|
Name |
Accession |
Description |
Interval |
E-value |
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
18-272 |
1.58e-145 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 409.09 E-value: 1.58e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 18 RPVILEAKQLSQVFKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPERG 97
Cdd:COG1116 4 AAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 98 MVFQGYTLFPWKTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMD 177
Cdd:COG1116 84 VVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 178 EPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALKANPGEIKEIIEVNLPRPRSLELMSTPEFKQ 257
Cdd:COG1116 164 EPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSARPGRIVEEIDVDLPRPRDRELRTSPEFAA 243
|
250
....*....|....*
gi 446922839 258 LRSRVDYLVHAEEDE 272
Cdd:COG1116 244 LRAEILDLLREEAER 258
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
22-241 |
4.08e-124 |
|
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: 353.31 E-value: 4.08e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 22 LEAKQLSQVFKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPERGMVFQ 101
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 102 GYTLFPWKTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFG 181
Cdd:cd03293 81 QDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 182 ALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALKANPGEIKEIIEVNL 241
Cdd:cd03293 161 ALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSARPGRIVAEVEVDL 220
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
22-272 |
1.14e-94 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 280.21 E-value: 1.14e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 22 LEAKQLSQVFKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPERGMVFQ 101
Cdd:COG4525 4 LTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRGVVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 102 GYTLFPWKTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFG 181
Cdd:COG4525 84 KDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 182 ALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALKANPGEIKEIIEVNLPR-------PRSLElmSTPE 254
Cdd:COG4525 164 ALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPGPGRIVERLELDFSRrflagedARAIK--SDPA 241
|
250
....*....|....*...
gi 446922839 255 FKQLRSRVDYLVHAEEDE 272
Cdd:COG4525 242 FIALREELLDIIFAQEEA 259
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
18-233 |
2.47e-91 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 275.05 E-value: 2.47e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 18 RPVILEAKQLSQVFkhGQTerTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITG-PcPER 96
Cdd:COG3842 2 AMPALELENVSKRY--GDV--TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGlP-PEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 ---GMVFQGYTLFPWKTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKI 173
Cdd:COG3842 77 rnvGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 174 LLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALKAnpGEI 233
Cdd:COG3842 157 LLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMND--GRI 214
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
22-224 |
2.22e-84 |
|
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: 252.06 E-value: 2.22e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 22 LEAKQLSQVFKhgqtERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER---GM 98
Cdd:cd03259 1 LELKGLSKTYG----SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERrniGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 99 VFQGYTLFPWKTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDE 178
Cdd:cd03259 77 VFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446922839 179 PFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIV 224
Cdd:cd03259 157 PLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIA 202
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
41-265 |
3.26e-82 |
|
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: 247.38 E-value: 3.26e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 41 LNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPERGMVFQGYTLFPWKTVKENVMFGPQ 120
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVFQNYSLLPWLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 121 --MRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDL 198
Cdd:TIGR01184 81 rvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 199 WQNIDITIIFVTHDMDEAILLADRIVALKANPG-EIKEIIEVNLPRPRS-LELMSTPEFKQLRSR-VDYL 265
Cdd:TIGR01184 161 WEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAaNIGQILEVPFPRPRDrLEVVEDPSYYDLRNEaLYFL 230
|
|
| ABC_ATP_SaoA |
NF040729 |
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC ... |
22-245 |
3.38e-80 |
|
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC transporter in which both the permease subunit SaoP, and the substrate-binding protein SaoB, are nearly always selenoproteins that were unrecognized as such until recently (2022). The SAO system is found in Clostridium difficile and various other anaerobic heterotrophs.
Pssm-ID: 468693 [Multi-domain] Cd Length: 248 Bit Score: 242.72 E-value: 3.38e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 22 LEAKQLSQVFKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPERGMVFQ 101
Cdd:NF040729 2 LKIQNISKTFINNKKENEVLKDISFDVEEGEFVSLLGPSGCGKTTLLTIIAGFQNATSGEILVNGNEVTKPGPDRGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 102 GYTLFPWKTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFG 181
Cdd:NF040729 82 NYALFPWMTVKENIEYPMKQQKMPKQEREKRLNELLEMAQLTGKENLYPHQISGGMKQRTAVIRALACKPEVLLMDEPLG 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446922839 182 ALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALKANPGEIKEIIEVNLPRPR 245
Cdd:NF040729 162 AVDFQMRQILQEELESIWLKDKTTVLMVTHDVDEAVYLSDRVIVMSRDKGKILEDLKIDLPRPR 225
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
19-238 |
1.13e-79 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 240.72 E-value: 1.13e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 19 PVILEAKQLSQVFKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGpCPER-- 96
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISS-LSERel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 --------GMVFQGYTLFPWKTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALV 168
Cdd:COG1136 81 arlrrrhiGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 169 NQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMdEAILLADRIVALKAnpGEIKEIIE 238
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRD--GRIVSDER 227
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
22-251 |
1.24e-79 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 244.67 E-value: 1.24e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 22 LEAKQLSQVFKhgqtERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGE--CITGPCPER--G 97
Cdd:COG1118 3 IEVRNISKRFG----SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRdlFTNLPPRERrvG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 98 MVFQGYTLFPWKTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMD 177
Cdd:COG1118 79 FVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 178 EPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALkaNPGEI------KEIIEvnlpRPRSLELMS 251
Cdd:COG1118 159 EPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVM--NQGRIeqvgtpDEVYD----RPATPFVAR 232
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
27-236 |
9.62e-79 |
|
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: 238.68 E-value: 9.62e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 27 LSQVFKH-GQTerTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITG-PCPER--GMVFQG 102
Cdd:cd03300 3 LENVSKFyGGF--VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlPPHKRpvNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 103 YTLFPWKTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGA 182
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446922839 183 LDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALkaNPGEIKEI 236
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVM--NKGKIQQI 212
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
22-227 |
1.98e-76 |
|
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: 232.00 E-value: 1.98e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 22 LEAKQLSQVFKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER----- 96
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 ----GMVFQGYTLFPWKTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPK 172
Cdd:cd03255 81 rrhiGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446922839 173 ILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAiLLADRIVALK 227
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELR 214
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
37-233 |
6.52e-75 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 233.04 E-value: 6.52e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 37 ERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER---GMVFQGYTLFPWKTVKE 113
Cdd:COG3839 15 GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDrniAMVFQSYALYPHMTVYE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 114 NVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQK 193
Cdd:COG3839 95 NIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446922839 194 HLMDLWQNIDITIIFVTHDMDEAILLADRIVALKAnpGEI 233
Cdd:COG3839 175 EIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMND--GRI 212
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
20-233 |
1.14e-74 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 233.46 E-value: 1.14e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 20 VILEAKQLSQVF-----------KHGQTERTVLNKL---------DLKIHKREfICVI-GPSGCGKSTLSRVIAGLDPYH 78
Cdd:COG4175 2 PKIEVRNLYKIFgkrperalkllDQGKSKDEILEKTgqtvgvndaSFDVEEGE-IFVImGLSGSGKSTLVRCLNRLIEPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 79 SGEVLVDGECITGpCPER----------GMVFQGYTLFPWKTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQ 148
Cdd:COG4175 81 AGEVLIDGEDITK-LSKKelrelrrkkmSMVFQHFALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 149 YPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALKA 228
Cdd:COG4175 160 YPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKD 239
|
....*
gi 446922839 229 npGEI 233
Cdd:COG4175 240 --GRI 242
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
26-233 |
4.61e-71 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 221.50 E-value: 4.61e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 26 QLSQVFKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPE---RGM--VF 100
Cdd:COG1125 3 EFENVTKRYPDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVelrRRIgyVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 101 QGYTLFPWKTVKENVMFGPQMRGASQMTAEAQAREWINIIGL--EKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDE 178
Cdd:COG1125 83 QQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILLMDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446922839 179 PFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALKAnpGEI 233
Cdd:COG1125 163 PFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMRE--GRI 215
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
38-262 |
1.78e-70 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 218.42 E-value: 1.78e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 38 RTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPERGMVFQGYTLFPWKTVKENVMF 117
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGVVFQNEGLLPWRNVQDNVAF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 118 GPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMD 197
Cdd:PRK11248 94 GLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLK 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446922839 198 LWQNIDITIIFVTHDMDEAILLADRIVALKANPGEIKEIIEVNLPR-------PRSLElmSTPEFKQLRSRV 262
Cdd:PRK11248 174 LWQETGKQVLLITHDIEEAVFMATELVLLSPGPGRVVERLPLNFARrfvagesSRSIK--SDPQFIAMREYV 243
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
28-227 |
3.62e-70 |
|
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: 217.90 E-value: 3.62e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 28 SQVFKhgQTERTV-LNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER---------G 97
Cdd:cd03294 28 EEILK--KTGQTVgVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrkkiS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 98 MVFQGYTLFPWKTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMD 177
Cdd:cd03294 106 MVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMD 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446922839 178 EPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALK 227
Cdd:cd03294 186 EAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMK 235
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
41-242 |
9.07e-69 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes 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 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. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 217.41 E-value: 9.07e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 41 LNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER---------GMVFQGYTLFPWKTV 111
Cdd:TIGR01186 9 VNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVElrevrrkkiGMVFQQFALFPHMTI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 112 KENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKM 191
Cdd:TIGR01186 89 LQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLIRDSM 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446922839 192 QKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALKANpgeikEIIEVNLP 242
Cdd:TIGR01186 169 QDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAG-----EIVQVGTP 214
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
22-233 |
5.31e-68 |
|
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: 211.39 E-value: 5.31e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 22 LEAKQLSQVFKHGqteRTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER----- 96
Cdd:cd03295 1 IEFENVTKRYGGG---KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrrki 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 GMVFQGYTLFPWKTVKENVMFGPQMRGASQMTAEAQAREWINIIGLE--KYENQYPHQLSGGMKQRVAIARALVNQPKIL 174
Cdd:cd03295 78 GYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446922839 175 LMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALKAnpGEI 233
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKN--GEI 214
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
22-228 |
8.50e-68 |
|
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: 208.58 E-value: 8.50e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 22 LEAKQLSQVFKHgqteRTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER----- 96
Cdd:cd03229 1 LELKNVSKRYGQ----KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpplrr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 --GMVFQGYTLFPWKTVKENVMFGpqmrgasqmtaeaqarewiniiglekyenqyphqLSGGMKQRVAIARALVNQPKIL 174
Cdd:cd03229 77 riGMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446922839 175 LMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALKA 228
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
17-241 |
9.15e-67 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 212.89 E-value: 9.15e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 17 ERPVILEAKQLSQVFKHgqteRTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER 96
Cdd:PRK09452 10 SLSPLVELRGISKSFDG----KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 ---GMVFQGYTLFPWKTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKI 173
Cdd:PRK09452 86 rhvNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446922839 174 LLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALkaNPGEI------KEIIE--VNL 241
Cdd:PRK09452 166 LLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVM--RDGRIeqdgtpREIYEepKNL 239
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
39-236 |
9.56e-67 |
|
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: 211.82 E-value: 9.56e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 39 TVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER---GMVFQGYTLFPWKTVKENV 115
Cdd:TIGR03265 18 TALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKrdyGIVFQSYALFPNLTVADNI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 116 MFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHL 195
Cdd:TIGR03265 98 AYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSALDARVREHLRTEI 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446922839 196 MDLWQNIDITIIFVTHDMDEAILLADRIVALkaNPGEIKEI 236
Cdd:TIGR03265 178 RQLQRRLGVTTIMVTHDQEEALSMADRIVVM--NHGVIEQV 216
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
22-233 |
1.16e-66 |
|
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: 207.57 E-value: 1.16e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 22 LEAKQLSqvFKHgQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER----- 96
Cdd:COG1122 1 IELENLS--FSY-PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrrkv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 GMVFQgytlFPW-----KTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQP 171
Cdd:COG1122 78 GLVFQ----NPDdqlfaPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446922839 172 KILLMDEPFGALDPHTRQKMQKHLMDLWQNiDITIIFVTHDMDEAILLADRIVALKAnpGEI 233
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDD--GRI 212
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
17-236 |
7.96e-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: 7.96e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 17 ERPVILEAKQLSQVFK-HGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPE 95
Cdd:COG1123 256 AAEPLLEVRNLSKRYPvRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 96 R--------GMVFQG-YT-LFPWKTVKENVMFGPQMRG-ASQMTAEAQAREWINIIGL-EKYENQYPHQLSGGMKQRVAI 163
Cdd:COG1123 336 SlrelrrrvQMVFQDpYSsLNPRMTVGDIIAEPLRLHGlLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAI 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446922839 164 ARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALKAnpGEIKEI 236
Cdd:COG1123 416 ARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYD--GRIVED 486
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
37-236 |
2.49e-65 |
|
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: 203.64 E-value: 2.49e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 37 ERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCP-ER--GMVFQGYTLFPWKTVKE 113
Cdd:cd03301 12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPkDRdiAMVFQNYALYPHMTVYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 114 NVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQK 193
Cdd:cd03301 92 NIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446922839 194 HLMDLWQNIDITIIFVTHDMDEAILLADRIVALkaNPGEIKEI 236
Cdd:cd03301 172 ELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVM--NDGQIQQI 212
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
18-227 |
3.55e-65 |
|
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: 204.06 E-value: 3.55e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 18 RPVILEAKQLSQVFkhGqtERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGpCPER- 96
Cdd:COG1127 2 SEPMIEVRNLTKSF--G--DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITG-LSEKe 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 --------GMVFQGYTLFPWKTVKENVMFGPQMRGA-SQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARAL 167
Cdd:COG1127 77 lyelrrriGMLFQGGALFDSLTVFENVAFPLREHTDlSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 168 VNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALK 227
Cdd:COG1127 157 ALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLA 216
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
21-235 |
7.02e-64 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 200.99 E-value: 7.02e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 21 ILEAKQLSQVFkhGQTErtVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER---- 96
Cdd:COG1126 1 MIEIENLHKSF--GDLE--VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDInklr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 ---GMVFQGYTLFPWKTVKENVMFGP-QMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPK 172
Cdd:COG1126 77 rkvGMVFQQFNLFPHLTVLENVTLAPiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446922839 173 ILLMDEPFGALDPhtrqKMQKHLMDLWQNI---DITIIFVTHDMDEAILLADRIVALKAnpGEIKE 235
Cdd:COG1126 157 VMLFDEPTSALDP----ELVGEVLDVMRDLakeGMTMVVVTHEMGFAREVADRVVFMDG--GRIVE 216
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
23-227 |
9.87e-64 |
|
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: 199.62 E-value: 9.87e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 23 EAKQLSqvFKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER-----G 97
Cdd:cd03225 1 ELKNLS--FSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrrkvG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 98 MVFQgytlFP-----WKTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPK 172
Cdd:cd03225 79 LVFQ----NPddqffGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446922839 173 ILLMDEPFGALDPHTRQKMQKHLMDLWQNiDITIIFVTHDMDEAILLADRIVALK 227
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLE 208
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
37-247 |
1.82e-63 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 200.29 E-value: 1.82e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 37 ERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLvdgeciTGPCP------ERGMVFQGYTLFPWKT 110
Cdd:PRK11247 24 ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL------AGTAPlaeareDTRLMFQDARLLPWKK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 111 VKENVMFGpqMRGASQmtaeAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQK 190
Cdd:PRK11247 98 VIDNVGLG--LKGQWR----DAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446922839 191 MQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALKAnpGEIKEIIEVNLPRPRSL 247
Cdd:PRK11247 172 MQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEE--GKIGLDLTVDLPRPRRR 226
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
39-236 |
3.23e-63 |
|
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: 199.10 E-value: 3.23e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 39 TVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITG-PCPER--GMVFQGYTLFPWKTVKENV 115
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDvPVQERnvGFVFQHYALFRHMTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 116 MFGPQMRGASQMTAEAQAR----EWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKM 191
Cdd:cd03296 96 AFGLRVKPRSERPPEAEIRakvhELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKEL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446922839 192 QKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALkaNPGEIKEI 236
Cdd:cd03296 176 RRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVM--NKGRIEQV 218
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
21-245 |
5.74e-63 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 198.78 E-value: 5.74e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 21 ILEAKQLSQVFkhGQTerTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCP------ 94
Cdd:PRK09493 1 MIEFKNVSKHF--GPT--QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVderlir 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 95 -ERGMVFQGYTLFPWKTVKENVMFGP-QMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPK 172
Cdd:PRK09493 77 qEAGMVFQQFYLFPHLTALENVMFGPlRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446922839 173 ILLMDEPFGALDPHTRQKMQKHLMDLWQNiDITIIFVTHDMDEAILLADRIVALK----ANPGEIKEIIEvNLPRPR 245
Cdd:PRK09493 157 LMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDkgriAEDGDPQVLIK-NPPSQR 231
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
22-224 |
6.30e-63 |
|
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: 197.37 E-value: 6.30e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 22 LEAKQLSQVFKhgqtERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPE----R- 96
Cdd:cd03262 1 IEIKNLHKSFG----DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelRq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 --GMVFQGYTLFPWKTVKENVMFGP-QMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKI 173
Cdd:cd03262 77 kvGMVFQQFNLFPHLTVLENITLAPiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446922839 174 LLMDEPFGALDPHTRQKMQKHLMDLWQNiDITIIFVTHDMDEAILLADRIV 224
Cdd:cd03262 157 MLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVI 206
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
37-226 |
6.42e-62 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 195.80 E-value: 6.42e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 37 ERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER--------GMVFQGYTLFPW 108
Cdd:cd03261 12 GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrrrmGMLFQSGALFDS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 109 KTVKENVMFGPQMRGA-SQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHT 187
Cdd:cd03261 92 LTVFENVAFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIA 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 446922839 188 RQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVAL 226
Cdd:cd03261 172 SGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVL 210
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
56-236 |
6.80e-62 |
|
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: 198.87 E-value: 6.80e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 56 VIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER---GMVFQGYTLFPWKTVKENVMFGPQMRGASQMTAEAQ 132
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLrhiNMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 133 AREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHD 212
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180
....*....|....*....|....
gi 446922839 213 MDEAILLADRIVALkaNPGEIKEI 236
Cdd:TIGR01187 161 QEEAMTMSDRIAIM--RKGKIAQI 182
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
21-236 |
3.87e-61 |
|
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: 193.49 E-value: 3.87e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 21 ILEAKQLSQVFKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER---- 96
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 ----GMVFQGY--TLFPWKTVKENVMFGPQMRGASQMTAEAQAREWINIIGL---EKYENQYPHQLSGGMKQRVAIARAL 167
Cdd:cd03257 81 rkeiQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446922839 168 VNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALKAnpGEIKEI 236
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYA--GKIVEE 227
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
21-235 |
1.17e-60 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 192.41 E-value: 1.17e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 21 ILEAKQLSQVFKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECIT-----GPCPE 95
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTllsgkELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 96 R---GMVFQGYTLFPWKTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPK 172
Cdd:cd03258 81 RrriGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446922839 173 ILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALKAnpGEIKE 235
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEK--GEVVE 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
21-248 |
2.38e-59 |
|
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: 197.05 E-value: 2.38e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 21 ILEAKQLSQVFKHGqtERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYH---SGEVLVDGECITGPCP--- 94
Cdd:COG1123 4 LLEVRDLSVRYPGG--DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEalr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 95 --ERGMVFQ--GYTLFPWkTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQ 170
Cdd:COG1123 82 grRIGMVFQdpMTQLNPV-TVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 171 PKILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALKAnpGEIKEI--IEVNLPRPRSLE 248
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDD--GRIVEDgpPEEILAAPQALA 238
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
21-235 |
1.61e-58 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 190.29 E-value: 1.61e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 21 ILEAKQLSQVFKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGpCPER---- 96
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTA-LSERelra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 -----GMVFQGYTLFPWKTVKENVMFgPqMRGASQMTAEAQAR--EWINIIGLEKYENQYPHQLSGGMKQRVAIARALVN 169
Cdd:COG1135 80 arrkiGMIFQHFNLLSSRTVAENVAL-P-LEIAGVPKAEIRKRvaELLELVGLSDKADAYPSQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446922839 170 QPKILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMD--EAIllADRIVALKAnpGEIKE 235
Cdd:COG1135 158 NPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDvvRRI--CDRVAVLEN--GRIVE 221
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
43-229 |
2.62e-58 |
|
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: 185.96 E-value: 2.62e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 43 KLDLKIhKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGEC-------ITGPCPER--GMVFQGYTLFPWKTVKE 113
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkINLPPQQRkiGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 114 NVMFGpqMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQK 193
Cdd:cd03297 95 NLAFG--LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 446922839 194 HLMDLWQNIDITIIFVTHDMDEAILLADRIVALKAN 229
Cdd:cd03297 173 ELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDG 208
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
22-233 |
2.68e-58 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 186.42 E-value: 2.68e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 22 LEAKQLSQVFKhgqtERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPE-R---G 97
Cdd:COG1131 1 IEVRGLTKRYG----DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEvRrriG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 98 MVFQGYTLFPWKTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMD 177
Cdd:COG1131 77 YVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446922839 178 EPFGALDPHTRQKMQKHLMDLWQNiDITIIFVTHDMDEAILLADRIVALKAnpGEI 233
Cdd:COG1131 157 EPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDK--GRI 209
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
39-236 |
2.96e-58 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 186.54 E-value: 2.96e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 39 TVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER---GMVFQGYTLFPWKTVKENV 115
Cdd:TIGR00968 14 QALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDrkiGFVFQHYALFKHLTVRDNI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 116 MFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHL 195
Cdd:TIGR00968 94 AFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALDAKVRKELRSWL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446922839 196 MDLWQNIDITIIFVTHDMDEAILLADRIVALkaNPGEIKEI 236
Cdd:TIGR00968 174 RKLHDEVHVTTVFVTHDQEEAMEVADRIVVM--SNGKIEQI 212
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
26-235 |
1.98e-57 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 183.72 E-value: 1.98e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 26 QLSQVFKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER--------G 97
Cdd:COG2884 3 RFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrrriG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 98 MVFQGYTLFPWKTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMD 177
Cdd:COG2884 83 VVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLAD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446922839 178 EPFGALDPHTRQKmqkhLMDLWQNID---ITIIFVTHDMDeaiLLAD---RIVALKAnpGEIKE 235
Cdd:COG2884 163 EPTGNLDPETSWE----IMELLEEINrrgTTVLIATHDLE---LVDRmpkRVLELED--GRLVR 217
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
22-259 |
4.42e-57 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 183.85 E-value: 4.42e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 22 LEAKQLSQVFKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER----- 96
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrrrv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 GMVFQGYT--LFPWKTVKEnVMFGPqMRGASQMTAEAQAREWINIIGL-EKYENQYPHQLSGGMKQRVAIARALVNQPKI 173
Cdd:COG1124 82 QMVFQDPYasLHPRHTVDR-ILAEP-LRIHGLPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 174 LLMDEPFGALDPHTrqkmQKHLMDLWQNI----DITIIFVTHDMDEAILLADRIVALKAnpGEIKEIievnLPRPRSLEL 249
Cdd:COG1124 160 LLLDEPTSALDVSV----QAEILNLLKDLreerGLTYLFVSHDLAVVAHLCDRVAVMQN--GRIVEE----LTVADLLAG 229
|
250
....*....|
gi 446922839 250 MSTPEFKQLR 259
Cdd:COG1124 230 PKHPYTRELL 239
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
41-236 |
2.04e-56 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 185.28 E-value: 2.04e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 41 LNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER---GMVFQGYTLFPWKTVKENVMF 117
Cdd:NF040840 16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKrgiAYVYQNYMLFPHKTVFENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 118 GPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMD 197
Cdd:NF040840 96 GLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIREMKR 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446922839 198 LWQNIDITIIFVTHDMDEAILLADRIVALK----ANPGEIKEI 236
Cdd:NF040840 176 WHREFGFTAIHVTHNFEEALSLADRVGIMLngrlSQVGDVREV 218
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
21-233 |
8.82e-56 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 180.25 E-value: 8.82e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 21 ILEAKQLSQVFKHGqteRTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER---- 96
Cdd:COG3638 2 MLELRNLSKRYPGG---TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 ----GMVFQGYTLFPWKTVKENVMFG--PQMRG----ASQMTAE--AQAREWINIIGLEKYENQYPHQLSGGMKQRVAIA 164
Cdd:COG3638 79 rrriGMIFQQFNLVPRLSVLTNVLAGrlGRTSTwrslLGLFPPEdrERALEALERVGLADKAYQRADQLSGGQQQRVAIA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446922839 165 RALVNQPKILLMDEPFGALDPHTRQkmqkHLMDLWQNI----DITIIFVTHDMDEAILLADRIVALKAnpGEI 233
Cdd:COG3638 159 RALVQEPKLILADEPVASLDPKTAR----QVMDLLRRIaredGITVVVNLHQVDLARRYADRIIGLRD--GRV 225
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
54-228 |
9.73e-56 |
|
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: 183.76 E-value: 9.73e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 54 ICVI-GPSGCGKSTLSRVIAGLDPYHSGEVLVDGEC-------ITGPcPER---GMVFQGYTLFPWKTVKENVMFGpqMR 122
Cdd:COG4148 27 VTALfGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlqdsargIFLP-PHRrriGYVFQEARLFPHLSVRGNLLYG--RK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 123 GASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNI 202
Cdd:COG4148 104 RAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDEL 183
|
170 180
....*....|....*....|....*.
gi 446922839 203 DITIIFVTHDMDEAILLADRIVALKA 228
Cdd:COG4148 184 DIPILYVSHSLDEVARLADHVVLLEQ 209
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
22-228 |
3.84e-55 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 177.32 E-value: 3.84e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 22 LEAKQLSqvfkHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER----- 96
Cdd:COG4619 1 LELEGLS----FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrrqv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 GMVFQGYTLFPwKTVKENVMFGPQMRGasQMTAEAQAREWINIIGL-EKYENQYPHQLSGGMKQRVAIARALVNQPKILL 175
Cdd:COG4619 77 AYVPQEPALWG-GTVRDNLPFPFQLRE--RKFDRERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446922839 176 MDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALKA 228
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEA 206
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
21-235 |
1.10e-54 |
|
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: 177.24 E-value: 1.10e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 21 ILEAKQLSQVFKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITgPCPER---- 96
Cdd:COG4181 8 IIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLF-ALDEDarar 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 ------GMVFQGYTLFPWKTVKENVMFGPQMRGASQmtAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQ 170
Cdd:COG4181 87 lrarhvGFVFQSFQLLPTLTALENVMLPLELAGRRD--ARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446922839 171 PKILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDeailLA---DRIVALKAnpGEIKE 235
Cdd:COG4181 165 PAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPA----LAarcDRVLRLRA--GRLVE 226
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
37-250 |
1.21e-54 |
|
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: 178.41 E-value: 1.21e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 37 ERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER--------GMVFQ--GYTLF 106
Cdd:TIGR04521 17 EKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKlkdlrkkvGLVFQfpEHQLF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 107 PwKTVKENVMFGPQMRGASQMTAEAQAREWINIIGL-EKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDP 185
Cdd:TIGR04521 97 E-ETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDP 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446922839 186 HTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALKA-------NPGEI----KEIIEVNLPRPRSLELM 250
Cdd:TIGR04521 176 KGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKgkivldgTPREVfsdvDELEKIGLDVPEITELA 251
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
40-236 |
3.88e-54 |
|
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: 175.99 E-value: 3.88e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 40 VLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER---GMVFQGYTLFPWKTVKENVM 116
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKrdiSYVPQNYALFPHMTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 117 FGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLM 196
Cdd:cd03299 94 YGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELK 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446922839 197 DLWQNIDITIIFVTHDMDEAILLADRIVALKAnpGEIKEI 236
Cdd:cd03299 174 KIRKEFGVTVLHVTHDFEEAWALADKVAIMLN--GKLIQV 211
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
21-233 |
4.80e-54 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 176.00 E-value: 4.80e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 21 ILEAKQLSqvFKHGQteRTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCP-----E 95
Cdd:COG1120 1 MLEAENLS--VGYGG--RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRrelarR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 96 RGMVFQGYTL-FPWkTVKENVMFG--PQMRGASQMTAE--AQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQ 170
Cdd:COG1120 77 IAYVPQEPPApFGL-TVRELVALGryPHLGLFGRPSAEdrEAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446922839 171 PKILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALKAnpGEI 233
Cdd:COG1120 156 PPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKD--GRI 216
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
39-236 |
6.03e-53 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 176.45 E-value: 6.03e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 39 TVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITgpcpERG-------MVFQGYTLFPWKTV 111
Cdd:PRK11432 20 TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT----HRSiqqrdicMVFQSYALFPHMSL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 112 KENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKM 191
Cdd:PRK11432 96 GENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSM 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446922839 192 QKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALkaNPGEIKEI 236
Cdd:PRK11432 176 REKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVM--NKGKIMQI 218
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
45-224 |
8.17e-53 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 172.25 E-value: 8.17e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 45 DLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCP-ERG--MVFQGYTLFPWKTVKENVMFG--P 119
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPaERPvsMLFQENNLFPHLTVAQNIGLGlrP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 120 QMRgasqMTAEAQAR--EWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMD 197
Cdd:COG3840 99 GLK----LTAEQRAQveQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDE 174
|
170 180
....*....|....*....|....*..
