|
Name |
Accession |
Description |
Interval |
E-value |
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-237 |
9.80e-89 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 271.12 E-value: 9.80e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDALALGITA 80
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAGIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 81 VYQDLALVDQRNVIHNISLGNIPTKWGglVVDRKKMRETAENALSYMKAKLpSLDIPVSSMSGGQRQAVAIARACASGGQ 160
Cdd:COG1129 84 IHQELNLVPNLSVAENIFLGREPRRGG--LIDWRAMRRRARELLARLGLDI-DPDTPVGDLSVAQQQLVEIARALSRDAR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499272610 161 LVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAEVERNAVSHDEVVRLIL 237
Cdd:COG1129 161 VLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLMV 237
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-221 |
4.73e-72 |
|
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: 217.30 E-value: 4.73e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDALALGITAV 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 82 YQdlalvdqrnvihnislgniptkwgglvvdrkkmretaenalsymkaklpsldipvssMSGGQRQAVAIARACASGGQL 161
Cdd:cd03216 81 YQ---------------------------------------------------------LSVGERQMVEIARALARNARL 103
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 162 VIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAE 221
Cdd:cd03216 104 LILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-235 |
1.36e-66 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 214.12 E-value: 1.36e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDALALGITA 80
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALGIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 81 VYQDLALVDQRNVIHNISLGNIPTKwgGLVVDRKKMRETAEnALSymkAKLP---SLDIPVSSMSGGQRQAVAIARACAS 157
Cdd:COG3845 85 VHQHFMLVPNLTVAENIVLGLEPTK--GGRLDRKAARARIR-ELS---ERYGldvDPDAKVEDLSVGEQQRVEILKALYR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499272610 158 GGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAEVERNAVSHDEVVRL 235
Cdd:COG3845 159 GARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELAEL 236
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-234 |
6.61e-58 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 191.66 E-value: 6.61e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDALALGITAV 81
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGVAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 82 YQDLALVDQRNVIHNISLGNIPTKWGglVVDRKKMRETAENALSYMKAKLpSLDIPVSSMSGGQRQAVAIARACASGGQL 161
Cdd:PRK11288 85 YQELHLVPEMTVAENLYLGQLPHKGG--IVNRRLLNYEAREQLEHLGVDI-DPDTPLKYLSIGQRQMVEIAKALARNARV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499272610 162 VIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAEVERNA-VSHDEVVR 234
Cdd:PRK11288 162 IAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATFDDMAqVDRDQLVQ 235
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-221 |
7.09e-57 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 181.42 E-value: 7.09e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHmDSARDALALgITAV 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA-RDPAEVRRR-IGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 82 YQDLALVDQRNVIHNISLgniptkWGGLV-VDRKKMRETAENALSYMkaKL-PSLDIPVSSMSGGQRQAVAIARACASGG 159
Cdd:COG1131 79 PQEPALYPDLTVRENLRF------FARLYgLPRKEARERIDELLELF--GLtDAADRKVGTLSGGMKQRLGLALALLHDP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499272610 160 QLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAE 221
Cdd:COG1131 151 ELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVAD 212
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-235 |
8.52e-53 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 178.20 E-value: 8.52e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYkPT---QGSVWVNGKQVHMDSARDALALG 77
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIRDTERAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 78 ITAVYQDLALVDQRNVIHNISLGNIPTKWGglVVDRKKMRETAENALSYMKaklpsLDI----PVSSMSGGQRQAVAIAR 153
Cdd:PRK13549 84 IAIIHQELALVKELSVLENIFLGNEITPGG--IMDYDAMYLRAQKLLAQLK-----LDInpatPVGNLGLGQQQLVEIAK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 154 ACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAEVERNAVSHDEVV 233
Cdd:PRK13549 157 ALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDII 236
|
..
gi 499272610 234 RL 235
Cdd:PRK13549 237 TM 238
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-233 |
5.43e-52 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 168.77 E-value: 5.43e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDALALGITAV 81
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 82 YQDLALVDQRNVIHNISLGNIPTKWGGLVVDR-----KKMRETAENALSYMkaKLPSL-DIPVSSMSGGQRQAVAIARAC 155
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQARTGSGLLLARarreeREARERAEELLERV--GLADLaDRPAGELSYGQQRRLEIARAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499272610 156 ASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAEVERNAVSHDEVV 233
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPRV 236
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-237 |
1.39e-51 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 175.36 E-value: 1.39e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDALALGITA 80
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 81 VYQDLALVDQRNVIHNISLGNIPTK--WGGLVVDRKKMRETAENALSYMKAKLpSLDIPVSSMSGGQRQAVAIARACASG 158
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIGRHLTKkvCGVNIIDWREMRVRAAMMLLRVGLKV-DLDEKVANLSISHKQMLEIAKTLMLD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499272610 159 GQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAEVERNAVSHDEVVRLIL 237
Cdd:PRK09700 164 AKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVRLMV 242
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-221 |
2.83e-49 |
|
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: 162.52 E-value: 2.83e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDaLALGITA 80
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRE-LARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 81 VYQDLALVDQRNVIHNISLGNIPTKwGGLVVDRKKMRETAENALSYMK-AKLpsLDIPVSSMSGGQRQAVAIARACASGG 159
Cdd:COG1120 80 VPQEPPAPFGLTVRELVALGRYPHL-GLFGRPSAEDREAVEEALERTGlEHL--ADRPVDELSGGERQRVLIARALAQEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499272610 160 QLVIMDEPTAALGIREQRMVLDVVHDL-RAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAE 221
Cdd:COG1120 157 PLLLLDEPTSHLDLAHQLEVLELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQ 219
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-234 |
3.45e-49 |
|
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: 162.13 E-value: 3.45e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDALALGITA 80
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLGIAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 81 VYQDLALVDQRNVIHNISLG----------NIPTKWGGLVVDRKKMRETAENALSYMK-AKLpsLDIPVSSMSGGQRQAV 149
Cdd:COG0411 84 TFQNPRLFPELTVLENVLVAaharlgrgllAALLRLPRARREEREARERAEELLERVGlADR--ADEPAGNLSYGQQRRL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 150 AIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRA-HGTSVLIISHNLDHVFEVADDLLILRGGRVVAEVERNAVS 228
Cdd:COG0411 162 EIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDeRGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVR 241
|
....*.
