdd:cd03251 142 GQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERL-MKNRTTFVIA-HRLSTIENADRIVVLEDGKIV 215
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
29-211 |
2.07e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 116.69 E-value: 2.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 29 ALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVM-----FLKKLLNhlpeeqLAAIRGRhLGFIFQFfnl 103
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIidgvdITDKKVK------LSDIRKK-VGLVFQY--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 104 iPVLSVF------DNVFFPLVLNghVGKKEARERALHFIESVGLA--GFTERKPGQLSGGQQQRVAIARALAHDPQVVIA 175
Cdd:PRK13637 92 -PEYQLFeetiekDIAFGPINLG--LSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILIL 168
|
170 180 190
....*....|....*....|....*....|....*.
gi 556463668 176 DEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHS 211
Cdd:PRK13637 169 DEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHS 204
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
9-210 |
3.51e-31 |
|
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: 119.52 E-value: 3.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSYGSGE-GKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLkkllnhLPEEQL- 86
Cdd:TIGR03269 278 PIIKVRNVSKRYISVDrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVR------VGDEWVd 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 87 -----AAIRGR---HLGFIFQFFNLIPVLSVFDNVFFPLVLNghVGKKEARERALHFIESVGlagFTERK--------PG 150
Cdd:TIGR03269 352 mtkpgPDGRGRakrYIGILHQEYDLYPHRTVLDNLTEAIGLE--LPDELARMKAVITLKMVG---FDEEKaeeildkyPD 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 151 QLSGGQQQRVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTH 210
Cdd:TIGR03269 427 ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSH 486
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
11-232 |
4.33e-31 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 112.14 E-value: 4.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSgegkVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMflkkllnhlpeeqlaaIR 90
Cdd:cd03216 1 LELRGITKRFGG----VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEIL----------------VD 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 91 GRhlgfifqffnliPVLsvFDNVffplvlnghvgkKEARERALHFIEsvglagfterkpgQLSGGQQQRVAIARALAHDP 170
Cdd:cd03216 61 GK------------EVS--FASP------------RDARRAGIAMVY-------------QLSVGERQMVEIARALARNA 101
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556463668 171 QVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQLKERARRVVEIKDGVLVHD 232
Cdd:cd03216 102 RLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
12-227 |
9.03e-31 |
|
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: 112.74 E-value: 9.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 12 SLNNIYKSYGsgeGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNhlpeeqlAAIRG 91
Cdd:cd03226 1 RIENISFSYK---KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK-------AKERR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 92 RHLGFI-----FQFFnlipvlsvFDNVFFPLVLnghvGKKEA---RERALHFIESVGLAGFTERKPGQLSGGQQQRVAIA 163
Cdd:cd03226 71 KSIGYVmqdvdYQLF--------TDSVREELLL----GLKELdagNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIA 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556463668 164 RALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIIsTHSSQ-LKERARRVVEIKDG 227
Cdd:cd03226 139 AALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVI-THDYEfLAKVCDRVLLLANG 202
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
10-235 |
1.53e-30 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 112.75 E-value: 1.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 10 MISLNNIYKSYgsgegkvDALK-NINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQlaa 88
Cdd:PRK10771 1 MLKLTDITWLY-------HHLPmRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 89 irgRHLGFIFQFFNLIPVLSVFDNVFFPLvlngHVGKK---EARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARA 165
Cdd:PRK10771 71 ---RPVSMLFQENNLFSHLTVAQNIGLGL----NPGLKlnaAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARC 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556463668 166 LAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQLKER-ARRVVEIKDGVLVHDSQT 235
Cdd:PRK10771 144 LVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARiAPRSLVVADGRIAWDGPT 214
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
10-232 |
2.01e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 114.56 E-value: 2.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 10 MISLNNIYKSYGSG-EGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTV-----------MFLKKL 77
Cdd:PRK13631 21 ILRVKNLYCVFDEKqENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdkkNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 78 LNHLPEEQLAAIRGRHL-GFIFQFfnliPVLSVF------DNVFFPLVLNghVGKKEARERALHFIESVGL-AGFTERKP 149
Cdd:PRK13631 101 TNPYSKKIKNFKELRRRvSMVFQF----PEYQLFkdtiekDIMFGPVALG--VKKSEAKKLAKFYLNKMGLdDSYLERSP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 150 GQLSGGQQQRVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIIsTHSSQlkerarRVVEIKDGVL 229
Cdd:PRK13631 175 FGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVI-THTME------HVLEVADEVI 247
|
...
gi 556463668 230 VHD 232
Cdd:PRK13631 248 VMD 250
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
9-200 |
2.32e-30 |
|
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: 112.38 E-value: 2.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSYGsgegKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAA 88
Cdd:COG0410 2 PMLEVENLHAGYG----GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 89 iRGrhLGFIFQFFNLIPVLSVFDNvffpLVLNGHVGKKEARERALhfIESVG-----LAGFTERKPGQLSGGQQQRVAIA 163
Cdd:COG0410 78 -LG--IGYVPEGRRIFPSLTVEEN----LLLGAYARRDRAEVRAD--LERVYelfprLKERRRQRAGTLSGGEQQMLAIG 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 556463668 164 RALAHDPQVVIADEPTGNL--DLVtgEAILDLLLKINQE 200
Cdd:COG0410 149 RALMSRPKLLLLDEPSLGLapLIV--EEIFEIIRRLNRE 185
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
23-222 |
4.14e-30 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 110.40 E-value: 4.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 23 GEGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVmflkkllnhlpeeqlAAIRGRHLGFIFQFFN 102
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV---------------RRAGGARVAYVPQRSE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 103 LIPVL--SVFDNV----FFPLVLNGHVGKkEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHDPQVVIAD 176
Cdd:NF040873 66 VPDSLplTVRDLVamgrWARRGLWRRLTR-DDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLD 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 556463668 177 EPTGNLDLVTGEAILDLLLKINQETRTTFIIsTHSSQLKERARRVV 222
Cdd:NF040873 145 EPTTGLDAESRERIIALLAEEHARGATVVVV-THDLELVRRADPCV 189
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
9-235 |
6.75e-30 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 111.79 E-value: 6.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSYGsgegKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDK--PTV---GTVMFLKKLLnHLPE 83
Cdd:PRK14239 4 PILQVSDLSVYYN----KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEVtitGSIVYNGHNI-YSPR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 84 EQLAAIRgRHLGFIFQFFNLIPvLSVFDNVFFPLVLNGHVGKK---EARERALhfiesVGLAGFTERKPG------QLSG 154
Cdd:PRK14239 79 TDTVDLR-KEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQvldEAVEKSL-----KGASIWDEVKDRlhdsalGLSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 155 GQQQRVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQEtrTTFIISTHSSQLKER-ARRVVEIKDGVLVHDS 233
Cdd:PRK14239 152 GQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD--YTMLLVTRSMQQASRiSDRTGFFLDGDLIEYN 229
|
..
gi 556463668 234 QT 235
Cdd:PRK14239 230 DT 231
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
34-227 |
7.18e-30 |
|
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: 110.72 E-value: 7.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 34 NLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQlaairgRHLGFIFQFFNLIPVLSVFDNv 113
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQ------RPVSMLFQENNLFAHLTVRQN- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 114 ffpLVLNGHVGKK---EARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHDPQVVIADEPTGNLDLVTGEAI 190
Cdd:TIGR01277 91 ---IGLGLHPGLKlnaEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEM 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 556463668 191 LDLLLKINQETRTTFIISTHS-SQLKERARRVVEIKDG 227
Cdd:TIGR01277 168 LALVKQLCSERQRTLLMVTHHlSDARAIASQIAVVSQG 205
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
30-233 |
9.08e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 112.23 E-value: 9.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 30 LKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLN-HLPEEQLAAIRgRHLGFIFQFfnliPVLS 108
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpETGNKNLKKLR-KKVSLVFQF----PEAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 109 VFDNVFFPLV----LNGHVGKKEARERALHFIESVGLA-GFTERKPGQLSGGQQQRVAIARALAHDPQVVIADEPTGNLD 183
Cdd:PRK13641 98 LFENTVLKDVefgpKNFGFSEDEAKEKALKWLKKVGLSeDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 556463668 184 LVTGEAILDLLLKINQETRTTFIISTHSSQLKERARRVVEIKDGVLV-HDS 233
Cdd:PRK13641 178 PEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIkHAS 228
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
26-232 |
9.76e-30 |
|
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: 110.37 E-value: 9.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 26 KVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVmflkkLLNHLPEEQL--AAIRgRHLGFIFQ---- 99
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSV-----LLDGTDIRQLdpADLR-RNIGYVPQdvtl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 100 FFNlipvlSVFDNvffpLVLNGHVGKKEARERALHFIesvGLAGFTERKP----------GQ-LSGGQQQRVAIARALAH 168
Cdd:cd03245 90 FYG-----TLRDN----ITLGAPLADDERILRAAELA---GVTDFVNKHPngldlqigerGRgLSGGQRQAVALARALLN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556463668 169 DPQVVIADEPTGNLDLVTGEAILDlllKINQETRT-TFIISTHSSQLKERARRVVEIKDGVLVHD 232
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKE---RLRQLLGDkTLIIITHRPSLLDLVDRIIVMDSGRIVAD 219
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
11-230 |
1.59e-29 |
|
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: 110.01 E-value: 1.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYgsgEGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAair 90
Cdd:cd03254 3 IEFENVNFSY---DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLR--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 91 gRHLGFIFQffnlIPVL---SVFDNV-FFPLVLNGHVGKKEARE-RALHFIESV--GLAGFTERKPGQLSGGQQQRVAIA 163
Cdd:cd03254 77 -SMIGVVLQ----DTFLfsgTIMENIrLGRPNATDEEVIEAAKEaGAHDFIMKLpnGYDTVLGENGGNLSQGERQLLAIA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556463668 164 RALAHDPQVVIADEPTGNLDLVTGEAILDLLLKInQETRTTFIISTHSSQLKErARRVVEIKDGVLV 230
Cdd:cd03254 152 RAMLRDPKILILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLSTIKN-ADKILVLDDGKII 216
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
26-230 |
1.61e-29 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 115.72 E-value: 1.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 26 KVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAAIRgRHLGFIFQ--FFNL 103
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALR-RDIQFIFQdpYASL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 104 IPVLSVFDNVFFPLVLNGHVGKKEARERALHFIESVGL-AGFTERKPGQLSGGQQQRVAIARALAHDPQVVIADEPTGNL 182
Cdd:PRK10261 415 DPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 556463668 183 DLVTGEAILDLLLKINQETRTTFIISTHSSQLKER-ARRVVEIKDGVLV 230
Cdd:PRK10261 495 DVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERiSHRVAVMYLGQIV 543
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
10-210 |
2.57e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 111.09 E-value: 2.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 10 MISLNNIYKSYGSGegkVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHlPEEQLAAI 89
Cdd:PRK13636 5 ILKVEELNYNYSDG---THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDY-SRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 90 RgRHLGFIFQF-FNLIPVLSVFDNVFFPlVLNGHVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAH 168
Cdd:PRK13636 81 R-ESVGMVFQDpDNQLFSASVYQDVSFG-AVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 556463668 169 DPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTH 210
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATH 200
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
33-227 |
2.68e-29 |
|
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: 112.51 E-value: 2.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 33 INLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNH------LPEEQlaairgRHLGFIFQFFNLIPV 106
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPEK------RRIGYVFQEARLFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 107 LSVFDNVFFplvlnghvGKKEAR--ERALHF---IESVGLAGFTERKPGQLSGGQQQRVAIARALAHDPQVVIADEPTGN 181
Cdd:TIGR02142 90 LSVRGNLRY--------GMKRARpsERRISFervIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 556463668 182 LDLVTGEAILDLLLKINQETRTTFIISTHSSQLKER-ARRVVEIKDG 227
Cdd:TIGR02142 162 LDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRlADRVVVLEDG 208
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
9-235 |
4.64e-29 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 114.03 E-value: 4.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSYGSGEGKVDALKNINLEIEKGEFLALCGPSGSGKS-TLLNILSGIDKPTV----GTVMFLKKLLNHLPE 83
Cdd:PRK15134 4 PLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPVvypsGDIRFHGESLLHASE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 84 EQLAAIRGRHLGFIFQ--FFNLIPVLSVFDNVFFPLVLNGHVGKKEARERALHFIESVGLAGFTER---KPGQLSGGQQQ 158
Cdd:PRK15134 84 QTLRGVRGNKIAMIFQepMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRltdYPHQLSGGERQ 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556463668 159 RVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHS-SQLKERARRVVEIKDGVLVHDSQT 235
Cdd:PRK15134 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNlSIVRKLADRVAVMQNGRCVEQNRA 241
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
9-230 |
5.01e-29 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 110.97 E-value: 5.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSYGSGEGKVDALKNINLEIEKGEFLALCGPSGSGKS----TLLNILS--GIdkpTVGTVMFL-KKLLNhL 81
Cdd:PRK09473 11 ALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAanGR---IGGSATFNgREILN-L 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 82 PEEQLAAIRGRHLGFIFQ--FFNLIPVLSVFDNVFFPLVLNGHVGKKEARERALHFIESVGLAGFTERK---PGQLSGGQ 156
Cdd:PRK09473 87 PEKELNKLRAEQISMIFQdpMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMkmyPHEFSGGM 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556463668 157 QQRVAIARALAHDPQVVIADEPTGNLDlVTGEA-ILDLLLKINQETRTTFIISTHSSQLkerarrVVEIKDGVLV 230
Cdd:PRK09473 167 RQRVMIAMALLCRPKLLIADEPTTALD-VTVQAqIMTLLNELKREFNTAIIMITHDLGV------VAGICDKVLV 234
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
29-231 |
7.38e-29 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 112.05 E-value: 7.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 29 ALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAAIRGRHLGFIFQFFNLIPVLS 108
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 109 VFDNVFFPLVLNGhVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHDPQVVIADEPTGNLDLVTGE 188
Cdd:PRK10070 123 VLDNTAFGMELAG-INAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 556463668 189 AILDLLLKINQETRTTFIISTHSsqLKERAR---RVVEIKDGVLVH 231
Cdd:PRK10070 202 EMQDELVKLQAKHQRTIVFISHD--LDEAMRigdRIAIMQNGEVVQ 245
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-211 |
9.35e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 108.78 E-value: 9.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSGEgkvdALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGI-----DKPTVGTV-MFLKKLLNhlPEE 84
Cdd:PRK14267 5 IETVNLRVYYGSNH----VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVrLFGRNIYS--PDV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 85 QLAAIRgRHLGFIFQFFNLIPVLSVFDNVFFPLVLNGHV-GKKEARERALHFIESVGLagFTERK------PGQLSGGQQ 157
Cdd:PRK14267 79 DPIEVR-REVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVkSKKELDERVEWALKKAAL--WDEVKdrlndyPSNLSGGQR 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 556463668 158 QRVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQEtrTTFIISTHS 211
Cdd:PRK14267 156 QRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHS 207
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
29-232 |
1.23e-28 |
|
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: 113.04 E-value: 1.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 29 ALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVmflkkLLNHLPEEQL--AAIRgRHLGFIFQFfnliPV 106
Cdd:TIGR03375 480 ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSV-----LLDGVDIRQIdpADLR-RNIGYVPQD----PR 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 107 L---SVFDNVFFplvlnghvGKKEARERA-LHFIESVGLAGFTERKP-----------GQLSGGQQQRVAIARALAHDPQ 171
Cdd:TIGR03375 550 LfygTLRDNIAL--------GAPYADDEEiLRAAELAGVTEFVRRHPdgldmqigergRSLSGGQRQAVALARALLRDPP 621
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556463668 172 VVIADEPTGNLDLVTGEAILDLLLKINQEtrTTFIISTHSSQLKERARRVVEIKDGVLVHD 232
Cdd:TIGR03375 622 ILLLDEPTSAMDNRSEERFKDRLKRWLAG--KTLVLVTHRTSLLDLVDRIIVMDNGRIVAD 680
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
11-230 |
1.50e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 109.10 E-value: 1.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSGEG-KVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLK-KLLNHLPEEQLAA 88
Cdd:PRK13646 3 IRFDNVSYTYQKGTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDiTITHKTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 89 IRGRhLGFIFQFfnliPVLSVF-DNV-----FFPLVLNGHVgkKEARERALHFIESVGLA-GFTERKPGQLSGGQQQRVA 161
Cdd:PRK13646 83 VRKR-IGMVFQF----PESQLFeDTVereiiFGPKNFKMNL--DEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 162 IARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHS-SQLKERARRVVEIKDGVLV 230
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDmNEVARYADEVIVMKEGSIV 225
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
10-232 |
1.76e-28 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 107.86 E-value: 1.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 10 MISLNNIYKSYGsgeGKVdALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAai 89
Cdd:COG4604 1 MIEIKNVSKRYG---GKV-VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELA-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 90 rgRHLGFIFQFFNLIPVLSVFDNVFFplvlnG----HVGK-----KEARERALHFiesVGLAGFTERKPGQLSGGQQQRV 160
Cdd:COG4604 75 --KRLAILRQENHINSRLTVRELVAF-----GrfpySKGRltaedREIIDEAIAY---LDLEDLADRYLDELSGGQRQRA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 161 AIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFII--------STHSSqlkerarRVVEIKDGVLVHD 232
Cdd:COG4604 145 FIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIvlhdinfaSCYAD-------HIVAMKDGRVVAQ 217
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
11-229 |
1.95e-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: 112.06 E-value: 1.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYksYGSGEGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLaair 90
Cdd:TIGR01842 317 LSVENVT--IVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETF---- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 91 GRHLGFIFQFFNLIPvlsvfdnvffplvlnGHVGKKEARER----ALHFIESVGLAGFTE---RKP-----------GQL 152
Cdd:TIGR01842 391 GKHIGYLPQDVELFP---------------GTVAENIARFGenadPEKIIEAAKLAGVHElilRLPdgydtvigpggATL 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556463668 153 SGGQQQRVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIIsTHSSQLKERARRVVEIKDGVL 229
Cdd:TIGR01842 456 SGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVI-THRPSLLGCVDKILVLQDGRI 531
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
11-210 |
2.26e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 108.29 E-value: 2.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSG---EGKvdALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLL-NHLPEEQL 86
Cdd:PRK13649 3 INLQNVSYTYQAGtpfEGR--ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItSTSKNKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 87 AAIRgRHLGFIFQFfnliPVLSVFDNVFFPLVL----NGHVGKKEARERALHFIESVGLA-GFTERKPGQLSGGQQQRVA 161
Cdd:PRK13649 81 KQIR-KKVGLVFQF----PESQLFEETVLKDVAfgpqNFGVSQEEAEALAREKLALVGISeSLFEKNPFELSGGQMRRVA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 556463668 162 IARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETrTTFIISTH 210
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSG-MTIVLVTH 203
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
29-211 |
7.38e-28 |
|
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: 110.53 E-value: 7.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 29 ALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVmflkkLLNHLPeeqLAAIRGRHLGFIFQFFNLIPVL- 107
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEV-----TLDGVP---VSSLDQDEVRRRVSVCAQDAHLf 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 108 --SVFDNVffplvlngHVGKKEAR-ERALHFIESVGLAGFTERKPG-----------QLSGGQQQRVAIARALAHDPQVV 173
Cdd:TIGR02868 422 dtTVRENL--------RLARPDATdEELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPIL 493
|
170 180 190
....*....|....*....|....*....|....*...