gi 446922839 198 LWQNIDITIIFVTHDMDEAILLADRIV 224
Cdd:COG3840 175 LCRERGLTVLMVTHDPEDAARIADRVL 201
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
22-233 |
4.24e-52 |
|
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: 170.83 E-value: 4.24e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 22 LEAKQLSQVFKHGqteRTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECIT--GPCPER--- 96
Cdd:cd03256 1 IEVENLSKTYPNG---KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINklKGKALRqlr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 ---GMVFQGYTLFPWKTVKENVMFG-----PQMRGASQMTAEAQ---AREWINIIGLEKYENQYPHQLSGGMKQRVAIAR 165
Cdd:cd03256 78 rqiGMIFQQFNLIERLSVLENVLSGrlgrrSTWRSLFGLFPKEEkqrALAALERVGLLDKAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446922839 166 ALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALKAnpGEI 233
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKD--GRI 223
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
22-236 |
5.27e-52 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 174.12 E-value: 5.27e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 22 LEAKQLSQVFKHGQtertVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITG-PCPER--GM 98
Cdd:PRK10851 3 IEIANIKKSFGRTQ----VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRlHARDRkvGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 99 VFQGYTLFPWKTVKENVMFG----PQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKIL 174
Cdd:PRK10851 79 VFQHYALFRHMTVFDNIAFGltvlPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446922839 175 LMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALkaNPGEIKEI 236
Cdd:PRK10851 159 LLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVM--SQGNIEQA 218
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
37-236 |
2.92e-51 |
|
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: 168.13 E-value: 2.92e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 37 ERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGL-DPY----HSGEVLVDGECITGPCPER-------GMVFQGYT 104
Cdd:cd03260 12 DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLnDLIpgapDEGEVLLDGKDIYDLDVDVlelrrrvGMVFQKPN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 105 LFPwKTVKENVMFGPQMRGASQMTA-EAQAREWINIIGL--EKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFG 181
Cdd:cd03260 92 PFP-GSIYDNVAYGLRLHGIKLKEElDERVEEALRKAALwdEVKDRLHALGLSGGQQQRLCLARALANEPEVLLLDEPTS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446922839 182 ALDPHTRQKMQKHLMDLwqNIDITIIFVTHDMDEAILLADRIVALkaNPGEIKEI 236
Cdd:cd03260 171 ALDPISTAKIEELIAEL--KKEYTIVIVTHNMQQAARVADRTAFL--LNGRLVEF 221
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
38-227 |
2.73e-50 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 169.79 E-value: 2.73e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 38 RTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGL--DPYHSGEVLVDGECITGPCPER---GMVFQGYTLFPWKTVK 112
Cdd:TIGR03258 18 NTVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFvkAAGLTGRIAIADRDLTHAPPHKrglALLFQNYALFPHLKVE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 113 ENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQ 192
Cdd:TIGR03258 98 DNVAFGLRAQKMPKADIAERVADALKLVGLGDAAAHLPAQLSGGMQQRIAIARAIAIEPDVLLLDEPLSALDANIRANMR 177
|
170 180 190
....*....|....*....|....*....|....*.
gi 446922839 193 KHLMDLWQNI-DITIIFVTHDMDEAILLADRIVALK 227
Cdd:TIGR03258 178 EEIAALHEELpELTILCVTHDQDDALTLADKAGIMK 213
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
21-238 |
4.99e-50 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 169.63 E-value: 4.99e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 21 ILEAKQLSQVFKhGQTertVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER---G 97
Cdd:PRK11607 19 LLEIRNLTKSFD-GQH---AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQrpiN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 98 MVFQGYTLFPWKTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMD 177
Cdd:PRK11607 95 MMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446922839 178 EPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALKANP----GEIKEIIE 238
Cdd:PRK11607 175 EPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKfvqiGEPEEIYE 239
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
26-239 |
1.04e-49 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 168.10 E-value: 1.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 26 QLSQVFKH--GQTErtVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCP-ERG--MVF 100
Cdd:PRK11650 5 KLQAVRKSydGKTQ--VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPaDRDiaMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 101 QGYTLFPWKTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPF 180
Cdd:PRK11650 83 QNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446922839 181 GALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALkaNPGEIKEI---IEV 239
Cdd:PRK11650 163 SNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVM--NGGVAEQIgtpVEV 222
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
22-233 |
1.85e-49 |
|
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: 161.80 E-value: 1.85e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 22 LEAKQLSQVFKhgqtERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER----G 97
Cdd:cd03230 1 IEVRNLSKRYG----KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVkrriG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 98 MVFQGYTLFPWKTVKENVmfgpqmrgasqmtaeaqarewiniiglekyenqyphQLSGGMKQRVAIARALVNQPKILLMD 177
Cdd:cd03230 77 YLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446922839 178 EPFGALDPHTRQKMQKHLMDLwQNIDITIIFVTHDMDEAILLADRIVALKAnpGEI 233
Cdd:cd03230 121 EPTSGLDPESRREFWELLREL-KKEGKTILLSSHILEEAERLCDRVAILNN--GRI 173
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
39-236 |
3.83e-49 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 166.74 E-value: 3.83e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 39 TVLNK-LDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITG-PCPER--GMVFQGYTLFPWKTVKEN 114
Cdd:PRK11000 16 VVISKdINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDvPPAERgvGMVFQSYALYPHLSVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 115 VMFGPQMRGASQmtAEAQAR--EWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQ 192
Cdd:PRK11000 96 MSFGLKLAGAKK--EEINQRvnQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMR 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446922839 193 KHLMDLWQNIDITIIFVTHDMDEAILLADRIVALKAnpGEIKEI 236
Cdd:PRK11000 174 IEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDA--GRVAQV 215
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
21-233 |
1.96e-48 |
|
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: 161.31 E-value: 1.96e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 21 ILEAKQLSQVFKHGqteRTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER---- 96
Cdd:TIGR02315 1 MLEVENLSKVYPNG---KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrkl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 ----GMVFQGYTLFPWKTVKENVMFG-----PQMRGASQMTAEAQAREWINI---IGLEKYENQYPHQLSGGMKQRVAIA 164
Cdd:TIGR02315 78 rrriGMIFQHYNLIERLTVLENVLHGrlgykPTWRSLLGRFSEEDKERALSAlerVGLADKAYQRADQLSGGQQQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446922839 165 RALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALKAnpGEI 233
Cdd:TIGR02315 158 RALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKA--GEI 224
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
21-224 |
3.73e-48 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 162.92 E-value: 3.73e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 21 ILEAKQLSQVFKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYH---SGEVLVDGECITGpCPER- 96
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLK-LSEKe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 ---------GMVFQG-YT-LFPWKTVKENVMFGPQM-RGASQMTAEAQAREWINIIGL---EKYENQYPHQLSGGMKQRV 161
Cdd:COG0444 80 lrkirgreiQMIFQDpMTsLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446922839 162 AIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIV 224
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVA 222
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
22-249 |
4.00e-48 |
|
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: 161.44 E-value: 4.00e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 22 LEAKQLSqvFKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDG------ECItgpcPE 95
Cdd:TIGR04520 1 IEVENVS--FSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGldtldeENL----WE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 96 -R---GMVFQ-------GytlfpwKTVKENVMFGPQMRGASqmTAEAQAR--EWINIIGLEKYENQYPHQLSGGMKQRVA 162
Cdd:TIGR04520 75 iRkkvGMVFQnpdnqfvG------ATVEDDVAFGLENLGVP--REEMRKRvdEALKLVGMEDFRDREPHLLSGGQKQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 163 IARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAIlLADRIVALKAN-------PGEI-- 233
Cdd:TIGR04520 147 IAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKGkivaegtPREIfs 225
|
250
....*....|....*...
gi 446922839 234 --KEIIEVNLPRPRSLEL 249
Cdd:TIGR04520 226 qvELLKEIGLDVPFITEL 243
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
19-226 |
6.65e-48 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 159.87 E-value: 6.65e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 19 PVILEAKQLSqvFKHGqtERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPERGM 98
Cdd:COG1121 4 MPAIELENLT--VSYG--GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 99 VFQgYTLFPWK---TVKENVMFG--PQMRGASQMTAE--AQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQP 171
Cdd:COG1121 80 VPQ-RAEVDWDfpiTVRDVVLMGryGRRGLFRRPSRAdrEAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446922839 172 KILLMDEPFGALDPHTrqkmQKHLMDL---WQNIDITIIFVTHDMDEAILLADRIVAL 226
Cdd:COG1121 159 DLLLLDEPFAGVDAAT----EEALYELlreLRREGKTILVVTHDLGAVREYFDRVLLL 212
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
19-226 |
6.99e-48 |
|
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: 160.20 E-value: 6.99e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 19 PVILEAKQLSQVFkhGqtERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER-- 96
Cdd:COG0411 2 DPLLEVRGLTKRF--G--GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRia 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 --GMV--FQGYTLFPWKTVKENVMFGPQMRGASQMT---------------AEAQAREWINIIGLEKYENQYPHQLSGGM 157
Cdd:COG0411 78 rlGIArtFQNPRLFPELTVLENVLVAAHARLGRGLLaallrlprarreereARERAEELLERVGLADRADEPAGNLSYGQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 158 KQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDeAIL-LADRIVAL 226
Cdd:COG0411 158 QRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMD-LVMgLADRIVVL 226
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
23-227 |
1.56e-47 |
|
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: 156.25 E-value: 1.56e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 23 EAKQLSQVFKhgqtERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITgpcpergmvfqg 102
Cdd:cd00267 1 EIENLSFRYG----GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIA------------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 103 ytlfpwktvkenvmfgpqmrgasqmtaEAQAREWINIIGLEkyenqypHQLSGGMKQRVAIARALVNQPKILLMDEPFGA 182
Cdd:cd00267 65 ---------------------------KLPLEELRRRIGYV-------PQLSGGQRQRVALARALLLNPDLLLLDEPTSG 110
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446922839 183 LDPHTRQKMQKHLMDLWQNiDITIIFVTHDMDEAILLADRIVALK 227
Cdd:cd00267 111 LDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLK 154
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
23-235 |
8.87e-47 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 159.97 E-value: 8.87e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 23 EAKQLSQVFKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECIT-----GPCPER- 96
Cdd:PRK11153 3 ELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTalsekELRKARr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 --GMVFQGYTLFPWKTVKENVMFGPQMRGASQmtAEAQAR--EWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPK 172
Cdd:PRK11153 83 qiGMIFQHFNLLSSRTVFDNVALPLELAGTPK--AEIKARvtELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446922839 173 ILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALKAnpGEIKE 235
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDA--GRLVE 221
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
22-235 |
1.33e-46 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 166.16 E-value: 1.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 22 LEAKQLSqvFKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPE--R--- 96
Cdd:COG2274 474 IELENVS--FRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPAslRrqi 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 GMVFQGYTLFPwKTVKENVMFGpqmrgASQMTaEAQAREWINIIGLEKYENQYPH-----------QLSGGMKQRVAIAR 165
Cdd:COG2274 552 GVVLQDVFLFS-GTIRENITLG-----DPDAT-DEEIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIAR 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 166 ALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNidITIIFVTHDMdEAILLADRIVALKAnpGEIKE 235
Cdd:COG2274 625 ALLRNPRILILDEATSALDAETEAIILENLRRLLKG--RTVIIIAHRL-STIRLADRIIVLDK--GRIVE 689
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
23-227 |
6.55e-46 |
|
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: 152.59 E-value: 6.55e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 23 EAKQLSqvFKHGQteRTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECItgpcpergmvfqg 102
Cdd:cd03214 1 EVENLS--VGYGG--RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDL------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 103 ytlfpwktvkenvmfgpqmrgaSQMTAEAQARE------WINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLM 176
Cdd:cd03214 64 ----------------------ASLSPKELARKiayvpqALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446922839 177 DEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALK 227
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLK 172
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
22-227 |
1.01e-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: 152.15 E-value: 1.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 22 LEAKQLSqvFKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER----- 96
Cdd:cd03228 1 IEFKNVS--FSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrkni 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 GMVFQGYTLFPwKTVKENVmfgpqmrgasqmtaeaqarewiniiglekyenqyphqLSGGMKQRVAIARALVNQPKILLM 176
Cdd:cd03228 79 AYVPQDPFLFS-GTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446922839 177 DEPFGALDPHTRQKMQKHLMDLWQniDITIIFVTHDMdEAILLADRIVALK 227
Cdd:cd03228 121 DEATSALDPETEALILEALRALAK--GKTVIVIAHRL-STIRDADRIIVLD 168
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
22-227 |
1.62e-45 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 153.86 E-value: 1.62e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 22 LEAKQLSQVFKhgqtERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER----G 97
Cdd:COG4555 2 IEVENLSKKYG----KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREArrqiG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 98 MVFQGYTLFPWKTVKENV-MFGPQMRGASQmTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLM 176
Cdd:COG4555 78 VLPDERGLYDRLTVRENIrYFAELYGLFDE-ELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446922839 177 DEPFGALDPHTRQKMQKHLMDLwQNIDITIIFVTHDMDEAILLADRIVALK 227
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILH 206
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
21-235 |
2.40e-45 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 152.89 E-value: 2.40e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 21 ILEAKQLSQVFKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER---- 96
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNErakl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 -----GMVFQGYTLFPWKTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQP 171
Cdd:TIGR02211 81 rnkklGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446922839 172 KILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDeailLADRI-VALKANPGEIKE 235
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLE----LAKKLdRVLEMKDGQLFN 221
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
39-226 |
7.50e-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: 151.82 E-value: 7.50e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 39 TVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCP----ERGMV--FQGYTLFPWKTVK 112
Cdd:cd03219 14 VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPheiaRLGIGrtFQIPRLFPELTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 113 ENVMFGPQMRG----------ASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGA 182
Cdd:cd03219 94 ENVMVAAQARTgsglllararREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAG 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446922839 183 LDPHTRQKMQKHLMDLWQNiDITIIFVTHDMDEAILLADRIVAL 226
Cdd:cd03219 174 LNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVL 216
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
41-180 |
1.99e-44 |
|
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: 147.79 E-value: 1.99e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 41 LNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER-----GMVFQGYTLFPWKTVKENV 115
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlrkeiGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446922839 116 MFGPQMRGASQMTAEAQAREWINIIGLEKYENQ----YPHQLSGGMKQRVAIARALVNQPKILLMDEPF 180
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
34-227 |
2.17e-44 |
|
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: 149.99 E-value: 2.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 34 GQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGpcpERGMVfqGY--------TL 105
Cdd:cd03235 8 SYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK---ERKRI--GYvpqrrsidRD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 106 FPwKTVKENVMFG--PQMRGASQMTAE--AQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFG 181
Cdd:cd03235 83 FP-ISVRDVVLMGlyGHKGLFRRLSKAdkAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446922839 182 ALDPHTrqkmQKHLMDL---WQNIDITIIFVTHDMDEAILLADRIVALK 227
Cdd:cd03235 162 GVDPKT----QEDIYELlreLRREGMTILVVTHDLGLVLEYFDRVLLLN 206
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
26-226 |
2.42e-44 |
|
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: 149.71 E-value: 2.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 26 QLSQVFKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITgPCPER--------- 96
Cdd:TIGR02673 3 EFHNVSKAYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVN-RLRGRqlpllrrri 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 GMVFQGYTLFPWKTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLM 176
Cdd:TIGR02673 82 GVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446922839 177 DEPFGALDPHTRQKmqkhLMDLWQNIDI---TIIFVTHDMDEAILLADRIVAL 226
Cdd:TIGR02673 162 DEPTGNLDPDLSER----ILDLLKRLNKrgtTVIVATHDLSLVDRVAHRVIIL 210
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
33-223 |
3.11e-44 |
|
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of a conserved four gene ABC transporter operon found next to ectoine unilization operons and ectoine biosynthesis operons. Ectoine is a compatible solute that protects enzymes from high osmolarity. It is released by some species in response to hypoosmotic shock, and it is taken up by a number of bacteria as a compatible solute or for consumption. This family shows strong sequence similiarity to a number of amino acid ABC transporter ATP-binding proteins.
Pssm-ID: 132050 [Multi-domain] Cd Length: 252 Bit Score: 150.75 E-value: 3.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 33 HGQTER----TVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECIT---------GPCPER--- 96
Cdd:TIGR03005 4 SDVTKRfgilTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYhmpgrngplVPADEKhlr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 ------GMVFQGYTLFPWKTVKENVMFGP-QMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVN 169
Cdd:TIGR03005 84 qmrnkiGMVFQSFNLFPHKTVLDNVTEAPvLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARALAM 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446922839 170 QPKILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRI 223
Cdd:TIGR03005 164 RPKVMLFDEVTSALDPELVGEVLNVIRRLASEHDLTMLLVTHEMGFAREFADRV 217
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
43-276 |
4.06e-44 |
|
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: 153.34 E-value: 4.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 43 KLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECI----TGPC--PER---GMVFQGYTLFPWKTVKE 113
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsrKGIFlpPEKrriGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 114 NVMFG-PQMRGASQMTAEAqarEWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQ 192
Cdd:TIGR02142 95 NLRYGmKRARPSERRISFE---RVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEIL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 193 KHLMDLWQNIDITIIFVTHDMDEAILLADRIVALKAnpGEIKEI--IEvnlprprslELMSTPEFKQL-RSRVDYLVHAE 269
Cdd:TIGR02142 172 PYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLED--GRVAAAgpIA---------EVWASPDLPWLaREDQGSLIEGV 240
|
....*..
gi 446922839 270 EDELDPA 276
Cdd:TIGR02142 241 VAEHDQH 247
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
44-226 |
3.82e-43 |
|
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: 146.87 E-value: 3.82e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 44 LDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER---GMVFQGYTLFPWKTVKENVMFG-- 118
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADrpvSMLFQENNLFAHLTVEQNVGLGls 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 119 PQMRgasqMTAEAQARewINII----GLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKH 194
Cdd:cd03298 97 PGLK----LTAEDRQA--IEVAlarvGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190
....*....|....*....|....*....|..
gi 446922839 195 LMDLWQNIDITIIFVTHDMDEAILLADRIVAL 226
Cdd:cd03298 171 VLDLHAETKMTVLMVTHQPEDAKRLAQRVVFL 202
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
25-226 |
1.45e-42 |
|
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: 145.07 E-value: 1.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 25 KQLSQVFKHgqteRTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER-------- 96
Cdd:TIGR03608 2 KNISKKFGD----KVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKaskfrrek 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 -GMVFQGYTLFPWKTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILL 175
Cdd:TIGR03608 78 lGYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLIL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446922839 176 MDEPFGALDPHTRQKMQKHLMDLwQNIDITIIFVTHDMdEAILLADRIVAL 226
Cdd:TIGR03608 158 ADEPTGSLDPKNRDEVLDLLLEL-NDEGKTIIIVTHDP-EVAKQADRVIEL 206
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
45-222 |
5.58e-42 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 144.34 E-value: 5.58e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 45 DLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER---GMVFQGYTLFPWKTVKENVMFG--P 119
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRrpvSMLFQENNLFSHLTVAQNIGLGlnP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 120 QMR--GASQMTAEAQAREwiniIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMD 197
Cdd:PRK10771 99 GLKlnAAQREKLHAIARQ----MGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQ 174
|
170 180
....*....|....*....|....*
gi 446922839 198 LWQNIDITIIFVTHDMDEAILLADR 222
Cdd:PRK10771 175 VCQERQLTLLMVSHSLEDAARIAPR 199
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
22-224 |
2.09e-41 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 143.35 E-value: 2.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 22 LEAKQLSQVFkHGQTertVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCP------- 94
Cdd:PRK11264 4 IEVKNLVKKF-HGQT---VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSlsqqkgl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 95 ------ERGMVFQGYTLFPWKTVKENVMFGP-QMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARAL 167
Cdd:PRK11264 80 irqlrqHVGFVFQNFNLFPHRTVLENIIEGPvIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446922839 168 VNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNiDITIIFVTHDMDEAILLADRIV 224
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAI 215
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
38-226 |
2.57e-41 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 141.85 E-value: 2.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 38 RTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAG-LDP--YHSGEVLVDGECITGPCPER---GMVFQGYTLFPWKTV 111
Cdd:COG4136 14 RPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPafSASGEVLLNGRRLTALPAEQrriGILFQDDLLFPHLSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 112 KENVMFG--PQMRGASQMTAEAQAREWIniiGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQ 189
Cdd:COG4136 94 GENLAFAlpPTIGRAQRRARVEQALEEA---GLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRA 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 446922839 190 KMQKHLMDLWQNIDITIIFVTHDMDEAiLLADRIVAL 226
Cdd:COG4136 171 QFREFVFEQIRQRGIPALLVTHDEEDA-PAAGRVLDL 206
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
22-234 |
8.53e-41 |
|
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: 140.72 E-value: 8.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 22 LEAKQLSQVFKhgQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGP---CPER-G 97
Cdd:cd03263 1 LQIRNLTKTYK--KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDrkaARQSlG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 98 MVFQGYTLFPWKTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMD 177
Cdd:cd03263 79 YCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446922839 178 EPFGALDPHTRQkmqkhlmDLWQNI-----DITIIFVTHDMDEAILLADRIVALKAnpGEIK 234
Cdd:cd03263 159 EPTSGLDPASRR-------AIWDLIlevrkGRSIILTTHSMDEAEALCDRIAIMSD--GKLR 211
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
21-212 |
2.62e-40 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 139.91 E-value: 2.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 21 ILEAKQLSQVFKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER---- 96
Cdd:PRK10584 6 IVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEArakl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 -----GMVFQGYTLFPWKTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQP 171
Cdd:PRK10584 86 rakhvGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446922839 172 KILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHD 212
Cdd:PRK10584 166 DVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
37-261 |
4.01e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 141.34 E-value: 4.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 37 ERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPC-------PERGMVFQ--GYTLFP 107
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKvklsdirKKVGLVFQypEYQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 108 wKTVKENVMFGPQMRGASQMTAEAQAREWINIIGL--EKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDP 185
Cdd:PRK13637 99 -ETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 186 HTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRI-------VALKANPGEI-KEII---EVNLPRPRSLELMstpe 254
Cdd:PRK13637 178 KGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIivmnkgkCELQGTPREVfKEVEtleSIGLAVPQVTYLV---- 253
|
....*..
gi 446922839 255 fKQLRSR 261
Cdd:PRK13637 254 -RKLRKK 259
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
22-228 |
4.48e-40 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 138.38 E-value: 4.48e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 22 LEAKQLSQVFKhgqtERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPErgmvFQ 101
Cdd:COG4133 3 LEAENLSCRRG----ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED----YR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 102 GYTLF-----PWK---TVKENVMFGPQMRGASQmtAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKI 173
Cdd:COG4133 75 RRLAYlghadGLKpelTVRENLRFWAALYGLRA--DREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446922839 174 LLMDEPFGALDPHTRQKMQKHLMDLWQNiDITIIFVTHDMDEaiLLADRIVALKA 228
Cdd:COG4133 153 WLLDEPFTALDAAGVALLAELIAAHLAR-GGAVLLTTHQPLE--LAAARVLDLGD 204
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
8-260 |
5.35e-39 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 140.94 E-value: 5.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 8 AHEYFQKIYERPVILEAKQLSQVFKHGQtertvlnkldLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGE 87
Cdd:PRK10070 21 AFKYIEQGLSKEQILEKTGLSLGVKDAS----------LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 88 CITGPCPER---------GMVFQGYTLFPWKTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMK 158
Cdd:PRK10070 91 DIAKISDAElrevrrkkiAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 159 QRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALKANpgeikEIIE 238
Cdd:PRK10070 171 QRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNG-----EVVQ 245
|
250 260
....*....|....*....|..
gi 446922839 239 VNLPRprslELMSTPEFKQLRS 260
Cdd:PRK10070 246 VGTPD----EILNNPANDYVRT 263
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
19-222 |
1.50e-38 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 136.32 E-value: 1.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 19 PVILEAKQLSqvFKHGqtERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGL-DPY----HSGEVLVDGECITGP- 92
Cdd:COG1117 9 EPKIEVRNLN--VYYG--DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMnDLIpgarVEGEILLDGEDIYDPd 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 93 ---CPER---GMVFQGYTLFPwKTVKENVMFGPQMRGASQmTAEAQAR-EWIniigLEK---YE------NQYPHQLSGG 156
Cdd:COG1117 85 vdvVELRrrvGMVFQKPNPFP-KSIYDNVAYGLRLHGIKS-KSELDEIvEES----LRKaalWDevkdrlKKSALGLSGG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446922839 157 MKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQniDITIIFVTHDMDEAILLADR 222
Cdd:COG1117 159 QQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKK--DYTIVIVTHNMQQAARVSDY 222
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
43-226 |
1.53e-38 |
|
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: 134.99 E-value: 1.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 43 KLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER---GMVFQGYTLFPWKTVKENVMFG- 118
Cdd:TIGR01277 16 EFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQrpvSMLFQENNLFAHLTVRQNIGLGl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 119 -PQMR--GASQMTAEAQAREwiniIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHL 195
Cdd:TIGR01277 96 hPGLKlnAEQQEKVVDAAQQ----VGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALV 171
|
170 180 190
....*....|....*....|....*....|.