gi 499272610 229 HDEVVR 234
Cdd:COG0411 242 ADPRVI 247
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6-237 |
1.10e-48 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 167.21 E-value: 1.10e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 6 NLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDALALGITAVYQDL 85
Cdd:PRK10982 3 NISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 86 ALVDQRNVIHNISLGNIPTKwgGLVVDRKKM-RETaenalsymKAKLPSLDI------PVSSMSGGQRQAVAIARACASG 158
Cdd:PRK10982 83 NLVLQRSVMDNMWLGRYPTK--GMFVDQDKMyRDT--------KAIFDELDIdidpraKVATLSVSQMQMIEIAKAFSYN 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499272610 159 GQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAEVERNAVSHDEVVRLIL 237
Cdd:PRK10982 153 AKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMV 231
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-221 |
1.75e-48 |
|
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: 159.42 E-value: 1.75e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRF-GHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDalalgita 80
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRE-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 81 VYQDLALV-----DQ---RNVIHNISLGniPTKWGglvVDRKKMRETAENALSYMK-AKLpsLDIPVSSMSGGQRQAVAI 151
Cdd:COG1122 73 LRRKVGLVfqnpdDQlfaPTVEEDVAFG--PENLG---LPREEIRERVEEALELVGlEHL--ADRPPHELSGGQKQRVAI 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 152 ARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAE 221
Cdd:COG1122 146 AGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVAD 215
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-218 |
7.62e-48 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 156.02 E-value: 7.62e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHmdSARDALALGITAV 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK--KEPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 82 YQDLALVDQRNVIHNISLgniptkwgglvvdrkkmretaenalsymkaklpsldipvssmSGGQRQAVAIARACASGGQL 161
Cdd:cd03230 79 PEEPSLYENLTVRENLKL------------------------------------------SGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499272610 162 VIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRV 218
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-221 |
9.47e-48 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 158.10 E-value: 9.47e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDALALGIta 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 81 VYQDLALVDQRNVIHNIS-LGNIptkWGglvVDRKKMRETAENALSymKAKLPS-LDIPVSSMSGGQRQAVAIARACASG 158
Cdd:COG4555 79 LPDERGLYDRLTVRENIRyFAEL---YG---LFDEELKKRIEELIE--LLGLEEfLDRRVGELSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499272610 159 GQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAE 221
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQ 213
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-236 |
2.24e-47 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 163.64 E-value: 2.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDALALGITA 80
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGIGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 81 VYQDLALVDQRNVIHNISLGNIPT-KWGGlvVDRKKMRETAENALSYMKAKLPSlDIPVSSMSGGQRQAVAIARACASGG 159
Cdd:PRK10762 84 IHQELNLIPQLTIAENIFLGREFVnRFGR--IDWKKMYAEADKLLARLNLRFSS-DKLVGELSIGEQQMVEIAKVLSFES 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499272610 160 QLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAEVERNAVSHDevvRLI 236
Cdd:PRK10762 161 KVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTED---SLI 234
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-235 |
3.88e-46 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 154.06 E-value: 3.88e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRF-GHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDALAL--G 77
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrrR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 78 ITAVYQDLALVDQRNVIHNI---SLGNIPTKWGGLVVDRKKMRETAENALSY--MKAKLpslDIPVSSMSGGQRQAVAIA 152
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVlagRLGRTSTWRSLLGLFPPEDRERALEALERvgLADKA---YQRADQLSGGQQQRVAIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 153 RACASGGQLVIMDEPTAALGIREQRMVLDVVHDL-RAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAEVERNAVSHDE 231
Cdd:COG3638 159 RALVQEPKLILADEPVASLDPKTARQVMDLLRRIaREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAELTDAV 238
|
....
gi 499272610 232 VVRL 235
Cdd:COG3638 239 LREI 242
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-227 |
2.15e-45 |
|
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: 158.91 E-value: 2.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRF-----GHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDALA 75
Cdd:COG1123 260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 76 LG--ITAVYQD--LALVDQRNVIHNISLGniPTKWGGLvvDRKKMRETAENALSymKAKLPS--LDIPVSSMSGGQRQAV 149
Cdd:COG1123 340 LRrrVQMVFQDpySSLNPRMTVGDIIAEP--LRLHGLL--SRAERRERVAELLE--RVGLPPdlADRYPHELSGGQRQRV 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499272610 150 AIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRA-HGTSVLIISHNLDHVFEVADDLLILRGGRVVAEVERNAV 227
Cdd:COG1123 414 AIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQReLGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEV 492
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-242 |
3.42e-45 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 157.87 E-value: 3.42e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRfghvTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDALALGIta 80
Cdd:COG1129 256 VLEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAGI-- 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 81 VY-----QDLALVDQRNVIHNISLGNIPTKWGGLVVDRKKMRETAENALSYMKAKLPSLDIPVSSMSGGQRQAVAIARAC 155
Cdd:COG1129 330 AYvpedrKGEGLVLDLSIRENITLASLDRLSRGGLLDRRRERALAEEYIKRLRIKTPSPEQPVGNLSGGNQQKVVLAKWL 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 156 ASGGQLVIMDEPTAalGI-----REqrmVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAEVERNAVSHD 230
Cdd:COG1129 410 ATDPKVLILDEPTR--GIdvgakAE---IYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGELDREEATEE 484
|
250
....*....|..