gi 556463668 174 IADEPTGNLDLVTGEAILDLLLKINQETRTTFIisTHS 211
Cdd:TIGR02868 494 LLDEPTEHLDAETADELLEDLLAALSGRTVVLI--THH 529
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
9-210 |
7.54e-28 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 106.55 E-value: 7.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSYGSGEGkvdaLKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKK-----LLNHLPE 83
Cdd:PRK11701 5 PLLSVRGLTKLYGPRKG----CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 84 EQLaairgRHL-----GFIFQffN----LIPVLSVFDNVFFPLVLNG--HVGkkEARERALHFIESVGLAgfTER---KP 149
Cdd:PRK11701 81 AER-----RRLlrtewGFVHQ--HprdgLRMQVSAGGNIGERLMAVGarHYG--DIRATAGDWLERVEID--AARiddLP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556463668 150 GQLSGGQQQRVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTH 210
Cdd:PRK11701 150 TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTH 210
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
32-210 |
7.94e-28 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 106.77 E-value: 7.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 32 NINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAAIRGRhLGFIFQFFNLIPVLSVFD 111
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKR-MSMLFQSGALFTDMNVFD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 112 NVFFPLVLNGHVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHDPQVVIADEPTGNLDLVTGEAIL 191
Cdd:PRK11831 104 NVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLV 183
|
170
....*....|....*....
gi 556463668 192 DLLLKINQETRTTFIISTH 210
Cdd:PRK11831 184 KLISELNSALGVTCVVVSH 202
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
10-232 |
1.17e-27 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 105.55 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 10 MISLNNIYKSY------------------GSGEGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTV 71
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 72 mflkkllnhlpeeqlaAIRGRH-----LGFIFQffnliPVLSVFDNVFFPLVLNGhVGKKEARERaLHFIESV-GLAGFT 145
Cdd:COG1134 84 ----------------EVNGRVsalleLGAGFH-----PELTGRENIYLNGRLLG-LSRKEIDEK-FDEIVEFaELGDFI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 146 ERKPGQLSGGQQQRVAIARALAHDPQVVIADEPtgnldLVTG---------EAILDLLlkinqETRTTFIISTHS-SQLK 215
Cdd:COG1134 141 DQPVKTYSSGMRARLAFAVATAVDPDILLVDEV-----LAVGdaafqkkclARIRELR-----ESGRTVIFVSHSmGAVR 210
|
250
....*....|....*..
gi 556463668 216 ERARRVVEIKDGVLVHD 232
Cdd:COG1134 211 RLCDRAIWLEKGRLVMD 227
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
10-232 |
1.45e-27 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 105.48 E-value: 1.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 10 MISLNNIYKSYGsgegKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAai 89
Cdd:PRK11231 2 TLRTENLTVGYG----TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 90 rgRHLGFIFQFfNLIPV-LSVFDNVFF---P-LVLNGHVGKKEaRERALHFIESVGLAGFTERKPGQLSGGQQQRVAIAR 164
Cdd:PRK11231 76 --RRLALLPQH-HLTPEgITVRELVAYgrsPwLSLWGRLSAED-NARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAM 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556463668 165 ALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQLKERARRVVEIKDGVLVHD 232
Cdd:PRK11231 152 VLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQ 219
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
30-230 |
1.62e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 105.51 E-value: 1.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 30 LKNINLEIEKGEFLALCGPSGSGKSTLLNILSGI-----DKPTV-GTVMFLKKLLNhlpeeQLAAIRGR-HLGFIFQFFN 102
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydSKIKVdGKVLYFGKDIF-----QIDAIKLRkEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 103 LIPVLSVFDNVFFPLVLNGHVGKKEARERALHFIESVGLAGFTERK----PGQLSGGQQQRVAIARALAHDPQVVIADEP 178
Cdd:PRK14246 101 PFPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 556463668 179 TGNLDLVTGEAILDLLLKINQETrTTFIISTHSSQLKERARRVVEIKDGVLV 230
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNEI-AIVIVSHNPQQVARVADYVAFLYNGELV 231
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
29-230 |
2.15e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 105.97 E-value: 2.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 29 ALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAAIRGRHLGFIFQFfnliPVLS 108
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQF----PESQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 109 VFDNVFFPLVLNG----HVGKKEARERALHFIESVGLAG-FTERKPGQLSGGQQQRVAIARALAHDPQVVIADEPTGNLD 183
Cdd:PRK13643 97 LFEETVLKDVAFGpqnfGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 556463668 184 LVTGEAILDLLLKINQETRTTFIISTHSSQLKERARRVVEIKDGVLV 230
Cdd:PRK13643 177 PKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHII 223
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
10-227 |
2.20e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 105.58 E-value: 2.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 10 MISLNNIYKSYGSGEGKVDaLKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNhlpEEQLAAI 89
Cdd:PRK13650 4 IIEVKNLTFKYKEDQEKYT-LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLT---EENVWDI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 90 RgRHLGFIFQF-FNLIPVLSVFDNVFFPLVlNGHVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAH 168
Cdd:PRK13650 80 R-HKIGMVFQNpDNQFVGATVEDDVAFGLE-NKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556463668 169 DPQVVIADEPTGNLDlvtGEAILDLL---LKINQETRTTFIISTHSsqLKERA--RRVVEIKDG 227
Cdd:PRK13650 158 RPKIIILDEATSMLD---PEGRLELIktiKGIRDDYQMTVISITHD--LDEVAlsDRVLVMKNG 216
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
21-212 |
6.29e-27 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 102.24 E-value: 6.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 21 GSGEGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSG--IDKPTVGTVmflkkLLNHLPEEqLAAIRgRHLGFIF 98
Cdd:cd03213 16 SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEV-----LINGRPLD-KRSFR-KIIGYVP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 99 QFFNLIPVLSVFDNVFFPLVLNGhvgkkeareralhfiesvglagfterkpgqLSGGQQQRVAIARALAHDPQVVIADEP 178
Cdd:cd03213 89 QDDILHPTLTVRETLMFAAKLRG------------------------------LSGGERKRVSIALELVSNPSLLFLDEP 138
|
170 180 190
....*....|....*....|....*....|....
gi 556463668 179 TGNLDLVTGEAILDLLLKINQETRTTfIISTHSS 212
Cdd:cd03213 139 TSGLDSSSALQVMSLLRRLADTGRTI-ICSIHQP 171
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
11-230 |
1.06e-26 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 107.20 E-value: 1.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSgegkVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGID--KPTVGTVMF--------------- 73
Cdd:TIGR03269 1 IEVKNLTKKFDG----KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIYhvalcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 74 -----LKKLLNHLPEEQL----------AAIRGRhLGFIFQ-FFNLIPVLSVFDNVFFPLVLNGHVGKkEARERALHFIE 137
Cdd:TIGR03269 77 kvgepCPVCGGTLEPEEVdfwnlsdklrRRIRKR-IAIMLQrTFALYGDDTVLDNVLEALEEIGYEGK-EAVGRAVDLIE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 138 SVGLAGFTERKPGQLSGGQQQRVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQ-LKE 216
Cdd:TIGR03269 155 MVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEvIED 234
|
250
....*....|....
gi 556463668 217 RARRVVEIKDGVLV 230
Cdd:TIGR03269 235 LSDKAIWLENGEIK 248
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
10-230 |
1.50e-26 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 104.44 E-value: 1.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 10 MISLNNIYKSYGSGEGKVDALKNINLEIEKGEFLALCGPSGSGKS-TLLNILSGIDKPtvGTVM-----FLKKLLNHLPE 83
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVMaekleFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 84 EQLAAIRGRHLGFIFQ--FFNLIPVLSVFDNVFFPLVLNGHVGKKEARERALHFIESVGLAGFTER---KPGQLSGGQQQ 158
Cdd:PRK11022 81 KERRNLVGAEVAMIFQdpMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556463668 159 RVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQL-KERARRVVEIKDGVLV 230
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALvAEAAHKIIVMYAGQVV 233
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
9-235 |
4.59e-26 |
|
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: 101.83 E-value: 4.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSYGSGEGkvdaLKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAA 88
Cdd:TIGR02323 2 PLLQVSGLSKSYGGGKG----CRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 89 IRGRHL-----GFIFQ--FFNLIPVLSVFDNVFFPLVLNG--HVGKkeARERALHFIESVGL-AGFTERKPGQLSGGQQQ 158
Cdd:TIGR02323 78 AERRRLmrtewGFVHQnpRDGLRMRVSAGANIGERLMAIGarHYGN--IRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556463668 159 RVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHS-SQLKERARRVVEIKDGVLVHDSQT 235
Cdd:TIGR02323 156 RLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDlGVARLLAQRLLVMQQGRVVESGLT 233
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
10-211 |
4.65e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 101.70 E-value: 4.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 10 MISLNNIYKSYGSGEG-KVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQlaa 88
Cdd:COG1101 1 MLELKNLSKTFNPGTVnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYK--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 89 iRGRHLGFIFQ--FFNLIPVLSVFDNvffpLVLNGHVGKK-------EARERAlHFIESV---GLaGFTER---KPGQLS 153
Cdd:COG1101 78 -RAKYIGRVFQdpMMGTAPSMTIEEN----LALAYRRGKRrglrrglTKKRRE-LFRELLatlGL-GLENRldtKVGLLS 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 556463668 154 GGQQQRVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETR-TTFIIsTHS 211
Cdd:COG1101 151 GGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNlTTLMV-THN 208
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
9-210 |
5.36e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 101.75 E-value: 5.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSYGSGEGKvdALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNhlpEEQLAA 88
Cdd:PRK13648 6 SIIVFKNVSFQYQSDASF--TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAIT---DDNFEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 89 IRgRHLGFIFQFFNLIPVLSV--FDnVFFPLVlNGHVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARAL 166
Cdd:PRK13648 81 LR-KHIGIVFQNPDNQFVGSIvkYD-VAFGLE-NHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 556463668 167 AHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTH 210
Cdd:PRK13648 158 ALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITH 201
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
9-230 |
5.83e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 105.29 E-value: 5.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSYGSGEGKVdaLKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAA 88
Cdd:PRK11160 337 VSLTLNNVSFTYPDQPQPV--LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 89 irgrhlgfifqffnLIPVLS----VF-----DNvffpLVLnghvGKKEARERALHFI-ESVGLAGFTERKPG-------- 150
Cdd:PRK11160 415 --------------AISVVSqrvhLFsatlrDN----LLL----AAPNASDEALIEVlQQVGLEKLLEDDKGlnawlgeg 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 151 --QLSGGQQQRVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQEtrTTFIISTHSSQLKERARRVVEIKDGV 228
Cdd:PRK11160 473 grQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQN--KTVLMITHRLTGLEQFDRICVMDNGQ 550
|
..
gi 556463668 229 LV 230
Cdd:PRK11160 551 II 552
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
10-230 |
8.19e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 101.60 E-value: 8.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 10 MISLNNIYKSYGSGegkVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVmfLKKLLNHLPEEQLAAI 89
Cdd:PRK13644 1 MIRLENVSYSYPDG---TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKV--LVSGIDTGDFSKLQGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 90 RgRHLGFIFQF--FNLIPVLSVFDNVFFPLvlNGHVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALA 167
Cdd:PRK13644 76 R-KLVGIVFQNpeTQFVGRTVEEDLAFGPE--NLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556463668 168 HDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIIsTHSSQLKERARRVVEIKDGVLV 230
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYI-THNLEELHDADRIIVMDRGKIV 214
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
30-229 |
9.35e-26 |
|
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: 100.24 E-value: 9.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 30 LKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMflkkllnhLPEEQLAAIRGRHLGFIFQFFNLIPVL-- 107
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVL--------LDGKPISQYEHKYLHSKVSLVGQEPVLfa 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 108 -SVFDNVFFPL--VLNGHVGKKEARERALHFIESVGLAGFTE--RKPGQLSGGQQQRVAIARALAHDPQVVIADEPTGNL 182
Cdd:cd03248 102 rSLQDNIAYGLqsCSFECVKEAAQKAHAHSFISELASGYDTEvgEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSAL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 556463668 183 DLVTGEAILDLLLKINQetRTTFIISTHSSQLKERARRVVEIKDGVL 229
Cdd:cd03248 182 DAESEQQVQQALYDWPE--RRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
11-230 |
1.19e-25 |
|
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: 98.54 E-value: 1.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSGEGKVdaLKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVmflkkLLNHLPEEQLAAIR 90
Cdd:cd03247 1 LSINNVSFSYPEQEQQV--LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI-----TLDGVPVSDLEKAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 91 GRHLGFIFQFFNLipvlsvfdnvfFPLVLNGHVGKkeareralhfiesvglagfterkpgQLSGGQQQRVAIARALAHDP 170
Cdd:cd03247 74 SSLISVLNQRPYL-----------FDTTLRNNLGR-------------------------RFSGGERQRLALARILLQDA 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 171 QVVIADEPTGNLDLVTGEAILDLLLKINQEtrTTFIISTHSSQLKERARRVVEIKDGVLV 230
Cdd:cd03247 118 PIVLLDEPTVGLDPITERQLLSLIFEVLKD--KTLIWITHHLTGIEHMDKILFLENGKII 175
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
11-231 |
1.21e-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: 104.44 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIykSYGSGEGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLaair 90
Cdd:COG4618 331 LSVENL--TVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREEL---- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 91 GRHLGFIFQ---FFNLipvlSVFDNVF-FPLVLNGHVgkKEARERA-LH-FIES--------VGLAGFTerkpgqLSGGQ 156
Cdd:COG4618 405 GRHIGYLPQdveLFDG----TIAENIArFGDADPEKV--VAAAKLAgVHeMILRlpdgydtrIGEGGAR------LSGGQ 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556463668 157 QQRVAIARALAHDPQVVIADEPTGNLDlVTGEAILDLLLKINQETRTTFIISTHSSQLKERARRVVEIKDGVLVH 231
Cdd:COG4618 473 RQRIGLARALYGDPRLVVLDEPNSNLD-DEGEAALAAAIRALKARGATVVVITHRPSLLAAVDKLLVLRDGRVQA 546
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
10-230 |
1.68e-25 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 104.17 E-value: 1.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 10 MISLNNIYKSYGSGEGKVDALKNINLEIEKGEFLALCGPSGSGKS-TLLNILSGIDKpTVGTV----MFLKKL------L 78
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-AGGLVqcdkMLLRRRsrqvieL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 79 NHLPEEQLAAIRGRHLGFIFQ--FFNLIPVLSVFDNVFFPLVLNGHVGKKEARERALHFIESVGLA---GFTERKPGQLS 153
Cdd:PRK10261 91 SEQSAAQMRHVRGADMAMIFQepMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPeaqTILSRYPHQLS 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556463668 154 GGQQQRVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQLkerarrVVEIKDGVLV 230
Cdd:PRK10261 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGV------VAEIADRVLV 241
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
25-224 |
2.08e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 100.24 E-value: 2.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 25 GKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDK--PTV---GTVMFLKKLLNHlPEEQLAAIRgRHLGFIFQ 99
Cdd:PRK14243 21 GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGFrveGKVTFHGKNLYA-PDVDPVEVR-RRIGMVFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 100 FFNLIPVlSVFDNVFFPLVLNGHVGK-KEARERALHfiesvGLAGFTE-----RKPGQ-LSGGQQQRVAIARALAHDPQV 172
Cdd:PRK14243 99 KPNPFPK-SIYDNIAYGARINGYKGDmDELVERSLR-----QAALWDEvkdklKQSGLsLSGGQQQRLCIARAIAVQPEV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 556463668 173 VIADEPTGNLDLVTGEAILDLLLKINQetRTTFIISTHSSQlkeRARRVVEI 224
Cdd:PRK14243 173 ILMDEPCSALDPISTLRIEELMHELKE--QYTIIIVTHNMQ---QAARVSDM 219
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
29-210 |
2.64e-25 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 98.20 E-value: 2.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 29 ALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVmflkkLLNHLPEEQLAAIRGRHLGFIFQFFNLIPVLS 108
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEV-----RWNGTPLAEQRDEPHENILYLGHLPGLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 109 VFDNVFFPLVLngHVGKKEARERALhfiESVGLAGFTERKPGQLSGGQQQRVAIARALAHDPQVVIADEPTGNLDlVTGE 188
Cdd:TIGR01189 90 ALENLHFWAAI--HGGAQRTIEDAL---AAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD-KAGV 163
|
170 180
....*....|....*....|..
gi 556463668 189 AILDLLLKINQETRTTFIISTH 210
Cdd:TIGR01189 164 ALLAGLLRAHLARGGIVLLTTH 185
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
26-230 |
4.23e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 99.87 E-value: 4.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 26 KVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKP-----TVGTVMFLKkllnhLPEEQLAAIRGRhLGFIFQF 100
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnpnSKITVDGIT-----LTAKTVWDIREK-VGIVFQN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 101 -FNLIPVLSVFDNVFFPLVlNGHVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHDPQVVIADEPT 179
Cdd:PRK13640 93 pDNQFVGATVGDDVAFGLE-NRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDEST 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 556463668 180 GNLDLVTGEAILDLLLKINQETRTTFIISTHSSQLKERARRVVEIKDGVLV 230
Cdd:PRK13640 172 SMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLL 222
|
|
| GldA_ABC_ATP |
TIGR03522 |
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein ... |
11-232 |
4.48e-25 |
|
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldA is an ABC transporter ATP-binding protein (pfam00005) linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae and Cytophaga hutchinsonii. Knockouts of GldA abolish the gliding phenotype. Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. Bacteroidetes with members of this protein family appear to have all of the genes associated with gliding motility.