gi 446922839 196 MDLWQNIDITIIFVTHDMDEAILLADRIVAL 226
Cdd:TIGR01277 172 KQLCSERQRTLLMVTHHLSDARAIASQIAVV 202
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
18-235 |
1.67e-38 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 136.08 E-value: 1.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 18 RPVILEAKQLSQVFkhGQTErtVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECI-------- 89
Cdd:COG4598 5 APPALEVRDLHKSF--GDLE--VLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkpdrdg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 90 -TGPCPER---------GMVFQGYTLFPWKTVKENVMFGP-QMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMK 158
Cdd:COG4598 81 eLVPADRRqlqrirtrlGMVFQSFNLWSHMTVLENVIEAPvHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446922839 159 QRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNiDITIIFVTHDMDEAILLADRIVALkaNPGEIKE 235
Cdd:COG4598 161 QRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSHVVFL--HQGRIEE 234
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
17-235 |
1.69e-38 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 142.20 E-value: 1.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 17 ERPVILEAKQLSqvFKHGQtERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPE- 95
Cdd:COG4988 332 AGPPSIELEDVS--FSYPG-GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAs 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 96 -RGMVF---QGYTLFPWkTVKENVMFGpqMRGASqmtaEAQAREWINIIGLEKYENQYPH-----------QLSGGMKQR 160
Cdd:COG4988 409 wRRQIAwvpQNPYLFAG-TIRENLRLG--RPDAS----DEELEAALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQR 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446922839 161 VAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQniDITIIFVTHDMdEAILLADRIVALKAnpGEIKE 235
Cdd:COG4988 482 LALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRL-ALLAQADRILVLDD--GRIVE 551
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-236 |
1.84e-38 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 136.68 E-value: 1.84e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 21 ILEAKQLSqvFKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITgpcPER---- 96
Cdd:PRK13635 5 IIRVEHIS--FRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLS---EETvwdv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 ----GMVFQGY-TLFPWKTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQP 171
Cdd:PRK13635 80 rrqvGMVFQNPdNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446922839 172 KILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAiLLADRIVALkaNPGEIKEI 236
Cdd:PRK13635 160 DIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVM--NKGEILEE 221
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
22-228 |
2.23e-38 |
|
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: 134.33 E-value: 2.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 22 LEAKQLSQVFKhgqtERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECIT-------GPCP 94
Cdd:cd03269 1 LEVENVTKRFG----RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDiaarnriGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 95 E-RGmvfqgytLFPWKTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKI 173
Cdd:cd03269 77 EeRG-------LYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPEL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446922839 174 LLMDEPFGALDPHTRQKMQKHLMDLWQNiDITIIFVTHDMDEAILLADRIVALKA 228
Cdd:cd03269 150 LILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNK 203
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
18-261 |
2.75e-38 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 141.83 E-value: 2.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 18 RPVILEAKQLSqvFKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECIT------- 90
Cdd:COG4987 330 GGPSLELEDVS--FRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRdldeddl 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 91 ----GPCPERGMVFQGytlfpwkTVKENVMFG-PQmrgASqmtaEAQAREWINIIGLEKYENQYPH-----------QLS 154
Cdd:COG4987 408 rrriAVVPQRPHLFDT-------TLRENLRLArPD---AT----DEELWAALERVGLGDWLAALPDgldtwlgeggrRLS 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 155 GGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQniDITIIFVTHDMdEAILLADRIVALKAnpGEIK 234
Cdd:COG4987 474 GGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRL-AGLERMDRILVLED--GRIV 548
|
250 260
....*....|....*....|....*...
gi 446922839 235 EiievnlpRPRSLELMSTPE-FKQLRSR 261
Cdd:COG4987 549 E-------QGTHEELLAQNGrYRQLYQR 569
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
21-273 |
7.09e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 135.24 E-value: 7.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 21 ILEAKQLSQVFKHGQTERTvLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITgpcPER---- 96
Cdd:PRK13650 4 IIEVKNLTFKYKEDQEKYT-LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLT---EENvwdi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 ----GMVFQGY-TLFPWKTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQP 171
Cdd:PRK13650 80 rhkiGMVFQNPdNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 172 KILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEaILLADRIVALK-------ANPGEI----KEIIEVN 240
Cdd:PRK13650 160 KIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKngqvestSTPRELfsrgNDLLQLG 238
|
250 260 270
....*....|....*....|....*....|....
gi 446922839 241 LPRPRSLELMSTPEFKQLRSRVDYLVHAE-EDEL 273
Cdd:PRK13650 239 LDIPFTTSLVQSLRQNGYDLPEGYLTEKElEEQL 272
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
22-227 |
2.16e-37 |
|
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: 131.76 E-value: 2.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 22 LEAKQLSQVFKHGQTertVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITG------PCPE 95
Cdd:cd03292 1 IEFINVTKTYPNGTA---ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrgraiPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 96 R--GMVFQGYTLFPWKTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKI 173
Cdd:cd03292 78 RkiGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446922839 174 LLMDEPFGALDPHTRQKmqkhLMDLWQNID---ITIIFVTHDMDEAILLADRIVALK 227
Cdd:cd03292 158 LIADEPTGNLDPDTTWE----IMNLLKKINkagTTVVVATHAKELVDTTRHRVIALE 210
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
31-239 |
2.32e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 133.58 E-value: 2.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 31 FKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER-----GMVFQGY-T 104
Cdd:PRK13632 15 FSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEirkkiGIIFQNPdN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 105 LFPWKTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALD 184
Cdd:PRK13632 95 QFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446922839 185 PHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAIlLADRIVALK-------ANPGEI---KEIIEV 239
Cdd:PRK13632 175 PKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSegkliaqGKPKEIlnnKEILEK 238
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
56-226 |
1.20e-36 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 133.46 E-value: 1.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 56 VIGPSGCGKSTLSRVIAGLDPYHSGE------VLVDGE---CITgpcPER---GMVFQGYTLFPWKTVKENVMFGpqMRG 123
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRivlngrVLFDAEkgiCLP---PEKrriGYVFQDARLFPHYKVRGNLRYG--MAK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 124 ASQmtaeAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALD-PHTRQKMQkHLMDLWQNI 202
Cdd:PRK11144 104 SMV----AQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKRELLP-YLERLAREI 178
|
170 180
....*....|....*....|....
gi 446922839 203 DITIIFVTHDMDEAILLADRIVAL 226
Cdd:PRK11144 179 NIPILYVSHSLDEILRLADRVVVL 202
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
22-227 |
1.53e-36 |
|
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: 127.93 E-value: 1.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 22 LEAKQLSQVFkhGQTerTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPergmvfq 101
Cdd:cd03216 1 LELRGITKRF--GGV--KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASP------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 102 gytlfpwktvkenvmfgpqmrgasqmtAEAQAREwINIIglekyenqypHQLSGGMKQRVAIARALVNQPKILLMDEPFG 181
Cdd:cd03216 70 ---------------------------RDARRAG-IAMV----------YQLSVGERQMVEIARALARNARLLILDEPTA 111
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446922839 182 ALDPHTRQKMQKHLMDLwQNIDITIIFVTHDMDEAILLADRIVALK 227
Cdd:cd03216 112 ALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLR 156
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
26-267 |
2.02e-36 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 130.13 E-value: 2.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 26 QLSQV-FKHGQTErtVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECI---TGPCPER----- 96
Cdd:PRK11124 4 QLNGInCFYGAHQ--ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAirelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 ---GMVFQGYTLFPWKTVKENVMFGP-QMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPK 172
Cdd:PRK11124 82 rnvGMVFQQYNLWPHLTVQQNLIEAPcRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 173 ILLMDEPFGALDPHTRQKMQKHLMDLwQNIDITIIFVTHDMDEAILLADRIVALkanpgEIKEIIEVNlpRPRSLELMST 252
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYM-----ENGHIVEQG--DASCFTQPQT 233
|
250
....*....|....*
gi 446922839 253 PEFKQlrsrvdYLVH 267
Cdd:PRK11124 234 EAFKN------YLSH 242
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
21-250 |
3.93e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 130.58 E-value: 3.93e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 21 ILEAKQLSQVFKHGqTErtVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECI----TGPCPER 96
Cdd:PRK13639 1 ILETRDLKYSYPDG-TE--ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkydkKSLLEVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 ---GMVFQGY--TLFPwKTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQP 171
Cdd:PRK13639 78 ktvGIVFQNPddQLFA-PTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 172 KILLMDEPFGALDPHTRQKMQKHLMDLWQNiDITIIFVTHDMDEAILLADRIVAL-------KANPGEI---KEIIE-VN 240
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMsdgkiikEGTPKEVfsdIETIRkAN 235
|
250
....*....|
gi 446922839 241 LPRPRSLELM 250
Cdd:PRK13639 236 LRLPRVAHLI 245
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
23-229 |
6.40e-36 |
|
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: 127.76 E-value: 6.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 23 EAKQLSQVFKHGQTertVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGEcitgPCPER------ 96
Cdd:cd03226 1 RIENISFSYKKGTE---ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGK----PIKAKerrksi 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 GMVFQ--GYTLFPwKTVKENVMFGPQMRGASQMTAEAQAREwiniIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKIL 174
Cdd:cd03226 74 GYVMQdvDYQLFT-DSVREELLLGLKELDAGNEQAETVLKD----LDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446922839 175 LMDEPFGALDPHTRQKMQKHLMDLwQNIDITIIFVTHDMDEAILLADRIVALKAN 229
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELIREL-AAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
37-236 |
9.04e-36 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 134.91 E-value: 9.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 37 ERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGL-DPYhSGEVLVDG------------ECItgpcperGMVFQGY 103
Cdd:COG1132 352 DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFyDPT-SGRILIDGvdirdltleslrRQI-------GVVPQDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 104 TLFPwKTVKENVMFG------PQMRGASQMtaeAQAREWIniiglEKYENQYPHQ-------LSGGMKQRVAIARALVNQ 170
Cdd:COG1132 424 FLFS-GTIRENIRYGrpdatdEEVEEAAKA---AQAHEFI-----EALPDGYDTVvgergvnLSGGQRQRIAIARALLKD 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446922839 171 PKILLMDEPFGALDPHTRQKMQKHLMDLWQniDITIIFVTHDMdEAILLADRIVALKAnpGEIKEI 236
Cdd:COG1132 495 PPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRL-STIRNADRILVLDD--GRIVEQ 555
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
22-226 |
1.23e-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: 127.55 E-value: 1.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 22 LEAKQLSQvfKHGQTErtVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITG-PCPER---- 96
Cdd:cd03224 1 LEVENLNA--GYGKSQ--ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGlPPHERarag 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 -GMVFQGYTLFPWKTVKENVMFGPQMRGASqmtAEAQAREWIniiglekYE---------NQYPHQLSGGMKQRVAIARA 166
Cdd:cd03224 77 iGYVPEGRRIFPELTVEENLLLGAYARRRA---KRKARLERV-------YElfprlkerrKQLAGTLSGGEQQMLAIARA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446922839 167 LVNQPKILLMDEPFGALDPhtrqKMQKHLMDLWQNI---DITIIFVTHDMDEAILLADRIVAL 226
Cdd:cd03224 147 LMSRPKLLLLDEPSEGLAP----KIVEEIFEAIRELrdeGVTILLVEQNARFALEIADRAYVL 205
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
26-238 |
2.27e-35 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 127.44 E-value: 2.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 26 QLSQV-FKHGQTErtVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECI---TGPCPER----- 96
Cdd:COG4161 4 QLKNInCFYGSHQ--ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAirllr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 ---GMVFQGYTLFPWKTVKENVMFGP-QMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPK 172
Cdd:COG4161 82 qkvGMVFQQYNLWPHLTVMENLIEAPcKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446922839 173 ILLMDEPFGALDPHTRQKMQKHLMDLwQNIDITIIFVTHDMDEAILLADRIVALkanpgEIKEIIE 238
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYM-----EKGRIIE 221
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
22-234 |
2.70e-35 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 126.72 E-value: 2.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 22 LEAKQLsqVFKHGQTErtVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITG-PCPER---G 97
Cdd:cd03265 1 IEVENL--VKKYGDFE--AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVRePREVRrriG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 98 MVFQGYTLFPWKTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMD 177
Cdd:cd03265 77 IVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446922839 178 EPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRI-------VALKANPGEIK 234
Cdd:cd03265 157 EPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVaiidhgrIIAEGTPEELK 220
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
44-287 |
2.77e-35 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. 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. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 129.05 E-value: 2.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 44 LDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDG-ECITGPCPER---GMVFQGYTLFPWKTVKENVMFGP 119
Cdd:TIGR01188 12 VNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGyDVVREPRKVRrsiGIVPQYASVDEDLTGRENLEMMG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 120 QMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLw 199
Cdd:TIGR01188 92 RLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDYIRAL- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 200 QNIDITIIFVTHDMDEAILLADRI-------VALKANPGEIKEIIEVNLPRPRSLELmstpefKQLRSRVDYLVHaeedE 272
Cdd:TIGR01188 171 KEEGVTILLTTHYMEEADKLCDRIaiidhgrIIAEGTPEELKRRLGKDTLESRPRDI------QSLKVEVSMLIA----E 240
|
250
....*....|....*
gi 446922839 273 LDPALQDLPKIPRMT 287
Cdd:TIGR01188 241 LGETGLGLLAVTVDS 255
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-236 |
2.93e-35 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 128.69 E-value: 2.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 21 ILEAKQLSQVFKhgqtERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECIT-------GPC 93
Cdd:COG4152 1 MLELKGLTKRFG----DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDpedrrriGYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 94 PE-RGmvfqgytLFPWKTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPK 172
Cdd:COG4152 77 PEeRG-------LYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPE 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446922839 173 ILLMDEPFGALDPHTRQKMQKHLMDLWQNiDITIIFVTHDMDEAILLADRIVALK-----ANpGEIKEI 236
Cdd:COG4152 150 LLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINkgrkvLS-GSVDEI 216
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
22-233 |
6.13e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 127.64 E-value: 6.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 22 LEAKQLSQVFKHGQT-ERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER---- 96
Cdd:PRK13641 3 IKFENVDYIYSPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnlkk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 -----GMVFQgytlFPW-----KTVKENVMFGPQMRGASQMTAEAQAREWINIIGL-EKYENQYPHQLSGGMKQRVAIAR 165
Cdd:PRK13641 83 lrkkvSLVFQ----FPEaqlfeNTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446922839 166 ALVNQPKILLMDEPFGALDPHTRQKMQKHLMDlWQNIDITIIFVTHDMDEAILLADRIVALK-------ANPGEI 233
Cdd:PRK13641 159 VMAYEPEILCLDEPAAGLDPEGRKEMMQLFKD-YQKAGHTVILVTHNMDDVAEYADDVLVLEhgklikhASPKEI 232
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
21-235 |
1.04e-34 |
|
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: 131.35 E-value: 1.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 21 ILEAKQLSQVFKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYH----SGEVLVDGECITGpCPER 96
Cdd:COG4172 6 LLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPaahpSGSILFDGQDLLG-LSER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 ----------GMVFQ--GYTLFPWKTVkenvmfGPQM-------RGASQMTAEAQAREWINIIGL---EKYENQYPHQLS 154
Cdd:COG4172 85 elrrirgnriAMIFQepMTSLNPLHTI------GKQIaevlrlhRGLSGAAARARALELLERVGIpdpERRLDAYPHQLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 155 GGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMdeAIL--LADRIVALKAnpGE 232
Cdd:COG4172 159 GGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDL--GVVrrFADRVAVMRQ--GE 234
|
...
gi 446922839 233 IKE 235
Cdd:COG4172 235 IVE 237
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
35-249 |
1.54e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 126.36 E-value: 1.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 35 QTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDG------ECITGPCPERGMVFQG------ 102
Cdd:PRK13633 20 STEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsdeENLWDIRNKAGMVFQNpdnqiv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 103 YTLfpwktVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGA 182
Cdd:PRK13633 100 ATI-----VEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAM 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446922839 183 LDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAIlLADRI-------VALKANPGEI----KEIIEVNLPRPRSLEL 249
Cdd:PRK13633 175 LDPSGRREVVNTIKELNKKYGITIILITHYMEEAV-EADRIivmdsgkVVMEGTPKEIfkevEMMKKIGLDVPQVTEL 251
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
37-228 |
3.36e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 125.63 E-value: 3.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 37 ERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER---------GMVFQgytlFP 107
Cdd:PRK13649 19 EGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdikqirkkvGLVFQ----FP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 108 W-----KTVKENVMFGPQMRGASQMTAEAQAREWINIIGL-EKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFG 181
Cdd:PRK13649 95 EsqlfeETVLKDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446922839 182 ALDPHTRqkmqKHLMDLWQNID---ITIIFVTHDMDEAILLADRIVALKA 228
Cdd:PRK13649 175 GLDPKGR----KELMTLFKKLHqsgMTIVLVTHLMDDVANYADFVYVLEK 220
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
22-227 |
3.99e-34 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 124.46 E-value: 3.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 22 LEAKQLSqvFKHGQteRTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAG-LDPYhSGEVLVDGECITGPCPE----- 95
Cdd:COG4559 2 LEAENLS--VRLGG--RTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGeLTPS-SGEVRLNGRPLAAWSPWelarr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 96 RGMVFQGYTL-FPWkTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALV------ 168
Cdd:COG4559 77 RAVLPQHSSLaFPF-TVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepv 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446922839 169 -NQPKILLMDEPFGALDP-HtrqkmQKHLMDL---WQNIDITIIFVTHDMDEAILLADRIVALK 227
Cdd:COG4559 156 dGGPRWLFLDEPTSALDLaH-----QHAVLRLarqLARRGGGVVAVLHDLNLAAQYADRILLLH 214
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
37-227 |
9.26e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 124.36 E-value: 9.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 37 ERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER---------GMVFQgytlFP 107
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKklkplrkkvGIVFQ----FP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 108 W-----KTVKENVMFGPQMRGASQMTAEAQAREWINIIGL-EKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFG 181
Cdd:PRK13634 95 EhqlfeETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446922839 182 ALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALK 227
Cdd:PRK13634 175 GLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMH 220
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
21-227 |
1.27e-33 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 123.58 E-value: 1.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 21 ILEAKQLSQVFKHGQTertvLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGL---DPYHSGEVLVDGEC--------- 88
Cdd:PRK09984 4 IIRVEKLAKTFNQHQA----LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTvqregrlar 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 89 -ITGPCPERGMVFQGYTLFPWKTVKENVMFG-----PQMRGASQMTAEAQ---AREWINIIGLEKYENQYPHQLSGGMKQ 159
Cdd:PRK09984 80 dIRKSRANTGYIFQQFNLVNRLSVLENVLIGalgstPFWRTCFSWFTREQkqrALQALTRVGMVHFAHQRVSTLSGGQQQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446922839 160 RVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALK 227
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALR 227
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
21-223 |
1.79e-33 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 122.23 E-value: 1.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 21 ILEAKQLSQVFKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCP------ 94
Cdd:PRK11629 5 LLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakael 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 95 ---ERGMVFQGYTLFPWKTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQP 171
Cdd:PRK11629 85 rnqKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446922839 172 KILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDeailLADRI 223
Cdd:PRK11629 165 RLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQ----LAKRM 212
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
40-216 |
2.32e-33 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 120.61 E-value: 2.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 40 VLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECI----TGPCPER---GMVFQG--YTLFpWKT 110
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLdysrKGLLERRqrvGLVFQDpdDQLF-AAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 111 VKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQK 190
Cdd:TIGR01166 86 VDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGREQ 165
|
170 180
....*....|....*....|....*.
gi 446922839 191 MQKHLMDLwQNIDITIIFVTHDMDEA 216
Cdd:TIGR01166 166 MLAILRRL-RAEGMTVVISTHDVDLA 190
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
22-234 |
2.52e-33 |
|
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: 121.15 E-value: 2.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 22 LEAKQLSQVFKHGQtertVLNKLDLKIhKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGEcitgPCPERGMVFQ 101
Cdd:cd03264 1 LQLENLTKRYGKKR----ALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQ----DVLKQPQKLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 102 ---GY-----TLFPWKTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKI 173
Cdd:cd03264 72 rriGYlpqefGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446922839 174 LLMDEPFGALDPHTRQKMQKHLMDLWQniDITIIFVTHDMDEAILLADRIVALKAnpGEIK 234
Cdd:cd03264 152 LIVDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNK--GKLV 208
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
37-237 |
2.90e-33 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 122.12 E-value: 2.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 37 ERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAG-LDPYHSGEVLVDGEcitgpcpERGmvfqGYTLFPWK------ 109
Cdd:COG1119 15 GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRLFGE-------RRG----GEDVWELRkriglv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 110 ------------TVKENVM------------FGPQMRgasqmtaeAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIAR 165
Cdd:COG1119 84 spalqlrfprdeTVLDVVLsgffdsiglyrePTDEQR--------ERARELLELLGLAHLADRPFGTLSQGEQRRVLIAR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 166 ALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDE-------AILLAD-RIVALkanpGEIKEII 237
Cdd:COG1119 156 ALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEippgithVLLLKDgRVVAA----GPKEEVL 231
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
22-227 |
3.18e-33 |
|
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: 120.78 E-value: 3.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 22 LEAKQLSQVFKHgqteRTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECIT--GPCPER-GM 98
Cdd:cd03268 1 LKTNDLTKTYGK----KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQknIEALRRiGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 99 VFQGYTLFPWKTVKENVMFGPQMRGASqmtaEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDE 178
Cdd:cd03268 77 LIEAPGFYPNLTARENLRLLARLLGIR----KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446922839 179 PFGALDPHTRQKMQKHLMDLwQNIDITIIFVTHDMDEAILLADRIVALK 227
Cdd:cd03268 153 PTNGLDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIIN 200
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-227 |
5.56e-33 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 126.29 E-value: 5.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 19 PVILEAKQLSQVFkhGQTerTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCP---- 94
Cdd:COG1129 2 EPLLEMRGISKSF--GGV--KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPrdaq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 95 ERG--MVFQGYTLFPWKTVKENVMFGPQMRGA-----SQMtaEAQAREWINIIGLEkyENqyPHQ----LSGGMKQRVAI 163
Cdd:COG1129 78 AAGiaIIHQELNLVPNLSVAENIFLGREPRRGglidwRAM--RRRARELLARLGLD--ID--PDTpvgdLSVAQQQLVEI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446922839 164 ARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLwQNIDITIIFVTHDMDEAILLADRIVALK 227
Cdd:COG1129 152 ARALSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLDEVFEIADRVTVLR 214
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
20-213 |
8.74e-33 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 122.92 E-value: 8.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 20 VILEAKQLSQVFK-----HGQTERTV--LNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGP 92
Cdd:COG4608 6 PLLEVRDLKKHFPvrgglFGRTVGVVkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 93 CPER--------GMVFQG-YT-LFPWKTVKENVMFGPQMRG-ASQMTAEAQAREWINIIGLEK-YENQYPHQLSGGMKQR 160
Cdd:COG4608 86 SGRElrplrrrmQMVFQDpYAsLNPRMTVGDIIAEPLRIHGlASKAERRERVAELLELVGLRPeHADRYPHEFSGGQRQR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446922839 161 VAIARALVNQPKILLMDEPFGALDphtrQKMQKH----LMDLWQNIDITIIFVTHDM 213
Cdd:COG4608 166 IGIARALALNPKLIVCDEPVSALD----VSIQAQvlnlLEDLQDELGLTYLFISHDL 218
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
22-226 |
1.02e-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: 118.47 E-value: 1.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 22 LEAKQLSqvFKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER----- 96
Cdd:cd03246 1 LEVENVS--FRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElgdhv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 GMVFQGYTLFPwKTVKENVmfgpqmrgasqmtaeaqarewiniiglekyenqyphqLSGGMKQRVAIARALVNQPKILLM 176
Cdd:cd03246 79 GYLPQDDELFS-GSIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446922839 177 DEPFGALDPHTRQkmqkHLMDLWQNIDI---TIIFVTHDMdEAILLADRIVAL 226
Cdd:cd03246 121 DEPNSHLDVEGER----ALNQAIAALKAagaTRIVIAHRP-ETLASADRILVL 168
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
21-213 |
2.69e-32 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 119.94 E-value: 2.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 21 ILEAKQLSQVFKH-----GQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECIT-GPCP 94
Cdd:COG4167 4 LLEVRNLSKTFKYrtglfRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEyGDYK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 95 ERG----MVFQ--GYTLFPWKTVKEnVMFGPqMRGASQMTAEAQAREWINIIG----LEKYENQYPHQLSGGMKQRVAIA 164
Cdd:COG4167 84 YRCkhirMIFQdpNTSLNPRLNIGQ-ILEEP-LRLNTDLTAEEREERIFATLRlvglLPEHANFYPHMLSSGQKQRVALA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446922839 165 RALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDM 213
Cdd:COG4167 162 RALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHL 210
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-240 |
3.24e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 119.81 E-value: 3.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 21 ILEAKQLSQVFKHGQ-TERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER--- 96
Cdd:COG1101 1 MLELKNLSKTFNPGTvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKrak 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 --GMVFQGYTL--FPWKTVKENVMFGpQMRGASQ-----MTAE--AQAREWINII--GLEKYENQYPHQLSGGMKQRVAI 163
Cdd:COG1101 81 yiGRVFQDPMMgtAPSMTIEENLALA-YRRGKRRglrrgLTKKrrELFRELLATLglGLENRLDTKVGLLSGGQRQALSL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 164 ARALVNQPKILLMDEPFGALDPHTRQKmqkhLMDLWQNI----DITIIFVTHDMDEAILLADRIVALKAnpGEIkeIIEV 239
Cdd:COG1101 160 LMATLTKPKLLLLDEHTAALDPKTAAL----VLELTEKIveenNLTTLMVTHNMEQALDYGNRLIMMHE--GRI--ILDV 231
|
.
gi 446922839 240 N 240
Cdd:COG1101 232 S 232
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
21-233 |
3.59e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 119.91 E-value: 3.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 21 ILEAKQLSQVFKhgqTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER---- 96
Cdd:PRK13652 3 LIETRDLCYSYS---GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREvrkf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 -GMVFQGY--TLFPwKTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKI 173
Cdd:PRK13652 80 vGLVFQNPddQIFS-PTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 174 LLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALkaNPGEI 233
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVM--DKGRI 216
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
21-261 |
3.68e-32 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 125.22 E-value: 3.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 21 ILEAKQLSQVFKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER---- 96
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAlaql 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 -----GMVFQGYTLFPWKTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQP 171
Cdd:PRK10535 84 rrehfGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 172 KILLMDEPFGALDPHTRQKMQKHLMDLWQNiDITIIFVTHDMDEAIlLADRIVALK-----ANPGEIKEIIEVNLPRPrs 246
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVAA-QAERVIEIRdgeivRNPPAQEKVNVAGGTEP-- 239
|
250
....*....|....*
gi 446922839 247 lELMSTPEFKQLRSR 261
Cdd:PRK10535 240 -VVNTASGWRQFVSG 253
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
22-227 |
3.70e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 120.58 E-value: 3.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 22 LEAKQLSQVF-KHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEV-----------------L 83
Cdd:PRK13651 3 IKVKNIVKIFnKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekeK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 84 VDGECITGPCPER------------GMVFQ--GYTLFPwKTVKENVMFGPQMRGASQMTAEAQAREWINIIGL-EKYENQ 148
Cdd:PRK13651 83 VLEKLVIQKTRFKkikkikeirrrvGVVFQfaEYQLFE-QTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446922839 149 YPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNiDITIIFVTHDMDEAILLADRIVALK 227
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFK 239
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
20-227 |
8.72e-32 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 118.34 E-value: 8.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 20 VILEAKQLSqvFKHGQteRTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAG-LDPYhSGEVLVDGECITGPCPE--- 95
Cdd:PRK13548 1 AMLEARNLS--VRLGG--RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGeLSPD-SGEVRLNGRPLADWSPAela 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 96 --RGMVFQGYTL-FPWkTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALV---- 168
Cdd:PRK13548 76 rrRAVLPQHSSLsFPF-TVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwe 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446922839 169 --NQPKILLMDEPFGALDP-HtrqkmQKHLMDLWQNI----DITIIFVTHDMDEAILLADRIVALK 227
Cdd:PRK13548 155 pdGPPRWLLLDEPTSALDLaH-----QHHVLRLARQLaherGLAVIVVLHDLNLAARYADRIVLLH 215
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
14-236 |
2.29e-31 |
|
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: 116.48 E-value: 2.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 14 KIYERPVILEAKQLSQVFKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGEcITGPc 93
Cdd:cd03220 11 PTYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR-VSSL- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 94 PERGMVFQgytlfPWKTVKENVMFGPQMRGASQmtAEAQAREwINII---GLEKYENQYPHQLSGGMKQRVAIARALVNQ 170
Cdd:cd03220 89 LGLGGGFN-----PELTGRENIYLNGRLLGLSR--KEIDEKI-DEIIefsELGDFIDLPVKTYSSGMKARLAFAIATALE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446922839 171 PKILLMDEPFGALDPHTRQKMQKHLMDLWQNiDITIIFVTHDMDEAILLADRIVALKAnpGEIKEI 236
Cdd:cd03220 161 PDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEK--GKIRFD 223
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
11-226 |
2.69e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 118.80 E-value: 2.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 11 YFQKIYERP------VILEAKQLSQVFKHGQTER-TVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVL 83
Cdd:PRK13631 5 FMKKKLKVPnplsddIILRVKNLYCVFDEKQENElVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 84 V---------DGECITGPCPER------------GMVFQ--GYTLFPwKTVKENVMFGPQMRGASQMTAEAQAREWINII 140
Cdd:PRK13631 85 VgdiyigdkkNNHELITNPYSKkiknfkelrrrvSMVFQfpEYQLFK-DTIEKDIMFGPVALGVKKSEAKKLAKFYLNKM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 141 GL-EKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNiDITIIFVTHDMDEAILL 219
Cdd:PRK13631 164 GLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEV 242
|
....*..