gi 499272610 231 EVVRLILAGQPR 242
Cdd:COG1129 485 AIMAAATGGAAA 496
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-218 |
3.08e-44 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 149.08 E-value: 3.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARdalalgita 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR--------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 81 vyqdLALVDQRNVIHN---------ISLGNIPTK--WGGLvvdRKKMRETAENALSYMKAkLPSLDIPVSSMSGGQRQAV 149
Cdd:COG1121 77 ----IGYVPQRAEVDWdfpitvrdvVLMGRYGRRglFRRP---SRADREAVDEALERVGL-EDLADRPIGELSGGQQQRV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499272610 150 AIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRV 218
Cdd:COG1121 149 LLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-237 |
4.19e-44 |
|
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: 154.98 E-value: 4.19e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYK--PTQGSVWVNGKQVHMDSARDALALGI 78
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 79 TAVYQDLALVDQRNVIHNISLGNIPTKWGGLVvDRKKMRETAENALSYMKAKLPSLDIPVSSMSGGQRQAVAIARACASG 158
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEITLPGGRM-AYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499272610 159 GQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAEVERNAVSHDEVVRLIL 237
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMV 238
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-221 |
9.98e-44 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 145.66 E-value: 9.98e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 3 RVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDaLALGITAVY 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKE-LARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 83 QDLALVDqrnvihnislgniptkwgglvvdrkkmretaenaLSYMKAKlpsldiPVSSMSGGQRQAVAIARACASGGQLV 162
Cdd:cd03214 80 QALELLG----------------------------------LAHLADR------PFNELSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 163 IMDEPTAALGIREQRMVLDVVHDL-RAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAE 221
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRLaRERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-223 |
1.72e-43 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 146.73 E-value: 1.72e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFG----HVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHM--DSARDAL 74
Cdd:COG1136 4 LLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlsERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 75 ---ALGItaVYQDLALVDQRNVIHNISLgniPTKWGGlvVDRKKMRETAENALSYM-----KAKLPSldipvsSMSGGQR 146
Cdd:COG1136 84 rrrHIGF--VFQFFNLLPELTALENVAL---PLLLAG--VSRKERRERARELLERVglgdrLDHRPS------QLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499272610 147 QAVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDL-RAHGTSVLIISHNLDhVFEVADDLLILRGGRVVAEVE 223
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnRELGTTIVMVTHDPE-LAARADRVIRLRDGRIVSDER 227
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1-234 |
3.04e-43 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 152.64 E-value: 3.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYkPT---QGSVWVNGKQVHMDSARDALALG 77
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEVCRFKDIRDSEALG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 78 ITAVYQDLALVDQRNVIHNISLGNIPTKWGglVVDRKKMRETAENALSymKAKLP-SLDIPVSSMSGGQRQAVAIARACA 156
Cdd:NF040905 80 IVIIHQELALIPYLSIAENIFLGNERAKRG--VIDWNETNRRARELLA--KVGLDeSPDTLVTDIGVGKQQLVEIAKALS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 157 SGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVA--EVERNAVSHDEVVR 234
Cdd:NF040905 156 KDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIEtlDCRADEVTEDRIIR 235
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-220 |
5.67e-42 |
|
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: 142.29 E-value: 5.67e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 3 RVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARdalalgitavy 82
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 83 qdLALVDQR---------NVIHNISLGNIPtKWGGLVVDRKKMRETAENALSY--MKAKLpslDIPVSSMSGGQRQAVAI 151
Cdd:cd03235 70 --IGYVPQRrsidrdfpiSVRDVVLMGLYG-HKGLFRRLSKADKAKVDEALERvgLSELA---DRQIGELSGGQQQRVLL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499272610 152 ARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILrGGRVVA 220
Cdd:cd03235 144 ARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL-NRTVVA 211
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-220 |
5.72e-42 |
|
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: 142.27 E-value: 5.72e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQV-HMDSARDALALgita 80
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVtGVPPERRNIGM---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 81 VYQDLALVDQRNVIHNISLgniptkwgGLVVDRKKMRETAENALSYMKA--KLPSLDIPVSSMSGGQRQAVAIARACASG 158
Cdd:cd03259 77 VFQDYALFPHLTVAENIAF--------GLKLRGVPKAEIRARVRELLELvgLEGLLNRYPHELSGGQQQRVALARALARE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499272610 159 GQLVIMDEPTAAL--GIREqRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVA 220
Cdd:cd03259 149 PSLLLLDEPLSALdaKLRE-ELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQ 211
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-234 |
7.49e-42 |
|
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: 142.81 E-value: 7.49e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDALALGITA 80
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 81 VYQDlalvdqRNVIH------NISLGniptkwGGLVVDRKKMRETAENALSYmkakLPSL----DIPVSSMSGGQRQAVA 150
Cdd:COG0410 83 VPEG------RRIFPsltveeNLLLG------AYARRDRAEVRADLERVYEL----FPRLkerrRQRAGTLSGGEQQMLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 151 IARACASGGQLVIMDEPTAALG--IREQrmVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAEVERNAVS 228
Cdd:COG0410 147 IGRALMSRPKLLLLDEPSLGLAplIVEE--IFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELL 224
|
....*.