Pssm-ID: 132561 [Multi-domain] Cd Length: 301 Bit Score: 99.85 E-value: 4.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGsgegKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQlaair 90
Cdd:TIGR03522 3 IRVSSLTKLYG----TQNALDEVSFEAQKGRIVGFLGPNGAGKSTTMKIITGYLPPDSGSVQVCGEDVLQNPKEV----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 91 GRHLGFIFQFFNLIPVLSVFDNVFFPLVLNGHVGKKEaRERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHDP 170
Cdd:TIGR03522 74 QRNIGYLPEHNPLYLDMYVREYLQFIAGIYGMKGQLL-KQRVEEMIELVGLRPEQHKKIGQLSKGYRQRVGLAQALIHDP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556463668 171 QVVIADEPTGNLDLVTGEAILDLLLKINQEtrTTFIISTHSSQLKER-ARRVVEIKDGVLVHD 232
Cdd:TIGR03522 153 KVLILDEPTTGLDPNQLVEIRNVIKNIGKD--KTIILSTHIMQEVEAiCDRVIIINKGKIVAD 213
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
29-230 |
6.89e-25 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 100.17 E-value: 6.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 29 ALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAAIRgRHLGFIFQ--FFNLIPV 106
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVR-SDIQMIFQdpLASLNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 107 LSVFDNVFFPL-VLNGHVGKKEARERALHFIESVGL-AGFTERKPGQLSGGQQQRVAIARALAHDPQVVIADEPTGNLDL 184
Cdd:PRK15079 115 MTIGEIIAEPLrTYHPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 556463668 185 VTGEAILDLLLKINQETRTTFIISTHSSQLkerarrVVEIKDGVLV 230
Cdd:PRK15079 195 SIQAQVVNLLQQLQREMGLSLIFIAHDLAV------VKHISDRVLV 234
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
11-230 |
1.51e-24 |
|
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: 101.33 E-value: 1.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSGEgkVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLpeeQLAAIR 90
Cdd:TIGR02203 331 VEFRNVTFRYPGRD--RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADY---TLASLR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 91 gRHLGFIFQ---FFNLipvlSVFDNVFFPLVlnGHVGKKEARE-----RALHFIESVGLAGFTE--RKPGQLSGGQQQRV 160
Cdd:TIGR02203 406 -RQVALVSQdvvLFND----TIANNIAYGRT--EQADRAEIERalaaaYAQDFVDKLPLGLDTPigENGVLLSGGQRQRL 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 161 AIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQEtRTTFIIStHSSQLKERARRVVEIKDGVLV 230
Cdd:TIGR02203 479 AIARALLKDAPILILDEATSALDNESERLVQAALERLMQG-RTTLVIA-HRLSTIEKADRIVVMDDGRIV 546
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
12-179 |
2.24e-24 |
|
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: 96.44 E-value: 2.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 12 SLNNIYKSYGSGEgkvdALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAAiRG 91
Cdd:TIGR03410 2 EVSNLNVYYGQSH----ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERAR-AG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 92 rhLGFIFQFFNLIPVLSVFDNVFFPLvlnghvgkkEARERALHFIESVGLAGF------TERKPGQLSGGQQQRVAIARA 165
Cdd:TIGR03410 77 --IAYVPQGREIFPRLTVEENLLTGL---------AALPRRSRKIPDEIYELFpvlkemLGRRGGDLSGGQQQQLAIARA 145
|
170
....*....|....
gi 556463668 166 LAHDPQVVIADEPT 179
Cdd:TIGR03410 146 LVTRPKLLLLDEPT 159
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
30-214 |
3.79e-24 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 100.12 E-value: 3.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 30 LKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPtvGTVMFLKKLLNHLP--EEQLAAIRgrhlGFIFQFFNLIPVL 107
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPK--GVKGSGSVLLNGMPidAKEMRAIS----AYVQQDDLFIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 108 SVFDNVFFP--LVLNGHVGKKEARERALHFIESVGLA-------GFTERKPGqLSGGQQQRVAIARALAHDPQVVIADEP 178
Cdd:TIGR00955 115 TVREHLMFQahLRMPRRVTKKEKRERVDEVLQALGLRkcantriGVPGRVKG-LSGGERKRLAFASELLTDPPLLFCDEP 193
|
170 180 190
....*....|....*....|....*....|....*...
gi 556463668 179 TGNLDLVTGEAILDLLLKINQEtRTTFIISTH--SSQL 214
Cdd:TIGR00955 194 TSGLDSFMAYSVVQVLKGLAQK-GKTIICTIHqpSSEL 230
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
13-229 |
4.60e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 99.75 E-value: 4.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 13 LNNIYKSYGsgeGKVdALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLlnhlpeeqlaairgr 92
Cdd:COG0488 1 LENLSKSFG---GRP-LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL--------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 93 HLGFIFQFFNLIPVLSVFDNVFFPLvlnGHVGKKEARERAL-------------------HF-----------IESV--G 140
Cdd:COG0488 62 RIGYLPQEPPLDDDLTVLDTVLDGD---AELRALEAELEELeaklaepdedlerlaelqeEFealggweaearAEEIlsG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 141 LaGFTE----RKPGQLSGGQQQRVAIARALAHDPQVVIADEPTGNLDLvtgEAIL---DLLlkinQETRTTFIISTHssq 213
Cdd:COG0488 139 L-GFPEedldRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL---ESIEwleEFL----KNYPGTVLVVSH--- 207
|
250 260
....*....|....*....|..
gi 556463668 214 lkER------ARRVVEIKDGVL 229
Cdd:COG0488 208 --DRyfldrvATRILELDRGKL 227
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
11-232 |
5.10e-24 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 95.29 E-value: 5.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSGE------------------GKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVM 72
Cdd:cd03220 1 IELENVSKSYPTYKggssslkklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 73 FLKKllnhlpeeqLAAIRGRHLGFifqffnlIPVLSVFDNVFFPLVLNGHvGKKEARERaLHFIESV-GLAGFTERKPGQ 151
Cdd:cd03220 81 VRGR---------VSSLLGLGGGF-------NPELTGRENIYLNGRLLGL-SRKEIDEK-IDEIIEFsELGDFIDLPVKT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 152 LSGGQQQRVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRtTFIISTHS-SQLKERARRVVEIKDGVLV 230
Cdd:cd03220 143 YSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGK-TVILVSHDpSSIKRLCDRALVLEKGKIR 221
|
..
gi 556463668 231 HD 232
Cdd:cd03220 222 FD 223
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
29-213 |
8.89e-24 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 99.01 E-value: 8.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 29 ALKNINLEIEKGEFLALCGPSGSGKST----LLNILsgidkPTVGTVMFLKKLLNHLPEEQLAAIRgRHLGFIFQFFN-- 102
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLLPVR-HRIQVVFQDPNss 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 103 LIPVLSVFDNVFFPL-VLNGHVGKKEARERALHFIESVGLAGFT-ERKPGQLSGGQQQRVAIARALAHDPQVVIADEPTG 180
Cdd:PRK15134 375 LNPRLNVLQIIEEGLrVHQPTLSAAQREQQVIAVMEEVGLDPETrHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
|
170 180 190
....*....|....*....|....*....|...
gi 556463668 181 NLDLVTGEAILDLLLKINQETRTTFIISTHSSQ 213
Cdd:PRK15134 455 SLDKTVQAQILALLKSLQQKHQLAYLFISHDLH 487
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-231 |
9.73e-24 |
|
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: 9.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSYGsgeGKVdALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVmflkkllnhlpeeqlaa 88
Cdd:COG0488 314 KVLELEGLSKSYG---DKT-LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV----------------- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 89 IRGRHL--GFIFQFF-NLIPVLSVFDNvffplVLNGHVGKKEARERAlhFIESVGLAGFTERKP-GQLSGGQQQRVAIAR 164
Cdd:COG0488 373 KLGETVkiGYFDQHQeELDPDKTVLDE-----LRDGAPGGTEQEVRG--YLGRFLFSGDDAFKPvGVLSGGEKARLALAK 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556463668 165 ALAHDPQVVIADEPTGNLDLVTGEAILDLLlkinQETRTTFIISTHSSQLKER-ARRVVEIKDGVLVH 231
Cdd:COG0488 446 LLLSPPNVLLLDEPTNHLDIETLEALEEAL----DDFPGTVLLVSHDRYFLDRvATRILEFEDGGVRE 509
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
27-230 |
2.09e-23 |
|
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: 94.14 E-value: 2.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 27 VDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMF----LKKL-LNHLpeeqlaaiRgRHLGFIFQff 101
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLdgvdIRDLnLRWL--------R-SQIGLVSQ-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 102 nlIPVL---SVFDNVFFplvlnghvGKKEA----RERA-----LH-FIES--------VGLAGFterkpgQLSGGQQQRV 160
Cdd:cd03249 85 --EPVLfdgTIAENIRY--------GKPDAtdeeVEEAakkanIHdFIMSlpdgydtlVGERGS------QLSGGQKQRI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 161 AIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKInQETRTTFIISTHSSQLKeRARRVVEIKDGVLV 230
Cdd:cd03249 149 AIARALLRNPKILLLDEATSALDAESEKLVQEALDRA-MKGRTTIVIAHRLSTIR-NADLIAVLQNGQVV 216
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
26-210 |
2.10e-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: 93.87 E-value: 2.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 26 KVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGID---KPTVGTVMFLKKLLNhlPEEQLaairgRHLGFIFQFFN 102
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQPRK--PDQFQ-----KCVAYVRQDDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 103 LIPVLSVFDNVFFPLVLNGHVGKKEARERALHFIESVGLAGFTE---RKPGQLSGGQQQRVAIARALAHDPQVVIADEPT 179
Cdd:cd03234 92 LLPGLTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLRDLALTRiggNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190
....*....|....*....|....*....|.
gi 556463668 180 GNLDLVTGEAILDLLLKINQETRTTfIISTH 210
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLARRNRIV-ILTIH 201
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
28-227 |
2.99e-23 |
|
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: 92.50 E-value: 2.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 28 DALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLN-------------HLPEEqlaaiRGRHL 94
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTrrsprdairagiaYVPED-----RKREG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 95 gfifqffnLIPVLSVFDNVFFPLvlnghvgkkeareralhfiesvglagfterkpgQLSGGQQQRVAIARALAHDPQVVI 174
Cdd:cd03215 89 --------LVLDLSVAENIALSS---------------------------------LLSGGNQQKVVLARWLARDPRVLI 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 556463668 175 ADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQLKERARRVVEIKDG 227
Cdd:cd03215 128 LDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
11-227 |
3.07e-23 |
|
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: 91.36 E-value: 3.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSGegkvDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLlnhlpeeqlaair 90
Cdd:cd03221 1 IELENLSKTYGGK----LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 91 grhlgfifqffnlipVLSVFDnvffplvlnghvgkkeareralhfiesvglagfterkpgQLSGGQQQRVAIARALAHDP 170
Cdd:cd03221 64 ---------------KIGYFE---------------------------------------QLSGGEKMRLALAKLLLENP 89
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 556463668 171 QVVIADEPTGNLDLVTGEAILDLLlkinQETRTTFIISTHSSQ-LKERARRVVEIKDG 227
Cdd:cd03221 90 NLLLLDEPTNHLDLESIEALEEAL----KEYPGTVILVSHDRYfLDQVATKIIELEDG 143
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
31-230 |
3.11e-23 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 94.00 E-value: 3.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 31 KNINLEIEKGEFLALCGPSGSGKS----TLLNILSGIDKPTVGTVmflkkLLNHLPEEqLAAIRGRHLGFIFQ----FFN 102
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRV-----LLDGKPVA-PCALRGRKIATIMQnprsAFN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 103 liPVLSVFDNVFFPLVlngHVGKKEARERALHFIESVGLAG---FTERKPGQLSGGQQQRVAIARALAHDPQVVIADEPT 179
Cdd:PRK10418 94 --PLHTMHTHARETCL---ALGKPADDATLTAALEAVGLENaarVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 556463668 180 GNLDLVTGEAILDLLLKINQETRTTFIISTHSSQLKER-ARRVVEIKDGVLV 230
Cdd:PRK10418 169 TDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARlADDVAVMSHGRIV 220
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
25-232 |
3.28e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 94.48 E-value: 3.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 25 GKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKllnHLPEEQLAAIRgRHLGFIFQFFNli 104
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGE---PITKENIREVR-KFVGLVFQNPD-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 105 pvlsvfDNVFFPLV--------LNGHVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHDPQVVIAD 176
Cdd:PRK13652 89 ------DQIFSPTVeqdiafgpINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 556463668 177 EPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQLkerarrVVEIKDGVLVHD 232
Cdd:PRK13652 163 EPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDL------VPEMADYIYVMD 212
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
29-230 |
3.46e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 93.90 E-value: 3.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 29 ALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAairgRHlGFI--FQFFNLIPV 106
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA----RM-GVVrtFQHVRLFRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 107 LSVFDNVffpLV-----LNGHV------------GKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHD 169
Cdd:PRK11300 95 MTVIENL---LVaqhqqLKTGLfsgllktpafrrAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQ 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556463668 170 PQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQLkerarrVVEIKDGVLV 230
Cdd:PRK11300 172 PEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKL------VMGISDRIYV 226
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
11-230 |
3.57e-23 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 97.34 E-value: 3.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGsgeGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTV----MFLKKLlnhlpeeQL 86
Cdd:PRK13657 335 VEFDDVSFSYD---NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRIlidgTDIRTV-------TR 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 87 AAIRgRHLGFIFQ---FFNLipvlSVFDNVffplvlngHVGKKEARERALHFIESVGLA-GFTERKPG-----------Q 151
Cdd:PRK13657 405 ASLR-RNIAVVFQdagLFNR----SIEDNI--------RVGRPDATDEEMRAAAERAQAhDFIERKPDgydtvvgergrQ 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556463668 152 LSGGQQQRVAIARALAHDPQVVIADEPTGNLDLVTgEAILDLLLKINQETRTTFIISTHSSQLKErARRVVEIKDGVLV 230
Cdd:PRK13657 472 LSGGERQRLAIARALLKDPPILILDEATSALDVET-EAKVKAALDELMKGRTTFIIAHRLSTVRN-ADRILVFDNGRVV 548
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
9-232 |
4.49e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 96.06 E-value: 4.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSYGSgegkVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVmflkkLLNHLPEEQLAA 88
Cdd:PRK09536 2 PMIDVSDLSVEFGD----TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTV-----LVAGDDVEALSA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 89 I----------RGRHLGFIFQFFNLI-----PVLSVFDnvffplvlnghvGKKEARERAL-HFIESVGLAGFTERKPGQL 152
Cdd:PRK09536 73 RaasrrvasvpQDTSLSFEFDVRQVVemgrtPHRSRFD------------TWTETDRAAVeRAMERTGVAQFADRPVTSL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 153 SGGQQQRVAIARALAHDPQVVIADEPTGNLDlvtgeaildlllkINQETRTTfiisthssqlkERARRVVEIKDGVL--V 230
Cdd:PRK09536 141 SGGERQRVLLARALAQATPVLLLDEPTASLD-------------INHQVRTL-----------ELVRRLVDDGKTAVaaI 196
|
..
gi 556463668 231 HD 232
Cdd:PRK09536 197 HD 198
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
7-230 |
6.28e-23 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 93.02 E-value: 6.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 7 ELPMISLNNIYKSYGsgegKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLpeeQL 86
Cdd:PRK11614 2 EKVMLSFDKVSAHYG----KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDW---QT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 87 AAIRGRHLGFIFQFFNLIPVLSVFDNvffpLVLNGHVGKKEARERALHFIESVGLAGFTER--KPGQLSGGQQQRVAIAR 164
Cdd:PRK11614 75 AKIMREAVAIVPEGRRVFSRMTVEEN----LAMGGFFAERDQFQERIKWVYELFPRLHERRiqRAGTMSGGEQQMLAIGR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556463668 165 ALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQLKERARRVVEIKDGVLV 230
Cdd:PRK11614 151 ALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
9-227 |
7.97e-23 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 96.15 E-value: 7.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSYGSgegkVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIdKPT---VGTVMFLKKLL--NHLPE 83
Cdd:PRK13549 4 YLLEMKNITKTFGG----VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEELqaSNIRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 84 EQLAAIrgrhlGFIFQFFNLIPVLSVFDNVFF--PLVLNGHVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVA 161
Cdd:PRK13549 79 TERAGI-----AIIHQELALVKELSVLENIFLgnEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556463668 162 IARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQLKERARRVVEIKDG 227
Cdd:PRK13549 154 IAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDG 219
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
11-227 |
8.30e-23 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 91.76 E-value: 8.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSGEGKVD-ALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVmflkkllnhlpeeqlaaI 89
Cdd:cd03250 1 ISVEDASFTWDSGEQETSfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV-----------------S 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 90 RGRHLGFIFQFfnliPVL---SVFDNVFFplvlnghvGKKEARERALHFIES-----------------VGLAGFTerkp 149
Cdd:cd03250 64 VPGSIAYVSQE----PWIqngTIRENILF--------GKPFDEERYEKVIKAcalepdleilpdgdlteIGEKGIN---- 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556463668 150 gqLSGGQQQRVAIARALAHDPQVVIADEPTGNLDLVTGEAILD-LLLKINQETRTTfIISTHSSQLKERARRVVEIKDG 227
Cdd:cd03250 128 --LSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEnCILGLLLNNKTR-ILVTHQLQLLPHADQIVVLDNG 203
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
9-212 |
8.55e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 92.47 E-value: 8.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIykSYGSGEGKVdaLKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAa 88
Cdd:PRK10247 6 PLLQLQNV--GYLAGDAKI--LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYR- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 89 irgRHLGFIFQffnlIPVL---SVFDNVFFPLVLNghvGKKEARERALHFIESVGLAGFTERKP-GQLSGGQQQRVAIAR 164
Cdd:PRK10247 81 ---QQVSYCAQ----TPTLfgdTVYDNLIFPWQIR---NQQPDPAIFLDDLERFALPDTILTKNiAELSGGEKQRISLIR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 556463668 165 ALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSS 212
Cdd:PRK10247 151 NLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDK 198
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
11-232 |
9.18e-23 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 96.35 E-value: 9.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSGEgkvDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMF------------LKKLL 78
Cdd:TIGR01193 474 IVINDVSYSYGYGS---NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLngfslkdidrhtLRQFI 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 79 NHLPEEQlaairgrhlgFIFQFfnlipvlSVFDNvffpLVLNGHVG-KKEARERALHFIE--------SVGLAGFTERKP 149
Cdd:TIGR01193 551 NYLPQEP----------YIFSG-------SILEN----LLLGAKENvSQDEIWAACEIAEikddienmPLGYQTELSEEG 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 150 GQLSGGQQQRVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQEtrtTFIISTHSSQLKERARRVVEIKDGVL 229
Cdd:TIGR01193 610 SSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQSDKIIVLDHGKI 686
|
...