gi 446922839 220 ADRIVAL 226
Cdd:PRK13631 243 ADEVIVM 249
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
21-233 |
2.97e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 117.59 E-value: 2.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 21 ILEAKQLSqvFKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGL---DPYHSGEVLVDGECITGP----C 93
Cdd:PRK13640 5 IVEFKHVS--FTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAKtvwdI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 94 PER-GMVFQGY-TLFPWKTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQP 171
Cdd:PRK13640 83 REKvGIVFQNPdNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446922839 172 KILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAIlLADRIVALkaNPGEI 233
Cdd:PRK13640 163 KIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVL--DDGKL 221
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
19-226 |
6.06e-31 |
|
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: 114.57 E-value: 6.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 19 PVILEAKQLSQVFKHGQTE--RTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYH--SGEVLVDGECITGPCP 94
Cdd:cd03213 1 GVTLSFRNLTVTVKSSPSKsgKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPLDKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 95 ER--GMVFQGYTLFPWKTVKENVMFGPQMRGasqmtaeaqarewiniiglekyenqyphqLSGGMKQRVAIARALVNQPK 172
Cdd:cd03213 81 RKiiGYVPQDDILHPTLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPS 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446922839 173 ILLMDEPFGALDPHTRQKMQKHLMDLWQNiDITIIFVTHD-MDEAILLADRIVAL 226
Cdd:cd03213 132 LLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQpSSEIFELFDKLLLL 185
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
37-250 |
8.37e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 116.65 E-value: 8.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 37 ERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCP----------ERGMVFQ--GYT 104
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKkikevkrlrkEIGLVFQfpEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 105 LFPwKTVKENVMFGPQMRGASQMTAEAQAREWINIIGL-EKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGAL 183
Cdd:PRK13645 103 LFQ-ETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGL 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446922839 184 DPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVAL-------KANPGEIKEIIE----VNLPRPRSLELM 250
Cdd:PRK13645 182 DPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMhegkvisIGSPFEIFSNQElltkIEIDPPKLYQLM 259
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
38-253 |
8.87e-31 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 117.62 E-value: 8.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 38 RTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGEcitgPCPER--------GMVFQGYTLFPWK 109
Cdd:PRK13536 54 KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGV----PVPARarlarariGVVPQFDNLDLEF 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 110 TVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQ 189
Cdd:PRK13536 130 TVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARH 209
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446922839 190 KMQKHLMDLWQNiDITIIFVTHDMDEAILLADRIVALKA-------NPGE-IKE-----IIEVNLPRPRSLELMSTP 253
Cdd:PRK13536 210 LIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAgrkiaegRPHAlIDEhigcqVIEIYGGDPHELSSLVKP 285
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
17-235 |
1.41e-30 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 114.43 E-value: 1.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 17 ERPVILEAKQLSqvFKHGqtERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPE- 95
Cdd:PRK10247 3 ENSPLLQLQNVG--YLAG--DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEi 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 96 -RGMV---FQGYTLFPwKTVKENVMFGPQMRG-ASQMTAEAQarewiniiGLEKYE------NQYPHQLSGGMKQRVAIA 164
Cdd:PRK10247 79 yRQQVsycAQTPTLFG-DTVYDNLIFPWQIRNqQPDPAIFLD--------DLERFAlpdtilTKNIAELSGGEKQRISLI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446922839 165 RALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEaILLADRIVALKANPGEIKE 235
Cdd:PRK10247 150 RNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE-INHADKVITLQPHAGEMQE 219
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
22-226 |
1.45e-30 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 120.08 E-value: 1.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 22 LEAKQLSQVFkhgQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER----- 96
Cdd:TIGR02857 322 LEFSGVSVAY---PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwrdqi 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 GMVFQGYTLFPwKTVKENVMFG------PQMRGASQMTAeaqAREWINII--GLEKYENQYPHQLSGGMKQRVAIARALV 168
Cdd:TIGR02857 399 AWVPQHPFLFA-GTIAENIRLArpdasdAEIREALERAG---LDEFVAALpqGLDTPIGEGGAGLSGGQAQRLALARAFL 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446922839 169 NQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNidITIIFVTHDmDEAILLADRIVAL 226
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRALAQG--RTVLLVTHR-LALAALADRIVVL 529
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
21-262 |
1.60e-30 |
|
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: 115.29 E-value: 1.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 21 ILEAKQLSQVFKHG-----QTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPE 95
Cdd:TIGR02769 2 LLEVRDVTHTYRTGglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 96 RG--------MVFQ-GYTLF-PWKTVKEnvMFGPQMRGASQMTAEAQAR---EWINIIGLE-KYENQYPHQLSGGMKQRV 161
Cdd:TIGR02769 82 QRrafrrdvqLVFQdSPSAVnPRMTVRQ--IIGEPLRHLTSLDESEQKAriaELLDMVGLRsEDADKLPRQLSGGQLQRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 162 AIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALkaNPGEIKEIIEVNl 241
Cdd:TIGR02769 160 NIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVM--DKGQIVEECDVA- 236
|
250 260
....*....|....*....|.
gi 446922839 242 prprSLELMSTPEFKQLRSRV 262
Cdd:TIGR02769 237 ----QLLSFKHPAGRNLQSAV 253
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
21-222 |
3.04e-30 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 114.49 E-value: 3.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 21 ILEAKQLSQVFkhgqTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVI---AGLDP--YHSGEVLVDGECITGPC-- 93
Cdd:PRK14239 5 ILQVSDLSVYY----NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmNDLNPevTITGSIVYNGHNIYSPRtd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 94 -----PERGMVFQGYTLFPWkTVKENVMFGPQMRGASQMTAEAQAREwINIIGLEKYENQYPH------QLSGGMKQRVA 162
Cdd:PRK14239 81 tvdlrKEIGMVFQQPNPFPM-SIYENVVYGLRLKGIKDKQVLDEAVE-KSLKGASIWDEVKDRlhdsalGLSGGQQQRVC 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 163 IARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQniDITIIFVTHDMDEAILLADR 222
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKD--DYTMLLVTRSMQQASRISDR 216
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
38-226 |
3.06e-30 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 112.71 E-value: 3.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 38 RTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPERGMVfqgytlfPWK---TVKEN 114
Cdd:NF040873 5 RPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEV-------PDSlplTVRDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 115 VMFGP-QMRGAS-QMTAEAQAR--EWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQK 190
Cdd:NF040873 78 VAMGRwARRGLWrRLTRDDRAAvdDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRER 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 446922839 191 MQKhLMDLWQNIDITIIFVTHDMDEAiLLADRIVAL 226
Cdd:NF040873 158 IIA-LLAEEHARGATVVVVTHDLELV-RRADPCVLL 191
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
17-235 |
3.90e-30 |
|
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: 118.63 E-value: 3.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 17 ERPVILEAKQLS-------QVFKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPyHSGEVLVDGECI 89
Cdd:COG4172 271 DAPPLLEARDLKvwfpikrGLFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 90 TGpCPERGM---------VFQ---GyTLFPWKTVKENVMFG-----PQMRGASQmtaEAQAREWINIIGL-EKYENQYPH 151
Cdd:COG4172 350 DG-LSRRALrplrrrmqvVFQdpfG-SLSPRMTVGQIIAEGlrvhgPGLSAAER---RARVAEALEEVGLdPAARHRYPH 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 152 QLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMD--EAilLADRIVALKAn 229
Cdd:COG4172 425 EFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAvvRA--LAHRVMVMKD- 501
|
....*.
gi 446922839 230 pGEIKE 235
Cdd:COG4172 502 -GKVVE 506
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
30-226 |
5.53e-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: 112.68 E-value: 5.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 30 VFKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECIT--GPCPER---GMVFQGYT 104
Cdd:cd03245 9 SFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRqlDPADLRrniGYVPQDVT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 105 LFpWKTVKENVMFGPQMrGASQMTAEAqarewINIIGLEKYENQYPH-----------QLSGGMKQRVAIARALVNQPKI 173
Cdd:cd03245 89 LF-YGTLRDNITLGAPL-ADDERILRA-----AELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446922839 174 LLMDEPFGALDPHTRQKMqKHLMDLWQnIDITIIFVTHDMdeAIL-LADRIVAL 226
Cdd:cd03245 162 LLLDEPTSAMDMNSEERL-KERLRQLL-GDKTLIIITHRP--SLLdLVDRIIVM 211
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
40-243 |
5.62e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 113.78 E-value: 5.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 40 VLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGL-----DPYHSGEVLVDGECITGPC-------PERGMVFQGYTLFP 107
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDvdpievrREVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 108 WKTVKENVMFGPQMRGASQMTAEAQAR-EWiniiGLEKYE---------NQYPHQLSGGMKQRVAIARALVNQPKILLMD 177
Cdd:PRK14267 99 HLTIYDNVAIGVKLNGLVKSKKELDERvEW----ALKKAAlwdevkdrlNDYPSNLSGGQRQRLVIARALAMKPKILLMD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446922839 178 EPFGALDPHTRQKMQKHLMDLWQniDITIIFVTHDMDEAILLADRIVALKanpgeIKEIIEVNLPR 243
Cdd:PRK14267 175 EPTANIDPVGTAKIEELLFELKK--EYTIVLVTHSPAQAARVSDYVAFLY-----LGKLIEVGPTR 233
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
21-279 |
6.28e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 114.03 E-value: 6.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 21 ILEAKQLsqVFKH-GQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPC-----P 94
Cdd:PRK13642 4 ILEVENL--VFKYeKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENvwnlrR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 95 ERGMVFQGY-TLFPWKTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKI 173
Cdd:PRK13642 82 KIGMVFQNPdNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 174 LLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAIlLADRIVALKAN-------PGEI----KEIIEVNLP 242
Cdd:PRK13642 162 IILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAA-SSDRILVMKAGeiikeaaPSELfatsEDMVEIGLD 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 446922839 243 RPRSLELMSTPEFKQLRSRVDYLvhaEEDELDPALQD 279
Cdd:PRK13642 241 VPFSSNLMKDLRKNGFDLPEKYL---SEDELVELLAD 274
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
22-235 |
7.22e-30 |
|
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: 112.62 E-value: 7.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 22 LEAKQLSQVFkhGQTErtVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPE----RG 97
Cdd:TIGR03410 1 LEVSNLNVYY--GQSH--ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHerarAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 98 M--VFQGYTLFPWKTVKENVMFGPQMRGASQMTAEAQAREWINIigLEKYENQYPHQLSGGMKQRVAIARALVNQPKILL 175
Cdd:TIGR03410 77 IayVPQGREIFPRLTVEENLLTGLAALPRRSRKIPDEIYELFPV--LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 176 MDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALKAnpGEIKE 235
Cdd:TIGR03410 155 LDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMER--GRVVA 212
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
21-256 |
9.67e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 113.79 E-value: 9.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 21 ILEAKQLSQVFKHGqTErtVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECI----TGPCPER 96
Cdd:PRK13636 5 ILKVEELNYNYSDG-TH--ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysrKGLMKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 ---GMVFQG--YTLFPwKTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQP 171
Cdd:PRK13636 82 esvGMVFQDpdNQLFS-ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 172 KILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRI-------VALKANPGEI---KEIIE-VN 240
Cdd:PRK13636 161 KVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVfvmkegrVILQGNPKEVfaeKEMLRkVN 240
|
250
....*....|....*.
gi 446922839 241 LPRPRSLELMSTPEFK 256
Cdd:PRK13636 241 LRLPRIGHLMEILKEK 256
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
21-226 |
1.08e-29 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 112.38 E-value: 1.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 21 ILEAKQLSQVfkHGQTErtVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER---- 96
Cdd:COG0410 3 MLEVENLHAG--YGGIH--VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRiarl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 --GMVFQGYTLFPWKTVKENVMFGPQMRGASQmtAEAQAREWIniiglekYE---------NQYPHQLSGGMKQRVAIAR 165
Cdd:COG0410 79 giGYVPEGRRIFPSLTVEENLLLGAYARRDRA--EVRADLERV-------YElfprlkerrRQRAGTLSGGEQQMLAIGR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446922839 166 ALVNQPKILLMDEPFGALDPhtrqKMQKHLMDLWQNI---DITIIFVTHDMDEAILLADRIVAL 226
Cdd:COG0410 150 ALMSRPKLLLLDEPSLGLAP----LIVEEIFEIIRRLnreGVTILLVEQNARFALEIADRAYVL 209
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
21-255 |
1.24e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 112.92 E-value: 1.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 21 ILEAKQLSqvFKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER---- 96
Cdd:PRK13648 7 IIVFKNVS--FQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKlrkh 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 -GMVFQG-YTLFPWKTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKIL 174
Cdd:PRK13648 85 iGIVFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 175 LMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEA------ILLADRIVALKANPGEI----KEIIEVNLPRP 244
Cdd:PRK13648 165 ILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAmeadhvIVMNKGTVYKEGTPTEIfdhaEELTRIGLDLP 244
|
250
....*....|.
gi 446922839 245 RSLELMSTPEF 255
Cdd:PRK13648 245 FPIKINQMLGH 255
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
37-235 |
1.42e-29 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 112.25 E-value: 1.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 37 ERTVLNKLDLKIHKREFICVIGPSGCGKSTlsrvIAGL-----DPYhSGEVLVDGECITGPCPER-----GMVFQGYTLF 106
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKST----VVSLlerfyDPT-SGEILLDGVDIRDLNLRWlrsqiGLVSQEPVLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 107 PwKTVKENVMFGpqMRGASQMTAEAQAREwIN----IIGL-EKYENQY-PH--QLSGGMKQRVAIARALVNQPKILLMDE 178
Cdd:cd03249 90 D-GTIAENIRYG--KPDATDEEVEEAAKK-ANihdfIMSLpDGYDTLVgERgsQLSGGQKQRIAIARALLRNPKILLLDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446922839 179 PFGALDPHTRQKMQKHLMDLwqNIDITIIFVTHDMdEAILLADRIVALKanPGEIKE 235
Cdd:cd03249 166 ATSALDAESEKLVQEALDRA--MKGRTTIVIAHRL-STIRNADLIAVLQ--NGQVVE 217
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
21-226 |
2.51e-29 |
|
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: 110.92 E-value: 2.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 21 ILEAKQLSQVFKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDG-ECITGPCPER--- 96
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVKEPAEARrrl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 GMVFQGYTLFPWKTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLM 176
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446922839 177 DEPFGALDPHTRQKMQ---KHLMDLWQnidiTIIFVTHDMDEAILLADRIVAL 226
Cdd:cd03266 161 DEPTTGLDVMATRALRefiRQLRALGK----CILFSTHIMQEVERLCDRVVVL 209
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
21-228 |
2.90e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 112.14 E-value: 2.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 21 ILEAKQLSQVFKHGqTErtVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITgPCPER---- 96
Cdd:PRK13647 4 IIEVEDLHFRYKDG-TK--ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN-AENEKwvrs 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 --GMVFQGY--TLFPwKTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPK 172
Cdd:PRK13647 80 kvGLVFQDPddQVFS-STVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446922839 173 ILLMDEPFGALDPHTRQKMQKhLMDLWQNIDITIIFVTHDMDEAILLADRIVALKA 228
Cdd:PRK13647 159 VIVLDEPMAYLDPRGQETLME-ILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKE 213
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
23-227 |
3.89e-29 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 111.33 E-value: 3.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 23 EAKQLSqvFKHGQTerTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGpcpergmvfqg 102
Cdd:COG4604 3 EIKNVS--KRYGGK--VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVAT----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 103 ytlfpWK---------------------TVKENVMFG--PQMRGasQMTAEAQA--REWINIIGLEKYENQYPHQLSGGM 157
Cdd:COG4604 68 -----TPsrelakrlailrqenhinsrlTVRELVAFGrfPYSKG--RLTAEDREiiDEAIAYLDLEDLADRYLDELSGGQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446922839 158 KQRVAIARALVNQPKILLMDEPFGALDP-HTRQKMqKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALK 227
Cdd:COG4604 141 RQRAFIAMVLAQDTDYVLLDEPLNNLDMkHSVQMM-KLLRRLADELGKTVVIVLHDINFASCYADHIVAMK 210
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
21-222 |
4.57e-29 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 115.67 E-value: 4.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 21 ILEAKQLSQvfKHGQTERTVLNKLD---LKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLV----DGECITGPC 93
Cdd:TIGR03269 279 IIKVRNVSK--RYISVDRGVVKAVDnvsLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 94 PER--------GMVFQGYTLFPWKTVKENVMFGPQMRGASQMtAEAQAREWINIIGLEKYE-----NQYPHQLSGGMKQR 160
Cdd:TIGR03269 357 PDGrgrakryiGILHQEYDLYPHRTVLDNLTEAIGLELPDEL-ARMKAVITLKMVGFDEEKaeeilDKYPDELSEGERHR 435
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446922839 161 VAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADR 222
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDR 497
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-233 |
4.67e-29 |
|
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: 109.06 E-value: 4.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 19 PVILEAKQLSQvfkhgqteRTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCP---- 94
Cdd:cd03215 2 EPVLEVRGLSV--------KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPrdai 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 95 ERGMVF-----QGYTLFPWKTVKENVMFgpqmrgasqmtaeaqarewiniiglekyenqyPHQLSGGMKQRVAIARALVN 169
Cdd:cd03215 74 RAGIAYvpedrKREGLVLDLSVAENIAL--------------------------------SSLLSGGNQQKVVLARWLAR 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446922839 170 QPKILLMDEPFGALDPHTRQKMQKHLMDLWQNiDITIIFVTHDMDEAILLADRIVALKAnpGEI 233
Cdd:cd03215 122 DPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYE--GRI 182
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
31-235 |
5.14e-29 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 110.65 E-value: 5.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 31 FKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER-----GMVFQGYTL 105
Cdd:cd03252 8 FRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWlrrqvGVVLQENVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 106 FPwKTVKENVMF---GPQMRGASQMTAEAQAREWINIIGlEKYENQYPHQ---LSGGMKQRVAIARALVNQPKILLMDEP 179
Cdd:cd03252 88 FN-RSIRDNIALadpGMSMERVIEAAKLAGAHDFISELP-EGYDTIVGEQgagLSGGQRQRIAIARALIHNPRILIFDEA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446922839 180 FGALDPHTRQKMQKHLMDLWQNidITIIFVTHDMdEAILLADRIVALKAnpGEIKE 235
Cdd:cd03252 166 TSALDYESEHAIMRNMHDICAG--RTVIIIAHRL-STVKNADRIIVMEK--GRIVE 216
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
22-223 |
8.26e-29 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 109.80 E-value: 8.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 22 LEAKQLSQVFKhgqtERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER-GMVF 100
Cdd:TIGR03740 1 LETKNLSKRFG----KQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKDLHKiGSLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 101 QGYTLFPWKTVKENVMFGPQMRGASqmtaEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPF 180
Cdd:TIGR03740 77 ESPPLYENLTARENLKVHTTLLGLP----DSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPT 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446922839 181 GALDPHTRQKMQKhLMDLWQNIDITIIFVTHDMDEAILLADRI 223
Cdd:TIGR03740 153 NGLDPIGIQELRE-LIRSFPEQGITVILSSHILSEVQQLADHI 194
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
14-238 |
8.54e-29 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 110.17 E-value: 8.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 14 KIYERPVILEAKQLSQVFKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGEcITGPC 93
Cdd:COG1134 15 RLYHEPSRSLKELLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR-VSALL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 94 pERGMVFQGyTLfpwkTVKENVMFGPQMRGASQMTAEAQAREwinII---GLEKYENQyP-HQLSGGMKQRVAIARALVN 169
Cdd:COG1134 94 -ELGAGFHP-EL----TGRENIYLNGRLLGLSRKEIDEKFDE---IVefaELGDFIDQ-PvKTYSSGMRARLAFAVATAV 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446922839 170 QPKILLMDEPFGALDPHTRQKMQKHLMDLWQNiDITIIFVTHDM-------DEAILLAD-RIVALkanpGEIKEIIE 238
Cdd:COG1134 164 DPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMgavrrlcDRAIWLEKgRLVMD----GDPEEVIA 235
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
31-236 |
8.61e-29 |
|
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: 110.01 E-value: 8.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 31 FKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECI---TGPCPER--GMVFQGYTL 105
Cdd:cd03251 8 FRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVrdyTLASLRRqiGLVSQDVFL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 106 FPwKTVKENVMFGpqMRGASQMTAE-----AQAREWIniiglEKYENQYPH-------QLSGGMKQRVAIARALVNQPKI 173
Cdd:cd03251 88 FN-DTVAENIAYG--RPGATREEVEeaaraANAHEFI-----MELPEGYDTvigergvKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446922839 174 LLMDEPFGALDPHTRQKMQKHLMDLWQNidITIIFVTHDMdEAILLADRIVALKAnpGEIKEI 236
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKN--RTTFVIAHRL-STIENADRIVVLED--GKIVER 217
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
32-235 |
1.42e-28 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 110.06 E-value: 1.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 32 KHGQTErtVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPERG-------------- 97
Cdd:PRK10619 14 RYGEHE--VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGqlkvadknqlrllr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 98 ----MVFQGYTLFPWKTVKENVMFGP-QMRGASQMTAEAQAREWINIIGL-EKYENQYPHQLSGGMKQRVAIARALVNQP 171
Cdd:PRK10619 92 trltMVFQHFNLWSHMTVLENVMEAPiQVLGLSKQEARERAVKYLAKVGIdERAQGKYPVHLSGGQQQRVSIARALAMEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446922839 172 KILLMDEPFGALDPHTRQKMQKHLMDLWQNiDITIIFVTHDMDEAILLADRIVALkaNPGEIKE 235
Cdd:PRK10619 172 EVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFL--HQGKIEE 232
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
22-222 |
1.73e-28 |
|
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: 109.17 E-value: 1.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 22 LEAKQLSQVFKhgqtERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITG-PCPER---G 97
Cdd:cd03218 1 LRAENLSKRYG----KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKlPMHKRarlG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 98 MVF--QGYTLFPWKTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILL 175
Cdd:cd03218 77 IGYlpQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446922839 176 MDEPFGALDP---HTRQKMQKHLMDlwQNIDITIifVTHDMDEAILLADR 222
Cdd:cd03218 157 LDEPFAGVDPiavQDIQKIIKILKD--RGIGVLI--TDHNVRETLSITDR 202
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
38-231 |
1.82e-28 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 114.13 E-value: 1.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 38 RTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVdgecitgPCPERgMVF---QGYtlFPWKTVKEN 114
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR-------PAGAR-VLFlpqRPY--LPLGTLREA 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 115 VMFgPQmrGASQMTaEAQAREWINIIGLEKY------ENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTR 188
Cdd:COG4178 446 LLY-PA--TAEAFS-DAELREALEAVGLGHLaerldeEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENE 521
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446922839 189 QKMQKHLMDlwQNIDITIIFVTHDmDEAILLADRIVALKANPG 231
Cdd:COG4178 522 AALYQLLRE--ELPGTTVISVGHR-STLAAFHDRVLELTGDGS 561
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
19-213 |
2.07e-28 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 111.21 E-value: 2.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 19 PVILEAKQLSQVF--KHG--QTERTV--LNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGP 92
Cdd:PRK11308 3 QPLLQAIDLKKHYpvKRGlfKPERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 93 CPER--------GMVFQG-Y-TLFPWKTVkENVMFGPQMRGASQMTAE--AQAREWINIIGL--EKYeNQYPHQLSGGMK 158
Cdd:PRK11308 83 DPEAqkllrqkiQIVFQNpYgSLNPRKKV-GQILEEPLLINTSLSAAErrEKALAMMAKVGLrpEHY-DRYPHMFSGGQR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446922839 159 QRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDM 213
Cdd:PRK11308 161 QRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDL 215
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
40-228 |
2.23e-28 |
|
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: 107.94 E-value: 2.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 40 VLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECitGPCPErgmvfqgytlFPW---KTVKENVM 116
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSI--AYVSQ----------EPWiqnGTIRENIL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 117 FGPQMRgasqmtaEAQAREWINIIGLEKYENQYPHQ-----------LSGGMKQRVAIARALVNQPKILLMDEPFGALDP 185
Cdd:cd03250 88 FGKPFD-------EERYEKVIKACALEPDLEILPDGdlteigekginLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446922839 186 HTRQK-MQKHLMDLWQNiDITIIFVTHDMdEAILLADRIVALKA 228
Cdd:cd03250 161 HVGRHiFENCILGLLLN-NKTRILVTHQL-QLLPHADQIVVLDN 202
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
35-235 |
3.56e-28 |
|
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: 108.47 E-value: 3.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 35 QTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGL-DPyHSGEVLVDGECITGPCPER-----GMVFQGYTLFPw 108
Cdd:cd03253 11 DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFyDV-SSGSILIDGQDIREVTLDSlrraiGVVPQDTVLFN- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 109 KTVKENVMFGPQMRGASQMTAEAQAREWINIIglEKYENQYPHQ-------LSGGMKQRVAIARALVNQPKILLMDEPFG 181
Cdd:cd03253 89 DTIGYNIRYGRPDATDEEVIEAAKAAQIHDKI--MRFPDGYDTIvgerglkLSGGEKQRVAIARAILKNPPILLLDEATS 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446922839 182 ALDPHTRQKMQKHLMDLWQNidITIIFVTHDMDEaILLADRIVALKAnpGEIKE 235
Cdd:cd03253 167 ALDTHTEREIQAALRDVSKG--RTTIVIAHRLST-IVNADKIIVLKD--GRIVE 215
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
21-262 |
3.88e-28 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 109.01 E-value: 3.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 21 ILEAKQLSQVFKHG-----QTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPE 95
Cdd:PRK10419 3 LLNVSGLSHHYAHGglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 96 RG--------MVFQGY--TLFPWKTVKENVmfGPQMR---GASQMTAEAQAREWINIIGL-EKYENQYPHQLSGGMKQRV 161
Cdd:PRK10419 83 QRkafrrdiqMVFQDSisAVNPRKTVREII--REPLRhllSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 162 AIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALKAnpGEIKEIIEVNL 241
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDN--GQIVETQPVGD 238
|
250 260
....*....|....*....|.