gi 499272610 229 HDEVVR 234
Cdd:COG0410 225 ADPEVR 230
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-221 |
1.10e-41 |
|
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: 142.26 E-value: 1.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRF----GHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDALAL 76
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 77 G--ITAVYQD--LALVDQRNVIHNIslgniptkWGGLVVDRKKMRETAENALSYMKAKLPSLDIPVSS-----MSGGQRQ 147
Cdd:cd03257 81 RkeIQMVFQDpmSSLNPRMTIGEQI--------AEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNrypheLSGGQRQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499272610 148 AVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRA-HGTSVLIISHNLDHVFEVADDLLILRGGRVVAE 221
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEeLGLTLLFITHDLGVVAKIADRVAVMYAGKIVEE 227
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-230 |
1.38e-41 |
|
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: 141.80 E-value: 1.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDALALGITAV 81
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 82 YQDLALVDQRNVIHNISLgniptkwGGLVVDRKKMRETAENALSYMKAKLPSLDIPVSSMSGGQRQAVAIARACASGGQL 161
Cdd:cd03224 81 PEGRRIFPELTVEENLLL-------GAYARRRAKRKARLERVYELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499272610 162 VIMDEPTAAL--GIREQrmVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAEVERNAVSHD 230
Cdd:cd03224 154 LLLDEPSEGLapKIVEE--IFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-218 |
7.89e-41 |
|
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: 139.55 E-value: 7.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFG----HVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVH--MDSARDAL- 74
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISklSEKELAAFr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 75 --ALGItaVYQDLALVDQRNVIHNISLGNIPTKwgglvVDRKKMRETAENALSYMKakLP-SLDIPVSSMSGGQRQAVAI 151
Cdd:cd03255 81 rrHIGF--VFQSFNLLPDLTALENVELPLLLAG-----VPKKERRERAEELLERVG--LGdRLNHYPSELSGGQQQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499272610 152 ARACASGGQLVIMDEPTAALGIREQRMVLDVVHDL-RAHGTSVLIISHNLDhVFEVADDLLILRGGRV 218
Cdd:cd03255 152 ARALANDPKIILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHDPE-LAEYADRIIELRDGKI 218
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-217 |
1.12e-40 |
|
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: 139.14 E-value: 1.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 3 RVQNLTKRFGHVT--AISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDaLALGITA 80
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKE-LRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 81 VYQDLAlvDQ---RNVIHNISLGniPTKWGglvVDRKKMRETAENALSYMKakLPSL-DIPVSSMSGGQRQAVAIARACA 156
Cdd:cd03225 80 VFQNPD--DQffgPTVEEEVAFG--LENLG---LPEEEIEERVEEALELVG--LEGLrDRSPFTLSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499272610 157 SGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGR 217
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-234 |
1.24e-40 |
|
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: 139.73 E-value: 1.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHM--DSARDALALGI 78
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGlsEKELYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 79 TAVYQDLALVDQRNVIHNISL-----GNIPtkwgglvvdRKKMRETAENALSY-----MKAKLPsldipvSSMSGGQRQA 148
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVAFplrehTDLS---------EAEIRELVLEKLELvglpgAADKMP------SELSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 149 VAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLR-AHGTSVLIISHNLDHVFEVADDLLILRGGRVVAEVERNAV 227
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRdELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL 229
|
....*....
gi 499272610 228 --SHDEVVR 234
Cdd:COG1127 230 laSDDPWVR 238
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-223 |
2.02e-40 |
|
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: 138.76 E-value: 2.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGH----VTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARdalalg 77
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 78 ITAVYQDLALVDQRNVIHNISLgniptkwgGLVVDRKKMRETAENALSYMKA--------KLPsldipvSSMSGGQRQAV 149
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVAL--------GLELQGVPKAEARERAEELLELvglsgfenAYP------HQLSGGMRQRV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 150 AIARACASGGQLVIMDEPTAAL--GIRE--QRMVLDVVHDlraHGTSVLIISHNLDHVFEVADDLLIL--RGGRVVAEVE 223
Cdd:cd03293 141 ALARALAVDPDVLLLDEPFSALdaLTREqlQEELLDIWRE---TGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAEVE 217
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-220 |
7.46e-40 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 137.03 E-value: 7.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHmDSARDALAL----- 76
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD-IAARNRIGYlpeer 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 77 GItavYQDLALVDQrnVIHNISLGNIptkwgglvvdrkKMRETAENALSYMKaKL---PSLDIPVSSMSGGQRQAVAIAR 153
Cdd:cd03269 80 GL---YPKMKVIDQ--LVYLAQLKGL------------KKEEARRRIDEWLE-RLelsEYANKRVEELSKGNQQKVQFIA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499272610 154 ACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVA 220
Cdd:cd03269 142 AVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVL 208
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-217 |
1.37e-39 |
|
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: 135.01 E-value: 1.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVH-MDSARDALALGITA 80
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 81 VYQDLALVDQRNVIHNISLGniptkwgglvvdrkkmretaenalsymkaklpsldipvssMSGGQRQAVAIARACASGGQ 160
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG----------------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499272610 161 LVIMDEPTAALGIREQRMVLDVVHDLRA-HGTSVLIISHNLDHVFEVADDLLILRGGR 217
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAqLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-223 |
2.93e-39 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 136.76 E-value: 2.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRF----GHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARdalal 76
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 77 gITAVYQDLALVDQRNVIHNISLGnipTKWGGlvVDRKKMRETAENALSYM-----KAKLPSldipvsSMSGGQRQAVAI 151
Cdd:COG1116 82 -RGVVFQEPALLPWLTVLDNVALG---LELRG--VPKAERRERARELLELVglagfEDAYPH------QLSGGMRQRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499272610 152 ARACASGGQLVIMDEPTAAL--GIRE--QRMVLDVvhdLRAHGTSVLIISHNLDHVFEVADDLLIL--RGGRVVAEVE 223
Cdd:COG1116 150 ARALANDPEVLLMDEPFGALdaLTRErlQDELLRL---WQETGKTVLFVTHDVDEAVFLADRVVVLsaRPGRIVEEID 224
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-198 |
9.91e-39 |
|
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: 133.76 E-value: 9.91e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHmdSARDALALGITA 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIR--DAREDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 81 VYQDLALVDQRNVIHNISLGnipTKWGGLVVDrkkmRETAENALSYMkaKLPSL-DIPVSSMSGGQRQAVAIARACASGG 159
Cdd:COG4133 80 LGHADGLKPELTVRENLRFW---AALYGLRAD----REAIDEALEAV--GLAGLaDLPVRQLSAGQKRRVALARLLLSPA 150
|
170 180 190
....*....|....*....|....*....|....*....