gi 556463668 230 VHD 232
Cdd:TIGR01193 687 IEQ 689
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
30-227 |
1.01e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 96.03 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 30 LKNINLEIEKGEFLALCGPSGSGKSTLLNILSG--------IDKPTVGTVMFLkkllnhlPEEqlaairgrhlgfifqff 101
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGlwpygsgrIARPAGARVLFL-------PQR----------------- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 102 NLIPVLSVFDNVFFPLvLNGHVGKKEARErALhfiESVGLAGFTER------KPGQLSGGQQQRVAIARALAHDPQVVIA 175
Cdd:COG4178 435 PYLPLGTLREALLYPA-TAEAFSDAELRE-AL---EAVGLGHLAERldeeadWDQVLSLGEQQRLAFARLLLHKPDWLFL 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 556463668 176 DEPTGNLDLVTGEAILDLLLKINQEtrTTFIISTHSSQLKERARRVVEIKDG 227
Cdd:COG4178 510 DEATSALDEENEAALYQLLREELPG--TTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1-227 |
1.13e-22 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 95.63 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 1 MSGIIKELPmislnniyksygsgegKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIdKPT---VGTVMFlkkl 77
Cdd:NF040905 4 MRGITKTFP----------------GVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHgsyEGEILF---- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 78 lnhlpEEQLAAIRG----RHLGF--IFQFFNLIPVLSVFDNVFF--PLVLNGHVGKKEARERALHFIESVGLAGFTERKP 149
Cdd:NF040905 63 -----DGEVCRFKDirdsEALGIviIHQELALIPYLSIAENIFLgnERAKRGVIDWNETNRRARELLAKVGLDESPDTLV 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556463668 150 GQLSGGQQQRVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQLKERARRVVEIKDG 227
Cdd:NF040905 138 TDIGVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDG 215
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
11-179 |
1.21e-22 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 95.96 E-value: 1.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGsgegKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLkkllnhlpEEQLAAIR 90
Cdd:NF033858 2 ARLEGVSHRYG----KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVL--------GGDMADAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 91 GRH------------LGFifqffNLIPVLSVFDNVFFPLVLNGHvGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQ 158
Cdd:NF033858 70 HRRavcpriaympqgLGK-----NLYPTLSVFENLDFFGRLFGQ-DAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQ 143
|
170 180
....*....|....*....|.
gi 556463668 159 RVAIARALAHDPQVVIADEPT 179
Cdd:NF033858 144 KLGLCCALIHDPDLLILDEPT 164
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
11-232 |
1.35e-22 |
|
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: 92.16 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSGEGkvDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKkllNHLPEEQLAAIR 90
Cdd:cd03252 1 ITFEHVRFRYKPDGP--VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDG---HDLALADPAWLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 91 gRHLGFIFQFfNLIPVLSVFDNVffplvlnGHVGKKEARERalhFIESVGLAG---------------FTERKPGqLSGG 155
Cdd:cd03252 76 -RQVGVVLQE-NVLFNRSIRDNI-------ALADPGMSMER---VIEAAKLAGahdfiselpegydtiVGEQGAG-LSGG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556463668 156 QQQRVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINqETRTTFIISTHSSQLKeRARRVVEIKDGVLVHD 232
Cdd:cd03252 143 QRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTVK-NADRIIVMEKGRIVEQ 217
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
9-182 |
1.43e-22 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 95.36 E-value: 1.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSYGSgegkVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMflkkllnhlpeeqlaa 88
Cdd:PRK11288 3 PYLSFDGIGKTFPG----VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSIL---------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 89 IRGRHLGF-------------IFQFFNLIPVLSVFDNVF---FPLVLnGHVGKKEARERALHFIESVGLAGFTERKPGQL 152
Cdd:PRK11288 63 IDGQEMRFasttaalaagvaiIYQELHLVPEMTVAENLYlgqLPHKG-GIVNRRLLNYEAREQLEHLGVDIDPDTPLKYL 141
|
170 180 190
....*....|....*....|....*....|
gi 556463668 153 SGGQQQRVAIARALAHDPQVVIADEPTGNL 182
Cdd:PRK11288 142 SIGQRQMVEIAKALARNARVIAFDEPTSSL 171
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
10-227 |
2.12e-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: 94.89 E-value: 2.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 10 MISLNNIYKSYGSgegkVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTV--GTVMFLKKLL--NHLPEEQ 85
Cdd:TIGR02633 1 LLEMKGIVKTFGG----VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLkaSNIRDTE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 86 LAAIrgrhlGFIFQFFNLIPVLSVFDNVFF--PLVLNGHVGKKEAR-ERALHFIESVGLAGFTERKP-GQLSGGQQQRVA 161
Cdd:TIGR02633 77 RAGI-----VIIHQELTLVPELSVAENIFLgnEITLPGGRMAYNAMyLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556463668 162 IARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQLKERARRVVEIKDG 227
Cdd:TIGR02633 152 IAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
11-226 |
2.93e-22 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 91.14 E-value: 2.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSGegkVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMF----LKKLlnhlpeeQL 86
Cdd:cd03253 1 IEFENVTFAYDPG---RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIdgqdIREV-------TL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 87 AAIRgRHLGFIFQ---FFNLipvlSVFDNVFF--PLVLNGHVgkKEARERA-LH-FIES--------VGlagftERkpG- 150
Cdd:cd03253 71 DSLR-RAIGVVPQdtvLFND----TIGYNIRYgrPDATDEEV--IEAAKAAqIHdKIMRfpdgydtiVG-----ER--Gl 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556463668 151 QLSGGQQQRVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQeTRTTFIIsthssqlkerARRVVEIKD 226
Cdd:cd03253 137 KLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVI----------AHRLSTIVN 201
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
9-217 |
2.95e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 92.56 E-value: 2.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSYGSgEGKVDalkNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKllnhlPEEQLAA 88
Cdd:PRK13537 6 APIDFRNVEKRYGD-KLVVD---GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGE-----PVPSRAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 89 IRGRHLGFIFQFFNLIPVLSVFDNVffpLVLNGHVG--KKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARAL 166
Cdd:PRK13537 77 HARQRVGVVPQFDNLDPDFTVRENL---LVFGRYFGlsAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARAL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 556463668 167 AHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRtTFIISTHSSQLKER 217
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGK-TILLTTHFMEEAER 203
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
11-183 |
3.03e-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: 91.07 E-value: 3.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSGEgkvdALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAair 90
Cdd:cd03218 1 LRAENLSKRYGKRK----VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 91 GRHLGFIFQFFNLIPVLSVFDNVFfpLVLNGH-VGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHD 169
Cdd:cd03218 74 RLGIGYLPQEASIFRKLTVEENIL--AVLEIRgLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATN 151
|
170
....*....|....
gi 556463668 170 PQVVIADEPTGNLD 183
Cdd:cd03218 152 PKFLLLDEPFAGVD 165
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
11-230 |
4.29e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 91.99 E-value: 4.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSGEG-KVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMF--------LKKLlnhl 81
Cdd:PRK13645 7 IILDNVSYTYAKKTPfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgdyaipanLKKI---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 82 peEQLAAIRgRHLGFIFQFfnliPVLSVF------DNVFFPLVLNGHvgKKEARERALHFIESVGLA-GFTERKPGQLSG 154
Cdd:PRK13645 83 --KEVKRLR-KEIGLVFQF----PEYQLFqetiekDIAFGPVNLGEN--KQEAYKKVPELLKLVQLPeDYVKRSPFELSG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556463668 155 GQQQRVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQlkerarRVVEIKDGVLV 230
Cdd:PRK13645 154 GQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMD------QVLRIADEVIV 223
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
28-179 |
6.18e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 93.54 E-value: 6.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 28 DALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNH-------------LPEEqlaaiRgRHL 94
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIrsprdairagiayVPED-----R-KGE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 95 GfifqffnLIPVLSVFDNVFFP----LVLNGHVGKKEARERALHFIESVGL-AGFTERKPGQLSGGQQQRVAIARALAHD 169
Cdd:COG1129 340 G-------LVLDLSIRENITLAsldrLSRGGLLDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATD 412
|
170
....*....|
gi 556463668 170 PQVVIADEPT 179
Cdd:COG1129 413 PKVLILDEPT 422
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
30-224 |
8.16e-22 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 89.09 E-value: 8.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 30 LKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVmflkkLLNHLPEEQLAAIRGRHLGFIFQFFNLIPVLSV 109
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRV-----LLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 110 FDNVFFPLVLNGhvgkKEARERALhfiESVGLAGFTERKPGQLSGGQQQRVAIARALAHDPQVVIADEPTGNLDlVTGEA 189
Cdd:cd03231 91 LENLRFWHADHS----DEQVEEAL---ARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD-KAGVA 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 556463668 190 ILDLLLKINQETRTTFIISTHSS-QLKERARRVVEI 224
Cdd:cd03231 163 RFAEAMAGHCARGGMVVLTTHQDlGLSEAGARELDL 198
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
23-196 |
1.77e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 92.01 E-value: 1.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 23 GEGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPeeqLAAIRGRHLGFI---FQ 99
Cdd:COG3845 267 DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLS---PRERRRLGVAYIpedRL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 100 FFNLIPVLSVFDNVFF------PLVLNGHVGKKEARERALHFIE--SVGLAGfTERKPGQLSGGQQQRVAIARALAHDPQ 171
Cdd:COG3845 344 GRGLVPDMSVAENLILgryrrpPFSRGGFLDRKAIRAFAEELIEefDVRTPG-PDTPARSLSGGNQQKVILARELSRDPK 422
|
170 180
....*....|....*....|....*
gi 556463668 172 VVIADEPTGNLDLVTGEAILDLLLK 196
Cdd:COG3845 423 LLIAAQPTRGLDVGAIEFIHQRLLE 447
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
30-212 |
2.61e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 88.01 E-value: 2.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 30 LKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVmflkKLLNHLPEEQLAAIRGRHLGFIfqffN-LIPVLS 108
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTI----KLDGGDIDDPDVAEACHYLGHR----NaMKPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 109 VFDNV-FFPLVLNGHvgkkeaRERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHDPQVVIADEPTGNLDlVTG 187
Cdd:PRK13539 90 VAENLeFWAAFLGGE------ELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD-AAA 162
|
170 180
....*....|....*....|....*
gi 556463668 188 EAILDLLLKINQETRTTFIISTHSS 212
Cdd:PRK13539 163 VALFAELIRAHLAQGGIVIAATHIP 187
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
27-235 |
3.13e-21 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 89.08 E-value: 3.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 27 VDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMflkkLLNHLPEEQLAAIRGRHLGFIFQ--FFNLI 104
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELL----IDDHPLHFGDYSYRSQRIRMIFQdpSTSLN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 105 PVLSVFDNVFFPLVLNGHVGKKEARERALHFIESVGL-AGFTERKPGQLSGGQQQRVAIARALAHDPQVVIADEPTGNLD 183
Cdd:PRK15112 102 PRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 556463668 184 LVTGEAILDLLLKINQETRTTFIIST-HSSQLKERARRVVEIKDGVLVHDSQT 235
Cdd:PRK15112 182 MSMRSQLINLMLELQEKQGISYIYVTqHLGMMKHISDQVLVMHQGEVVERGST 234
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
9-230 |
3.42e-21 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 91.22 E-value: 3.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSYGSgegkVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKK--LLNHLPEEQL 86
Cdd:PRK10762 3 ALLQLKGIDKAFPG----VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKevTFNGPKSSQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 87 AAIrgrhlGFIFQFFNLIPVLSVFDNVFFPLVLNGHVGK---KEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIA 163
Cdd:PRK10762 79 AGI-----GIIHQELNLIPQLTIAENIFLGREFVNRFGRidwKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556463668 164 RALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIIStHssQLKErarrVVEIKDGVLV 230
Cdd:PRK10762 154 KVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYIS-H--RLKE----IFEICDDVTV 213
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
24-210 |
4.11e-21 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 89.58 E-value: 4.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 24 EGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKP----TVGTVMFLKKLLNHLPEEQLAAIRGRHLGFIFQ 99
Cdd:COG4170 17 QGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPRERRKIIGREIAMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 100 --FFNLIPVLSVFDNVFFPL---VLNGHV--GKKEARERALHFIESVG-------LAGFterkPGQLSGGQQQRVAIARA 165
Cdd:COG4170 97 epSSCLDPSAKIGDQLIEAIpswTFKGKWwqRFKWRKKRAIELLHRVGikdhkdiMNSY----PHELTEGECQKVMIAMA 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 556463668 166 LAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTH 210
Cdd:COG4170 173 IANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISH 217
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
9-178 |
5.98e-21 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 87.78 E-value: 5.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSYGsgegKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQlaa 88
Cdd:COG1137 2 MTLEAENLVKSYG----KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHK--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 89 iRGRH-LGF------IFQffnlipVLSVFDNVFfpLVLNGH-VGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRV 160
Cdd:COG1137 75 -RARLgIGYlpqeasIFR------KLTVEDNIL--AVLELRkLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRV 145
|
170
....*....|....*...
gi 556463668 161 AIARALAHDPQVVIADEP 178
Cdd:COG1137 146 EIARALATNPKFILLDEP 163
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
9-229 |
9.20e-21 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 88.02 E-value: 9.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSYGSGEgkvDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAA 88
Cdd:PRK15056 5 AGIVVNDVTVTWRNGH---TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 89 IRGRHLGFIFQFfnliPVLsVFDNVFfpLVLNGHVG-----KKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIA 163
Cdd:PRK15056 82 YVPQSEEVDWSF----PVL-VEDVVM--MGRYGHMGwlrraKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556463668 164 RALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRtTFIISTHS-SQLKERARRVVEIKDGVL 229
Cdd:PRK15056 155 RAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGK-TMLVSTHNlGSVTEFCDYTVMVKGTVL 220
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-230 |
1.18e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 89.90 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 22 SGEGKVdALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIdKPTVGTVMFLKKLLNHLPEEQLAairgRHLGFIFQff 101
Cdd:PRK11174 359 SPDGKT-LAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDPESWR----KHLSWVGQ-- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 102 N-LIPVLSVFDNVFFplvlnghvGKKEARERAL-HFIESVGLAGFTERKP-----------GQLSGGQQQRVAIARALAH 168
Cdd:PRK11174 431 NpQLPHGTLRDNVLL--------GNPDASDEQLqQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQ 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556463668 169 DPQVVIADEPTGNLDLVTGEAILDLLLKINQeTRTTFIIsTHS-SQLKERARRVVeIKDGVLV 230
Cdd:PRK11174 503 PCQLLLLDEPTASLDAHSEQLVMQALNAASR-RQTTLMV-THQlEDLAQWDQIWV-MQDGQIV 562
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
8-210 |
1.80e-20 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 89.69 E-value: 1.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 8 LPMISLNNIYKSYG-SGEGKVDALkniNLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLnhlpEEQL 86
Cdd:TIGR01257 926 VPGVCVKNLVKIFEpSGRPAVDRL---NITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNL 998
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 87 AAIRgRHLGFIFQFFNLIPVLSVFDNVFFPLVLNGHvGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARAL 166
Cdd:TIGR01257 999 DAVR-QSLGMCPQHNILFHHLTVAEHILFYAQLKGR-SWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAF 1076
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 556463668 167 AHDPQVVIADEPTGNLDLVTGEAILDLLLKInqETRTTFIISTH 210
Cdd:TIGR01257 1077 VGDAKVVVLDEPTSGVDPYSRRSIWDLLLKY--RSGRTIIMSTH 1118
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
11-235 |
2.07e-20 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 89.39 E-value: 2.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSGEgkvDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVmflkkLLNHLPEEQL--AA 88
Cdd:PRK10790 341 IDIDNVSFAYRDDN---LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEI-----RLDGRPLSSLshSV 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 89 IRgRHLGFIFQffnlIPVL---SVFDNVffplvlngHVGKKEARERALHFIESVGLAGFTERKPG-----------QLSG 154
Cdd:PRK10790 413 LR-QGVAMVQQ----DPVVladTFLANV--------TLGRDISEEQVWQALETVQLAELARSLPDglytplgeqgnNLSV 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 155 GQQQRVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQetRTTFIISTHssqlkeRARRVVEiKDGVLV-HDS 233
Cdd:PRK10790 480 GQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVRE--HTTLVVIAH------RLSTIVE-ADTILVlHRG 550
|
..
gi 556463668 234 QT 235
Cdd:PRK10790 551 QA 552
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
30-230 |
2.60e-20 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 89.01 E-value: 2.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 30 LKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVmflkkLLNHLPEEQL--AAIRgRHLGFIFQFfnliPVL 107
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQV-----LLDGVPLVQYdhHYLH-RQVALVGQE----PVL 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 108 ---SVFDNVFFPL-------VLNGhvgkkeARERALH-FIESVGLAGFTE--RKPGQLSGGQQQRVAIARALAHDPQVVI 174
Cdd:TIGR00958 567 fsgSVRENIAYGLtdtpdeeIMAA------AKAANAHdFIMEFPNGYDTEvgEKGSQLSGGQKQRIAIARALVRKPRVLI 640
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 556463668 175 ADEPTGNLDLVTGEAILDLLlkiNQETRTTFIIsTHSSQLKERARRVVEIKDGVLV 230
Cdd:TIGR00958 641 LDEATSALDAECEQLLQESR---SRASRTVLLI-AHRLSTVERADQILVLKKGSVV 692
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
30-230 |
3.00e-20 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 86.05 E-value: 3.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 30 LKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIdKPTVGTVMFLKKLLNHLPEEQLAairgRHLGFIFQFFNLIPVLSV 109
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAELA----RHRAYLSQQQSPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 110 FDNvffpLVLNGH-VGKKEARERALHFI-ESVGLAGFTERKPGQLSGGQQQRVAIARALAH-------DPQVVIADEPTG 180
Cdd:COG4138 87 FQY----LALHQPaGASSEAVEQLLAQLaEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMN 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 556463668 181 NLDlVTGEAILDLLL-KINQETRTTfIISTHSSQLKER-ARRVVEIKDGVLV 230
Cdd:COG4138 163 SLD-VAQQAALDRLLrELCQQGITV-VMSSHDLNHTLRhADRVWLLKQGKLV 212
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
11-217 |
3.23e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 87.58 E-value: 3.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGsGEGKVDALkniNLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKkllnhLPEEQLAAIR 90
Cdd:PRK13536 42 IDLAGVSKSYG-DKAVVNGL---SFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG-----VPVPARARLA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 91 GRHLGFIFQFFNLIPVLSVFDNvffpLVLNGHVGKKEAREralhfIESV--GLAGFT--ERKP----GQLSGGQQQRVAI 162
Cdd:PRK13536 113 RARIGVVPQFDNLDLEFTVREN----LLVFGRYFGMSTRE-----IEAVipSLLEFArlESKAdarvSDLSGGMKRRLTL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 556463668 163 ARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRtTFIISTHSSQLKER 217
Cdd:PRK13536 184 ARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGK-TILLTTHFMEEAER 237
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
32-211 |
4.18e-20 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 87.24 E-value: 4.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 32 NINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLN------HLPEEQlaairgRHLGFIFQFFNLIP 105
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFdaekgiCLPPEK------RRIGYVFQDARLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 106 VLSVFDNVFFPLvlnghvgkkeARERALHFIESVGLAGFT---ERKPGQLSGGQQQRVAIARALAHDPQVVIADEPTGNL 182
Cdd:PRK11144 90 HYKVRGNLRYGM----------AKSMVAQFDKIVALLGIEpllDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASL 159
|
170 180
....*....|....*....|....*....