gi 446922839 242 PrprslELMSTPEFKQLRSRV 262
Cdd:PRK10419 239 K-----LTFSSPAGRVLQNAV 254
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
37-225 |
8.28e-28 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 108.31 E-value: 8.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 37 ERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECItgPCPERG----------MVFQGYTLF 106
Cdd:PRK11831 19 NRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENI--PAMSRSrlytvrkrmsMLFQSGALF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 107 PWKTVKENVMF---------GPQMRGASQMTAEAqarewiniIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMD 177
Cdd:PRK11831 97 TDMNVFDNVAYplrehtqlpAPLLHSTVMMKLEA--------VGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446922839 178 EPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADR--IVA 225
Cdd:PRK11831 169 EPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHayIVA 218
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
21-185 |
1.21e-27 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 107.04 E-value: 1.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 21 ILEAKQLSQVFKHgqteRTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITG-PCPER--- 96
Cdd:COG1137 3 TLEAENLVKSYGK----RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlPMHKRarl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 GMvfqGY-----TLFpWK-TVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQ 170
Cdd:COG1137 79 GI---GYlpqeaSIF-RKlTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATN 154
|
170
....*....|....*
gi 446922839 171 PKILLMDEPFGALDP 185
Cdd:COG1137 155 PKFILLDEPFAGVDP 169
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
45-224 |
2.24e-27 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 110.50 E-value: 2.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 45 DLKIHKREFICVIGPSGCGKSTLSRVIAGLdpYH--SGEVLVDGE--CITGPcpeR-------GMVFQGYTLFPWKTVKE 113
Cdd:COG3845 25 SLTVRPGEIHALLGENGAGKSTLMKILYGL--YQpdSGEILIDGKpvRIRSP---RdaialgiGMVHQHFMLVPNLTVAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 114 NVMFG--PQMRGASQM-TAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQK 190
Cdd:COG3845 100 NIVLGlePTKGGRLDRkAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADE 179
|
170 180 190
....*....|....*....|....*....|....
gi 446922839 191 MQKHLMDLWQNiDITIIFVTHDMDEAILLADRIV 224
Cdd:COG3845 180 LFEILRRLAAE-GKSIIFITHKLREVMAIADRVT 212
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
25-223 |
3.25e-27 |
|
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: 111.26 E-value: 3.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 25 KQLSQVFKhgQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECIT----------GPCP 94
Cdd:TIGR01257 932 KNLVKIFE--PSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIEtnldavrqslGMCP 1009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 95 ERGMVFQGYTlfpwktVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKIL 174
Cdd:TIGR01257 1010 QHNILFHHLT------VAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVV 1083
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446922839 175 LMDEPFGALDPHTRQKMQKHLMDLWQNidITIIFVTHDMDEAILLADRI 223
Cdd:TIGR01257 1084 VLDEPTSGVDPYSRRSIWDLLLKYRSG--RTIIMSTHHMDEADLLGDRI 1130
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
46-221 |
3.97e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 106.40 E-value: 3.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 46 LKIHKREFICVIGPSGCGKSTLSRV------------IAGLDPYHsGEVLVDGEciTGPCPER---GMVFQGYTLFPwKT 110
Cdd:PRK14243 31 LDIPKNQITAFIGPSGCGKSTILRCfnrlndlipgfrVEGKVTFH-GKNLYAPD--VDPVEVRrriGMVFQKPNPFP-KS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 111 VKENVMFGPQMRGASQMTAEA------QAREWINIiglEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALD 184
Cdd:PRK14243 107 IYDNIAYGARINGYKGDMDELverslrQAALWDEV---KDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALD 183
|
170 180 190
....*....|....*....|....*....|....*..
gi 446922839 185 PHTRQKMQKHLMDLWQniDITIIFVTHDMDEAILLAD 221
Cdd:PRK14243 184 PISTLRIEELMHELKE--QYTIIIVTHNMQQAARVSD 218
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-226 |
6.95e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 105.38 E-value: 6.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 22 LEAKQLSQVFkhGQTErtVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGL-----DPYHSGEVLVDGECI-TGPCPE 95
Cdd:PRK14247 4 IEIRDLKVSF--GQVE--VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIfKMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 96 R----GMVFQGYTLFPWKTVKENVMFGPQMRGASQMTAEAQAR-EWiniiGLEKYE---------NQYPHQLSGGMKQRV 161
Cdd:PRK14247 80 LrrrvQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKKELQERvRW----ALEKAQlwdevkdrlDAPAGKLSGGQQQRL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446922839 162 AIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQniDITIIFVTHDMDEAILLADRIVAL 226
Cdd:PRK14247 156 CIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKK--DMTIVLVTHFPQQAARISDYVAFL 218
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
22-212 |
7.82e-27 |
|
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: 109.37 E-value: 7.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 22 LEAKQLSqvFKHGQTERtVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECIT----------- 90
Cdd:TIGR02868 335 LELRDLS--AGYPGAPP-VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSsldqdevrrrv 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 91 GPCPERGMVFQgytlfpwKTVKENVMFG-PQMRGASQMTAEAQAR--EWINII--GLEKYENQYPHQLSGGMKQRVAIAR 165
Cdd:TIGR02868 412 SVCAQDAHLFD-------TTVRENLRLArPDATDEELWAALERVGlaDWLRALpdGLDTVLGEGGARLSGGERQRLALAR 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446922839 166 ALVNQPKILLMDEPFGALDPHTRQKMqkhLMDLWQNID-ITIIFVTHD 212
Cdd:TIGR02868 485 ALLADAPILLLDEPTEHLDAETADEL---LEDLLAALSgRTVVLITHH 529
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
17-251 |
7.91e-27 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 107.10 E-value: 7.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 17 ERPVILEAKQLSQVFK----------HGQTERTVlNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDG 86
Cdd:PRK15079 4 GKKVLLEVADLKVHFDikdgkqwfwqPPKTLKAV-DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 87 ECITGPCPER--------GMVFQG--YTLFPWKTVKENV-----MFGPQMrgaSQMTAEAQAREWINIIGL-EKYENQYP 150
Cdd:PRK15079 83 KDLLGMKDDEwravrsdiQMIFQDplASLNPRMTIGEIIaeplrTYHPKL---SRQEVKDRVKAMMLKVGLlPNLINRYP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 151 HQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRI-VALKAN 229
Cdd:PRK15079 160 HEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVlVMYLGH 239
|
250 260
....*....|....*....|....
gi 446922839 230 PGEIKEIIEV--NLPRPRSLELMS 251
Cdd:PRK15079 240 AVELGTYDEVyhNPLHPYTKALMS 263
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
37-226 |
1.55e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 108.61 E-value: 1.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 37 ERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECitgpcpERGMVFQGYTLFPWKTVKENVM 116
Cdd:COG0488 10 GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL------RIGYLPQEPPLDDDLTVLDTVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 117 --FGPQMRGASQM------------------------------TAEAQAREWINIIGL-EKYENQYPHQLSGGMKQRVAI 163
Cdd:COG0488 84 dgDAELRALEAELeeleaklaepdedlerlaelqeefealggwEAEARAEEILSGLGFpEEDLDRPVSELSGGWRRRVAL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446922839 164 ARALVNQPKILLMDEPFGALDPHTRQKMQKHLmdlwQNIDITIIFVTHD---MDEailLADRIVAL 226
Cdd:COG0488 164 ARALLSEPDLLLLDEPTNHLDLESIEWLEEFL----KNYPGTVLVVSHDryfLDR---VATRILEL 222
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
37-238 |
1.73e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 105.66 E-value: 1.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 37 ERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGEcitgPCPER--------GMVFQGYTLFPW 108
Cdd:PRK13537 19 DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGE----PVPSRarharqrvGVVPQFDNLDPD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 109 KTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTR 188
Cdd:PRK13537 95 FTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQAR 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446922839 189 QKMQKHLMDLWQNiDITIIFVTHDMDEAILLADRIVAL----KANPGEIKEIIE 238
Cdd:PRK13537 175 HLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIeegrKIAEGAPHALIE 227
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
25-213 |
5.07e-26 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 102.26 E-value: 5.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 25 KQLSQVFKHGqteRTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITG------PCPER-- 96
Cdd:PRK10908 5 EHVSKAYLGG---RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRlknrevPFLRRqi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 GMVFQGYTLFPWKTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLM 176
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 446922839 177 DEPFGALDPHTRQKMQKhLMDLWQNIDITIIFVTHDM 213
Cdd:PRK10908 162 DEPTGNLDDALSEGILR-LFEEFNRVGVTVLMATHDI 197
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
41-227 |
9.16e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 103.27 E-value: 9.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 41 LNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER---------GMVFQgytlFPW--- 108
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikpvrkkvGVVFQ----FPEsql 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 109 --KTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEK-YENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDP 185
Cdd:PRK13643 98 feETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446922839 186 HTRQKMQKhLMDLWQNIDITIIFVTHDMDEAILLADRIVALK 227
Cdd:PRK13643 178 KARIEMMQ-LFESIHQSGQTVVLVTHLMDDVADYADYVYLLE 218
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
21-290 |
9.56e-26 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 106.33 E-value: 9.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 21 ILEAKQLSQVFKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDP-----YHSGEVLVDGECITGPCPE 95
Cdd:PRK15134 5 LLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPsppvvYPSGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 96 -----RG----MVFQG--YTLFPWKTVKEnvmfgpQM-------RGASQMTAEAQAREWINIIGLE---KYENQYPHQLS 154
Cdd:PRK15134 85 tlrgvRGnkiaMIFQEpmVSLNPLHTLEK------QLyevlslhRGMRREAARGEILNCLDRVGIRqaaKRLTDYPHQLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 155 GGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALKANpgeik 234
Cdd:PRK15134 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNG----- 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 446922839 235 EIIEVNlprpRSLELMSTPEFKQLRSrvdyLVHAE-EDELDPALQDLPKIPRMTQVS 290
Cdd:PRK15134 234 RCVEQN----RAATLFSAPTHPYTQK----LLNSEpSGDPVPLPEPASPLLDVEQLQ 282
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
42-224 |
4.12e-25 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 100.83 E-value: 4.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 42 NKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITG----PCPERGMV--FQGYTLFPWKTVKENV 115
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGlpghQIARMGVVrtFQHVRLFREMTVIENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 116 MFG----------------PQMRGAsQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEP 179
Cdd:PRK11300 102 LVAqhqqlktglfsgllktPAFRRA-ESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEP 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446922839 180 FGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIV 224
Cdd:PRK11300 181 AAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIY 225
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
19-228 |
6.89e-25 |
|
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: 99.43 E-value: 6.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 19 PVILEAKQLSQVFK-HGQ--TERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVI-------AGLDPYHSGEVLVDgec 88
Cdd:COG4778 2 TTLLEVENLSKTFTlHLQggKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIygnylpdSGSILVRHDGGWVD--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 89 ITGpCPER----------GMVFQGYTLFPWKTVKENVMFGPQMRGASQMTAEAQAREWINIIGL-EKYENQYPHQLSGGM 157
Cdd:COG4778 79 LAQ-ASPReilalrrrtiGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLpERLWDLPPATFSGGE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446922839 158 KQRVAIARALVNQPKILLMDEPFGALDPHTRQKmqkhLMDLWQNI---DITIIFVTHDMD--EAilLADRIVALKA 228
Cdd:COG4778 158 QQRVNIARGFIADPPLLLLDEPTASLDAANRAV----VVELIEEAkarGTAIIGIFHDEEvrEA--VADRVVDVTP 227
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
44-235 |
7.09e-25 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 99.37 E-value: 7.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 44 LDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYH----SGEVLVDGECITgPCPERG----MVFQG-YTLF-PWKTVKE 113
Cdd:TIGR02770 5 LNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGltqtSGEILLDGRPLL-PLSIRGrhiaTIMQNpRTAFnPLFTMGN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 114 NVMFGPQMRGASQMTAEAQAREWINIIGLEKYE---NQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQK 190
Cdd:TIGR02770 84 HAIETLRSLGKLSKQARALILEALEAVGLPDPEevlKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQAR 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446922839 191 MQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALKAnpGEIKE 235
Cdd:TIGR02770 164 VLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDD--GRIVE 206
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
38-241 |
1.33e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 99.73 E-value: 1.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 38 RTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHsGEVLVDG--ECITGPCPER-----------GMVFQGYT 104
Cdd:PRK14258 20 QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGrvEFFNQNIYERrvnlnrlrrqvSMVHPKPN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 105 LFPwKTVKENVMFGPQMRGASQM--------TAEAQAREWINIiglEKYENQYPHQLSGGMKQRVAIARALVNQPKILLM 176
Cdd:PRK14258 99 LFP-MSVYDNVAYGVKIVGWRPKleiddiveSALKDADLWDEI---KHKIHKSALDLSGGQQQRLCIARALAVKPKVLLM 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446922839 177 DEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALKANPGEIKEIIEVNL 241
Cdd:PRK14258 175 DEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENRIGQLVEFGL 239
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
22-185 |
2.36e-24 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 97.04 E-value: 2.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 22 LEAKQLSQVfkhgQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECI--TGPCPERGMV 99
Cdd:TIGR01189 1 LAARNLACS----RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLaeQRDEPHENIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 100 FQGYT--LFPWKTVKENVMF-GPQMRGASQMTAEAQARewiniIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLM 176
Cdd:TIGR01189 77 YLGHLpgLKPELSALENLHFwAAIHGGAQRTIEDALAA-----VGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWIL 151
|
....*....
gi 446922839 177 DEPFGALDP 185
Cdd:TIGR01189 152 DEPTTALDK 160
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
41-226 |
2.95e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 98.91 E-value: 2.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 41 LNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDG--ECITGPCPE----RGMVFQG-YTLFPWKTVKE 113
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidTGDFSKLQGirklVGIVFQNpETQFVGRTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 114 NVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQK 193
Cdd:PRK13644 98 DLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLE 177
|
170 180 190
....*....|....*....|....*....|...
gi 446922839 194 HLMDLWQNiDITIIFVTHDMDEaILLADRIVAL 226
Cdd:PRK13644 178 RIKKLHEK-GKTIVYITHNLEE-LHDADRIIVM 208
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
31-187 |
5.25e-24 |
|
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: 96.96 E-value: 5.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 31 FKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYH---SGEVLVDGE---------CItgpcperGM 98
Cdd:cd03234 13 AKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQprkpdqfqkCV-------AY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 99 VFQGYTLFPWKTVKENVMFGPQMRGASQMTAEAQAREW----INIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKIL 174
Cdd:cd03234 86 VRQDDILLPGLTVRETLTYTAILRLPRKSSDAIRKKRVedvlLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVL 165
|
170
....*....|...
gi 446922839 175 LMDEPFGALDPHT 187
Cdd:cd03234 166 ILDEPTSGLDSFT 178
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
37-235 |
5.32e-24 |
|
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: 96.91 E-value: 5.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 37 ERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER-----GMVFQGYTLFPwKTV 111
Cdd:cd03254 15 KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrsmiGVVLQDTFLFS-GTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 112 KENVMFG---PQMRGASQMTAEAQAREWINII--GLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPH 186
Cdd:cd03254 94 MENIRLGrpnATDEEVIEAAKEAGAHDFIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446922839 187 TRQKMQKHLMDLWQNidITIIFVTHDMDeAILLADRIVALkaNPGEIKE 235
Cdd:cd03254 174 TEKLIQEALEKLMKG--RTSIIIAHRLS-TIKNADKILVL--DDGKIIE 217
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
37-226 |
1.17e-23 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 96.00 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 37 ERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER-----GMVFQGYTLFPwKTV 111
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYlhskvSLVGQEPVLFA-RSL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 112 KENVMFGPQMRGASQMTAEAQ---AREWINIIGLEKYEN--QYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPH 186
Cdd:cd03248 105 QDNIAYGLQSCSFECVKEAAQkahAHSFISELASGYDTEvgEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446922839 187 TRQKMQKHLMDlwQNIDITIIFVTHDMdEAILLADRIVAL 226
Cdd:cd03248 185 SEQQVQQALYD--WPERRTVLVIAHRL-STVERADQILVL 221
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
4-236 |
1.48e-23 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 100.05 E-value: 1.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 4 STFNAHEYFQKIYERPVileakqlsqVFkHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVL 83
Cdd:PRK10522 312 PRPQAFPDWQTLELRNV---------TF-AYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEIL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 84 VDGECITGPCPER-----GMVFQGYTLFpwktvkeNVMFGPQmrgaSQMTAEAQAREWINIIGL-EKYENQYPH----QL 153
Cdd:PRK10522 382 LDGKPVTAEQPEDyrklfSAVFTDFHLF-------DQLLGPE----GKPANPALVEKWLERLKMaHKLELEDGRisnlKL 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 154 SGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDmDEAILLADRIvaLKANPGEI 233
Cdd:PRK10522 451 SKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRL--LEMRNGQL 527
|
...
gi 446922839 234 KEI 236
Cdd:PRK10522 528 SEL 530
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-238 |
1.67e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 99.71 E-value: 1.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 19 PVILEAKQLSQvfkhgqteRTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCP---- 94
Cdd:COG1129 254 EVVLEVEGLSV--------GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPrdai 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 95 ERGMVF-------QGytLFPWKTVKENVMFGPQMRGA-----SQMTAEAQAREWI---NIigleKYENqyPHQ----LSG 155
Cdd:COG1129 326 RAGIAYvpedrkgEG--LVLDLSIRENITLASLDRLSrggllDRRRERALAEEYIkrlRI----KTPS--PEQpvgnLSG 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 156 GMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNiDITIIFVTHDMDEAILLADRIVALKAnpGEIKE 235
Cdd:COG1129 398 GNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMRE--GRIVG 474
|
...
gi 446922839 236 IIE 238
Cdd:COG1129 475 ELD 477
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
19-227 |
2.32e-23 |
|
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: 96.05 E-value: 2.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 19 PVILEAKQLSQVFKHGQTERTVlnklDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDG------ECITGP 92
Cdd:TIGR02323 1 KPLLQVSGLSKSYGGGKGCRDV----SFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMrsgaelELYQLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 93 CPERGMVFQGytlfPWKTVKENVMFGPQMR-------GASQMTA--------EAQAREWiniigLEKYE------NQYPH 151
Cdd:TIGR02323 77 EAERRRLMRT----EWGFVHQNPRDGLRMRvsaganiGERLMAIgarhygniRATAQDW-----LEEVEidptriDDLPR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446922839 152 QLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALK 227
Cdd:TIGR02323 148 AFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQ 223
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
38-211 |
3.45e-23 |
|
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: 92.99 E-value: 3.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 38 RTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLvdgecitgpCPERgmvfqgytlfpwktvkENVMF 117
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG---------MPEG----------------EDLLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 118 GPQmrgASQMTAeAQAREWINiiglekyenqYP--HQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPhtrqKMQKHL 195
Cdd:cd03223 69 LPQ---RPYLPL-GTLREQLI----------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDE----ESEDRL 130
|
170
....*....|....*.
gi 446922839 196 MDLWQNIDITIIFVTH 211
Cdd:cd03223 131 YQLLKELGITVISVGH 146
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
21-235 |
4.16e-23 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 95.38 E-value: 4.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 21 ILEAKQLSQVFKHGQTERTVlnklDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDG------ECITGPCP 94
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDV----SFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlrDLYALSEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 95 ERGMVFQGytlfPWKTVKENVMFGPQMR-------GASQMTA--------EAQAREWiniigLEKYE------NQYPHQL 153
Cdd:PRK11701 82 ERRRLLRT----EWGFVHQHPRDGLRMQvsaggniGERLMAVgarhygdiRATAGDW-----LERVEidaariDDLPTTF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 154 SGGMKQRVAIARALVNQPKILLMDEPFGALDphtrQKMQKHLMDLWQNI----DITIIFVTHDMDEAILLADRIVALKAn 229
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLD----VSVQARLLDLLRGLvrelGLAVVIVTHDLAVARLLAHRLLVMKQ- 227
|
....*.
gi 446922839 230 pGEIKE 235
Cdd:PRK11701 228 -GRVVE 232
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
36-227 |
4.72e-23 |
|
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: 98.67 E-value: 4.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 36 TERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPERGMVFQGY-----TLFPwKT 110
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYlpqdvELFD-GT 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 111 VKENV-MFGP----------QMRGASQMtaeaqarewinIIGLEK-YENQY---PHQLSGGMKQRVAIARALVNQPKILL 175
Cdd:COG4618 422 IAENIaRFGDadpekvvaaaKLAGVHEM-----------ILRLPDgYDTRIgegGARLSGGQRQRIGLARALYGDPRLVV 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446922839 176 MDEPFGALDPHTRQKMQKHLMDLWQNiDITIIFVTHDMdeAIL-LADRIVALK 227
Cdd:COG4618 491 LDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRP--SLLaAVDKLLVLR 540
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
22-221 |
5.52e-23 |
|
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: 93.15 E-value: 5.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 22 LEAKQLSqvFKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAG-LDPyHSGEVLVDGECITgpcpergmvf 100
Cdd:cd03247 1 LSINNVS--FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGdLKP-QQGEITLDGVPVS---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 101 qgytlfpwktvkenvmfgpqmrgasqmTAEAQAREWINIIglekyeNQYPH------------QLSGGMKQRVAIARALV 168
Cdd:cd03247 68 ---------------------------DLEKALSSLISVL------NQRPYlfdttlrnnlgrRFSGGERQRLALARILL 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446922839 169 NQPKILLMDEPFGALDPHTRQKMQKHLMDLWQniDITIIFVTH------DMDEAILLAD 221
Cdd:cd03247 115 QDAPIVLLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHhltgieHMDKILFLEN 171
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
22-227 |
1.79e-22 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 90.59 E-value: 1.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 22 LEAKQLSqvFKHGqtERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVlvdgecitgpcpergmvfq 101
Cdd:cd03221 1 IELENLS--KTYG--GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 102 gytlfpwkTVKENVMFGpqmrgasqmtaeaqarewiniiglekyenqYPHQLSGGMKQRVAIARALVNQPKILLMDEPFG 181
Cdd:cd03221 58 --------TWGSTVKIG------------------------------YFEQLSGGEKMRLALAKLLLENPNLLLLDEPTN 99
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446922839 182 ALDPHTRQKMQKHLmdlwQNIDITIIFVTHD---MDEailLADRIVALK 227
Cdd:cd03221 100 HLDLESIEALEEAL----KEYPGTVILVSHDryfLDQ---VATKIIELE 141
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
35-224 |
3.47e-22 |
|
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: 96.04 E-value: 3.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 35 QTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGL-DPyHSGEVLVDGECITGPCPE--R---GMVFQGYTLFPw 108
Cdd:COG5265 368 DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFyDV-TSGRILIDGQDIRDVTQAslRaaiGIVPQDTVLFN- 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 109 KTVKENVMFGpqmR-GASQMTAEAQAR-----EWINiiGL-EKYENQYPH---QLSGGMKQRVAIARALVNQPKILLMDE 178
Cdd:COG5265 446 DTIAYNIAYG---RpDASEEEVEAAARaaqihDFIE--SLpDGYDTRVGErglKLSGGEKQRVAIARTLLKNPPILIFDE 520
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446922839 179 PFGALDPHTRQKMQKHLMDLWQNidITIIFVTH------DMDEAILLAD-RIV 224
Cdd:COG5265 521 ATSALDSRTERAIQAALREVARG--RTTLVIAHrlstivDADEILVLEAgRIV 571
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
21-265 |
3.80e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 94.04 E-value: 3.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 21 ILEAKQLSQVFKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYhSGEVLVDGECITG------PCP 94
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDY-PGRVMAEKLEFNGqdlqriSEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 95 ER--------GMVFQG--YTLFPWKTVKENVMFGPQM-RGASQMTAEAQAREWINIIGLEKYENQ---YPHQLSGGMKQR 160
Cdd:PRK11022 82 ERrnlvgaevAMIFQDpmTSLNPCYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 161 VAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALKA----NPGEIKEI 236
Cdd:PRK11022 162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAgqvvETGKAHDI 241
|
250 260 270
....*....|....*....|....*....|
gi 446922839 237 IEVNL-PRPRSLeLMSTPEFKQLRSRVDYL 265
Cdd:PRK11022 242 FRAPRhPYTQAL-LRALPEFAQDKARLASL 270
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
37-227 |
5.65e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 95.56 E-value: 5.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 37 ERTVLNKLDLKIHKREFICVIGPSGCGKSTlsrVIAGLDPYH---SGEVLVDGEcitgPCPER---------GMVFQGYT 104
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKST---VAALLQNLYqptGGQVLLDGV----PLVQYdhhylhrqvALVGQEPV 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 105 LFPwKTVKENVMFGPQMRGASQMTAEAQAREWINIIGleKYENQY-----PH--QLSGGMKQRVAIARALVNQPKILLMD 177
Cdd:TIGR00958 566 LFS-GSVRENIAYGLTDTPDEEIMAAAKAANAHDFIM--EFPNGYdtevgEKgsQLSGGQKQRIAIARALVRKPRVLILD 642
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446922839 178 EPFGALDPHTRQKMQKhlmdlWQNI-DITIIFVTHDMdEAILLADRIVALK 227
Cdd:TIGR00958 643 EATSALDAECEQLLQE-----SRSRaSRTVLLIAHRL-STVERADQILVLK 687
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
18-213 |
8.95e-22 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 93.25 E-value: 8.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 18 RPVILEAKQLSQVFKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGL---DPYHSGEVLVDGECITGpCP 94
Cdd:PRK09473 9 ADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLlaaNGRIGGSATFNGREILN-LP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 95 ER----------GMVFQG--YTLFPWKTVKENVMFGPQM-RGASQMTA-EAQAR--EWINIIGLEKYENQYPHQLSGGMK 158
Cdd:PRK09473 88 EKelnklraeqiSMIFQDpmTSLNPYMRVGEQLMEVLMLhKGMSKAEAfEESVRmlDAVKMPEARKRMKMYPHEFSGGMR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446922839 159 QRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDM 213
Cdd:PRK09473 168 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDL 222
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
25-243 |
9.71e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 92.15 E-value: 9.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 25 KQLSQVFKHGQT-ERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER------- 96
Cdd:PRK13646 6 DNVSYTYQKGTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKyirpvrk 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 --GMVFQgytlFPWK-----TVKENVMFGPQMRGASQMTAEAQAREWINIIGLEK-YENQYPHQLSGGMKQRVAIARALV 168
Cdd:PRK13646 86 riGMVFQ----FPESqlfedTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRdVMSQSPFQMSGGQMRKIAIVSILA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446922839 169 NQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALKANpgeikEIIEVNLPR 243
Cdd:PRK13646 162 MNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEG-----SIVSQTSPK 231
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
22-195 |
9.74e-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: 90.24 E-value: 9.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 22 LEAKQLSQvfkhGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPE--RGMV 99
Cdd:cd03231 1 LEADELTC----ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiaRGLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 100 FQGY------TLfpwkTVKENVMFGPQMRGASQMTaEAQARewiniIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKI 173
Cdd:cd03231 77 YLGHapgiktTL----SVLENLRFWHADHSDEQVE-EALAR-----VGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPL 146
|
170 180
....*....|....*....|..