gi 499272610 160 QLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISH 198
Cdd:COG4133 151 PLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-217 |
1.35e-38 |
|
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: 131.98 E-value: 1.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 3 RVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHmdsardalalgitavy 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 83 qdlalvdqrnvihnislgniptkwgglvvdrKKMRETAENALSYmkaklpsldipVSSMSGGQRQAVAIARACASGGQLV 162
Cdd:cd00267 65 -------------------------------KLPLEELRRRIGY-----------VPQLSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499272610 163 IMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGR 217
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-220 |
4.36e-38 |
|
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: 132.63 E-value: 4.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFG--HVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDsardalalgIT 79
Cdd:cd03263 1 LQIRNLTKTYKkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTD---------RK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 80 AVYQDLALVDQRNVIhnislgniptkWGGLVV-------------DRKKMRETAENALSYMKAKlPSLDIPVSSMSGGQR 146
Cdd:cd03263 72 AARQSLGYCPQFDAL-----------FDELTVrehlrfyarlkglPKSEIKEEVELLLRVLGLT-DKANKRARTLSGGMK 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499272610 147 QAVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRaHGTSVLIISHNLDHVFEVADDLLILRGGRVVA 220
Cdd:cd03263 140 RKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKLRC 212
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-235 |
4.89e-38 |
|
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: 133.08 E-value: 4.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGH-VTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDALAL--GI 78
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrrQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 79 TAVYQDLALVDQRNVIHNI---SLGNIPTKWGGLvvdRKKMRETAENALSYMKAK--LPSLDIPVSSMSGGQRQAVAIAR 153
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVlsgRLGRRSTWRSLF---GLFPKEEKQRALAALERVglLDKAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 154 ACASGGQLVIMDEPTAALGIREQRMVLDVVHDL-RAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAEVERNAVSHDEV 232
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEVL 237
|
...
gi 499272610 233 VRL 235
Cdd:cd03256 238 DEI 240
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-221 |
2.07e-37 |
|
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: 130.41 E-value: 2.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKqvhmDSARDALALG-ITA 80
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK----SYQKNIEALRrIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 81 VYQDLALVDQRNVIHNISLG----NIPTKWGGLVVDRKKMRETAenalsymkaklpslDIPVSSMSGGQRQAVAIARACA 156
Cdd:cd03268 77 LIEAPGFYPNLTARENLRLLarllGIRKKRIDEVLDVVGLKDSA--------------KKKVKGFSLGMKQRLGIALALL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499272610 157 SGGQLVIMDEPTAAL---GIREQRmvlDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAE 221
Cdd:cd03268 143 GNPDLLILDEPTNGLdpdGIKELR---ELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-227 |
4.08e-37 |
|
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: 130.69 E-value: 4.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFG----HVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHmDSARDALAL 76
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVT-RRRRKAFRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 77 GITAVYQD-LALVDQRNVIHNI------SLGniptkwgglvvdRKKMRETAENALSymKAKLPS--LDIPVSSMSGGQRQ 147
Cdd:COG1124 80 RVQMVFQDpYASLHPRHTVDRIlaeplrIHG------------LPDREERIAELLE--QVGLPPsfLDRYPHQLSGGQRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 148 AVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRA-HGTSVLIISHNLDHVFEVADDLLILRGGRVVAEVERNA 226
Cdd:COG1124 146 RVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREeRGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVAD 225
|
.
gi 499272610 227 V 227
Cdd:COG1124 226 L 226
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-224 |
5.82e-37 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 129.79 E-value: 5.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGH-VTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHmDSARDALA---- 75
Cdd:COG2884 1 MIRFENVSKRYPGgREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLS-RLKRREIPylrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 76 -LGItaVYQDLALVDQRNVIHNISLgniPTKWGGlvVDRKKMRETAENALSY--MKAKlpsLDIPVSSMSGGQRQAVAIA 152
Cdd:COG2884 80 rIGV--VFQDFRLLPDRTVYENVAL---PLRVTG--KSRKEIRRRVREVLDLvgLSDK---AKALPHELSGGEQQRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499272610 153 RACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAEVER 224
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEAR 221
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-221 |
6.82e-37 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 130.11 E-value: 6.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHmDSARDALAL---- 76
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKLrrkv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 77 GItaVYQDLALVDQRNVIHNISLGniPTKWGGlvVDRKKMRETAENALSYM----KA-KLPSldipvsSMSGGQRQAVAI 151
Cdd:COG1126 80 GM--VFQQFNLFPHLTVLENVTLA--PIKVKK--MSKAEAEERAMELLERVgladKAdAYPA------QLSGGQQQRVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499272610 152 ARACASGGQLVIMDEPTAALG---IREqrmVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAE 221
Cdd:COG1126 148 ARALAMEPKVMLFDEPTSALDpelVGE---VLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEE 217
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-218 |
1.22e-36 |
|
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: 129.38 E-value: 1.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDAlalGITAV 81
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER---NVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 82 YQDLALVDQRNVIHNISLGnIPTKWGGLVVDRKKMRETAENALSYMkaKLPSL-DIPVSSMSGGQRQAVAIARACASGGQ 160
Cdd:cd03296 80 FQHYALFRHMTVFDNVAFG-LRVKPRSERPPEAEIRAKVHELLKLV--QLDWLaDRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499272610 161 LVIMDEPTAALGI---REQRMVLDVVHDlRAHGTSVLiISHNLDHVFEVADDLLILRGGRV 218
Cdd:cd03296 157 VLLLDEPFGALDAkvrKELRRWLRRLHD-ELHVTTVF-VTHDQEEALEVADRVVVMNKGRI 215
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-221 |
2.90e-36 |
|