gi 556463668 183 DLVTGEAILDLLLKINQETRTTFIISTHS 211
Cdd:PRK11144 160 DLPRKRELLPYLERLAREINIPILYVSHS 188
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
33-230 |
1.13e-19 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 84.60 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 33 INLEIEKGEFLALCGPSGSGKSTLLNILSGIdKPTVGTVMFLKKLLNHLPEEQLAairgRHLGFIFQffNLIPVLSVfdN 112
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELA----RHRAYLSQ--QQTPPFAM--P 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 113 VFFPLVLNGHVG-KKEARERALHFI-ESVGLAGFTERKPGQLSGGQQQRVAIA-------RALAHDPQVVIADEPTGNLD 183
Cdd:PRK03695 86 VFQYLTLHQPDKtRTEAVASALNEVaEALGLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNSLD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 556463668 184 lVTGEAILDLLLKINQETRTTFIISTHS-SQLKERARRVVEIKDGVLV 230
Cdd:PRK03695 166 -VAQQAALDRLLSELCQQGIAVVMSSHDlNHTLRHADRVWLLKQGKLL 212
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-211 |
1.23e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 84.70 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 6 KELPMISLNNIYKSYGSGEgkvdALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDK-----PTVGTVMFLKKllnH 80
Cdd:PRK14258 3 KLIPAIKVNNLSFYYDTQK----ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQ---N 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 81 LPEEQLAAIR-GRHLGFIFQFFNLIPvLSVFDNVFFPLVLNGHVGKKEARERALHFIESVGLAGFTERK----PGQLSGG 155
Cdd:PRK14258 76 IYERRVNLNRlRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIKHKihksALDLSGG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 556463668 156 QQQRVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHS 211
Cdd:PRK14258 155 QQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHN 210
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
23-230 |
1.50e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 84.65 E-value: 1.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 23 GEGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAairgRHLGFIFQFFN 102
Cdd:PRK10253 16 GYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA----RRIGLLAQNAT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 103 LIPVLSVFDnvffpLVLNGHVG--------KKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHDPQVVI 174
Cdd:PRK10253 92 TPGDITVQE-----LVARGRYPhqplftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 556463668 175 ADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHS-SQLKERARRVVEIKDGVLV 230
Cdd:PRK10253 167 LDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDlNQACRYASHLIALREGKIV 223
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
24-233 |
1.77e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 84.37 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 24 EGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVmflKKLLNHLPEEQLAAIRgRHLGFIFQF-FN 102
Cdd:PRK13642 17 ESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKV---KIDGELLTAENVWNLR-RKIGMVFQNpDN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 103 LIPVLSVFDNVFFPLVLNGhVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHDPQVVIADEPTGNL 182
Cdd:PRK13642 93 QFVGATVEDDVAFGMENQG-IPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSML 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 556463668 183 DLVTGEAILDLLLKINQETRTTFIISTHSSQLKERARRVVEIKDGVLVHDS 233
Cdd:PRK13642 172 DPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEA 222
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
32-178 |
2.53e-19 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 82.54 E-value: 2.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 32 NINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEE---QLAAIrGRHLGfifqffnLIPVLS 108
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEyhqDLLYL-GHQPG-------IKTELT 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 109 VFDNVFFPLVLNGHVGKkEARERALhfiESVGLAGFTERKPGQLSGGQQQRVAIARALAHDPQVVIADEP 178
Cdd:PRK13538 91 ALENLRFYQRLHGPGDD-EALWEAL---AQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEP 156
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
21-216 |
2.66e-19 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 83.08 E-value: 2.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 21 GSGEGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGI--DKPTVGTVMFLKkllNHLPEEqlaairgrhlgfif 98
Cdd:COG2401 37 ELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAlkGTPVAGCVDVPD---NQFGRE-------------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 99 qffnlipvLSVFDnvffplvlngHVGKKEARERALHFIESVGL--AGFTERKPGQLSGGQQQRVAIARALAHDPQVVIAD 176
Cdd:COG2401 100 --------ASLID----------AIGRKGDFKDAVELLNAVGLsdAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVID 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 556463668 177 EPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQLKE 216
Cdd:COG2401 162 EFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVID 201
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
44-235 |
1.16e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 82.45 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 44 ALCGPSGSGKSTLLNILSGIDKPTVG------TVMFLKKLLNHlpeEQLAAIRgRHLGFIFQFFNLIPvLSVFDNVFFPL 117
Cdd:PRK14271 51 SLMGPTGSGKTTFLRTLNRMNDKVSGyrysgdVLLGGRSIFNY---RDVLEFR-RRVGMLFQRPNPFP-MSIMDNVLAGV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 118 VLNGHVGKKEARERALHFIESVGLAGFTERK----PGQLSGGQQQRVAIARALAHDPQVVIADEPTGNLDLVTGEAILDL 193
Cdd:PRK14271 126 RAHKLVPRKEFRGVAQARLTEVGLWDAVKDRlsdsPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEF 205
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 556463668 194 LLKINQetRTTFIISTHS-SQLKERARRVVEIKDGVLVHDSQT 235
Cdd:PRK14271 206 IRSLAD--RLTVIIVTHNlAQAARISDRAALFFDGRLVEEGPT 246
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
9-214 |
1.22e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 81.70 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSYGSGEgkvdALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVmflkkllnhlpeEQLAA 88
Cdd:PRK09544 3 SLVSLENVSVSFGQRR----VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------------KRNGK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 89 IRgrhLGFIFQFFNLIPVLSVFDNVFF---PLVLNGHVGKKEARERALHFIESvglagfterkPGQ-LSGGQQQRVAIAR 164
Cdd:PRK09544 67 LR---IGYVPQKLYLDTTLPLTVNRFLrlrPGTKKEDILPALKRVQAGHLIDA----------PMQkLSGGETQRVLLAR 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 556463668 165 ALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQL 214
Cdd:PRK09544 134 ALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHL 183
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
11-226 |
2.55e-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: 2.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIykSYGSGEGKVdALKNINLEIEKGEFLALCGPSGSGKSTLLNILSG--------IDKPTVGTVMFLkkllnhlP 82
Cdd:cd03223 1 IELENL--SLATPDGRV-LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGlwpwgsgrIGMPEGEDLLFL-------P 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 83 EEQLaairgrhlgfifqffnlIPVLSVFDNVFFPLvlnGHVgkkeareralhfiesvglagfterkpgqLSGGQQQRVAI 162
Cdd:cd03223 71 QRPY-----------------LPLGTLREQLIYPW---DDV----------------------------LSGGEQQRLAF 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556463668 163 ARALAHDPQVVIADEPTGNLDlvtgEAILDLLLKINQETRTTFIISTHSSQLKERARRVVEIKD 226
Cdd:cd03223 103 ARLLLHKPKFVFLDEATSALD----EESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
29-230 |
2.57e-18 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 83.14 E-value: 2.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 29 ALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMflkkLLNH-LPEEQLAAIRgRHLGFIFQ---FFNLi 104
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEIL----LDGHdLRDYTLASLR-NQVALVSQnvhLFND- 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 105 pvlSVFDNVFFPlvlnghVGKKEARER---------ALHFIESV--GLAGFTERKPGQLSGGQQQRVAIARALAHDPQVV 173
Cdd:PRK11176 432 ---TIANNIAYA------RTEQYSREQieeaarmayAMDFINKMdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPIL 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 174 IADEPTGNLDLVTGEAI---LDLLlkinQETRTTFIISTHSSQLkERARRVVEIKDGVLV 230
Cdd:PRK11176 503 ILDEATSALDTESERAIqaaLDEL----QKNRTSLVIAHRLSTI-EKADEILVVEDGEIV 557
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
15-186 |
3.33e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 80.32 E-value: 3.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 15 NIYKSYgsgEGKvDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAAirgRHL 94
Cdd:PRK10895 8 NLAKAY---KGR-RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARAR---RGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 95 GFIFQFFNLIPVLSVFDNVFFPLVLNGHVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHDPQVVI 174
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170
....*....|..
gi 556463668 175 ADEPTGNLDLVT 186
Cdd:PRK10895 161 LDEPFAGVDPIS 172
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
30-209 |
5.72e-18 |
|
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: 82.18 E-value: 5.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 30 LKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVmflkkLLNH--LPEEQLAAIRgRHLGFIFQ---FFNli 104
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRI-----LIDGqdIRDVTQASLR-AAIGIVPQdtvLFN-- 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 105 pvlsvfDNVFFplvlNGHVGKKEARE-------RALH---FIES--------VGlagftER--KpgqLSGGQQQRVAIAR 164
Cdd:COG5265 446 ------DTIAY----NIAYGRPDASEeeveaaaRAAQihdFIESlpdgydtrVG-----ERglK---LSGGEKQRVAIAR 507
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 556463668 165 ALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQEtRTTFII----ST 209
Cdd:COG5265 508 TLLKNPPILIFDEATSALDSRTERAIQAALREVARG-RTTLVIahrlST 555
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
9-230 |
8.60e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 81.64 E-value: 8.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSYGSgegkVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQlAA 88
Cdd:PRK15439 10 PLLCARSISKQYSG----VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAK-AH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 89 IRGRHLgfIFQFFNLIPVLSVFDNVFFPLvlnghVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAH 168
Cdd:PRK15439 85 QLGIYL--VPQEPLLFPNLSVKENILFGL-----PKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556463668 169 DPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQLKERARRVVEIKDGVLV 230
Cdd:PRK15439 158 DSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIA 219
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
30-230 |
1.22e-17 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 77.95 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 30 LKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTV--GTVMFLKKLLNHLPEEQLAAiRGrhLGFIFQFFNLIPVL 107
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVteGEILFKGEDITDLPPEERAR-LG--IFLAFQYPPEIPGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 108 SVfdnvffplvlnghvgkkeareraLHFIESVGlAGFterkpgqlSGGQQQRVAIARALAHDPQVVIADEPTGNLDLVTG 187
Cdd:cd03217 93 KN-----------------------ADFLRYVN-EGF--------SGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDAL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 556463668 188 EAILDLLLKINQETrTTFIISTHSSQLKE--RARRVVEIKDGVLV 230
Cdd:cd03217 141 RLVAEVINKLREEG-KSVLIITHYQRLLDyiKPDRVHVLYDGRIV 184
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
11-194 |
2.43e-17 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 77.53 E-value: 2.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSGEGKVdaLKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPeeqLAAIR 90
Cdd:cd03244 3 IEFKNVSLRYRPNLPPV--LKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG---LHDLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 91 gRHLGFIFQffnlIPVL---SVFDNVFFplvLNGHvgKKEARERALhfiESVGLAGFTERKPGQL-----------SGGQ 156
Cdd:cd03244 78 -SRISIIPQ----DPVLfsgTIRSNLDP---FGEY--SDEELWQAL---ERVGLKEFVESLPGGLdtvveeggenlSVGQ 144
|
170 180 190
....*....|....*....|....*....|....*...
gi 556463668 157 QQRVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLL 194
Cdd:cd03244 145 RQLLCLARALLRKSKILVLDEATASVDPETDALIQKTI 182
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
8-214 |
3.49e-17 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 79.08 E-value: 3.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 8 LPMISLNNIYKSYGSGEGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKP----TVGTVMFLKKLLNHLPE 83
Cdd:PRK15093 1 MPLLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 84 EQLAAIRGRHLGFIFQFFN--LIPVLSVFDNVFFPLVLNGHVGKKEAR-----ERALHFIESVGLAGFTE---RKPGQLS 153
Cdd:PRK15093 81 RERRKLVGHNVSMIFQEPQscLDPSERVGRQLMQNIPGWTYKGRWWQRfgwrkRRAIELLHRVGIKDHKDamrSFPYELT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556463668 154 GGQQQRVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQL 214
Cdd:PRK15093 161 EGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQM 221
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
29-210 |
3.92e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 79.78 E-value: 3.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 29 ALKNINLEIEKGE---FLalcGPSGSGKSTLLNILSGIDKPTVGTVmflkKLLNHLPEEQLAAIRgRHLGFIFQFFNLIP 105
Cdd:NF033858 281 AVDHVSFRIRRGEifgFL---GSNGCGKSTTMKMLTGLLPASEGEA----WLFGQPVDAGDIATR-RRVGYMSQAFSLYG 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 106 VLSVFDNvffpLVLNG---HVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHDPQVVIADEPTGNL 182
Cdd:NF033858 353 ELTVRQN----LELHArlfHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGV 428
|
170 180
....*....|....*....|....*...
gi 556463668 183 DLVTGEAILDLLLKINQETRTTFIISTH 210
Cdd:NF033858 429 DPVARDMFWRLLIELSREDGVTIFISTH 456
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
30-214 |
3.88e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 74.72 E-value: 3.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 30 LKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDK--PTVGTVMFLKKLLNHLPEEQLAAiRGrhLGFIFQFFNLIPVL 107
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSPDERAR-AG--IFLAFQYPVEIPGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 108 SVFDnvFFPLVLNGHVGKK----EARERALHFIESVGLA----------GFterkpgqlSGGQQQRVAIARALAHDPQVV 173
Cdd:COG0396 93 SVSN--FLRTALNARRGEElsarEFLKLLKEKMKELGLDedfldryvneGF--------SGGEKKRNEILQMLLLEPKLA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 556463668 174 IADEPTGNLDLvtgEAILDLLLKINQ--ETRTTFIISTHSSQL 214
Cdd:COG0396 163 ILDETDSGLDI---DALRIVAEGVNKlrSPDRGILIITHYQRI 202
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
28-210 |
1.58e-15 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 75.13 E-value: 1.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 28 DALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKllnHLPEEQLAAIRGRhlgfiFQFFNLIPVL 107
Cdd:PRK10789 329 PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDI---PLTKLQLDSWRSR-----LAVVSQTPFL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 108 ---SVFDNVffplvlngHVGKKEARERAlhfIESVG-LAGFTE---RKP-------GQ----LSGGQQQRVAIARALAHD 169
Cdd:PRK10789 401 fsdTVANNI--------ALGRPDATQQE---IEHVArLASVHDdilRLPqgydtevGErgvmLSGGQKQRISIARALLLN 469
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 556463668 170 PQVVIADEPTGNLDLVTGEAILDLLLKINQEtrTTFIISTH 210
Cdd:PRK10789 470 AEILILDDALSAVDGRTEHQILHNLRQWGEG--RTVIISAH 508
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
9-234 |
1.61e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.09 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIyksygSGEGkvdaLKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMF-------------LK 75
Cdd:PRK15439 267 PVLTVEDL-----TGEG----FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLngkeinalstaqrLA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 76 KLLNHLPEEQLAAirGRHLGFIFQFfNlIPVLSVFDNVFFplvlnghvgKKEARERAL--HFIESVGLAGFTERKP-GQL 152
Cdd:PRK15439 338 RGLVYLPEDRQSS--GLYLDAPLAW-N-VCALTHNRRGFW---------IKPARENAVleRYRRALNIKFNHAEQAaRTL 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 153 SGGQQQRVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKI-NQETRTTFIisthSSQLKErarrVVEIKDGVLV- 230
Cdd:PRK15439 405 SGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIaAQNVAVLFI----SSDLEE----IEQMADRVLVm 476
|
....
gi 556463668 231 HDSQ 234
Cdd:PRK15439 477 HQGE 480
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
30-230 |
2.90e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 72.73 E-value: 2.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 30 LKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHlPEEQLAAIRgRHLGFIFQffnlIPVLSV 109
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDY-SKRGLLALR-QQVATVFQ----DPEQQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 110 F-----DNVFFPLvLNGHVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHDPQVVIADEPTGNLDL 184
Cdd:PRK13638 91 FytdidSDIAFSL-RNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 556463668 185 VTGEAILDLLLKINQETRTTfIISTHSSQLkerarrVVEIKDGVLV 230
Cdd:PRK13638 170 AGRTQMIAIIRRIVAQGNHV-IISSHDIDL------IYEISDAVYV 208
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
30-232 |
6.18e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 71.78 E-value: 6.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 30 LKNINLEIEKGEFLALCGPSGSGKSTLLNILSGiDKP---------TVGTVMFLKKLLNHLPEEQLAAIRG-----RHLG 95
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG-DLTgggaprgarVTGDVTLNGEPLAAIDAPRLARLRAvlpqaAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 96 FIFqffnlipvlSVFDNVF---FPLVLNGHVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAH---- 168
Cdd:PRK13547 96 FAF---------SAREIVLlgrYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpp 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 169 -----DPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQLKER-ARRVVEIKDGVLVHD 232
Cdd:PRK13547 167 hdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARhADRIAMLADGAIVAH 236
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
6-229 |
6.92e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 73.62 E-value: 6.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 6 KELPMISLNNIYKSYGSgEGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPeeQ 85
Cdd:PLN03130 610 PGLPAISIKNGYFSWDS-KAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVIRGTVAYVP--Q 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 86 LAAIrgrhlgfifqfFNLipvlSVFDNVFFplvlnGHVGKKEARERAlhfIESVGLAGFTERKPG-----------QLSG 154
Cdd:PLN03130 687 VSWI-----------FNA----TVRDNILF-----GSPFDPERYERA---IDVTALQHDLDLLPGgdlteigergvNISG 743
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556463668 155 GQQQRVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLK--INQETRttfIISTHSSQLKERARRVVEIKDGVL 229
Cdd:PLN03130 744 GQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKdeLRGKTR---VLVTNQLHFLSQVDRIILVHEGMI 817
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
40-230 |
7.30e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 73.38 E-value: 7.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 40 GEFLALCGPSGSGKSTLLNILSGidkpTVGTVMFLKKLL--NHLPEEQLAairgRHLGFIFQFFNLIPVLSVFDNVFFP- 116
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAG----RIQGNNFTGTILanNRKPTKQIL----KRTGFVTQDDILYPHLTVRETLVFCs 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 117 -LVLNGHVGKKEARERALHFIESVGLAGFTERKPGQ-----LSGGQQQRVAIARALAHDPQVVIADEPTGNLDLVTGEAI 190
Cdd:PLN03211 166 lLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRL 245
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 556463668 191 LDLLLKINQETRtTFIISTHssqlkERARRVVEIKDGVLV 230
Cdd:PLN03211 246 VLTLGSLAQKGK-TIVTSMH-----QPSSRVYQMFDSVLV 279
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
11-227 |
9.33e-15 |
|
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: 70.44 E-value: 9.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSGegkVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNhlpEEQLAAIR 90
Cdd:cd03290 1 VQVTNGYFSWGSG---LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNES---EPSFEATR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 91 GRHLGFIfQFFNLIPVL---SVFDNVFFPLVLNGHvgKKEARERALHFIESVGLAGFTER-----KPGQLSGGQQQRVAI 162
Cdd:cd03290 75 SRNRYSV-AYAAQKPWLlnaTVEENITFGSPFNKQ--RYKAVTDACSLQPDIDLLPFGDQteigeRGINLSGGQRQRICV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556463668 163 ARALAHDPQVVIADEPTGNLDLVTGEAILDL-LLKINQETRTTFIISTHSSQLKERARRVVEIKDG 227
Cdd:cd03290 152 ARALYQNTNIVFLDDPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
30-228 |
1.62e-14 |
|
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: 72.25 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 30 LKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVmflkkllnhlpeeqlaairgRHLG---FIFQFFNLIPV 106
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI--------------------KHSGrisFSPQTSWIMPG 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 107 lSVFDNVFFPLVLNGH-----VGKKEARERALHFIES----VGLAGFTerkpgqLSGGQQQRVAIARALAHDPQVVIADE 177
Cdd:TIGR01271 502 -TIKDNIIFGLSYDEYrytsvIKACQLEEDIALFPEKdktvLGEGGIT------LSGGQRARISLARAVYKDADLYLLDS 574
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 556463668 178 PTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQLKeRARRVVEIKDGV 228
Cdd:TIGR01271 575 PFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLK-KADKILLLHEGV 624
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
12-230 |
1.65e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 71.87 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 12 SLNNIY----KSYGSGEGKVDALKN------INLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNhl 81
Cdd:PRK11288 241 EIGDIYgyrpRPLGEVRLRLDGLKGpglrepISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID-- 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 82 PEEQLAAIRGrhlGFIF-----QFFNLIPVLSVFDNV---------FFPLVLNGhvgKKEArERALHFIESvgLAGFT-- 145
Cdd:PRK11288 319 IRSPRDAIRA---GIMLcpedrKAEGIIPVHSVADNInisarrhhlRAGCLINN---RWEA-ENADRFIRS--LNIKTps 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 146 -ERKPGQLSGGQQQRVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIIsthSSQLKErarrVVEI 224
Cdd:PRK11288 390 rEQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFV---SSDLPE----VLGV 462
|
....*.