gi 446922839 174 LLMDEPFGALDPHTRQKMQKHL 195
Cdd:cd03231 147 WILDEPTTALDKAGVARFAEAM 168
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
20-235 |
2.31e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.59 E-value: 2.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 20 VILEAKQLSQVFkhgqTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVlvdgecitgpcpERG-M 98
Cdd:COG0488 314 KVLELEGLSKSY----GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV------------KLGeT 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 99 VFQGY------TLFPWKTVKENVMfgpqmRGASQMTaEAQAREWiniigLEKY------ENQYPHQLSGGMKQRVAIARA 166
Cdd:COG0488 378 VKIGYfdqhqeELDPDKTVLDELR-----DGAPGGT-EQEVRGY-----LGRFlfsgddAFKPVGVLSGGEKARLALAKL 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446922839 167 LVNQPKILLMDEPFGALDPHTRQKmqkhLMDLWQNIDITIIFVTHD---MDEailLADRIVALKanPGEIKE 235
Cdd:COG0488 447 LLSPPNVLLLDEPTNHLDIETLEA----LEEALDDFPGTVLLVSHDryfLDR---VATRILEFE--DGGVRE 509
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
21-235 |
2.47e-21 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 90.62 E-value: 2.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 21 ILEAKQLSQVFK------HGQTERTVLNkLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECIT-GPC 93
Cdd:PRK15112 4 LLEVRNLSKTFRyrtgwfRRQTVEAVKP-LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfGDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 94 PERG----MVFQ--GYTLFPWKTVKENVMFgpQMRGASQMTAEAQAREWINI---IGL-EKYENQYPHQLSGGMKQRVAI 163
Cdd:PRK15112 83 SYRSqrirMIFQdpSTSLNPRQRISQILDF--PLRLNTDLEPEQREKQIIETlrqVGLlPDHASYYPHMLAPGQKQRLGL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446922839 164 ARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALKAnpGEIKE 235
Cdd:PRK15112 161 ARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQ--GEVVE 230
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
37-226 |
4.04e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 90.11 E-value: 4.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 37 ERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECI-----------TGPCPERGMVFQGYTL 105
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgkdifqidaIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 106 FPWKTVKENVMFGPQMRG-ASQMTAEAQAREWINIIGL--EKYE--NQYPHQLSGGMKQRVAIARALVNQPKILLMDEPF 180
Cdd:PRK14246 102 FPHLSIYDNIAYPLKSHGiKEKREIKKIVEECLRKVGLwkEVYDrlNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446922839 181 GALDPHTRQKMQKHLMDLWQniDITIIFVTHDMDEAILLADRIVAL 226
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKN--EIAIVIVSHNPQQVARVADYVAFL 225
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
21-222 |
4.46e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 89.57 E-value: 4.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 21 ILEAKQLSQVFKhgqtERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITG-PCPERGMV 99
Cdd:PRK10895 3 TLTAKNLAKAYK----GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLlPLHARARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 100 FQGY-----TLFPWKTVKENVMFGPQMRgaSQMTAEAQ---AREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQP 171
Cdd:PRK10895 79 GIGYlpqeaSIFRRLSVYDNLMAVLQIR--DDLSAEQRedrANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446922839 172 KILLMDEPFGALDPHTR---QKMQKHLMDLWQNIDITiifvTHDMDEAILLADR 222
Cdd:PRK10895 157 KFILLDEPFAGVDPISVidiKRIIEHLRDSGLGVLIT----DHNVRETLAVCER 206
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
17-235 |
5.67e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 92.60 E-value: 5.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 17 ERPVILEAKQLSqVFKH-GQTertVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHsGEVLVDGECITGPCPE 95
Cdd:PRK11174 345 NDPVTIEAEDLE-ILSPdGKT---LAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRELDPE 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 96 R-----GMVFQGYTLFPwKTVKENVMFG-PQMRGASQMTAEAQAreWINIIgLEKYENQYPHQ-------LSGGMKQRVA 162
Cdd:PRK11174 420 SwrkhlSWVGQNPQLPH-GTLRDNVLLGnPDASDEQLQQALENA--WVSEF-LPLLPQGLDTPigdqaagLSVGQAQRLA 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 163 IARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQniDITIIFVTH------DMDEAILLAD-RIV------ALKAN 229
Cdd:PRK11174 496 LARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHqledlaQWDQIWVMQDgQIVqqgdyaELSQA 573
|
....*.
gi 446922839 230 PGEIKE 235
Cdd:PRK11174 574 GGLFAT 579
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
22-211 |
2.83e-20 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 86.40 E-value: 2.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 22 LEAKQLSQVfkhgQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPE--RGMV 99
Cdd:PRK13538 2 LEARNLACE----RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEyhQDLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 100 FQGYT------LFPWktvkENVMFGPQMrgaSQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKI 173
Cdd:PRK13538 78 YLGHQpgikteLTAL----ENLRFYQRL---HGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPL 150
|
170 180 190
....*....|....*....|....*....|....*...
gi 446922839 174 LLMDEPFGALDPHTRQKMQKHLMDLWQNIDItIIFVTH 211
Cdd:PRK13538 151 WILDEPFTAIDKQGVARLEALLAQHAEQGGM-VILTTH 187
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
30-235 |
2.96e-20 |
|
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: 86.78 E-value: 2.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 30 VFKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER-----GMVFQGYT 104
Cdd:cd03244 9 SLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDlrsriSIIPQDPV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 105 LFPwKTVKENVmfGP-------QMRGAsqmTAEAQAREWIN--IIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILL 175
Cdd:cd03244 89 LFS-GTIRSNL--DPfgeysdeELWQA---LERVGLKEFVEslPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 176 MDEPFGALDPHTRQKMQKHLMDLWQniDITIIFVTHDMDeAILLADRIVALKAnpGEIKE 235
Cdd:cd03244 163 LDEATASVDPETDALIQKTIREAFK--DCTVLTIAHRLD-TIIDSDRILVLDK--GRVVE 217
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
19-226 |
2.99e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 90.09 E-value: 2.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 19 PVILEAKQLSQVFKHGqteRTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCP---- 94
Cdd:COG3845 255 EVVLEVENLSVRDDRG---VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPrerr 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 95 ERGMVF-----QGYTLFPWKTVKENVMFGPQMRGA-------SQMTAEAQAREWIniiglEKYENQYPH------QLSGG 156
Cdd:COG3845 332 RLGVAYipedrLGRGLVPDMSVAENLILGRYRRPPfsrggflDRKAIRAFAEELI-----EEFDVRTPGpdtparSLSGG 406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 157 MKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLwQNIDITIIFVTHDMDEAILLADRIVAL 226
Cdd:COG3845 407 NQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAVM 475
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
31-235 |
3.08e-20 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 90.55 E-value: 3.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 31 FKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDG---ECITGPCPER--GMVFQGYTL 105
Cdd:TIGR02203 338 FRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGhdlADYTLASLRRqvALVSQDVVL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 106 FPwKTVKENVMFGpQMRGASQ-----MTAEAQAREWINII--GLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDE 178
Cdd:TIGR02203 418 FN-DTIANNIAYG-RTEQADRaeierALAAAYAQDFVDKLplGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDE 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446922839 179 PFGALDPHTRQKMQKHLMDLWQNidITIIFVTHDMdEAILLADRIVALKAnpGEIKE 235
Cdd:TIGR02203 496 ATSALDNESERLVQAALERLMQG--RTTLVIAHRL-STIEKADRIVVMDD--GRIVE 547
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
22-233 |
4.95e-20 |
|
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: 89.86 E-value: 4.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 22 LEAKQLSQVFKhgqtERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYH--SGEVLVD----GEC------- 88
Cdd:TIGR03269 1 IEVKNLTKKFD----GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEptSGRIIYHvalcEKCgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 89 -ITGPCPERG---------------------------MVFQGYTLFPWKTVKENVMFGPQMRGASQMTAEAQAREWINII 140
Cdd:TIGR03269 77 kVGEPCPVCGgtlepeevdfwnlsdklrrrirkriaiMLQRTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 141 GLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTH------DM- 213
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHwpevieDLs 236
|
250 260
....*....|....*....|
gi 446922839 214 DEAILLADRIVALKANPGEI 233
Cdd:TIGR03269 237 DKAIWLENGEIKEEGTPDEV 256
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
22-196 |
6.00e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 85.70 E-value: 6.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 22 LEAKQLSQVfkHGqtERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPERGMVFQ 101
Cdd:PRK13539 3 LEGEDLACV--RG--GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 102 GY--TLFPWKTVKENVMFGPQMRGasqmTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEP 179
Cdd:PRK13539 79 GHrnAMKPALTVAENLEFWAAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEP 154
|
170
....*....|....*..
gi 446922839 180 FGALDPHTrQKMQKHLM 196
Cdd:PRK13539 155 TAALDAAA-VALFAELI 170
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
7-224 |
6.92e-20 |
|
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: 86.23 E-value: 6.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 7 NAHEYFQKIYERPVILEAkqLSQVFKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDG 86
Cdd:cd03267 5 NLSKSYRVYSKEPGLIGS--LKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 87 ECitgPCPER-------GMVFQGYTLFPWK-TVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMK 158
Cdd:cd03267 83 LV---PWKRRkkflrriGVVFGQKTQLWWDlPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446922839 159 QRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIV 224
Cdd:cd03267 160 MRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVL 225
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
34-222 |
1.56e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 85.92 E-value: 1.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 34 GQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDP-----YHSGEVLVDGECITGPCP------ERGMVFQG 102
Cdd:PRK14271 30 GFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDkvsgyRYSGDVLLGGRSIFNYRDvlefrrRVGMLFQR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 103 YTLFPwKTVKENVMFG---PQMRGASQMTAEAQARewINIIGL----EKYENQYPHQLSGGMKQRVAIARALVNQPKILL 175
Cdd:PRK14271 110 PNPFP-MSIMDNVLAGvraHKLVPRKEFRGVAQAR--LTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLL 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446922839 176 MDEPFGALDPHTRQKMQKHLMDLWQNidITIIFVTHDMDEAILLADR 222
Cdd:PRK14271 187 LDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDR 231
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
21-226 |
2.03e-19 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 87.99 E-value: 2.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 21 ILEAKQLSQVFKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPE----- 95
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQviels 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 96 ----------RG----MVFQG--YTLFPWKTVKENVMFGPQM-RGASQMTAEAQAREWINIIGLEKYE---NQYPHQLSG 155
Cdd:PRK10261 92 eqsaaqmrhvRGadmaMIFQEpmTSLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIPEAQtilSRYPHQLSG 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446922839 156 GMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVAL 226
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVM 242
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
52-236 |
2.67e-19 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 87.60 E-value: 2.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 52 EFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER--------GMVFQG--YTLFPWKTVKENVMFGPQM 121
Cdd:PRK10261 351 ETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKlqalrrdiQFIFQDpyASLDPRQTVGDSIMEPLRV 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 122 RGASQMTAEAQAREWI-NIIGLE-KYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLW 199
Cdd:PRK10261 431 HGLLPGKAAAARVAWLlERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQ 510
|
170 180 190
....*....|....*....|....*....|....*..
gi 446922839 200 QNIDITIIFVTHDMDEAILLADRIVALkaNPGEIKEI 236
Cdd:PRK10261 511 RDFGIAYLFISHDMAVVERISHRVAVM--YLGQIVEI 545
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
17-241 |
5.05e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 84.27 E-value: 5.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 17 ERPVILEAKQLSQvfkhGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER 96
Cdd:PRK10253 3 ESVARLRGEQLTL----GYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 -----GMVFQGYTLFPWKTVKENVMFG-----PQMRGASQMTAEAQAREwINIIGLEKYENQYPHQLSGGMKQRVAIARA 166
Cdd:PRK10253 79 varriGLLAQNATTPGDITVQELVARGryphqPLFTRWRKEDEEAVTKA-MQATGITHLADQSVDTLSGGQRQRAWIAMV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446922839 167 LVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALK----ANPGEIKEIIEVNL 241
Cdd:PRK10253 158 LAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALRegkiVAQGAPKEIVTAEL 236
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
37-184 |
6.45e-19 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 86.47 E-value: 6.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 37 ERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHS--GEVLVDGECITGPCPER-GMVFQGYTLFPWKTVKE 113
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQILKRtGFVTQDDILYPHLTVRE 159
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446922839 114 NVMFGPQMRGASQMTAEAQ---AREWINIIGLEKYE-----NQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALD 184
Cdd:PLN03211 160 TLVFCSLLRLPKSLTKQEKilvAESVISELGLTKCEntiigNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
38-226 |
1.18e-18 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 85.95 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 38 RTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPcpERGMVFQGYTLFPWK------TV 111
Cdd:TIGR01193 487 SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI--DRHTLRQFINYLPQEpyifsgSI 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 112 KENVMFGPQmRGASQMTAEaQAREWINI--------IGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGAL 183
Cdd:TIGR01193 565 LENLLLGAK-ENVSQDEIW-AACEIAEIkddienmpLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNL 642
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446922839 184 DPHTRQKMQKHLMDLwqnIDITIIFVTHDMDEAiLLADRIVAL 226
Cdd:TIGR01193 643 DTITEKKIVNNLLNL---QDKTIIFVAHRLSVA-KQSDKIIVL 681
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
17-253 |
1.30e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 85.49 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 17 ERPVILEAKQLSQVFkhgqTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER 96
Cdd:PRK15439 7 TAPPLLCARSISKQY----SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 G------MVFQGYTLFPWKTVKENVMFGPQMRGASQMTAEAQAREwiniigLEKYENqyPHQLSGGM----KQRVAIARA 166
Cdd:PRK15439 83 AhqlgiyLVPQEPLLFPNLSVKENILFGLPKRQASMQKMKQLLAA------LGCQLD--LDSSAGSLevadRQIVEILRG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 167 LVNQPKILLMDEPFGALDPHTRQKMQKHLMDLwQNIDITIIFVTHDMDEAILLADRIVALK----ANPGEIK-----EII 237
Cdd:PRK15439 155 LMRDSRILILDEPTASLTPAETERLFSRIREL-LAQGVGIVFISHKLPEIRQLADRISVMRdgtiALSGKTAdlstdDII 233
|
250
....*....|....*.
gi 446922839 238 EVNLPRPRSLELMSTP 253
Cdd:PRK15439 234 QAITPAAREKSLSASQ 249
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
26-225 |
1.73e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 85.26 E-value: 1.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 26 QLSQV-FKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIA-GLDPyHSGEVLVDGECITGPC---------- 93
Cdd:PRK11160 340 TLNNVsFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTrAWDP-QQGEILLNGQPIADYSeaalrqaisv 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 94 -PERGMVFQGytlfpwkTVKENVMFgpqmrgASQMTAEAQAREWINIIGLEKY-ENQYP---------HQLSGGMKQRVA 162
Cdd:PRK11160 419 vSQRVHLFSA-------TLRDNLLL------AAPNASDEALIEVLQQVGLEKLlEDDKGlnawlgeggRQLSGGEQRRLG 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 163 IARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQniDITIIFVTH------DMDEAILLAD-RIVA 225
Cdd:PRK11160 486 IARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHrltgleQFDRICVMDNgQIIE 553
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
37-226 |
2.18e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 84.51 E-value: 2.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 37 ERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECI-----TGPCPERGMVFQGYTLFPWKTV 111
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVealsaRAASRRVASVPQDTSLSFEFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 112 KENVMFG--PQMRGASQMTA--EAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHT 187
Cdd:PRK09536 95 RQVVEMGrtPHRSRFDTWTEtdRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINH 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 446922839 188 RQKMQKHLMDLWQNiDITIIFVTHDMDEAILLADRIVAL 226
Cdd:PRK09536 175 QVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLL 212
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
19-185 |
2.65e-18 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 81.43 E-value: 2.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 19 PVILEAKQLSqvfkHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPERGM 98
Cdd:PRK13543 9 PPLLAAHALA----FSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 99 VFQGY--TLFPWKTVKENVMF--GPQMRGASQMTAEAQArewinIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKIL 174
Cdd:PRK13543 85 AYLGHlpGLKADLSTLENLHFlcGLHGRRAKQMPGSALA-----IVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLW 159
|
170
....*....|.
gi 446922839 175 LMDEPFGALDP 185
Cdd:PRK13543 160 LLDEPYANLDL 170
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
41-227 |
2.80e-18 |
|
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: 81.61 E-value: 2.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 41 LNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPERGMVFQGYTLF-----PW---KTVK 112
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAyaaqkPWllnATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 113 ENVMFG-PQMRGASQMTAEAQAREW-INII--GLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPH-T 187
Cdd:cd03290 97 ENITFGsPFNKQRYKAVTDACSLQPdIDLLpfGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlS 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446922839 188 RQKMQKHLMDLWQNIDITIIFVTHDMdEAILLADRIVALK 227
Cdd:cd03290 177 DHLMQEGILKFLQDDKRTLVLVTHKL-QYLPHADWIIAMK 215
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
21-227 |
3.23e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 81.98 E-value: 3.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 21 ILEAKQLSQvfkhGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPERgmVF 100
Cdd:PRK11231 2 TLRTENLTV----GYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ--LA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 101 QGYTLFPWK-------TVKENVMFG--PQMRGASQMTAEAQAR-EW-INIIGLEKYENQYPHQLSGGMKQRVAIARALVN 169
Cdd:PRK11231 76 RRLALLPQHhltpegiTVRELVAYGrsPWLSLWGRLSAEDNARvNQaMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446922839 170 QPKILLMDEPFGALD-PHtrqkmQKHLMDLWQNIDI---TIIFVTHDMDEAILLADRIVALK 227
Cdd:PRK11231 156 DTPVVLLDEPTTYLDiNH-----QVELMRLMRELNTqgkTVVTVLHDLNQASRYCDHLVVLA 212
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
13-224 |
1.98e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 79.23 E-value: 1.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 13 QKIYERPVIL--EAKQLSQVF--KHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAG--LDPYHSGEVLVDg 86
Cdd:COG2401 14 TKVYSSVLDLseRVAIVLEAFgvELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVP- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 87 eciTGPCPERgmvfqgytlfpwKTVKENVmfgpqmrgaSQMTAEAQAREWINIIGLEkyENQY----PHQLSGGMKQRVA 162
Cdd:COG2401 93 ---DNQFGRE------------ASLIDAI---------GRKGDFKDAVELLNAVGLS--DAVLwlrrFKELSTGQKFRFR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446922839 163 IARALVNQPKILLMDEpFGA-LDPHTRQKMQKHLMDLWQNIDITIIFVTHDMD-EAILLADRIV 224
Cdd:COG2401 147 LALLLAERPKLLVIDE-FCShLDRQTAKRVARNLQKLARRAGITLVVATHHYDvIDDLQPDLLI 209
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
54-222 |
3.88e-17 |
|
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: 81.13 E-value: 3.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 54 ICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDgecitgPCPERGMVFQGYTLFPWKTVKENVMFG-PQMRGA-------- 124
Cdd:TIGR03719 34 IGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ------PGIKVGYLPQEPQLDPTKTVRENVEEGvAEIKDAldrfneis 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 125 -------SQMT--AEAQAR--EWINIIGLEKYENQY---------P------HQLSGGMKQRVAIARALVNQPKILLMDE 178
Cdd:TIGR03719 108 akyaepdADFDklAAEQAElqEIIDAADAWDLDSQLeiamdalrcPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDE 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446922839 179 PFGALDPHTRQKMQKHLmdlwQNIDITIIFVTHD---MDEA---ILLADR 222
Cdd:TIGR03719 188 PTNHLDAESVAWLERHL----QEYPGTVVAVTHDryfLDNVagwILELDR 233
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
41-227 |
4.35e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 81.13 E-value: 4.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 41 LNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPY--HSGEVLVDGECITG----PCPERGMV--FQGYTLFPWKTVK 112
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHgtYEGEIIFEGEELQAsnirDTERAGIAiiHQELALVKELSVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 113 ENVMFGPQ-MRGA----SQMTAEAQarEWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALdphT 187
Cdd:PRK13549 101 ENIFLGNEiTPGGimdyDAMYLRAQ--KLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASL---T 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446922839 188 RQKMQkHLMDLWQNI---DITIIFVTHDMDEAILLADRIVALK 227
Cdd:PRK13549 176 ESETA-VLLDIIRDLkahGIACIYISHKLNEVKAISDTICVIR 217
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
20-222 |
7.21e-17 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 78.00 E-value: 7.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 20 VILEAKQLSQVFKHGQtertVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPERGM- 98
Cdd:PRK11614 4 VMLSFDKVSAHYGKIQ----ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 99 -----VFQGYTLFPWKTVKENVMFGpQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKI 173
Cdd:PRK11614 80 eavaiVPEGRRVFSRMTVEENLAMG-GFFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446922839 174 LLMDEPFGALDPHTRQKMQKHLMDLWQNiDITIIFVTHDMDEAILLADR 222
Cdd:PRK11614 159 LLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADR 206
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
40-251 |
8.13e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 78.51 E-value: 8.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 40 VLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITgpCPERGMVF---QGYTLFP-------WK 109
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD--YSKRGLLAlrqQVATVFQdpeqqifYT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 110 TVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQ 189
Cdd:PRK13638 94 DIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRT 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446922839 190 KMQKHLMDLWQNIDITIIfVTHDMDEAILLADRIVALK-------ANPGEI---KEIIE-VNLPRPRSLELMS 251
Cdd:PRK13638 174 QMIAIIRRIVAQGNHVII-SSHDIDLIYEISDAVYVLRqgqilthGAPGEVfacTEAMEqAGLTQPWLVKLHT 245
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
17-235 |
8.52e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 80.13 E-value: 8.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 17 ERPVILEAKQLSQVF--KHGQTERTV-----LNKLDLKIHKREFICVIGPSGCGKST----LSRVIAGldpyhSGEVLVD 85
Cdd:PRK15134 271 PASPLLDVEQLQVAFpiRKGILKRTVdhnvvVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFD 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 86 GECITG-------PCPER-GMVFQ--GYTLFPWKTVKENVMFG-----PQMRGASQmtaEAQAREWINIIGLEKYENQ-Y 149
Cdd:PRK15134 346 GQPLHNlnrrqllPVRHRiQVVFQdpNSSLNPRLNVLQIIEEGlrvhqPTLSAAQR---EQQVIAVMEEVGLDPETRHrY 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 150 PHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALKAn 229
Cdd:PRK15134 423 PAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQ- 501
|
....*.
gi 446922839 230 pGEIKE 235
Cdd:PRK15134 502 -GEVVE 506
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
18-268 |
1.08e-16 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 77.82 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 18 RPVILEAKQLSQvfkhgQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDP----YHSGEVLVDGECITgPC 93
Cdd:PRK10418 1 MPQQIELRNIAL-----QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPagvrQTAGRVLLDGKPVA-PC 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 94 PERG----MVFQG-YTLF-PWKTVKENVMFGPQMRGasQMTAEAQAREWINIIGLEKYE---NQYPHQLSGGMKQRVAIA 164
Cdd:PRK10418 75 ALRGrkiaTIMQNpRSAFnPLHTMHTHARETCLALG--KPADDATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 165 RALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRiVALKANpGEIKEIIEVNlprp 244
Cdd:PRK10418 153 LALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADD-VAVMSH-GRIVEQGDVE---- 226
|
250 260
....*....|....*....|....
gi 446922839 245 rslELMSTPEFKQLRSrvdyLVHA 268
Cdd:PRK10418 227 ---TLFNAPKHAVTRS----LVSA 243
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
41-226 |
1.37e-16 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 79.61 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 41 LNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITG------PCPERGMVF---------QGYTL 105
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVArlqqdpPRNVEGTVYdfvaegieeQAEYL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 106 FPWKTVKENVMFGPQMRGASQMtaeAQAREWINIIGLEKYENQY----------PHQ----LSGGMKQRVAIARALVNQP 171
Cdd:PRK11147 99 KRYHDISHLVETDPSEKNLNEL---AKLQEQLDHHNLWQLENRInevlaqlgldPDAalssLSGGWLRKAALGRALVSNP 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446922839 172 KILLMDEPFGALDPHTRQKMQKHLMDLwqniDITIIFVTHDMDEAILLADRIVAL 226
Cdd:PRK11147 176 DVLLLDEPTNHLDIETIEWLEGFLKTF----QGSIIFISHDRSFIRNMATRIVDL 226
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
52-201 |
1.41e-16 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 79.62 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 52 EFICVIGPSGCGKST----LSRViagLDPyHSGEVLVDGECITGPCPER-----GMVFQGYTLFPwKTVKENVMFG---- 118
Cdd:PRK13657 362 QTVAIVGPTGAGKSTlinlLQRV---FDP-QSGRILIDGTDIRTVTRASlrrniAVVFQDAGLFN-RSIEDNIRVGrpda 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 119 --PQMRGASqmtAEAQAREWIniiglEKYENQYP-------HQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQ 189
Cdd:PRK13657 437 tdEEMRAAA---ERAQAHDFI-----ERKPDGYDtvvgergRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEA 508
|
170
....*....|..
gi 446922839 190 KMQKHLMDLWQN 201
Cdd:PRK13657 509 KVKAALDELMKG 520
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
40-257 |
1.50e-16 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 78.41 E-value: 1.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 40 VLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGL---------DPYHsgevLVDGECITGPCPER--------GMVFQG 102
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGItkdnwhvtaDRFR----WNGIDLLKLSPRERrkiigreiAMIFQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 103 YT--LFPWKTVKEN---VMFGPQMRG---ASQMTAEAQAREWINIIGLEKYE---NQYPHQLSGGMKQRVAIARALVNQP 171
Cdd:COG4170 98 PSscLDPSAKIGDQlieAIPSWTFKGkwwQRFKWRKKRAIELLHRVGIKDHKdimNSYPHELTEGECQKVMIAMAIANQP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 172 KILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVAL----KANPGEIKEIIEVNL-PRPRS 246
Cdd:COG4170 178 RLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLycgqTVESGPTEQILKSPHhPYTKA 257
|
250
....*....|.
gi 446922839 247 LeLMSTPEFKQ 257
Cdd:COG4170 258 L-LRSMPDFRQ 267
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
52-232 |
2.29e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 78.94 E-value: 2.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 52 EFICVIGPSGCGKSTLSRVIAGLDP---YHSGEVLVDGECITGPCPER--GMVFQGYTLFPWKTVKENVMFGPQMRGASQ 126
Cdd:TIGR00955 52 ELLAVMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNGMPIDAKEMRAisAYVQQDDLFIPTLTVREHLMFQAHLRMPRR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 127 MTA-EAQAR--EWINIIGLEKYEN---QYPHQ---LSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMD 197
Cdd:TIGR00955 132 VTKkEKRERvdEVLQALGLRKCANtriGVPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKG 211
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446922839 198 LWQNiDITIIFVTHD--------MDEAILLADRIVALKANPGE 232
Cdd:TIGR00955 212 LAQK-GKTIICTIHQpsselfelFDKIILMAEGRVAYLGSPDQ 253
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
54-222 |
9.10e-16 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 77.08 E-value: 9.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 54 ICVIGPSGCGKSTLSRVIAGLDPYHSGE-VLVDGECItgpcperGMVFQGYTLFPWKTVKENVMFGPQ------------ 120
Cdd:PRK11819 36 IGVLGLNGAGKSTLLRIMAGVDKEFEGEaRPAPGIKV-------GYLPQEPQLDPEKTVRENVEEGVAevkaaldrfnei 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 121 -MRGASQM-----TAEAQAR--EWINIIGLEKYENQY---------PH------QLSGGMKQRVAIARALVNQPKILLMD 177
Cdd:PRK11819 109 yAAYAEPDadfdaLAAEQGElqEIIDAADAWDLDSQLeiamdalrcPPwdakvtKLSGGERRRVALCRLLLEKPDMLLLD 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446922839 178 EPFGALDPHTRQKMQKHLmdlwQNIDITIIFVTHD---MDEA---ILLADR 222
Cdd:PRK11819 189 EPTNHLDAESVAWLEQFL----HDYPGTVVAVTHDryfLDNVagwILELDR 235
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
36-226 |
1.64e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 76.30 E-value: 1.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 36 TERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDG---ECITGPCPERG--MVFQGYTLFPwKT 110
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGrplSSLSHSVLRQGvaMVQQDPVVLA-DT 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 111 VKENVMFGPQMRGAS--QMTAEAQAREWINII--GLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPH 186
Cdd:PRK10790 431 FLANVTLGRDISEEQvwQALETVQLAELARSLpdGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSG 510
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446922839 187 TRQKMQKHLMDLWQNidITIIFVTHDMdEAILLADRIVAL 226
Cdd:PRK10790 511 TEQAIQQALAAVREH--TTLVVIAHRL-STIVEADTILVL 547
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
44-245 |
3.47e-15 |
|
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: 75.22 E-value: 3.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 44 LDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPE--RGM---VFQGYTLFpwktvkenvmfg 118
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREayRQLfsaVFSDFHLF------------ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 119 PQMRGASQMTAEAQAREWINIIGLE---KYENQY--PHQLSGGMKQRVAIARALVNQPKILLMDEpFGA-LDPHTRQKMQ 192
Cdd:COG4615 419 DRLLGLDGEADPARARELLERLELDhkvSVEDGRfsTTDLSQGQRKRLALLVALLEDRPILVFDE-WAAdQDPEFRRVFY 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446922839 193 KHLMDLWQNIDITIIFVTHDmDEAILLADRIVALKAnpGEIKEIIEVNLPRPR 245
Cdd:COG4615 498 TELLPELKARGKTVIAISHD-DRYFDLADRVLKMDY--GKLVELTGPAALAAS 547
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
39-227 |
4.80e-15 |
|
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: 74.86 E-value: 4.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 39 TVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPY--HSGEVLVDGECITGP----CPERGMVF--QGYTLFPWKT 110
Cdd:TIGR02633 15 KALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHgtWDGEIYWSGSPLKASnirdTERAGIVIihQELTLVPELS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 111 VKENVMFGPQMRGASQMTAEA----QAREWINIIGLEKYENQYP-HQLSGGMKQRVAIARALVNQPKILLMDEPFGALdp 185
Cdd:TIGR02633 95 VAENIFLGNEITLPGGRMAYNamylRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQARLLILDEPSSSL-- 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446922839 186 hTRQKMQKhLMDLWQNI---DITIIFVTHDMDEAILLADRIVALK 227
Cdd:TIGR02633 173 -TEKETEI-LLDIIRDLkahGVACVYISHKLNEVKAVCDTICVIR 215
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
40-236 |
1.05e-14 |
|
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: 71.29 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 40 VLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER-----GMVFQGYTLFPwKTVKEN 114
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDlrsslTIIPQDPTLFS-GTIRSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 115 V-MFGpqmrgasqMTAEAQAREWINIIglEKYENqyphqLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQK 193
Cdd:cd03369 102 LdPFD--------EYSDEEIYGALRVS--EGGLN-----LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQK 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446922839 194 HLMDLWQNidITIIFVTHDMdEAILLADRIVALKAnpGEIKEI 236
Cdd:cd03369 167 TIREEFTN--STILTIAHRL-RTIIDYDKILVMDA--GEVKEY 204
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
78-230 |
1.19e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 74.30 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 78 HSGEVLVDGECItgpCPER--------GMVFQGYTLFPwKTVKENVMFGPQ---MRGASQMTAEAQAREWINIIGlEKYE 146
Cdd:PTZ00265 1275 NSGKILLDGVDI---CDYNlkdlrnlfSIVSQEPMLFN-MSIYENIKFGKEdatREDVKRACKFAAIDEFIESLP-NKYD 1349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 147 NQ---YPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMdEAILLADRI 223
Cdd:PTZ00265 1350 TNvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI-ASIKRSDKI 1428
|
....*..