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: 127.87 E-value: 2.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 4 VQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDALALGItaVYQ 83
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGI--VFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 84 DLALVDQRNVIHNISLgniptkWGGLV-VDRKKMRETAENALSYMkAKLPSLDIPVSSMSGGQRQAVAIARACASGGQLV 162
Cdd:cd03265 81 DLSVDDELTGWENLYI------HARLYgVPGAERRERIDELLDFV-GLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 163 IMDEPTAALGIREQRMVLDVVHDL-RAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAE 221
Cdd:cd03265 154 FLDEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAE 213
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-219 |
3.77e-36 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 130.99 E-value: 3.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSA--RDalaLGI 78
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPekRN---VGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 79 taVYQDLALVDQRNVIHNISLGniPTKWGglvVDRKKMRETAENALSYMkaKLPSL-DIPVSSMSGGQRQAVAIARACAS 157
Cdd:COG3842 82 --VFQDYALFPHLTVAENVAFG--LRMRG---VPKAEIRARVAELLELV--GLEGLaDRYPHQLSGGQQQRVALARALAP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499272610 158 GGQLVIMDEPTAAL--GIREQrMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVV 219
Cdd:COG3842 153 EPRVLLLDEPLSALdaKLREE-MREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIE 215
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-221 |
6.12e-36 |
|
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: 127.31 E-value: 6.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGH----VTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDALAL 76
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 77 --GITAVYQDLALVDQRNVIHNISLgniPTKWGGlvVDRKKMRETAENALSYM----KAklpslDIPVSSMSGGQRQAVA 150
Cdd:cd03258 81 rrRIGMIFQHFNLLSSRTVFENVAL---PLEIAG--VPKAEIEERVLELLELVgledKA-----DAYPAQLSGGQKQRVG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499272610 151 IARACASGGQLVIMDEPTAALGIREQRMVLDVVHDL-RAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAE 221
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSILALLRDInRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEE 222
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-221 |
8.34e-36 |
|
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: 127.23 E-value: 8.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARD--ALALGIT 79
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 80 AVYQDLALVDQRNVIHNISL-----GNIPTKWgglvVDRKKMRETAENALSYMKAKLPsldipvSSMSGGQRQAVAIARA 154
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFplrehTRLSEEE----IREIVLEKLEAVGLRGAEDLYP------AELSGGMKKRVALARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499272610 155 CASGGQLVIMDEPTAALGIREQRMVLDVVHDL-RAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAE 221
Cdd:cd03261 151 LALDPELLLYDEPTAGLDPIASGVIDDLIRSLkKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAE 218
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-221 |
3.02e-35 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 127.15 E-value: 3.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARD-------- 72
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRigylpeer 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 73 ALalgitavYQDLALVDQ-----RnvIHNISLgniptkwgglvvdrkkmRETAENALSYMKAklpsLDI------PVSSM 141
Cdd:COG4152 81 GL-------YPKMKVGEQlvylaR--LKGLSK-----------------AEAKRRADEWLER----LGLgdrankKVEEL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 142 SGGQRQAVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAE 221
Cdd:COG4152 131 SKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLS 210
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-221 |
3.26e-35 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 125.17 E-value: 3.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRF----GHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDALAL 76
Cdd:cd03266 1 MITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 77 GItaVYQDLALVDQRNVIHNISLgniptkWGGL--------------VVDRKKMRETaenalsymkaklpsLDIPVSSMS 142
Cdd:cd03266 81 GF--VSDSTGLYDRLTARENLEY------FAGLyglkgdeltarleeLADRLGMEEL--------------LDRRVGGFS 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499272610 143 GGQRQAVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAE 221
Cdd:cd03266 139 TGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-233 |
7.09e-35 |
|
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: 131.88 E-value: 7.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFG--HVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNG---KQVHMDSARDALAL 76
Cdd:COG2274 474 IELENVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGidlRQIDPASLRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 77 gitaVYQDLALVdQRNVIHNISLGNiPTkwgglvVDRKKMRETAENA-LSYMKAKLPS-LDIPVSSM----SGGQRQAVA 150
Cdd:COG2274 554 ----VLQDVFLF-SGTIRENITLGD-PD------ATDEEIIEAARLAgLHDFIEALPMgYDTVVGEGgsnlSGGQRQRLA 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 151 IARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTsVLIISHNLDHVfEVADDLLILRGGRVVAEvernaVSHD 230
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRT-VIIIAHRLSTI-RLADRIIVLDKGRIVED-----GTHE 694
|
...
gi 499272610 231 EVV 233
Cdd:COG2274 695 ELL 697
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-221 |
1.17e-34 |
|
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: 130.26 E-value: 1.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRF-GHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHmdsardalALGITA 80
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLS--------DLDPAS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 81 VYQDLALVDQRNVI------HNISLGNIptkwgglVVDRKKMRETAENA-LSYMKAKLPS-LDIPV----SSMSGGQRQA 148
Cdd:COG4988 409 WRRQIAWVPQNPYLfagtirENLRLGRP-------DASDEELEAALEAAgLDEFVAALPDgLDTPLgeggRGLSGGQAQR 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499272610 149 VAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLrAHGTSVLIISHNLDHVfEVADDLLILRGGRVVAE 221
Cdd:COG4988 482 LALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHRLALL-AQADRILVLDDGRIVEQ 552
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-221 |
1.87e-34 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 124.07 E-value: 1.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHmDSARDALAlGITA 80
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLA-AWSPWELA-RRRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 81 VY-QDLALVDQRNVIHNISLGNIPtkWGGlvvDRKKMRETAENALSymKAKLPSL-DIPVSSMSGGQRQAVAIARA---- 154