gi 556463668 225 KDGVLV 230
Cdd:PRK11288 463 ADRIVV 468
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
33-210 |
2.34e-14 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 69.49 E-value: 2.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 33 INLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMflkklLNHLPEEQlaAIRGRHLGFIFQFFNLIPVLSVFDN 112
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQ-----IDGKTATR--GDRSRFMAYLGHLPGLKADLSTLEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 113 VFFplvLNGHVGKKeARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHDPQVVIADEPTGNLDLvTGEAILD 192
Cdd:PRK13543 103 LHF---LCGLHGRR-AKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL-EGITLVN 177
|
170
....*....|....*...
gi 556463668 193 LLLKINQETRTTFIISTH 210
Cdd:PRK13543 178 RMISAHLRGGGAALVTTH 195
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
30-227 |
4.38e-14 |
|
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: 69.89 E-value: 4.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 30 LKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVmflkkllnhlpeeqlaairgRHLG---FIFQFFNLIPV 106
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI--------------------KHSGrisFSSQFSWIMPG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 107 lSVFDNVFFPLVLNGHVGKK-----EARERALHFIES----VGLAGFTerkpgqLSGGQQQRVAIARALAHDPQVVIADE 177
Cdd:cd03291 113 -TIKENIIFGVSYDEYRYKSvvkacQLEEDITKFPEKdntvLGEGGIT------LSGGQRARISLARAVYKDADLYLLDS 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 556463668 178 PTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQLKeRARRVVEIKDG 227
Cdd:cd03291 186 PFGYLDVFTEKEIFESCVCKLMANKTRILVTSKMEHLK-KADKILILHEG 234
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
11-208 |
9.56e-14 |
|
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: 67.29 E-value: 9.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSGEGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTV---GTVMFlkkllNHLPEEQLA 87
Cdd:cd03233 4 LSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHY-----NGIPYKEFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 88 AIRGRHLGFIFQFFNLIPVLSVFDNVFFPLVLNGHvgkkeareralhfiESVglagfteRKpgqLSGGQQQRVAIARALA 167
Cdd:cd03233 79 EKYPGEIIYVSEEDVHFPTLTVRETLDFALRCKGN--------------EFV-------RG---ISGGERKRVSIAEALV 134
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 556463668 168 HDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIIS 208
Cdd:cd03233 135 SRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVS 175
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
38-183 |
1.14e-13 |
|
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: 69.43 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 38 EKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVmflkkllNHLP--EEQLAAIRGRHLGFIF--------------QFF 101
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDY-------DEEPswDEVLKRFRGTELQDYFkklangeikvahkpQYV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 102 NLIPvlsvfdnvffpLVLNGHVG----KKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHDPQVVIADE 177
Cdd:COG1245 170 DLIP-----------KVFKGTVRelleKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
....*.
gi 556463668 178 PTGNLD 183
Cdd:COG1245 239 PSSYLD 244
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
30-217 |
1.50e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 67.89 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 30 LKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAairgRHLGFIFQFFNLIPVLSV 109
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFA----RKVAYLPQQLPAAEGMTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 110 FDNVF---FPLvlNGHVGK--KEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHDPQVVIADEPTGNLDL 184
Cdd:PRK10575 103 RELVAigrYPW--HGALGRfgAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI 180
|
170 180 190
....*....|....*....|....*....|...
gi 556463668 185 VTGEAILDLLLKINQETRTTFIISTHSSQLKER 217
Cdd:PRK10575 181 AHQVDVLALVHRLSQERGLTVIAVLHDINMAAR 213
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
40-184 |
2.38e-13 |
|
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: 67.39 E-value: 2.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 40 GEFLALCGPSGSGKSTLLNILSGIDKPTVG---------TVM--F----LKKLLNHLPEEQLAAIRGRhlgfifQFFNLI 104
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGkfddppdwdEILdeFrgseLQNYFTKLLEGDVKVIVKP------QYVDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 105 PvlSVFDnvffplvlnGHVG----KKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHDPQVVIADEPTG 180
Cdd:cd03236 100 P--KAVK---------GKVGellkKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSS 168
|
....
gi 556463668 181 NLDL 184
Cdd:cd03236 169 YLDI 172
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
31-229 |
3.68e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.89 E-value: 3.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 31 KNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNhlPEEQLAAIRgRHLGFIFQffnlipvlSVF 110
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS--PRSPLDAVK-KGMAYITE--------SRR 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 111 DNVFFP-------------LVLNGHVG-------KKEAR----ERALHFIESVGLagftERKPGQLSGGQQQRVAIARAL 166
Cdd:PRK09700 349 DNGFFPnfsiaqnmaisrsLKDGGYKGamglfheVDEQRtaenQRELLALKCHSV----NQNITELSGGNQQKVLISKWL 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556463668 167 AHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQLKERARRVVEIKDGVL 229
Cdd:PRK09700 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
37-183 |
4.86e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 67.91 E-value: 4.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 37 IEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVmflkkllNHLP--EEQLAAIRGRHLGFIF--------------QF 100
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDY-------EEEPswDEVLKRFRGTELQNYFkklyngeikvvhkpQY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 101 FNLIPVlsvfdnvffplVLNGHVGK--KEARER--ALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHDPQVVIAD 176
Cdd:PRK13409 169 VDLIPK-----------VFKGKVREllKKVDERgkLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFD 237
|
....*..
gi 556463668 177 EPTGNLD 183
Cdd:PRK13409 238 EPTSYLD 244
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
22-199 |
1.04e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.57 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 22 SGEGkvdaLKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTV-MFLKKLLNHLPEEQLAAirgrhlGFIF-- 98
Cdd:PRK10762 264 SGPG----VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVtLDGHEVVTRSPQDGLAN------GIVYis 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 99 ---QFFNLIPVLSVFDNVFFPLV-----LNGHVGKKEARERALHFIESvglagFTERKP------GQLSGGQQQRVAIAR 164
Cdd:PRK10762 334 edrKRDGLVLGMSVKENMSLTALryfsrAGGSLKHADEQQAVSDFIRL-----FNIKTPsmeqaiGLLSGGNQQKVAIAR 408
|
170 180 190
....*....|....*....|....*....|....*
gi 556463668 165 ALAHDPQVVIADEPTGNLDLVTGEAILDLllkINQ 199
Cdd:PRK10762 409 GLMTRPKVLILDEPTRGVDVGAKKEIYQL---INQ 440
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
10-213 |
1.20e-12 |
|
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: 66.96 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 10 MISLNNIYKSY-GSGEGKVDALkniNLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFL-KKLLNHLPEEQla 87
Cdd:TIGR01257 1937 ILRLNELTKVYsGTSSPAVDRL---CVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAgKSILTNISDVH-- 2011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 88 airgRHLGFIFQFFNLIPVLSVFDNVFFPLVLNGhVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALA 167
Cdd:TIGR01257 2012 ----QNMGYCPQFDAIDDLLTGREHLYLYARLRG-VPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALI 2086
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 556463668 168 HDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTfIISTHSSQ 213
Cdd:TIGR01257 2087 GCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAV-VLTSHSME 2131
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
8-195 |
1.59e-12 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 66.42 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 8 LPMISLNNiyKSYGSGEGKVdALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMflkkllnHLPEEQLA 87
Cdd:PLN03073 506 PPIISFSD--ASFGYPGGPL-LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF-------RSAKVRMA 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 88 AIRGRHlgfifqffnlIPVLSVFDNvffPLVLNGHV--GKKEARERAlhFIESVGLAGFTERKPG-QLSGGQQQRVAIAR 164
Cdd:PLN03073 576 VFSQHH----------VDGLDLSSN---PLLYMMRCfpGVPEQKLRA--HLGSFGVTGNLALQPMyTLSGGQKSRVAFAK 640
|
170 180 190
....*....|....*....|....*....|.
gi 556463668 165 ALAHDPQVVIADEPTGNLDLVTGEAILDLLL 195
Cdd:PLN03073 641 ITFKKPHILLLDEPSNHLDLDAVEALIQGLV 671
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
6-184 |
1.63e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 65.05 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 6 KELPMISLNNIYKSYGSGEgkvdALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTV--GTVMFLKKLLNHLPE 83
Cdd:CHL00131 3 KNKPILEIKNLHASVNENE----ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKIleGDILFKGESILDLEP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 84 EQLAairgrHLGFIFQFFNLIPVLSVFDNVFFPLVLNG---HVGKKEAreRALHFIE-------SVGL-AGFTERKPGQ- 151
Cdd:CHL00131 79 EERA-----HLGIFLAFQYPIEIPGVSNADFLRLAYNSkrkFQGLPEL--DPLEFLEiineklkLVGMdPSFLSRNVNEg 151
|
170 180 190
....*....|....*....|....*....|...
gi 556463668 152 LSGGQQQRVAIARALAHDPQVVIADEPTGNLDL 184
Cdd:CHL00131 152 FSGGEKKRNEILQMALLDSELAILDETDSGLDI 184
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
11-195 |
1.71e-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: 66.11 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGsgeGKVdALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLlnhlpeeqlaair 90
Cdd:TIGR03719 323 IEAENLTKAFG---DKL-LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETV------------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 91 grHLGFIFQFF-NLIPVLSVFDnvffpLVLNGH----VGKKEARERALhfiesVGLAGFT----ERKPGQLSGGQQQRVA 161
Cdd:TIGR03719 386 --KLAYVDQSRdALDPNKTVWE-----EISGGLdiikLGKREIPSRAY-----VGRFNFKgsdqQKKVGQLSGGERNRVH 453
|
170 180 190
....*....|....*....|....*....|....
gi 556463668 162 IARALAHDPQVVIADEPTGNLDLVTGEAILDLLL 195
Cdd:TIGR03719 454 LAKTLKSGGNVLLLDEPTNDLDVETLRALEEALL 487
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
13-182 |
1.89e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.91 E-value: 1.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 13 LNNIYKSYGSgegkVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLN-HLPEEQLAAirg 91
Cdd:PRK10982 1 MSNISKSFPG----VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALEN--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 92 rHLGFIFQFFNLIPVLSVFDNVF---FPL--VLNGHvgKKEARERALHFIEsVGLAGFTERKPGQLSGGQQQRVAIARAL 166
Cdd:PRK10982 74 -GISMVHQELNLVLQRSVMDNMWlgrYPTkgMFVDQ--DKMYRDTKAIFDE-LDIDIDPRAKVATLSVSQMQMIEIAKAF 149
|
170
....*....|....*.
gi 556463668 167 AHDPQVVIADEPTGNL 182
Cdd:PRK10982 150 SYNAKIVIMDEPTSSL 165
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
30-203 |
2.48e-12 |
|
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: 63.42 E-value: 2.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 30 LKNINLEIEKGEFLALCGPSGSGKSTLLNILSGidKPTVGTVMFlKKLLNHLPEEQLAAirgRHLGFIFQFFNLIPVLSV 109
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVITG-EILINGRPLDKNFQ---RSTGYVEQQDVHSPNLTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 110 fdnvffplvlnghvgkkeaRErALHFieSVGLAGfterkpgqLSGGQQQRVAIARALAHDPQVVIADEPTGNLDLVTGEA 189
Cdd:cd03232 97 -------------------RE-ALRF--SALLRG--------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYN 146
|
170
....*....|....
gi 556463668 190 ILDLLLKINQETRT 203
Cdd:cd03232 147 IVRFLKKLADSGQA 160
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
10-230 |
3.63e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 65.36 E-value: 3.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 10 MISLNNIYKSYGsgegkvDA--LKNINLEIEKGEFLALCGPSGSGKSTLLNILSG---IDKptvGTVMFLKKL-LNHLPE 83
Cdd:PRK11147 3 LISIHGAWLSFS------DAplLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGevlLDD---GRIIYEQDLiVARLQQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 84 EQLAAIRGrhlgfifqffnlipvlSVFDNVFFPLvlnGHVGKK-EARERALHFIES------------------------ 138
Cdd:PRK11147 74 DPPRNVEG----------------TVYDFVAEGI---EEQAEYlKRYHDISHLVETdpseknlnelaklqeqldhhnlwq 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 139 -----------VGLAGftERKPGQLSGGQQQRVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLkinqETRTTFI- 206
Cdd:PRK11147 135 lenrinevlaqLGLDP--DAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLK----TFQGSIIf 208
|
250 260
....*....|....*....|....
gi 556463668 207 ISTHSSQLKERARRVVEIKDGVLV 230
Cdd:PRK11147 209 ISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
9-208 |
4.87e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 65.00 E-value: 4.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSYGSGEGKvDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEeqlaa 88
Cdd:PLN03232 613 PAISIKNGYFSWDSKTSK-PTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRGSVAYVPQ----- 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 89 irgrhLGFIFQffnlipvLSVFDNVFFplvlnghvGKKEARERALHFIESVGLAGFTERKPGQ-----------LSGGQQ 157
Cdd:PLN03232 687 -----VSWIFN-------ATVRENILF--------GSDFESERYWRAIDVTALQHDLDLLPGRdlteigergvnISGGQK 746
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 556463668 158 QRVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIIS 208
Cdd:PLN03232 747 QRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVT 797
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
29-229 |
2.02e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 63.07 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 29 ALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVmflkkLLNHLP--EEQLAAIRgRHLGFIFQFFNLipv 106
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEI-----LLDGKPvtAEQPEDYR-KLFSAVFTDFHL--- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 107 lsvFDNVFFPlvlNGHVGKKEARERALHFIE---SVGLAGFTERKPgQLSGGQQQRVAIARALAHDPQVVIADEPTGNLD 183
Cdd:PRK10522 409 ---FDQLLGP---EGKPANPALVEKWLERLKmahKLELEDGRISNL-KLSKGQKKRLALLLALAEERDILLLDEWAADQD 481
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 556463668 184 LVTGEAILDLLLKINQETRTTFIISTHSSQLKERARRVVEIKDGVL 229
Cdd:PRK10522 482 PHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQL 527
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
10-210 |
2.32e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 61.73 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 10 MISLNNIYKSYgsgEGKvDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTV--GTVMFLKKLLNHLPEEQLA 87
Cdd:PRK09580 1 MLSIKDLHVSV---EDK-AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVtgGTVEFKGKDLLELSPEDRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 88 airGRHLGFIFQFFNLIPVLSvfdNVFFplvLNGHVgkKEARE-RALHFIESVGLAGFTERKPGQL-------------- 152
Cdd:PRK09580 77 ---GEGIFMAFQYPVEIPGVS---NQFF---LQTAL--NAVRSyRGQEPLDRFDFQDLMEEKIALLkmpedlltrsvnvg 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 556463668 153 -SGGQQQRVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRtTFIISTH 210
Cdd:PRK09580 146 fSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKR-SFIIVTH 203
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
18-183 |
2.35e-11 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 61.66 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 18 KSYGSGEGKVDALKNinlEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAAIRGRHLGFI 97
Cdd:cd03237 6 MKKTLGEFTLEVEGG---SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADYEGTVRDLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 98 FQFFNLIPVLSVFDN-VFFPLvlnghvgkkeareralhfiesvGLAGFTERKPGQLSGGQQQRVAIARALAHDPQVVIAD 176
Cdd:cd03237 83 SSITKDFYTHPYFKTeIAKPL----------------------QIEQILDREVPELSGGELQRVAIAACLSKDADIYLLD 140
|
....*..
gi 556463668 177 EPTGNLD 183
Cdd:cd03237 141 EPSAYLD 147
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
6-183 |
3.34e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.13 E-value: 3.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 6 KELPMISLNNIYKSYGSGEGKVDALkninlEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMF-LKklLNHLPEE 84
Cdd:PRK13409 336 ERETLVEYPDLTKKLGDFSLEVEGG-----EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPeLK--ISYKPQY 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 85 qlaaIRGRHLGFIFQFFNLIPvlSVFDNVFFplvlnghvgKKEareralhFIESVGLAGFTERKPGQLSGGQQQRVAIAR 164
Cdd:PRK13409 409 ----IKPDYDGTVEDLLRSIT--DDLGSSYY---------KSE-------IIKPLQLERLLDKNVKDLSGGELQRVAIAA 466
|
170
....*....|....*....