gi 446922839 224 VALKaNP 230
Cdd:PTZ00265 1429 VVFN-NP 1434
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
37-213 |
1.53e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 71.68 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 37 ERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPERGMVFQGYTLfpwkTVKENVM 116
Cdd:PRK09544 16 QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTTLPL----TVNRFLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 117 FGPQMRGASQMTA--EAQAREWIniiglekyenQYPHQ-LSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQK 193
Cdd:PRK09544 92 LRPGTKKEDILPAlkRVQAGHLI----------DAPMQkLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYD 161
|
170 180
....*....|....*....|
gi 446922839 194 HLMDLWQNIDITIIFVTHDM 213
Cdd:PRK09544 162 LIDQLRRELDCAVLMVSHDL 181
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
48-232 |
2.66e-14 |
|
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: 70.90 E-value: 2.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 48 IHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITgpcpergmvfqgytlfpwktvkenvmFGPQ-MRGASQ 126
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS--------------------------YKPQyIKADYE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 127 MTAEAQAR--------------EWINIIGLEK-YENQYPhQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKM 191
Cdd:cd03237 76 GTVRDLLSsitkdfythpyfktEIAKPLQIEQiLDREVP-ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446922839 192 QKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALKANPGE 232
Cdd:cd03237 155 SKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFEGEPSV 195
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
28-221 |
3.41e-14 |
|
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: 73.06 E-value: 3.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 28 SQVFKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTL-SRVIAGLDPYHsGEVLVDGEciTGPCPERGMVfQGYTLf 106
Cdd:TIGR00957 641 NATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLlSALLAEMDKVE-GHVHMKGS--VAYVPQQAWI-QNDSL- 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 107 pwktvKENVMFGPQM---RGASQMTAEAQAREWINIIGLEKYE-NQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGA 182
Cdd:TIGR00957 716 -----RENILFGKALnekYYQQVLEACALLPDLEILPSGDRTEiGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSA 790
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446922839 183 LDPHTRQKMQKHL---MDLWQNidITIIFVTHDM------DEAILLAD 221
Cdd:TIGR00957 791 VDAHVGKHIFEHVigpEGVLKN--KTRILVTHGIsylpqvDVIIVMSG 836
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
50-225 |
3.43e-14 |
|
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: 68.55 E-value: 3.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 50 KREFICVIGPSGCGKSTLSRVIAG-LDPYHSGEVLVDGECItgpcpergmvfqgytlfpwktvkenvmfgpqmrgasqmt 128
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDGEDI--------------------------------------- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 129 aeaqaREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNI-----D 203
Cdd:smart00382 42 -----LEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLlksekN 116
|
170 180
....*....|....*....|..
gi 446922839 204 ITIIFVTHDMDEAILLADRIVA 225
Cdd:smart00382 117 LTVILTTNDEKDLGPALLRRRF 138
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
38-258 |
4.28e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 70.59 E-value: 4.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 38 RTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITG-----------------PCPErGMvf 100
Cdd:PRK10575 24 RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwsskafarkvaylpqqlPAAE-GM-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 101 qgytlfpwkTVKENVMFG--PQMRGASQMTAEAQAR--EWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLM 176
Cdd:PRK10575 101 ---------TVRELVAIGryPWHGALGRFGAADREKveEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 177 DEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALKANpgeikEIIEVNLPrprsLELMSTPEFK 256
Cdd:PRK10575 172 DEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGG-----EMIAQGTP----AELMRGETLE 242
|
..
gi 446922839 257 QL 258
Cdd:PRK10575 243 QI 244
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
52-241 |
1.16e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 69.10 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 52 EFICVIGPSGCGKSTLSRVIAGLDPYHsGEVLVDGECITG-PCPE----RGM------------VFQGYTLF-PWKTVKE 113
Cdd:COG4138 23 ELIHLIGPNGAGKSTLLARMAGLLPGQ-GEILLNGRPLSDwSAAElarhRAYlsqqqsppfampVFQYLALHqPAGASSE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 114 NVmfgpqmRGASQMTAEAqarewiniIGLEKYENQYPHQLSGGMKQRVAIARAL------VN-QPKILLMDEPFGALDPH 186
Cdd:COG4138 102 AV------EQLLAQLAEA--------LGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwptINpEGQLLLLDEPMNSLDVA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446922839 187 TRQKMQKHLMDLWQNiDITIIFVTHDMDEAILLADRIVALKA----NPGEIKEIIEVNL 241
Cdd:COG4138 168 QQAALDRLLRELCQQ-GITVVMSSHDLNHTLRHADRVWLLKQgklvASGETAEVMTPEN 225
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
47-224 |
1.30e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 70.80 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 47 KIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPERGM----VF-----QGYTLFPWKTVKENV-- 115
Cdd:PRK10762 274 TLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLangiVYisedrKRDGLVLGMSVKENMsl 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 116 -------MFGPQMRGASQMTAEAQAREWINI--------IGLekyenqyphqLSGGMKQRVAIARALVNQPKILLMDEPF 180
Cdd:PRK10762 354 talryfsRAGGSLKHADEQQAVSDFIRLFNIktpsmeqaIGL----------LSGGNQQKVAIARGLMTRPKVLILDEPT 423
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446922839 181 GALDPHTRQKMQKhLMDLWQNIDITIIFVTHDMDEAILLADRIV 224
Cdd:PRK10762 424 RGVDVGAKKEIYQ-LINQFKAEGLSIILVSSEMPEVLGMSDRIL 466
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
37-216 |
1.32e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 70.43 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 37 ERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPY-HSGEVLVDGEcitgpcpERGmvfQGYTLFPWK------ 109
Cdd:PRK10938 272 DRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQgYSNDLTLFGR-------RRG---SGETIWDIKkhigyv 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 110 ------------TVKENVMFGP-QMRGASQMTAEAQ---AREWINIIGLEKYENQYP-HQLSGGMKQRVAIARALVNQPK 172
Cdd:PRK10938 342 ssslhldyrvstSVRNVILSGFfDSIGIYQAVSDRQqklAQQWLDILGIDKRTADAPfHSLSWGQQRLALIVRALVKHPT 421
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446922839 173 ILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEA 216
Cdd:PRK10938 422 LLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-224 |
1.66e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 69.35 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 21 ILEAKQLSQVFKHGQTE---------------RTV--LNKLDLKIHKREFICVIGPSGCGKSTLSRVIAG-LDPyHSGEV 82
Cdd:COG4586 1 IIEVENLSKTYRVYEKEpglkgalkglfrreyREVeaVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGiLVP-TSGEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 83 LVDGECitgPCPER-------GMVF-------------QGYTLF------PWKTVKENVmfgpqmrgasqmtaeaqaREW 136
Cdd:COG4586 80 RVLGYV---PFKRRkefarriGVVFgqrsqlwwdlpaiDSFRLLkaiyriPDAEYKKRL------------------DEL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 137 INIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEA 216
Cdd:COG4586 139 VELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDI 218
|
....*...
gi 446922839 217 ILLADRIV 224
Cdd:COG4586 219 EALCDRVI 226
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
40-211 |
3.44e-13 |
|
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: 69.39 E-value: 3.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 40 VLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPERGMVFQGytlfpwkTVKENVMFgP 119
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPYMTLG-------TLRDQIIY-P 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 120 ------QMRGAS-----QMTAEAQ-----AREwiniIGLEKYENqYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGAL 183
Cdd:TIGR00954 539 dssedmKRRGLSdkdleQILDNVQlthilERE----GGWSAVQD-WMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAV 613
|
170 180
....*....|....*....|....*...
gi 446922839 184 DPHTRQKMQKHLmdlwQNIDITIIFVTH 211
Cdd:TIGR00954 614 SVDVEGYMYRLC----REFGITLFSVSH 637
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-238 |
3.96e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 69.04 E-value: 3.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 4 STFNAHEYFQKIYERPVILEAKQLSQvfkhgqTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVL 83
Cdd:PRK09700 248 NRFNAMKENVSNLAHETVFEVRNVTS------RDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIR 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 84 VDGECITGPCP----ERGMVF-------QGYtlFPWKTVKENVMFGPQMRGA-------------SQMTAEAQaREWINI 139
Cdd:PRK09700 322 LNGKDISPRSPldavKKGMAYitesrrdNGF--FPNFSIAQNMAISRSLKDGgykgamglfhevdEQRTAENQ-RELLAL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 140 igleKYE--NQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKhLMDLWQNIDITIIFVTHDMDEAI 217
Cdd:PRK09700 399 ----KCHsvNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYK-VMRQLADDGKVILMVSSELPEII 473
|
250 260
....*....|....*....|.
gi 446922839 218 LLADRIVALKAnpGEIKEIIE 238
Cdd:PRK09700 474 TVCDRIAVFCE--GRLTQILT 492
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
17-223 |
4.47e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 69.38 E-value: 4.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 17 ERPVIlEAKQLSQVFkhGqtERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGpcpeR 96
Cdd:NF033858 263 DEPAI-EARGLTMRF--G--DFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDA----G 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 GM--------VFQGYTLFPWKTVKENVM-----FG-PqmrgasqmTAEAQAR--EWINIIGLEKYENQYPHQLSGGMKQR 160
Cdd:NF033858 334 DIatrrrvgyMSQAFSLYGELTVRQNLElharlFHlP--------AAEIAARvaEMLERFDLADVADALPDSLPLGIRQR 405
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446922839 161 VAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITiIFV-THDMDEAiLLADRI 223
Cdd:NF033858 406 LSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVT-IFIsTHFMNEA-ERCDRI 467
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
38-226 |
6.14e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 67.54 E-value: 6.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 38 RTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYH--------SGEVLVDGE---CITGP---CPERGMVFQGY 103
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEplaAIDAPrlaRLRAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 104 TLFPWkTVKENVMFG--PQMRGASQMTAEAQAREW--INIIGLEKYENQYPHQLSGGMKQRVAIARALVN---------Q 170
Cdd:PRK13547 94 PAFAF-SAREIVLLGryPHARRAGALTHRDGEIAWqaLALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaqP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446922839 171 PKILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVAL 226
Cdd:PRK13547 173 PRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAML 228
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
149-223 |
6.35e-13 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 67.91 E-value: 6.35e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446922839 149 YPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRI 223
Cdd:PRK15093 155 FPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKI 229
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
21-226 |
8.16e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 68.89 E-value: 8.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 21 ILEAKQLSQVFKhgQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECI----------T 90
Cdd:TIGR01257 1937 ILRLNELTKVYS--GTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIltnisdvhqnM 2014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 91 GPCPERGMVFQgytlfpWKTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQ 170
Cdd:TIGR01257 2015 GYCPQFDAIDD------LLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGC 2088
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446922839 171 PKILLMDEPFGALDPHTRQKMQKHLMDLWQNiDITIIFVTHDMDEAILLADRIVAL 226
Cdd:TIGR01257 2089 PPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIM 2143
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
40-226 |
1.04e-12 |
|
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: 66.80 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 40 VLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAG-LDPY-----HSGEVLVdgecitgpCPERGMVFQGytlfpwkTVKE 113
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGeLEPSegkikHSGRISF--------SSQFSWIMPG-------TIKE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 114 NVMFGPQMRgasqmtaEAQAREWINIIGLEKYENQYPHQ-----------LSGGMKQRVAIARALVNQPKILLMDEPFGA 182
Cdd:cd03291 117 NIIFGVSYD-------EYRYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGY 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446922839 183 LDPHTRQKM-QKHLMDLWQNidITIIFVTHDMdEAILLADRIVAL 226
Cdd:cd03291 190 LDVFTEKEIfESCVCKLMAN--KTRILVTSKM-EHLKKADKILIL 231
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
31-235 |
1.30e-12 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 67.74 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 31 FKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECI-----TGPCPERGMVFQGYTL 105
Cdd:PRK11176 349 FTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLrdytlASLRNQVALVSQNVHL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 106 FPwKTVKENVMFG-------PQMRGASQMtaeAQAREWIN--------IIGlekyENQYphQLSGGMKQRVAIARALVNQ 170
Cdd:PRK11176 429 FN-DTIANNIAYArteqysrEQIEEAARM---AYAMDFINkmdngldtVIG----ENGV--LLSGGQRQRIAIARALLRD 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446922839 171 PKILLMDEPFGALDPHTRQKMQKHLMDLWQNidITIIFVTHDMdEAILLADRIVALKAnpGEIKE 235
Cdd:PRK11176 499 SPILILDEATSALDTESERAIQAALDELQKN--RTSLVIAHRL-STIEKADEILVVED--GEIVE 558
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
20-184 |
5.01e-12 |
|
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: 63.82 E-value: 5.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 20 VILEAKQLSQVFKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAG-LDPYHS--GEVLVDGEcitgPCPER 96
Cdd:cd03233 2 STLSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANrTEGNVSveGDIHYNGI----PYKEF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 97 GMVFQGYTLF--------PWKTVKENVMFGPQMRGasqmtaeaqarewiniiglekyeNQYPHQLSGGMKQRVAIARALV 168
Cdd:cd03233 78 AEKYPGEIIYvseedvhfPTLTVRETLDFALRCKG-----------------------NEFVRGISGGERKRVSIAEALV 134
|
170
....*....|....*.
gi 446922839 169 NQPKILLMDEPFGALD 184
Cdd:cd03233 135 SRASVLCWDNSTRGLD 150
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
40-226 |
5.88e-12 |
|
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: 66.09 E-value: 5.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 40 VLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAG-LDPY-----HSGEVLVdgecitgpCPErgmvfqgytlFPW---KT 110
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGeLEPSegkikHSGRISF--------SPQ----------TSWimpGT 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 111 VKENVMFGPQMRgasqmtaEAQAREWINIIGLEKYENQYPHQ-----------LSGGMKQRVAIARALVNQPKILLMDEP 179
Cdd:TIGR01271 503 IKDNIIFGLSYD-------EYRYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSP 575
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446922839 180 FGALDPHTRQKM-QKHLMDLWQNidITIIFVTHDMdEAILLADRIVAL 226
Cdd:TIGR01271 576 FTHLDVVTEKEIfESCLCKLMSN--KTRILVTSKL-EHLKKADKILLL 620
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
39-236 |
5.89e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.58 E-value: 5.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 39 TVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGPCPER------GMVFQGYTLFPWKTVK 112
Cdd:PRK09700 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLaaqlgiGIIYQELSVIDELTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 113 ENV---------MFGPQMRGASQMtaEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGAL 183
Cdd:PRK09700 99 ENLyigrhltkkVCGVNIIDWREM--RVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446922839 184 dphTRQKMQK--HLMDLWQNIDITIIFVTHDMDEAILLADRIVALK----ANPGEIKEI 236
Cdd:PRK09700 177 ---TNKEVDYlfLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKdgssVCSGMVSDV 232
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
41-227 |
1.03e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 64.93 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 41 LNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECI----TGPCPERG--MVFQGYTLFPWKTVKEN 114
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfasTTAALAAGvaIIYQELHLVPEMTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 115 VMFG--PQMRG-ASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKM 191
Cdd:PRK11288 100 LYLGqlPHKGGiVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQL 179
|
170 180 190
....*....|....*....|....*....|....*.
gi 446922839 192 QKHLMDLWQNIDItIIFVTHDMDEAILLADRIVALK 227
Cdd:PRK11288 180 FRVIRELRAEGRV-ILYVSHRMEEIFALCDAITVFK 214
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
37-184 |
3.07e-11 |
|
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: 61.39 E-value: 3.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 37 ERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYH--SGEVLVDGECITG-PCPER-----GMVFQgytlFPw 108
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKGEDITDlPPEERarlgiFLAFQ----YP- 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446922839 109 ktvkenvmfgPQMRGasqmtaeaqarewINIIGLEKYENQyphQLSGGMKQRVAIARALVNQPKILLMDEPFGALD 184
Cdd:cd03217 87 ----------PEIPG-------------VKNADFLRYVNE---GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLD 136
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
41-223 |
4.58e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 62.88 E-value: 4.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 41 LNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHS--GEVLVDGEcitgPC--------PERGMVF--QGYTLFPW 108
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGE----VCrfkdirdsEALGIVIihQELALIPY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 109 KTVKENVMFG--PQMRGA-SQMTAEAQAREWINIIGLEkyENqyPHQLSG----GMKQRVAIARALVNQPKILLMDEPFG 181
Cdd:NF040905 93 LSIAENIFLGneRAKRGViDWNETNRRARELLAKVGLD--ES--PDTLVTdigvGKQQLVEIAKALSKDVKLLILDEPTA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446922839 182 ALDPHTRQKMQKHLMDLWQNiDITIIFVTHDMDEAILLADRI 223
Cdd:NF040905 169 ALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSI 209
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
48-231 |
5.64e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.90 E-value: 5.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 48 IHKREFICVIGPSGCGKSTLSRVIAG-LDPyHSGEVLVDgecitgpcpergmvfqgytlfpwktVKenVMFGPQ-MRGAS 125
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGvLKP-DEGEVDPE-------------------------LK--ISYKPQyIKPDY 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 126 QMTAEAQAR-------------EWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTR---Q 189
Cdd:PRK13409 414 DGTVEDLLRsitddlgssyyksEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRlavA 493
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446922839 190 KMQKHLMDlwqNIDITIIFVTHD---MDeaiLLADRIVALKANPG 231
Cdd:PRK13409 494 KAIRRIAE---EREATALVVDHDiymID---YISDRLMVFEGEPG 532
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
35-235 |
6.57e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.07 E-value: 6.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 35 QTERTVLNKLDLKIHKREFICVIGPSGCGKSTL-SRVIAGLDPYHSGEVLVDGEciTGPCPERGMVFQGytlfpwkTVKE 113
Cdd:PLN03232 627 KTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLiSAMLGELSHAETSSVVIRGS--VAYVPQVSWIFNA-------TVRE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 114 NVMFGpqmrgaSQMTAEaqaREW--INIIGLEKYENQYPHQ-----------LSGGMKQRVAIARALVNQPKILLMDEPF 180
Cdd:PLN03232 698 NILFG------SDFESE---RYWraIDVTALQHDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYIFDDPL 768
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446922839 181 GALDPH-TRQKMQKHLMDLWQNidITIIFVTHDMdEAILLADRIVALkaNPGEIKE 235
Cdd:PLN03232 769 SALDAHvAHQVFDSCMKDELKG--KTRVLVTNQL-HFLPLMDRIILV--SEGMIKE 819
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
38-216 |
1.28e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 62.06 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 38 RTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGP------CPE-----RGMvfqGYTLF 106
Cdd:NF033858 14 TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADArhrravCPRiaympQGL---GKNLY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 107 PWKTVKENVMFGPQMRGasQMTAEAQAR--EWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALD 184
Cdd:NF033858 91 PTLSVFENLDFFGRLFG--QDAAERRRRidELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446922839 185 PHTRQKmqkhlmdLWQNID--------ITIIFVTHDMDEA 216
Cdd:NF033858 169 PLSRRQ-------FWELIDriraerpgMSVLVATAYMEEA 201
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
31-227 |
3.39e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 60.50 E-value: 3.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 31 FKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGEcitgPCPE------RG---MVFQ 101
Cdd:PRK10789 321 FTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDI----PLTKlqldswRSrlaVVSQ 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 102 GYTLFPwKTVKENVMFG-PqmrGASQMTAEAQAR-----EwiNIIGL-EKYENQYPHQ---LSGGMKQRVAIARALVNQP 171
Cdd:PRK10789 397 TPFLFS-DTVANNIALGrP---DATQQEIEHVARlasvhD--DILRLpQGYDTEVGERgvmLSGGQKQRISIARALLLNA 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446922839 172 KILLMDEPFGALDPHTRQKMQKHLMDLWQNidITIIFVTHDMdEAILLADRIVALK 227
Cdd:PRK10789 471 EILILDDALSAVDGRTEHQILHNLRQWGEG--RTVIISAHRL-SALTEASEILVMQ 523
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
44-223 |
3.47e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.45 E-value: 3.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 44 LDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECI----TGPCPERGMVF-----QGYTLF-----PWK 109
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEInalsTAQRLARGLVYlpedrQSSGLYldaplAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 110 TVkeNVMFGPQmrGASQMTAEAQARewiniigLEKY----------ENQYPHQLSGGMKQRVAIARALVNQPKILLMDEP 179
Cdd:PRK15439 362 VC--ALTHNRR--GFWIKPARENAV-------LERYrralnikfnhAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446922839 180 FGALDPHTRQkmqkhlmDLWQNI------DITIIFVTHDMDEAILLADRI 223
Cdd:PRK15439 431 TRGVDVSARN-------DIYQLIrsiaaqNVAVLFISSDLEEIEQMADRV 473
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
46-233 |
3.68e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 60.31 E-value: 3.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 46 LKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGEcitgPCPERGmvfqgytlfPWKTVKENVMFGPQMRGAS 125
Cdd:PRK11288 274 FSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGK----PIDIRS---------PRDAIRAGIMLCPEDRKAE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 126 QMTAEAQAREWINI-------------------------IGLEKYENQYPHQ----LSGGMKQRVAIARALVNQPKILLM 176
Cdd:PRK11288 341 GIIPVHSVADNINIsarrhhlragclinnrweaenadrfIRSLNIKTPSREQlimnLSGGNQQKAILGRWLSEDMKVILL 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446922839 177 DEPFGALDPHTRQKMQKHLMDLWQNiDITIIFVTHDMDEAILLADRIVALKAnpGEI 233
Cdd:PRK11288 421 DEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMRE--GRI 474
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-228 |
4.20e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 58.79 E-value: 4.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 26 QLSQVfkhgqTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYhSGEVLVDGECITG-PCPE----RG--- 97
Cdd:PRK03695 2 QLNDV-----AVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAwSAAElarhRAyls 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 98 --------M-VFQGYTLFpwktvkenvmfgpQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARAL- 167
Cdd:PRK03695 76 qqqtppfaMpVFQYLTLH-------------QPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVl 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446922839 168 ----VNQP--KILLMDEPFGALDPhTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIVALKA 228
Cdd:PRK03695 143 qvwpDINPagQLLLLDEPMNSLDV-AQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQ 208
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
20-197 |
4.45e-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: 4.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 20 VILEAKQLSQVFKHgqteRTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVdgecitGPCPERGMV 99
Cdd:TIGR03719 321 KVIEAENLTKAFGD----KLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI------GETVKLAYV 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 100 FQGY-TLFPWKTVKENVmfgpqMRGASQMT---AEAQAREWINIIGLEKYENQYP-HQLSGGMKQRVAIARALVNQPKIL 174
Cdd:TIGR03719 391 DQSRdALDPNKTVWEEI-----SGGLDIIKlgkREIPSRAYVGRFNFKGSDQQKKvGQLSGGERNRVHLAKTLKSGGNVL 465
|
170 180
....*....|....*....|...
gi 446922839 175 LMDEPFGALDPHTRQKMQKHLMD 197
Cdd:TIGR03719 466 LLDEPTNDLDVETLRALEEALLN 488
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
47-232 |
5.29e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 59.80 E-value: 5.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 47 KIHKREFICVIGPSGCGKSTLSRVIAG-LDPyHSGEVLvdgecitgpcpergmvfqgytlfpwKTVKenVMFGPQ-MRGA 124
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGvLKP-DEGEVD-------------------------EDLK--ISYKPQyISPD 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 125 SQMTAEAQAREWIN-----------II---GLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQK 190
Cdd:COG1245 414 YDGTVEEFLRSANTddfgssyykteIIkplGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLA 493
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446922839 191 MQKHLMDLWQNIDITIIFVTHD---MDeaiLLADRIVALKANPGE 232
Cdd:COG1245 494 VAKAIRRFAENRGKTAMVVDHDiylID---YISDRLMVFEGEPGV 535
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
37-235 |
5.48e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 60.14 E-value: 5.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 37 ERTVLNKLDLKIHKREFICVIGPSGCGKSTL-SRVIAGLDPYHSGEVLVDGEciTGPCPERGMVFQGytlfpwkTVKENV 115
Cdd:PLN03130 629 ERPTLSNINLDVPVGSLVAIVGSTGEGKTSLiSAMLGELPPRSDASVVIRGT--VAYVPQVSWIFNA-------TVRDNI 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 116 MFGPQMRgasqmtaeaQAREW--INIIGLEKYENQYPH-----------QLSGGMKQRVAIARALVNQPKILLMDEPFGA 182
Cdd:PLN03130 700 LFGSPFD---------PERYEraIDVTALQHDLDLLPGgdlteigergvNISGGQKQRVSMARAVYSNSDVYIFDDPLSA 770
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446922839 183 LDPHT-RQKMQKHLMDLWQNidITIIFVTHDMdEAILLADRIVALkaNPGEIKE 235
Cdd:PLN03130 771 LDAHVgRQVFDKCIKDELRG--KTRVLVTNQL-HFLSQVDRIILV--HEGMIKE 819
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
32-187 |
5.73e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.12 E-value: 5.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 32 KHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAG-LDPYHSGevlVDGEcIT--GPCPE------RGMVF-- 100
Cdd:TIGR00956 68 FRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASnTDGFHIG---VEGV-ITydGITPEeikkhyRGDVVyn 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 101 -QGYTLFPWKTVKENVMF-----GPQMRG--------ASQMTAEAQArewinIIGLE-----KYENQYPHQLSGGMKQRV 161
Cdd:TIGR00956 144 aETDVHFPHLTVGETLDFaarckTPQNRPdgvsreeyAKHIADVYMA-----TYGLShtrntKVGNDFVRGVSGGERKRV 218
|
170 180
....*....|....*....|....*.