Cdd:COG4559 79 VLpQHSSLAFPFTVEEVVALGRAP--HGS---SAAQDRQIVREALA--LVGLAHLaGRSYQTLSGGEQQRVQLARVlaql 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 155 ---CASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAE 221
Cdd:COG4559 152 wepVDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQ 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-218 |
3.46e-34 |
|
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: 122.25 E-value: 3.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHmDSARDALAL--GIT 79
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLT-DDKKNINELrqKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 80 AVYQDLALVDQRNVIHNISLGniPTKWGGLvvDRKKMRETAENAL-----SYMKAKLPsldipvSSMSGGQRQAVAIARA 154
Cdd:cd03262 80 MVFQQFNLFPHLTVLENITLA--PIKVKGM--SKAEAEERALELLekvglADKADAYP------AQLSGGQQQRVAIARA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499272610 155 CASGGQLVIMDEPTAALG---IREqrmVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRV 218
Cdd:cd03262 150 LAMNPKVMLFDEPTSALDpelVGE---VLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-217 |
4.91e-34 |
|
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: 120.57 E-value: 4.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFG--HVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKqvhmdsarDALALGIT 79
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGV--------DLRDLDLE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 80 AVYQDLALVDQRNVIHNISLgniptkwgglvvdrkkmretAENALsymkaklpsldipvssmSGGQRQAVAIARACASGG 159
Cdd:cd03228 73 SLRKNIAYVPQDPFLFSGTI--------------------RENIL-----------------SGGQRQRIAIARALLRDP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499272610 160 QLVIMDEPTAALGIREQRMVLDVVHDLRaHGTSVLIISHNLDHVfEVADDLLILRGGR 217
Cdd:cd03228 116 PILILDEATSALDPETEALILEALRALA-KGKTVIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-221 |
5.30e-34 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 122.96 E-value: 5.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHmDSARDALAlgita 80
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLA-DWSPAELA----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 81 vyQDLALVDQRN-------VIHNISLGNIPtkWGGlvvDRKKMRETAENALSymKAKLPSL-DIPVSSMSGGQRQAVAIA 152
Cdd:PRK13548 76 --RRRAVLPQHSslsfpftVEEVVAMGRAP--HGL---SRAEDDALVAAALA--QVDLAHLaGRDYPQLSGGEQQRVQLA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499272610 153 RA------CASGGQLVIMDEPTAALGIREQRMVLDVVHDL-RAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAE 221
Cdd:PRK13548 147 RVlaqlwePDGPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVAD 222
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-236 |
7.11e-34 |
|
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: 122.41 E-value: 7.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGH-VTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDALAL--G 77
Cdd:TIGR02315 1 MLEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 78 ITAVYQDLALVDQRNVIHNI---SLGNIPTKWGGLVVDRKKMRETAENALsymkAKLPSLD---IPVSSMSGGQRQAVAI 151
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVlhgRLGYKPTWRSLLGRFSEEDKERALSAL----ERVGLADkayQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 152 ARACASGGQLVIMDEPTAALGIREQRMVLDVVHDL-RAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAEVERNAVShD 230
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRInKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELD-D 235
|
....*.
gi 499272610 231 EVVRLI 236
Cdd:TIGR02315 236 EVLRHI 241
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-169 |
7.64e-34 |
|
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: 119.29 E-value: 7.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 17 ISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDALAlGITAVYQDLALVDQRNVIHN 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRK-EIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499272610 97 ISLGNIPTKWgglvvDRKKMRETAENALSYMKAKLPS---LDIPVSSMSGGQRQAVAIARACASGGQLVIMDEPTA 169
Cdd:pfam00005 80 LRLGLLLKGL-----SKREKDARAEEALEKLGLGDLAdrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-221 |
8.36e-34 |
|
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: 127.33 E-value: 8.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRF--GHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPT---QGSVWVNGKQVhMDSARDALA 75
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDL-LELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 76 LGITAVYQD-LALVDQRNVIHNISLGNIPTKwgglvVDRKKMRETAENALSymKAKLPS-LDIPVSSMSGGQRQAVAIAR 153
Cdd:COG1123 83 RRIGMVFQDpMTQLNPVTVGDQIAEALENLG-----LSRAEARARVLELLE--AVGLERrLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499272610 154 ACASGGQLVIMDEPTAALGIREQRMVLDVVHDL-RAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAE 221
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVED 224
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-234 |
9.03e-34 |
|
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: 121.88 E-value: 9.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQV---HMDS-ARdalaLG 77
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDItklPMHKrAR----LG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 78 ITAVYQDLALVDQRNVIHNISLGNIPTKwgglvVDRKKMRETAENALSYMKAKlPSLDIPVSSMSGGQRQAVAIARACAS 157
Cdd:cd03218 77 IGYLPQEASIFRKLTVEENILAVLEIRG-----LSKKEREEKLEELLEEFHIT-HLRKSKASSLSGGERRRVEIARALAT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 158 GGQLVIMDEPTAA---LGIRE-QRMvldvVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAEVERNAVSHDEVV 233
Cdd:cd03218 151 NPKFLLLDEPFAGvdpIAVQDiQKI----IKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELV 226
|
.
gi 499272610 234 R 234
Cdd:cd03218 227 R 227
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-219 |
2.79e-33 |
|
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: 122.85 E-value: 2.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRF----GHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKP---TQGSVWVNGKQVHMDSARDA 73
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 74 LAL---GITAVYQD--LALvdqrN-------------VIHNIslgniptkwgglvVDRKKMRETAENALSYMKaklpsLD 135
Cdd:COG0444 81 RKIrgrEIQMIFQDpmTSL----NpvmtvgdqiaeplRIHGG-------------LSKAEARERAIELLERVG-----LP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 136 IPVSSM-------SGGQRQAVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRA-HGTSVLIISHNLDHVFEVA 207
Cdd:COG0444 139 DPERRLdryphelSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQReLGLAILFITHDLGVVAEIA 218
|
250
....*....|..