gi 556463668 165 ALAHDPQVVIADEPTGNLD 183
Cdd:PRK13409 467 CLSRDADLYLLDEPSAHLD 485
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
30-227 |
7.83e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 61.33 E-value: 7.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 30 LKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVmFLKKLLNHLPEEQL---AAIRGRHLgfifqFFNLIPV 106
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-WAERSIAYVPQQAWimnATVRGNIL-----FFDEEDA 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 107 LSVFDNVffplvlngHVGKKEARERALhfieSVGLAGFTERKPGQLSGGQQQRVAIARALAHDPQVVIADEPTGNLDLVT 186
Cdd:PTZ00243 750 ARLADAV--------RVSQLEADLAQL----GGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHV 817
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 556463668 187 GEAIL-DLLL-KINQETRttfIISTHSSQLKERARRVVEIKDG 227
Cdd:PTZ00243 818 GERVVeECFLgALAGKTR---VLATHQVHVVPRADYVVALGDG 857
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
12-183 |
2.23e-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: 59.95 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 12 SLNNIYKSYGsgeGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKkllnhlpeeqlaairG 91
Cdd:TIGR03719 6 TMNRVSKVVP---PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQP---------------G 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 92 RHLGFIFQFFNLIPVLSVFDNVFFPL-------------------------VLNGHVGKKEARERA--LHFIES-VGLAG 143
Cdd:TIGR03719 68 IKVGYLPQEPQLDPTKTVRENVEEGVaeikdaldrfneisakyaepdadfdKLAAEQAELQEIIDAadAWDLDSqLEIAM 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 556463668 144 FTERKP------GQLSGGQQQRVAIARALAHDPQVVIADEPTGNLD 183
Cdd:TIGR03719 148 DALRCPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
30-231 |
3.12e-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: 58.04 E-value: 3.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 30 LKNINLEIEKGEFLALCGPSGSGKSTL-------------LNILSgidkptvgtvMFLKKLLNHLPEEQLAAIRGrhlgf 96
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryVESLS----------AYARQFLGQMDKPDVDSIEG----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 97 ifqffnLIPVLSVFDNVF----------------FPLVLNGHVGkkeARERaLHFIESVGLAGFT-ERKPGQLSGGQQQR 159
Cdd:cd03270 76 ------LSPAIAIDQKTTsrnprstvgtvteiydYLRLLFARVG---IRER-LGFLVDVGLGYLTlSRSAPTLSGGEAQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556463668 160 VAIARALAHDPQVV--IADEPTGNLDLVTGEAILDLLLKINQETRTTFIIStHSSQLKERARRVVEIKDGVLVH 231
Cdd:cd03270 146 IRLATQIGSGLTGVlyVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVE-HDEDTIRAADHVIDIGPGAGVH 218
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
9-183 |
4.05e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.87 E-value: 4.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSYGsgEGKVdaLKNINLEIEKGEFLALCGPSGSGKSTLLNILSGiDKPtvgtvmflKKLLNHL------- 81
Cdd:PRK10938 259 PRIVLNNGVVSYN--DRPI--LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHP--------QGYSNDLtlfgrrr 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 82 -PEEQLAAIRgRHLGFIFQFFNL-----IPVLSVFDNVFFplvlnGHVGKKEA-----RERALHFIESVGLAGFTERKPG 150
Cdd:PRK10938 326 gSGETIWDIK-KHIGYVSSSLHLdyrvsTSVRNVILSGFF-----DSIGIYQAvsdrqQKLAQQWLDILGIDKRTADAPF 399
|
170 180 190
....*....|....*....|....*....|....
gi 556463668 151 Q-LSGGQQQRVAIARALAHDPQVVIADEPTGNLD 183
Cdd:PRK10938 400 HsLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
151-225 |
5.74e-10 |
|
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: 56.21 E-value: 5.74e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556463668 151 QLSGGQQQRVAIARALAH----DPQVVIADEPTGNLDLVTGEAILDLLLKINQETRtTFIISTHSSQLKERARRVVEIK 225
Cdd:cd03227 77 QLSGGEKELSALALILALaslkPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGA-QVIVITHLPELAELADKLIHIK 154
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
92-222 |
2.24e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 57.35 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 92 RHLGFIFQFFNLIPVL---SVFDNVFFplvlnghvGKKEA-RERALHFIESVGLAGFTERKPGQ-----------LSGGQ 156
Cdd:PTZ00265 1292 KDLRNLFSIVSQEPMLfnmSIYENIKF--------GKEDAtREDVKRACKFAAIDEFIESLPNKydtnvgpygksLSGGQ 1363
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556463668 157 QQRVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQLKERARRVV 222
Cdd:PTZ00265 1364 KQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIV 1429
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
9-215 |
3.06e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 56.44 E-value: 3.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIYKSYGSGEGKVdALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVmflkkllnhlpeeqlaA 88
Cdd:PRK13545 20 PFDKLKDLFFRSKDGEYHY-ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV----------------D 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 89 IRGRhLGFIFQFFNLIPVLSVFDNVFFPLVLNGhVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAH 168
Cdd:PRK13545 83 IKGS-AALIAISSGLNGQLTGIENIELKGLMMG-LTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 556463668 169 DPQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQLK 215
Cdd:PRK13545 161 NPDILVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVK 207
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
29-183 |
4.16e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 54.49 E-value: 4.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 29 ALKNINLEIEKGEFLALC------------GPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAAIrGRHLGF 96
Cdd:PRK13541 3 SLHQLQFNIEQKNLFDLSitflpsaityikGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYI-GHNLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 97 IFQffnlipvLSVFDN-VFFPLVLNghvgKKEARERALHFIEsvgLAGFTERKPGQLSGGQQQRVAIARALAHDPQVVIA 175
Cdd:PRK13541 82 KLE-------MTVFENlKFWSEIYN----SAETLYAAIHYFK---LHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLL 147
|
....*...
gi 556463668 176 DEPTGNLD 183
Cdd:PRK13541 148 DEVETNLS 155
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
6-232 |
4.54e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 55.95 E-value: 4.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 6 KELPMISLNNIYKSYGSGEGKVDALkninlEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKL------LN 79
Cdd:COG1245 337 EEETLVEYPDLTKSYGGFSLEVEGG-----EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKIsykpqyIS 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 80 HLPEEQLAAIRGRHLGFIFQ--FFNlipvlsvfDNVFFPLVLnghvgkkearERALhfiesvglagftERKPGQLSGGQQ 157
Cdd:COG1245 412 PDYDGTVEEFLRSANTDDFGssYYK--------TEIIKPLGL----------EKLL------------DKNVKDLSGGEL 461
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556463668 158 QRVAIARALAHDPQVVIADEPTGNLDlvtgeaildlllkINQETRTTFIIsthssqlkeraRRVVEIKD-GVLV--HD 232
Cdd:COG1245 462 QRVAIAACLSRDADLYLLDEPSAHLD-------------VEQRLAVAKAI-----------RRFAENRGkTAMVvdHD 515
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
30-191 |
5.46e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.19 E-value: 5.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 30 LKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLnhlpEEQLAAIRgRHLGFIFQFFNLIPVLSV 109
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTYQ-KQLCFVGHRSGINPYLTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 110 FDNVFFPL-VLNGHVGKKEareralhFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHDPQVVIADEPTGNLDLVTGE 188
Cdd:PRK13540 92 RENCLYDIhFSPGAVGITE-------LCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLL 164
|
...
gi 556463668 189 AIL 191
Cdd:PRK13540 165 TII 167
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
39-227 |
1.92e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 51.99 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 39 KGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVmflkkllnhlpeeqlaairgrhlgfifqffnlipvlsvfdnvffpLV 118
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV---------------------------------------------IY 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 119 LNGHVGKKEARERALHFIesvglagfTERKPGQLSGGQQQRVAIARALAHDPQVVIADEPTGNLD-----LVTGEAILDL 193
Cdd:smart00382 36 IDGEDILEEVLDQLLLII--------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDaeqeaLLLLLEELRL 107
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 556463668 194 LLKINQETRTTFIISTHSSQ------LKERARRVVEIKDG 227
Cdd:smart00382 108 LLLLKSEKNLTVILTTNDEKdlgpalLRRRFDRRIVLLLI 147
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
29-229 |
2.06e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 53.28 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 29 ALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVmflkkllNHLPEEQLAAIRGrhlgfifqffNLIPVLS 108
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV-------DRNGEVSVIAISA----------GLSGQLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 109 VFDNVFFPLVLNGHvGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHDPQVVIADEPTGNLDLVTGE 188
Cdd:PRK13546 102 GIENIEFKMLCMGF-KRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQ 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 556463668 189 AILDLLLKINQETRTTFIISTHSSQLKERARRVVEIKDGVL 229
Cdd:PRK13546 181 KCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
10-208 |
2.41e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.74 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 10 MISLNNIYKSYGSgegkvDAL-KNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFlkkllnhLPEEQLAA 88
Cdd:PRK15064 1 MLSTANITMQFGA-----KPLfENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSL-------DPNERLGK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 89 IRGRHlgFIFQFFNLIPVlsvfdnvffplVLNGHV---GKKEARER--AL----------------HFIEsvgLAGFT-E 146
Cdd:PRK15064 69 LRQDQ--FAFEEFTVLDT-----------VIMGHTelwEVKQERDRiyALpemseedgmkvadlevKFAE---MDGYTaE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 147 RKPGQL------------------SGGQQQRVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLlkiNQETRTTFIIS 208
Cdd:PRK15064 133 ARAGELllgvgipeeqhyglmsevAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVL---NERNSTMIIIS 209
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
11-195 |
2.56e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.58 E-value: 2.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGsgeGKVdALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKP-----TVG-TVmflkkllnhlpee 84
Cdd:PRK11819 325 IEAENLSKSFG---DRL-LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPdsgtiKIGeTV------------- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 85 qlaairgrHLGFIFQFF-NLIPVLSVFDNVFfplvlNGH----VGKKEARERALhfiesVGLAGFT----ERKPGQLSGG 155
Cdd:PRK11819 388 --------KLAYVDQSRdALDPNKTVWEEIS-----GGLdiikVGNREIPSRAY-----VGRFNFKggdqQKKVGVLSGG 449
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 556463668 156 QQQRVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLL 195
Cdd:PRK11819 450 ERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALL 489
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
32-230 |
2.61e-08 |
|
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: 53.68 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 32 NINLEIEKGEFLALCGPSGSGKSTLLNILSG-----------IDKPTVGTVMFLKKL---LNHLPEEqlaaiRGRHlgfi 97
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGaypgkfegnvfINGKPVDIRNPAQAIragIAMVPED-----RKRH---- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 98 fqffNLIPVLSVFDNVFFPlVLNGHVGKKEARERA-----LHFIESVGLAGFTERKP-GQLSGGQQQRVAIARALAHDPQ 171
Cdd:TIGR02633 349 ----GIVPILGVGKNITLS-VLKSFCFKMRIDAAAelqiiGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPR 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 556463668 172 VVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIIsthSSQLKErarrVVEIKDGVLV 230
Cdd:TIGR02633 424 VLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVV---SSELAE----VLGLSDRVLV 475
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
30-211 |
2.74e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 53.80 E-value: 2.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 30 LKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMfLKKLLNHLPeeQLAAIRGRhlgfifqffnlipvlSV 109
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVH-MKGSVAYVP--QQAWIQND---------------SL 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 110 FDNVFFPLVLNghvgkkEARERALhfIESVGLAGFTERKPG-----------QLSGGQQQRVAIARALAHDPQVVIADEP 178
Cdd:TIGR00957 716 RENILFGKALN------EKYYQQV--LEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDP 787
|
170 180 190
....*....|....*....|....*....|....*..
gi 556463668 179 TGNLDLVTGEAILDLLLK----INQETRttfIISTHS 211
Cdd:TIGR00957 788 LSAVDAHVGKHIFEHVIGpegvLKNKTR---ILVTHG 821
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
10-214 |
3.53e-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: 53.21 E-value: 3.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 10 MISLNNIYKSYGSGEGKVDALkniNLEIEKGEFLALCGPSGSGKSTLLNILSGIdKPTVGTVMFLkkllnhlPEEQlaai 89
Cdd:TIGR00954 451 GIKFENIPLVTPNGDVLIESL---SFEVPSGNNLLICGPNGCGKSSLFRILGEL-WPVYGGRLTK-------PAKG---- 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 90 rgrHLGFIFQFfnliPVLSV---FDNVFFPLvlnghvGKKEARERAL------HFIESVGLAGFTERKPG---------Q 151
Cdd:TIGR00954 516 ---KLFYVPQR----PYMTLgtlRDQIIYPD------SSEDMKRRGLsdkdleQILDNVQLTHILEREGGwsavqdwmdV 582
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556463668 152 LSGGQQQRVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLLlkinQETRTTFIISTHSSQL 214
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLC----REFGITLFSVSHRKSL 641
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
13-231 |
3.55e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.36 E-value: 3.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 13 LNNIYKSYGSGEgkvdALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKllnhlpeeqlAAIrgr 92
Cdd:PRK15064 322 VENLTKGFDNGP----LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSEN----------ANI--- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 93 hlGFIFQ-----FFNlipVLSVFDNVffplvlnGHVGKKEARERALHFIesVGLAGFTE----RKPGQLSGGQQQRVAIA 163
Cdd:PRK15064 385 --GYYAQdhaydFEN---DLTLFDWM-------SQWRQEGDDEQAVRGT--LGRLLFSQddikKSVKVLSGGEKGRMLFG 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556463668 164 RALAHDPQVVIADEPTGNLDLvtgEAI--LDLLLKINQetrTTFIISTHS----SQLkerARRVVEIKDGVLVH 231
Cdd:PRK15064 451 KLMMQKPNVLVMDEPTNHMDM---ESIesLNMALEKYE---GTLIFVSHDrefvSSL---ATRIIEITPDGVVD 515
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
30-197 |
4.71e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.19 E-value: 4.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 30 LKNINLEIEKGEFLALCGPSGSGKSTLLNILSGidKPTVGTVMFLKKLLNHLPeeqLAAIRGRHLGFIFQFFNLIPVLSV 109
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTGVITGGDRLVNGRP---LDSSFQRSIGYVQQQDLHLPTSTV 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 110 FDNVFFP--LVLNGHVGKKEARERALHFIESVGLAGFTER---KPGQ-LSGGQQQRVAIARALAHDPQVVI-ADEPTGNL 182
Cdd:TIGR00956 854 RESLRFSayLRQPKSVSKSEKMEYVEEVIKLLEMESYADAvvgVPGEgLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGL 933
|
170
....*....|....*
gi 556463668 183 DLVTGEAILDLLLKI 197
Cdd:TIGR00956 934 DSQTAWSICKLMRKL 948
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
18-183 |
4.73e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 53.31 E-value: 4.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 18 KSYGSGEGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGidKPTVGTVM-------FLKKllnhlpEEQLAAIR 90
Cdd:PLN03140 884 KEQGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEgdirisgFPKK------QETFARIS 955
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 91 grhlGFIFQFFNLIPVLSVFDNVFFP--LVLNGHVGKKEAR---ERALHFIE-------SVGLAGFTerkpgQLSGGQQQ 158
Cdd:PLN03140 956 ----GYCEQNDIHSPQVTVRESLIYSafLRLPKEVSKEEKMmfvDEVMELVEldnlkdaIVGLPGVT-----GLSTEQRK 1026
|
170 180
....*....|....*....|....*
gi 556463668 159 RVAIARALAHDPQVVIADEPTGNLD 183
Cdd:PLN03140 1027 RLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
11-177 |
1.12e-07 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 51.72 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNI-YKSYGSGEGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVmflkkLLNH--LPEEQLA 87
Cdd:COG4615 328 LELRGVtYRYPGEDGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEI-----LLDGqpVTADNRE 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 88 AIRgRHLGFIFQFFNLipvlsvFDNVffpLVLNGHVGKKEARE--RALHFIESVGLAG--FTERKpgqLSGGQQQRVAIA 163
Cdd:COG4615 403 AYR-QLFSAVFSDFHL------FDRL---LGLDGEADPARAREllERLELDHKVSVEDgrFSTTD---LSQGQRKRLALL 469
|
170
....*....|....
gi 556463668 164 RALAHDPQVVIADE 177
Cdd:COG4615 470 VALLEDRPILVFDE 483
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
24-213 |
1.56e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.49 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 24 EGKVdALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLlnhlpeeQLAairgrhlgfifqFFN- 102
Cdd:PRK11147 330 DGKQ-LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKL-------EVA------------YFDq 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 103 ----LIPVLSVFDNVffplvlngHVGKKE----ARER-ALHFIESVGLAGFTERKPGQ-LSGGQQQRVAIARALAHDPQV 172
Cdd:PRK11147 390 hraeLDPEKTVMDNL--------AEGKQEvmvnGRPRhVLGYLQDFLFHPKRAMTPVKaLSGGERNRLLLARLFLKPSNL 461
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 556463668 173 VIADEPTGNLDLVTgeaiLDLLLKINQETRTTFIISTHSSQ 213
Cdd:PRK11147 462 LILDEPTNDLDVET----LELLEELLDSYQGTVLLVSHDRQ 498
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
11-209 |
1.77e-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: 50.10 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSGEGKVdaLKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPeeqLAAIR 90
Cdd:cd03369 7 IEVENLSVRYAPDLPPV--LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIP---LEDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 91 gRHLGFIFQffnlIPVL---SVFDNvffpLVLNGHVGKKEARErALHFIESvGLagfterkpgQLSGGQQQRVAIARALA 167
Cdd:cd03369 82 -SSLTIIPQ----DPTLfsgTIRSN----LDPFDEYSDEEIYG-ALRVSEG-GL---------NLSQGQRQLLCLARALL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 556463668 168 HDPQVVIADEPTGNLDLVTGEAIldlllkinQET-RTTFIIST 209
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALI--------QKTiREEFTNST 176
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
25-234 |
2.56e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 50.50 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 25 GKVDALKNINLEIEKGEFLALCGPSGSG--KSTLLNILSGID---KP-TVGTVMFLKKLLNHLPEEQLAAIRGRHLGFIF 98
Cdd:NF000106 24 GEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDagrRPwRF*TWCANRRALRRTIG*HRPVR*GRRESFSG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 99 QFfNLIPVLSVFDnvffplvlnghVGKKEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHDPQVVIADEP 178
Cdd:NF000106 104 RE-NLYMIGR*LD-----------LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 556463668 179 TGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQLKERARRVVEIKDGVLVHDSQ 234
Cdd:NF000106 172 TTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGK 227
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
24-190 |
2.86e-07 |
|
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: 49.85 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 24 EGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNilsgidkptvgtvMFLKkLLNHLPEEQLAAIRGRHLGF--IFQFF 101
Cdd:cd03289 14 EGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLS-------------AFLR-LLNTEGDIQIDGVSWNSVPLqkWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 102 NLIPvlsvfDNVFF---PLVLNGHVGKKEARERALHFIESVGLAGFTERKPGQL-----------SGGQQQRVAIARALA 167
Cdd:cd03289 80 GVIP-----QKVFIfsgTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVL 154
|
170 180
....*....|....*....|...