gi 446922839 162 AIARALVNQPKILLMDEPFGALDPHT 187
Cdd:TIGR00956 219 SIAEASLGGAKIQCWDNATRGLDSAT 244
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
32-218 |
8.60e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 59.54 E-value: 8.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 32 KHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLdPYHSGEVLVDG---ECIT--------GPCPERGMVF 100
Cdd:TIGR01271 1226 KYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGvswNSVTlqtwrkafGVIPQKVFIF 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 101 QGytlfpwkTVKENVmfGPQMRGASQMTAEAqAREwiniIGLEKYENQYPHQL-----------SGGMKQRVAIARALVN 169
Cdd:TIGR01271 1305 SG-------TFRKNL--DPYEQWSDEEIWKV-AEE----VGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILS 1370
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446922839 170 QPKILLMDEPFGALDPHTRQKMQKHLMDLWQNidITIIFVTHDMdEAIL 218
Cdd:TIGR01271 1371 KAKILLLDEPSAHLDPVTLQIIRKTLKQSFSN--CTVILSEHRV-EALL 1416
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
56-184 |
1.01e-09 |
|
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: 56.87 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 56 VIGPSGCGKSTLSRVIAG--LDPYHSGEVLVDGECITgPCPER--GMVFQGYTLFPWKTVKENVMFGPQMRGasqmtaea 131
Cdd:cd03232 38 LMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLD-KNFQRstGYVEQQDVHSPNLTVREALRFSALLRG-------- 108
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 446922839 132 qarewiniiglekyenqyphqLSGGMKQRVAIARALVNQPKILLMDEPFGALD 184
Cdd:cd03232 109 ---------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
37-184 |
1.09e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.88 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 37 ERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITGP--CPERGMVFQGYT--LFPWKTVK 112
Cdd:PRK13540 13 DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDlcTYQKQLCFVGHRsgINPYLTLR 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446922839 113 ENVMFGPQMR-GASQMTaeaqarEWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALD 184
Cdd:PRK13540 93 ENCLYDIHFSpGAVGIT------ELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
21-211 |
1.44e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 57.34 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 21 ILEAKQLsqvfKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYH--SGEVLVDGECITGPCPE--- 95
Cdd:CHL00131 7 ILEIKNL----HASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGESILDLEPEera 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 96 -RG--MVFQGYTLFPWKTVKENVMFGPQMRGASQMTAEAQAREWINIIGlEKYE--NQYPHQL--------SGGMKQRVA 162
Cdd:CHL00131 83 hLGifLAFQYPIEIPGVSNADFLRLAYNSKRKFQGLPELDPLEFLEIIN-EKLKlvGMDPSFLsrnvnegfSGGEKKRNE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446922839 163 IARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLwQNIDITIIFVTH 211
Cdd:CHL00131 162 ILQMALLDSELAILDETDSGLDIDALKIIAEGINKL-MTSENSIILITH 209
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
112-226 |
5.36e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 56.28 E-value: 5.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 112 KENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKM 191
Cdd:NF000106 104 RENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEV 183
|
90 100 110
....*....|....*....|....*....|....*
gi 446922839 192 QKHLMDLWQNiDITIIFVTHDMDEAILLADRIVAL 226
Cdd:NF000106 184 WDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVI 217
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
56-227 |
5.49e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 55.66 E-value: 5.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 56 VIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGEcitgpcPERGMVFQGYTLF-------PWK---TVKENVMFGPQ----- 120
Cdd:PRK15056 38 LVGVNGSGKSTLFKALMGFVRLASGKISILGQ------PTRQALQKNLVAYvpqseevDWSfpvLVEDVVMMGRYghmgw 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 121 MRGAS----QMTAEAQARewiniIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLM 196
Cdd:PRK15056 112 LRRAKkrdrQIVTAALAR-----VDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLR 186
|
170 180 190
....*....|....*....|....*....|.
gi 446922839 197 DLwQNIDITIIFVTHDMDEAILLADRIVALK 227
Cdd:PRK15056 187 EL-RDEGKTMLVSTHNLGSVTEFCDYTVMVK 216
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
143-244 |
7.25e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 56.58 E-value: 7.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 143 EKYEN---QYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMdEAILL 219
Cdd:PTZ00265 567 DKYETlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRL-STIRY 645
|
90 100
....*....|....*....|....*
gi 446922839 220 ADRIVALKANPGEIKEIIEVNLPRP 244
Cdd:PTZ00265 646 ANTIFVLSNRERGSTVDVDIIGEDP 670
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
22-229 |
1.70e-08 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 54.48 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 22 LEAKQLSQVFKHGQTerTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLdPYHSGEVLVDG---ECIT-------- 90
Cdd:cd03289 3 MTVKDLTAKYTEGGN--AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGvswNSVPlqkwrkaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 91 GPCPERGMVFQGytlfpwkTVKENVmfGPQMRGASQMTAEAqAREwiniIGLEKYENQYPHQL-----------SGGMKQ 159
Cdd:cd03289 80 GVIPQKVFIFSG-------TFRKNL--DPYGKWSDEEIWKV-AEE----VGLKSVIEQFPGQLdfvlvdggcvlSHGHKQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 160 RVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQniDITIIFVTHDMdEAILLADRIVALKAN 229
Cdd:cd03289 146 LMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFA--DCTVILSEHRI-EAMLECQRFLVIEEN 212
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
145-231 |
2.40e-08 |
|
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: 52.57 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 145 YENQYPhQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHDMDEAILLADRIV 224
Cdd:cd03222 65 YKPQYI-DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIH 143
|
....*..
gi 446922839 225 ALKANPG 231
Cdd:cd03222 144 VFEGEPG 150
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
26-215 |
2.86e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.25 E-value: 2.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 26 QLSQ-VFKHGQTeRTvLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDgecitgpcpergmvFQGYT 104
Cdd:PRK10938 5 QISQgTFRLSDT-KT-LQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQ--------------FSHIT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 105 LFPW----KTVKE------NVMFGPQMRGASQMTAE---------AQAREWINIIGLEKYENQYPHQLSGGMKQRVAIAR 165
Cdd:PRK10938 69 RLSFeqlqKLVSDewqrnnTDMLSPGEDDTGRTTAEiiqdevkdpARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446922839 166 ALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNiDITIIFVTHDMDE 215
Cdd:PRK10938 149 ALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDE 197
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-248 |
3.14e-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: 54.45 E-value: 3.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 20 VILEAKQLSqVFKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDP-YHSGEVLVDGECITGPCPERGm 98
Cdd:TIGR02633 256 VILEARNLT-CWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPVDIRNPAQA- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 99 VFQGYTLFPWKT----------VKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPH------QLSGGMKQRVA 162
Cdd:TIGR02633 334 IRAGIAMVPEDRkrhgivpilgVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASpflpigRLSGGNQQKAV 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 163 IARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNiDITIIFVTHDMDEAILLADRIVALkaNPGEIK-EIIEVNL 241
Cdd:TIGR02633 414 LAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVI--GEGKLKgDFVNHAL 490
|
....*..
gi 446922839 242 PRPRSLE 248
Cdd:TIGR02633 491 TQEQVLA 497
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
10-229 |
3.42e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.13 E-value: 3.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 10 EYFQKIYERPVILEAkqlsqvFKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECI 89
Cdd:PRK15064 310 EQDKKLHRNALEVEN------LTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENAN 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 90 TGPCP-------ERGMvfqgyTLFPW----KTVKENvmfgPQM-RGA------SQMTAEAQARewiniiglekyenqyph 151
Cdd:PRK15064 384 IGYYAqdhaydfENDL-----TLFDWmsqwRQEGDD----EQAvRGTlgrllfSQDDIKKSVK----------------- 437
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446922839 152 QLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLmdlwQNIDITIIFVTHDMDEAILLADRIVALKAN 229
Cdd:PRK15064 438 VLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMAL----EKYEGTLIFVSHDREFVSSLATRIIEITPD 511
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
14-259 |
4.34e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 54.13 E-value: 4.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 14 KIYERPvILEAKQLsqVFKHGQTE-RTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECitgp 92
Cdd:PRK13545 15 KMYNKP-FDKLKDL--FFRSKDGEyHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 93 cperGMVFQGYTLFPWKTVKENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPK 172
Cdd:PRK13545 88 ----ALIAISSGLNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 173 ILLMDEPFGALD-PHTRQKMQKhlMDLWQNIDITIIFVTHDMDEAILLADRIVALKANP----GEIKEIIEVNLPRPRSL 247
Cdd:PRK13545 164 ILVIDEALSVGDqTFTKKCLDK--MNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQvkeyGDIKEVVDHYDEFLKKY 241
|
250
....*....|..
gi 446922839 248 ELMSTPEFKQLR 259
Cdd:PRK13545 242 NQMSVEERKDFR 253
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
41-183 |
5.07e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 53.85 E-value: 5.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 41 LNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECIT--GPCPER----GMVFQGYTLFPWKTVKEN 114
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfnGPKSSQeagiGIIHQELNLIPQLTIAEN 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446922839 115 VMFGPQMRGA------SQMTAEAQ---ARewiniIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGAL 183
Cdd:PRK10762 100 IFLGREFVNRfgridwKKMYAEADkllAR-----LNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDAL 172
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
38-274 |
6.66e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 53.63 E-value: 6.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 38 RTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVdgecitgpcpERGMVF---QgytlfPW---KTV 111
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWA----------ERSIAYvpqQ-----AWimnATV 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 112 KENVMFGPQMRGA--------SQMTAEAQAREWiniiGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGAL 183
Cdd:PTZ00243 738 RGNILFFDEEDAArladavrvSQLEADLAQLGG----GLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSAL 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 184 DPHTRQKMQKHLMdLWQNIDITIIFVTHDMdEAILLADRIVALKAnpGEIKEIIEvnlprprSLELMSTPEFKQLRSRVD 263
Cdd:PTZ00243 814 DAHVGERVVEECF-LGALAGKTRVLATHQV-HVVPRADYVVALGD--GRVEFSGS-------SADFMRTSLYATLAAELK 882
|
250
....*....|.
gi 446922839 264 YLVHAEEDELD 274
Cdd:PTZ00243 883 ENKDSKEGDAD 893
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
32-263 |
1.02e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 52.13 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 32 KHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECitgpcperGMVFQGYTLFPWKTV 111
Cdd:PRK13546 31 KHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEV--------SVIAISAGLSGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 112 KENVMFGPQMRGASQMTAEAQAREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKM 191
Cdd:PRK13546 103 IENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKC 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446922839 192 QKHLMDlWQNIDITIIFVTHDMDEAILLADRIVALKAnpGEIKEIIEVNLPRP------RSLELMSTPEFKQLRSRVD 263
Cdd:PRK13546 183 LDKIYE-FKEQNKTIFFVSHNLGQVRQFCTKIAWIEG--GKLKDYGELDDVLPkyeaflNDFKKKSKAEQKEFRNKLD 257
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
37-188 |
1.35e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 51.03 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 37 ERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDgECITGPCPERGMVFQGYTLfPWK---TVKE 113
Cdd:PRK13541 12 EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYK-NCNINNIAKPYCTYIGHNL-GLKlemTVFE 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446922839 114 NVMFGPQMRGASQMTAEAqarewINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTR 188
Cdd:PRK13541 90 NLKFWSEIYNSAETLYAA-----IHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR 159
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
40-235 |
1.40e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 52.64 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 40 VLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECItGPCPERGMVFQgYTLFPwktvKENVMFGP 119
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNI-AKIGLHDLRFK-ITIIP----QDPVLFSG 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 120 QMR-GASQMTAEAQAREW--INIIGLEKYENQYP----HQ-------LSGGMKQRVAIARALVNQPKILLMDEPFGALDP 185
Cdd:TIGR00957 1375 SLRmNLDPFSQYSDEEVWwaLELAHLKTFVSALPdkldHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDL 1454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446922839 186 HTRQKMQKHLMDlwQNIDITIIFVTHDMDeAILLADRIVALkaNPGEIKE 235
Cdd:TIGR00957 1455 ETDNLIQSTIRT--QFEDCTVLTIAHRLN-TIMDYTRVIVL--DKGEVAE 1499
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
41-227 |
1.69e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.04 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 41 LNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECI----TGPCPERG--MVFQGYTLFPWKTVKEN 114
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfksSKEALENGisMVHQELNLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 115 VMFG--PqMRG----ASQMTAEAQA--REW-INIIGLEKYENqyphqLSGGMKQRVAIARALVNQPKILLMDEPFGALDp 185
Cdd:PRK10982 94 MWLGryP-TKGmfvdQDKMYRDTKAifDELdIDIDPRAKVAT-----LSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLT- 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446922839 186 htrQKMQKHLMDLWQNID---ITIIFVTHDMDEAILLADRIVALK 227
Cdd:PRK10982 167 ---EKEVNHLFTIIRKLKergCGIVYISHKMEEIFQLCDEITILR 208
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
20-234 |
2.18e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.85 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 20 VILEAKQLSqVFKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDP-YHSGEVLVDGECITGPCPERGM 98
Cdd:PRK13549 258 VILEVRNLT-AWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQAI 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 99 VfQG----------YTLFPWKTVKENVMFG--PQMRGASQMTAEAQAREWINIIGLEKYENQYPHQ----LSGGMKQRVA 162
Cdd:PRK13549 337 A-QGiamvpedrkrDGIVPVMGVGKNITLAalDRFTGGSRIDDAAELKTILESIQRLKVKTASPELaiarLSGGNQQKAV 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446922839 163 IARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNiDITIIFVTHDMDEAILLADRIvaLKANPGEIK 234
Cdd:PRK13549 416 LAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRV--LVMHEGKLK 484
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
57-212 |
2.94e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 51.43 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 57 IGPSGCGKSTLSRVIAG-LDPyHSGEVLVD-GECItgpcperGMVFQGYTLFPWKTVKENVMFG---------------- 118
Cdd:PRK15064 33 IGANGCGKSTFMKILGGdLEP-SAGNVSLDpNERL-------GKLRQDQFAFEEFTVLDTVIMGhtelwevkqerdriya 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 119 -PQMRGASQM---------------TAEAQAREWINIIGLEKYENQYP-HQLSGGMKQRVAIARALVNQPKILLMDEPFG 181
Cdd:PRK15064 105 lPEMSEEDGMkvadlevkfaemdgyTAEARAGELLLGVGIPEEQHYGLmSEVAPGWKLRVLLAQALFSNPDILLLDEPTN 184
|
170 180 190
....*....|....*....|....*....|.
gi 446922839 182 ALDPHTrqkmQKHLMDLWQNIDITIIFVTHD 212
Cdd:PRK15064 185 NLDINT----IRWLEDVLNERNSTMIIISHD 211
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
40-251 |
3.20e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.52 E-value: 3.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 40 VLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECIT-----------GPCPERGMVFQGytlfpw 108
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAkfgltdlrrvlSIIPQSPVLFSG------ 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 109 kTVKENVMFGPQMRGASQMTA--EAQAREWI--NIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALD 184
Cdd:PLN03232 1325 -TVRFNIDPFSEHNDADLWEAleRAHIKDVIdrNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVD 1403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446922839 185 PHTRQKMQKHLMDLWQNidITIIFVTHDMDeAILLADRIVALKANpgeikEIIEVNLPRprslELMS 251
Cdd:PLN03232 1404 VRTDSLIQRTIREEFKS--CTMLVIAHRLN-TIIDCDKILVLSSG-----QVLEYDSPQ----ELLS 1458
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
41-232 |
3.64e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 49.24 E-value: 3.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 41 LNKLDLKIHKREFICVIGPSGCGKSTLsrVIAGLdpYHSGevlvdgecitgpcpeRGMVFQGYTLFPwktvKENVMFGPQ 120
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGL--YASG---------------KARLISFLPKFS----RNKLIFIDQ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 121 MRGASQMTaeaqarewINIIGLekyeNQYPHQLSGGMKQRVAIARALVNQPK--ILLMDEPFGALDPHTRQKMQKHLMDL 198
Cdd:cd03238 68 LQFLIDVG--------LGYLTL----GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGL 135
|
170 180 190
....*....|....*....|....*....|....
gi 446922839 199 WQNiDITIIFVTHDmDEAILLADRIVALKANPGE 232
Cdd:cd03238 136 IDL-GNTVILIEHN-LDVLSSADWIIDFGPGSGK 167
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
153-240 |
3.98e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.88 E-value: 3.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 153 LSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNiDITIIFVTHDMDEAILLADRIVALkaNPGE 232
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVM--SNGL 468
|
....*...
gi 446922839 233 IKEIIEVN 240
Cdd:PRK10982 469 VAGIVDTK 476
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
133-231 |
4.33e-07 |
|
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: 50.94 E-value: 4.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 133 AREWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLwQNIDITIIFVTHD 212
Cdd:COG1245 193 LDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIREL-AEEGKYVLVVEHD 271
|
90 100
....*....|....*....|.
gi 446922839 213 MdeAIL--LADRIVALKANPG 231
Cdd:COG1245 272 L--AILdyLADYVHILYGEPG 290
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
56-231 |
5.19e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 49.67 E-value: 5.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 56 VIGPSGCGKSTLSRVIAG------------------LDPYHSGEV------LVDGE--CITGPcpergmvfQGYTLFPwK 109
Cdd:cd03236 31 LVGPNGIGKSTALKILAGklkpnlgkfddppdwdeiLDEFRGSELqnyftkLLEGDvkVIVKP--------QYVDLIP-K 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 110 TVKENVmfgpqmrgaSQMTAEAQAR----EWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDP 185
Cdd:cd03236 102 AVKGKV---------GELLKKKDERgkldELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446922839 186 HTRQKMQKHLMDLWQNiDITIIFVTHDMdeAIL--LADRIVALKANPG 231
Cdd:cd03236 173 KQRLNAARLIRELAED-DNYVLVVEHDL--AVLdyLSDYIHCLYGEPG 217
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
151-229 |
1.26e-06 |
|
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: 47.35 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 151 HQLSGGMKQRVAIARALVNQPK----ILLMDEPFGALDPHTRQKMQKHLMDLWQNiDITIIFVTHDmDEAILLADRIVAL 226
Cdd:cd03227 76 LQLSGGEKELSALALILALASLkprpLYILDEIDRGLDPRDGQALAEAILEHLVK-GAQVIVITHL-PELAELADKLIHI 153
|
...
gi 446922839 227 KAN 229
Cdd:cd03227 154 KKV 156
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
20-187 |
2.55e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.58 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 20 VILEAKQLSQVFKhgqtERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVdgecitGPCPERGMV 99
Cdd:PRK11819 323 KVIEAENLSKSFG----DRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI------GETVKLAYV 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 100 FQGY-TLFPWKTVKENVmfgpqMRGASQMT---AEAQAREWINIIGLEKYENQYP-HQLSGGMKQRVAIARALVNQPKIL 174
Cdd:PRK11819 393 DQSRdALDPNKTVWEEI-----SGGLDIIKvgnREIPSRAYVGRFNFKGGDQQKKvGVLSGGERNRLHLAKTLKQGGNVL 467
|
170
....*....|...
gi 446922839 175 LMDEPFGALDPHT 187
Cdd:PRK11819 468 LLDEPTNDLDVET 480
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
134-231 |
3.94e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.88 E-value: 3.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 134 REWINIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDLWQNidITIIFVTHDM 213
Cdd:PRK13409 194 DEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEG--KYVLVVEHDL 271
|
90 100
....*....|....*....|
gi 446922839 214 deAIL--LADRIVALKANPG 231
Cdd:PRK13409 272 --AVLdyLADNVHIAYGEPG 289
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
153-232 |
5.34e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 46.48 E-value: 5.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 153 LSGGMKQRVAIARALVNQPK--ILLMDEPFGALDPHTRQKMQKHLMDLwQNIDITIIFVTHDmDEAILLADRIVALKANP 230
Cdd:cd03270 138 LSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHD-EDTIRAADHVIDIGPGA 215
|
..
gi 446922839 231 GE 232
Cdd:cd03270 216 GV 217
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
34-212 |
6.27e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.47 E-value: 6.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 34 GQTERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAG-LDPYhSGEVLVDGECITGPCPERGMVFQGYTLFPWKTVk 112
Cdd:PRK10636 321 GYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGeLAPV-SGEIGLAKGIKLGYFAQHQLEFLRADESPLQHL- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 113 envmfgpqMRGASQMTaEAQAREWINIIGLEKYENQYP-HQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKM 191
Cdd:PRK10636 399 --------ARLAPQEL-EQKLRDYLGGFGFQGDKVTEEtRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQAL 469
|
170 180
....*....|....*....|.
gi 446922839 192 QKHLMDLwqniDITIIFVTHD 212
Cdd:PRK10636 470 TEALIDF----EGALVVVSHD 486
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
152-211 |
6.56e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.55 E-value: 6.56e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 152 QLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDlWQNidiTIIFVTH 211
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLK-WPK---TFIVVSH 399
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
2-227 |
6.81e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.41 E-value: 6.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 2 NDSTFNAHEYFQKIYERPVILEAKQLSQVFKHGQTERTVLNKLDLKIHKREFICVIGPSGCGKSTL-----SRVIAGLdp 76
Cdd:TIGR00956 740 DESDDVNDEKDMEKESGEDIFHWRNLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLlnvlaERVTTGV-- 817
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 77 YHSGEVLVDGecitgpcPERGMVFQ---GYTL-----FPWKTVKENVMFGPQMRGASQMTAEAQAR---EWINIIGLEKY 145
Cdd:TIGR00956 818 ITGGDRLVNG-------RPLDSSFQrsiGYVQqqdlhLPTSTVRESLRFSAYLRQPKSVSKSEKMEyveEVIKLLEMESY 890
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 146 ENQY---PHQ-LSGGMKQRVAIARALVNQPKILL-MDEPFGALDPHTR----QKMQKhLMDLWQNIDITIifvtHDmDEA 216
Cdd:TIGR00956 891 ADAVvgvPGEgLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAwsicKLMRK-LADHGQAILCTI----HQ-PSA 964
|
250
....*....|...
gi 446922839 217 ILLA--DRIVALK 227
Cdd:TIGR00956 965 ILFEefDRLLLLQ 977
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
56-184 |
8.30e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.15 E-value: 8.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 56 VIGPSGCGKSTLSRVIAGLDP--YHSGEVLVDG--------ECITGPCPergmvfQGYTLFPWKTVKENVMFGPQMRGAS 125
Cdd:PLN03140 911 LMGVSGAGKTTLMDVLAGRKTggYIEGDIRISGfpkkqetfARISGYCE------QNDIHSPQVTVRESLIYSAFLRLPK 984
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446922839 126 QMTAEAQAR---EWINIIGLEKYENQ---YP--HQLSGGMKQRVAIARALVNQPKILLMDEPFGALD 184
Cdd:PLN03140 985 EVSKEEKMMfvdEVMELVELDNLKDAivgLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
54-212 |
9.88e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.78 E-value: 9.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 54 ICVIGPSGCGKSTLSRVIAG-LDPYhSGEVLVDGECitgpcpeRGMVFQGYTLFPWKTVKENVMFgpqMRGASQMTAEAQ 132
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGeLQPS-SGTVFRSAKV-------RMAVFSQHHVDGLDLSSNPLLY---MMRCFPGVPEQK 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 133 AREWINIIGLE-KYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMdLWQNidiTIIFVTH 211
Cdd:PLN03073 607 LRAHLGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLV-LFQG---GVLMVSH 682
|
.
gi 446922839 212 D 212
Cdd:PLN03073 683 D 683
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
40-254 |
2.01e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.88 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 40 VLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECIT-----------GPCPERGMVFQGytlfpw 108
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISkfglmdlrkvlGIIPQAPVLFSG------ 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 109 kTVKENVMFGPQMRGASQMTA--EAQAREWI--NIIGLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALD 184
Cdd:PLN03130 1328 -TVRFNLDPFNEHNDADLWESleRAHLKDVIrrNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVD 1406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 185 PHTRQKMQKHLMDLWQNIDITIIfvTHDMDeAILLADRIVALKAnpGEIKEiievnlprprslelMSTPE 254
Cdd:PLN03130 1407 VRTDALIQKTIREEFKSCTMLII--AHRLN-TIIDCDRILVLDA--GRVVE--------------FDTPE 1457
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
37-95 |
4.81e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 44.01 E-value: 4.81e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446922839 37 ERTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYH--SGEVLVDGECITGPCPE 95
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvtGGTVEFKGKDLLELSPE 73
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
38-227 |
5.37e-05 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 43.74 E-value: 5.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 38 RTVLNKLDLKIHKREFICVIGPSGCGKSTLSRVIAGLDPYHSGEVLVDGECITG-PC----PERGMVFQGYTLFPwKTVK 112
Cdd:cd03288 34 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKlPLhtlrSRLSIILQDPILFS-GSIR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 113 ENVmfGPQMRGASQMTAEA----QAREWINII--GLEKYENQYPHQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPH 186
Cdd:cd03288 113 FNL--DPECKCTDDRLWEAleiaQLKNMVKSLpgGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMA 190
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446922839 187 TRQKMQKHLMDLWQniDITIIFVTHDMdEAILLADRIVALK 227
Cdd:cd03288 191 TENILQKVVMTAFA--DRTVVTIAHRV-STILDADLVLVLS 228
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
153-224 |
1.13e-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: 40.38 E-value: 1.13e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446922839 153 LSGGMKQRVAIAR----ALVNQpkILLMDEPFGALDPHTRQKMQKHLMDLwQNIDITIIFVTHDmDEAILLADRIV 224
Cdd:TIGR00630 489 LSGGEAQRIRLATqigsGLTGV--LYVLDEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHD-EDTIRAADYVI 560
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
150-212 |
1.99e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 38.45 E-value: 1.99e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446922839 150 PHQLSGGMKQRVAIARALVnqpkiLLMDepFGALDPHTRQKMQKHLMDLwqniditiIFVTHD 212
Cdd:COG0419 156 IETLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEEL--------AIITHV 203
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
128-224 |
2.47e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 39.38 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 128 TAEAQAREWINIIGLEKYENQYP-HQLSGGMKQRVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLmdlwQNIDITI 206
Cdd:PRK10636 124 TIRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWL----KSYQGTL 199
|
90
....*....|....*...
gi 446922839 207 IFVTHDMDEAILLADRIV 224
Cdd:PRK10636 200 ILISHDRDFLDPIVDKII 217
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
150-228 |
2.48e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446922839 150 PHQLSGGMK-Q-----RVAIARALVNQPKILLMDEPFGALDPHTRQKMQKHLMDL---WQniditIIFVTHDMDEAILLA 220
Cdd:COG4717 556 VEELSRGTReQlylalRLALAELLAGEPLPLILDDAFVNFDDERLRAALELLAELakgRQ-----VIYFTCHEELVELFQ 630
|
90
....*....|.
gi 446922839 221 D---RIVALKA 228
Cdd:COG4717 631 EegaHVIELES 641
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
143-212 |
3.92e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 38.14 E-value: 3.92e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446922839 143 EKYENQYPHQLSGGMKQ---RVAIARALVNQPKILLMDEPFGALDPhtrqKMQKHLMDLWQNI---DITIIFVTHD 212
Cdd:pfam13304 227 GGGGELPAFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHP----KLLRRLLELLKELsrnGAQLILTTHS 298
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
151-222 |
4.68e-03 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 38.10 E-value: 4.68e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446922839 151 HQLSGGMKQRVAIARALVN---QPKILLMDEPFGALDPHTRQKMQKHLMDLWQNIDITIIFVTHD---MDEAILLADR 222
Cdd:COG1106 201 SEESDGTKRLLALAGALLDalaKGGVLLIDEIEASLHPSLLRKLLKLFLDLANKNNAQLIFTTHStelLDAFLELLRR 278
|
|
| |