gi 556463668 168 HDPQVVIADEPTGNLDLVTGEAI 190
Cdd:cd03289 155 SKAKILLLDEPSAHLDPITYQVI 177
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
26-208 |
3.54e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.49 E-value: 3.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 26 KVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILS----GIDKPTVGTVMFlkklLNHLPEEQLAAIRGrHLGFIFQFF 101
Cdd:TIGR00956 73 TFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITY----DGITPEEIKKHYRG-DVVYNAETD 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 102 NLIPVLSVFDNVFFPLVLNG------HVGKKEARERALHFIESV-GLAGFTERKPGQ-----LSGGQQQRVAIARALAHD 169
Cdd:TIGR00956 148 VHFPHLTVGETLDFAARCKTpqnrpdGVSREEYAKHIADVYMATyGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGG 227
|
170 180 190
....*....|....*....|....*....|....*....
gi 556463668 170 PQVVIADEPTGNLDLVTGEAILDLLLKINQETRTTFIIS 208
Cdd:TIGR00956 228 AKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVA 266
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
29-214 |
4.11e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.11 E-value: 4.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 29 ALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFL-KKLLNHLPEEqlaAIRGrhlGF----------- 96
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHgKKINNHNANE---AINH---GFalvteerrstg 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 97 IFQFFNlIPVLSVFDNVFFPLVLNGHVGKKEARERALHFIESVGLAGFTERKP-GQLSGGQQQRVAIARALAHDPQVVIA 175
Cdd:PRK10982 337 IYAYLD-IGFNSLISNIRNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQiGSLSGGNQQKVIIGRWLLTQPEILML 415
|
170 180 190
....*....|....*....|....*....|....*....
gi 556463668 176 DEPTGNLDLVTGEAILDLLLKINQETRTTFIISTHSSQL 214
Cdd:PRK10982 416 DEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPEL 454
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
151-215 |
6.34e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 49.64 E-value: 6.34e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556463668 151 QLSGGQQQRVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLL--LKINqETRTTFIISTHSSQLK 215
Cdd:PTZ00265 579 KLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTInnLKGN-ENRITIIIAHRLSTIR 644
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
150-230 |
7.50e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.16 E-value: 7.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 150 GQLSGGQQQRVAIARALAHDPQVVIADEPTGNLDLVTGEAILDLllkINQETRTTFIISTHSSQLKErarrVVEIKDGVL 229
Cdd:PRK13549 404 ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKL---INQLVQQGVAIIVISSELPE----VLGLSDRVL 476
|
.
gi 556463668 230 V 230
Cdd:PRK13549 477 V 477
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
30-56 |
1.30e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 48.87 E-value: 1.30e-06
10 20
....*....|....*....|....*..
gi 556463668 30 LKNINLEIEKGEFLALCGPSGSGKSTL 56
Cdd:COG0178 16 LKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
26-224 |
1.89e-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: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 26 KVDALKNINLEIEKGEFLALCGPSGSGKSTLLNilsgidkptvgtvmflkkllnhlpeEQLAAIRGRHLGFIFQFFNLIP 105
Cdd:cd03238 7 NVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN-------------------------EGLYASGKARLISFLPKFSRNK 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 106 VLSVfdnvffplvlnghvgkkeareRALHFIESVGLAGFT-ERKPGQLSGGQQQRVAIARALAHDPQ--VVIADEPTGNL 182
Cdd:cd03238 62 LIFI---------------------DQLQFLIDVGLGYLTlGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGL 120
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 556463668 183 DLVTGEAILDLLLKINQETRTTFIIStHSSQLKERARRVVEI 224
Cdd:cd03238 121 HQQDINQLLEVIKGLIDLGNTVILIE-HNLDVLSSADWIIDF 161
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
9-234 |
2.07e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.86 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 9 PMISLNNIykSYGSGEGKVdaLKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKL-LNHLPEEQLA 87
Cdd:PRK10636 311 PLLKMEKV--SAGYGDRII--LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIkLGYFAQHQLE 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 88 AIRGRHLgfifqffnlipvlsvfdnvffPLVLNGHVGKKEARERALHFIESVGLAG--FTErKPGQLSGGQQQRVAIARA 165
Cdd:PRK10636 387 FLRADES---------------------PLQHLARLAPQELEQKLRDYLGGFGFQGdkVTE-ETRRFSGGEKARLVLALI 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556463668 166 LAHDPQVVIADEPTGNLDLVTGEAILDLLLkinqETRTTFIISTHSSQLkerARRVVEikDGVLVHDSQ 234
Cdd:PRK10636 445 VWQRPNLLLLDEPTNHLDLDMRQALTEALI----DFEGALVVVSHDRHL---LRSTTD--DLYLVHDGK 504
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
36-225 |
2.23e-06 |
|
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: 46.88 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 36 EIEKGEFLALCGPSGSGKSTLLNILS----GiDKPTVGTVMFLKKLLNhlPEEQLAAIrgrhlGFIFQffnlipvlsvfd 111
Cdd:cd03279 24 GLDNNGLFLICGPTGAGKSTILDAITyalyG-KTPRYGRQENLRSVFA--PGEDTAEV-----SFTFQ------------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 112 nvffplvLNGHVGKKEaRERALH---FIESVGL-----AGFTERKPGQLSGGQQQRVAIARALAHDPQV----------V 173
Cdd:cd03279 84 -------LGGKKYRVE-RSRGLDydqFTRIVLLpqgefDRFLARPVSTLSGGETFLASLSLALALSEVLqnrggarleaL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 556463668 174 IADEPTGNLDLVTGEAILDLLLKINQETRTTFIIStHSSQLKERARRVVEIK 225
Cdd:cd03279 156 FIDEGFGTLDPEALEAVATALELIRTENRMVGVIS-HVEELKERIPQRLEVI 206
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
11-210 |
4.66e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 47.21 E-value: 4.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 11 ISLNNIYKSYGSGEGKVdaLKNINLEIEKGEFLALCGPSGSGKSTLLNILSgidkptvgtvmflkKLLNHLPEEQLAAIR 90
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRAV--LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL--------------RLLSTEGEIQIDGVS 1281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 91 GRHLGF--IFQFFNLIPvLSVFdnVF---FPLVLNGHvgKKEARERALHFIESVGLAGFTERKPGQL-----------SG 154
Cdd:TIGR01271 1282 WNSVTLqtWRKAFGVIP-QKVF--IFsgtFRKNLDPY--EQWSDEEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSN 1356
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 556463668 155 GQQQRVAIARALAHDPQVVIADEPTGNLDLVTGEaILDLLLKiNQETRTTFIISTH 210
Cdd:TIGR01271 1357 GHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQ-IIRKTLK-QSFSNCTVILSEH 1410
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
12-183 |
4.76e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.04 E-value: 4.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 12 SLNNIYKSYGsgeGKVDALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGtvmflkkllnhlpEEQLAAirG 91
Cdd:PRK11819 8 TMNRVSKVVP---PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG-------------EARPAP--G 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 92 RHLGFIFQFFNLIPVLSVFDNvffplVLNGHVGKKEARER--------------------------------ALHFIES- 138
Cdd:PRK11819 70 IKVGYLPQEPQLDPEKTVREN-----VEEGVAEVKAALDRfneiyaayaepdadfdalaaeqgelqeiidaaDAWDLDSq 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 556463668 139 VGLAGFTERKP------GQLSGGQQQRVAIARALAHDPQVVIADEPTGNLD 183
Cdd:PRK11819 145 LEIAMDALRCPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
30-230 |
5.56e-06 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 46.06 E-value: 5.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 30 LKNINLEIEKGEFLALCGPSGSGKSTL-LNILSGIDkptvgtvMFLKKL------LNHLPeeqLAAIRGRhLGFIFQffn 102
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLsLAFFRMVD-------IFDGKIvidgidISKLP---LHTLRSR-LSIILQ--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 103 lipvlsvfDNVFFP--LVLNGHVGKKEARERALHFIESVGLAGFTERKPGQL-----------SGGQQQRVAIARALAHD 169
Cdd:cd03288 103 --------DPILFSgsIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRK 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556463668 170 PQVVIADEPTGNLDLVTgEAILDLLLKINQETRTTFIISTHSSQLKErARRVVEIKDGVLV 230
Cdd:cd03288 175 SSILIMDEATASIDMAT-ENILQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILV 233
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
30-58 |
1.04e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 45.83 E-value: 1.04e-05
10 20
....*....|....*....|....*....
gi 556463668 30 LKNINLEIEKGEFLALCGPSGSGKSTLLN 58
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLIN 653
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
30-60 |
1.22e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 45.79 E-value: 1.22e-05
10 20 30
....*....|....*....|....*....|..
gi 556463668 30 LKNINLEIEKGEFLALCGPSGSGKSTLLN-IL 60
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKSTLVNdIL 652
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
147-211 |
2.10e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.85 E-value: 2.10e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556463668 147 RKPGQLSGGQQQRVAIARALAHDPQVVIADEPTGNLDLvtgEAILDL---LLKINQetrtTFIISTHS 211
Cdd:PLN03073 340 KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL---HAVLWLetyLLKWPK----TFIVVSHA 400
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
30-182 |
2.74e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 44.14 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 30 LKNINLEIEKGEFLALCGPSGSGKSTLLN-ILSgidkPTVGTVMFLKKL--LNHLPEEQLAAI---------------RG 91
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINdTLY----PALARRLHLKKEqpGNHDRIEGLEHIdkvividqspigrtpRS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 92 RHLGFIfQFFNLIPVL----------------------SVFDnvffplVLNGHVgkKEARE---------RALHFIESVG 140
Cdd:cd03271 87 NPATYT-GVFDEIRELfcevckgkrynretlevrykgkSIAD------VLDMTV--EEALEffenipkiaRKLQTLCDVG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 556463668 141 LaGFTerKPGQ----LSGGQQQRVAIARAL---AHDPQVVIADEPTGNL 182
Cdd:cd03271 158 L-GYI--KLGQpattLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGL 203
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
47-225 |
3.82e-05 |
|
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: 43.36 E-value: 3.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 47 GPSGSGKSTllnILSGIDKPTVGTVMFLKKLLNHLPE-----EQLAAIrgrHLGFIFQFFNLIPV---LSVFDNVFFplv 118
Cdd:cd03240 29 GQNGAGKTT---IIEALKYALTGELPPNSKGGAHDPKliregEVRAQV---KLAFENANGKKYTItrsLAILENVIF--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 119 lnghvgkkeareraLHFIESVGLAgftERKPGQLSGGQQQ------RVAIARALAHDPQVVIADEPTGNLDlvtGE---- 188
Cdd:cd03240 100 --------------CHQGESNWPL---LDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLD---EEniee 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 556463668 189 AILDLLLKINQETRTTFIISTHSSQLKERARRVVEIK 225
Cdd:cd03240 160 SLAEIIEERKSQKNFQLIVITHDEELVDAADHIYRVE 196
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
30-58 |
4.22e-05 |
|
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: 44.23 E-value: 4.22e-05
10 20
....*....|....*....|....*....
gi 556463668 30 LKNINLEIEKGEFLALCGPSGSGKSTLLN 58
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLIN 652
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
15-71 |
6.22e-05 |
|
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: 42.77 E-value: 6.22e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556463668 15 NIYKSYG---------SGEGkVDALKNInLeieKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTV 71
Cdd:cd01854 56 EIYEKLGypvlavsakTGEG-LDELREL-L---KGKTSVLVGQSGVGKSTLLNALLPELVLATGEI 116
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
30-56 |
7.03e-05 |
|
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: 43.46 E-value: 7.03e-05
10 20
....*....|....*....|....*..
gi 556463668 30 LKNINLEIEKGEFLALCGPSGSGKSTL 56
Cdd:TIGR00630 12 LKNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
34-231 |
8.62e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.08 E-value: 8.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 34 NLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMFLKKLLNHLPEEQLAAIrgrhLGFIFQFFN---LIPVLSVF 110
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKL----VSDEWQRNNtdmLSPGEDDT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 111 DNVFFPLVLNGHvgkkEARERALHFIESVGLAGFTERKPGQLSGGQQQRVAIARALAHDPQVVIADEPTGNLDLVTGEAI 190
Cdd:PRK10938 99 GRTTAEIIQDEV----KDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 556463668 191 LDLLLKINQETRTTFIISTHSSQLKERARRVVEIKDGVLVH 231
Cdd:PRK10938 175 AELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAE 215
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
23-71 |
1.08e-04 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 42.61 E-value: 1.08e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 556463668 23 GEGkVDALKNInleIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTV 71
Cdd:PRK01889 182 GEG-LDVLAAW---LSGGKTVALLGSSGVGKSTLVNALLGEEVQKTGAV 226
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
30-56 |
1.51e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 42.37 E-value: 1.51e-04
10 20
....*....|....*....|....*..
gi 556463668 30 LKNINLEIEKGEFLALCGPSGSGKSTL 56
Cdd:PRK00349 16 LKNIDLDIPRDKLVVFTGLSGSGKSSL 42
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
150-179 |
3.02e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 41.31 E-value: 3.02e-04
10 20 30
....*....|....*....|....*....|
gi 556463668 150 GQLSGGQQQRVAIARALAHDPQVVIADEPT 179
Cdd:NF040905 403 GNLSGGNQQKVVLSKWLFTDPDVLILDEPT 432
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
30-233 |
8.25e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 40.34 E-value: 8.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 30 LKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTVMF------------LKKLLNHLPEEQL---AAIRgrhl 94
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIddcdvakfgltdLRRVLSIIPQSPVlfsGTVR---- 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 95 gfifqfFNLIPVLSVFDNVFFPLVLNGHVgkKEARERalhfiESVGLAGFTERKPGQLSGGQQQRVAIARALAHDPQVVI 174
Cdd:PLN03232 1328 ------FNIDPFSEHNDADLWEALERAHI--KDVIDR-----NPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILV 1394
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556463668 175 ADEPTGNLDLVTgeailDLLLK--INQETRT-TFIISTHSSQLKERARRVVEIKDG-VLVHDS 233
Cdd:PLN03232 1395 LDEATASVDVRT-----DSLIQrtIREEFKScTMLVIAHRLNTIIDCDKILVLSSGqVLEYDS 1452
|
|
| rad24 |
TIGR00602 |
checkpoint protein rad24; All proteins in this family for which functions are known are ... |
29-68 |
1.46e-03 |
|
checkpoint protein rad24; All proteins in this family for which functions are known are involved in DNA damage tolerance (likely cell cycle checkpoints).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: 129690 [Multi-domain] Cd Length: 637 Bit Score: 39.55 E-value: 1.46e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 556463668 29 ALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTV 68
Cdd:TIGR00602 99 WLKAQVLENAPKRILLITGPSGCGKSTTIKILSKELGIQV 138
|
|
| Rad17 |
pfam03215 |
Rad17 P-loop domain; |
29-68 |
2.78e-03 |
|
Rad17 P-loop domain;
Pssm-ID: 367398 [Multi-domain] Cd Length: 186 Bit Score: 37.63 E-value: 2.78e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 556463668 29 ALKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTV 68
Cdd:pfam03215 34 WLDAMFLENAKHRILLISGPSGCGKSTVIKELSKELGPKY 73
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
30-210 |
4.58e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 37.80 E-value: 4.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 30 LKNINLEIEKGEFLALCGPSGSGKSTLLNILSGIDKPTVGTV------------MFLKKLLNHLPEEQL---AAIRgrhl 94
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRIlidgcdiskfglMDLRKVLGIIPQAPVlfsGTVR---- 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 95 gfifqfFNLIPvlsvfdnvffplvLNGH--VGKKEARERAlHFIE-----SVGLAGFTERKPGQLSGGQQQRVAIARALA 167
Cdd:PLN03130 1331 ------FNLDP-------------FNEHndADLWESLERA-HLKDvirrnSLGLDAEVSEAGENFSVGQRQLLSLARALL 1390
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 556463668 168 HDPQVVIADEPTGNLDLVTgeailDLLLK--INQETRT-TFIISTH 210
Cdd:PLN03130 1391 RRSKILVLDEATAAVDVRT-----DALIQktIREEFKScTMLIIAH 1431
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
36-67 |
4.68e-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: 36.78 E-value: 4.68e-03
10 20 30
....*....|....*....|....*....|..
gi 556463668 36 EIEKGEFLALCGPSGSGKSTLLNILSGIDKPT 67
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPN 52
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
39-62 |
4.72e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 36.75 E-value: 4.72e-03
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
133-227 |
5.19e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 37.89 E-value: 5.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 133 LHFIESVGLAGFT-ERKPGQLSGGQQQRVAIARALAHDPQVV--IADEPTGNLDLVTGEAILDLLLKINQETRTTFIISt 209
Cdd:PRK00635 457 LSILIDLGLPYLTpERALATLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVE- 535
|
90
....*....|....*...
gi 556463668 210 HSSQLKERARRVVEIKDG 227
Cdd:PRK00635 536 HDEQMISLADRIIDIGPG 553
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
152-183 |
5.38e-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: 36.78 E-value: 5.38e-03
10 20 30
....*....|....*....|....*....|..
gi 556463668 152 LSGGQQQRVAIARALAHDPQVVIADEPTGNLD 183
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLD 103
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
26-114 |
7.90e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 37.12 E-value: 7.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 26 KVDALKNINLEIEKGEFLALCGPSGSGKSTLL--NILSGIDKPTVGTV-MFLKKLLNHLPEEQLAAIRGrhlgfifqffn 102
Cdd:PRK00635 12 TVRNLKNISIEFCPREIVLLTGVSGSGKSSLAfdTIYAAGRKRYLSTLpSFFATTLDSLPDPSVEKIEG----------- 80
|
90
....*....|..
gi 556463668 103 LIPVLSVFDNVF 114
Cdd:PRK00635 81 LSPTIAVKQNHF 92
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
126-231 |
9.84e-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: 36.91 E-value: 9.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556463668 126 KEARERaLHFIESVGLAGFT-ERKPGQLSGGQQQRVAIARALAHDPQVV--IADEPTGNLDLVTGEAILDLLLKInQETR 202
Cdd:TIGR00630 463 KEIRER-LGFLIDVGLDYLSlSRAAGTLSGGEAQRIRLATQIGSGLTGVlyVLDEPSIGLHQRDNRRLINTLKRL-RDLG 540
|
90 100
....*....|....*....|....*....
gi 556463668 203 TTFIISTHSSQLKERARRVVEIKDGVLVH 231
Cdd:TIGR00630 541 NTLIVVEHDEDTIRAADYVIDIGPGAGEH 569
|
|
| |