gi 499272610 208 DDLLILRGGRVV 219
Cdd:COG0444 219 DRVAVMYAGRIV 230
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-221 |
5.44e-33 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 120.50 E-value: 5.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARdALAlgita 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSR-QLA----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 81 vyQDLALVDQRNVIHN-------ISLGNIP--TKWGGLVVDRKK-----MRETAENALSymkaklpslDIPVSSMSGGQR 146
Cdd:PRK11231 76 --RRLALLPQHHLTPEgitvrelVAYGRSPwlSLWGRLSAEDNArvnqaMEQTRINHLA---------DRRLTDLSGGQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499272610 147 QAVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAE 221
Cdd:PRK11231 145 QRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQ 219
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-220 |
6.93e-33 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 122.18 E-value: 6.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVhmDSARDALALGITAV 81
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL--FTNLPPRERRVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 82 YQDLALVDQRNVIHNISLGniPTKwggLVVDRKKMRETAENALSYMKA-----KLPS-LdipvssmSGGQRQAVAIARAC 155
Cdd:COG1118 81 FQHYALFPHMTVAENIAFG--LRV---RPPSKAEIRARVEELLELVQLegladRYPSqL-------SGGQRQRVALARAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499272610 156 ASGGQLVIMDEPTAALGI---REQRMVLDVVHDlRAHGTSVLiISHNLDHVFEVADDLLILRGGRVVA 220
Cdd:COG1118 149 AVEPEVLLLDEPFGALDAkvrKELRRWLRRLHD-ELGGTTVF-VTHDQEEALELADRVVVMNQGRIEQ 214
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-220 |
1.16e-32 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 118.70 E-value: 1.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAisNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGkqvhmdsaRDALALG--- 77
Cdd:COG3840 1 MLRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNG--------QDLTALPpae 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 78 --ITAVYQDLALVDQRNVIHNISLGNIPtkwgGL---VVDRKKMRETAEN-ALSYMKAKLPsldipvSSMSGGQRQAVAI 151
Cdd:COG3840 71 rpVSMLFQENNLFPHLTVAQNIGLGLRP----GLkltAEQRAQVEQALERvGLAGLLDRLP------GQLSGGQRQRVAL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 152 ARACASGGQLVIMDEPTAALGIREQRMVLDVVHDL-RAHGTSVLIISHNLDHVFEVADDLLILRGGRVVA 220
Cdd:COG3840 141 ARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELcRERGLTVLMVTHDPEDAARIADRVLLVADGRIAA 210
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-219 |
1.57e-32 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 117.74 E-value: 1.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 3 RVQNLTKRFGHVTAI-SNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVH--------------- 66
Cdd:cd03226 1 RIENISFSYKKGTEIlDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKakerrksigyvmqdv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 67 -----MDSARDALALGITAVYQDLAlvDQRNVIhnislgniptkwgglvvdrKKMretaenALSYMKAKLPSldipvsSM 141
Cdd:cd03226 81 dyqlfTDSVREELLLGLKELDAGNE--QAETVL-------------------KDL------DLYALKERHPL------SL 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499272610 142 SGGQRQAVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVV 219
Cdd:cd03226 128 SGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-242 |
2.46e-32 |
|
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: 118.17 E-value: 2.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHVT-AISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVhmdSARDALAL--GI 78
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDI---REQDPVELrrKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 79 TAVYQDLALVDQRNVIHNISLgnIPT--KWgglvvDRKKMRETAENALsymkaKLPSLDIPV------SSMSGGQRQAVA 150
Cdd:cd03295 78 GYVIQQIGLFPHMTVEENIAL--VPKllKW-----PKEKIRERADELL-----ALVGLDPAEfadrypHELSGGQQQRVG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 151 IARACASGGQLVIMDEPTAALG--IRE--QRMVLDVVHDLrahGTSVLIISHNLDHVFEVADDLLILRGGRVV-----AE 221
Cdd:cd03295 146 VARALAADPPLLLMDEPFGALDpiTRDqlQEEFKRLQQEL---GKTIVFVTHDIDEAFRLADRIAIMKNGEIVqvgtpDE 222
|
250 260
....*....|....*....|.
gi 499272610 222 VERNavSHDEVVRLILaGQPR 242
Cdd:cd03295 223 ILRS--PANDFVAEFV-GADR 240
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
9-219 |
3.64e-32 |
|
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: 118.51 E-value: 3.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 9 KRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDALAL---GITAVYQDL 85
Cdd:cd03294 32 KKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkKISMVFQSF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 86 ALVDQRNVIHNISLGnipTKWGGlvVDRKKMRETAENALSYM-----KAKLPSldipvsSMSGGQRQAVAIARACASGGQ 160
Cdd:cd03294 112 ALLPHRTVLENVAFG---LEVQG--VPRAEREERAAEALELVglegwEHKYPD------ELSGGMQQRVGLARALAVDPD 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499272610 161 LVIMDEPTAALG--IReqRMVLDVVHDLRA-HGTSVLIISHNLDHVFEVADDLLILRGGRVV 219
Cdd:cd03294 181 ILLMDEAFSALDplIR--REMQDELLRLQAeLQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-227 |
5.60e-32 |
|
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: 116.90 E-value: 5.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICG-----TYKPTQGSVWVNGKQV-HMDSARDALA 75
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDIyDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 76 LGITAVYQdlalvdQRNVIH-----NISLGniptKWGGLVVDRKKMRETAENALS------YMKAKLPSLdipvsSMSGG 144
Cdd:cd03260 81 RRVGMVFQ------KPNPFPgsiydNVAYG----LRLHGIKLKEELDERVEEALRkaalwdEVKDRLHAL-----GLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 145 QRQAVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRaHGTSVLIISHNLDHVFEVADDLLILRGGRVVAEVER 224
Cdd:cd03260 146 QQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELK-KEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
|
...
gi 499272610 225 NAV 227
Cdd:cd03260 225 EQI 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-243 |
6.94e-32 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 122.06 E-value: 6.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLT-KRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDALALGITA 80
Cdd:COG3845 258 LEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVAY 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 81 VYQD---LALVDQRNVIHNISLGNI--PTKWGGLVVDRKKMRETAENALSYMKAKLPSLDIPVSSMSGGQRQAVAIARAC 155
Cdd:COG3845 338 IPEDrlgRGLVPDMSVAENLILGRYrrPPFSRGGFLDRKAIRAFAEELIEEFDVRTPGPDTPARSLSGGNQQKVILAREL 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 156 ASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAEVERNAVSHDEVVRL 235
Cdd:COG3845 418 SRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEATREEIGLL 497
|
....*...
gi 499272610 236 IlAGQPRD 243
Cdd:COG3845 498 M-AGVKEE 504
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-221 |
2.05e-31 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 118.26 E-value: 2.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRF----GHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDALAL 76
Cdd:COG1135 1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 77 --GITAVYQDLALVDQRNVIHNISLgniPTKWGGlvVDRKKMRETAENALSYM----KAK-LPsldipvSSMSGGQRQAV 149
Cdd:COG1135 81 rrKIGMIFQHFNLLSSRTVAENVAL---PLEIAG--VPKAEIRKRVAELLELVglsdKADaYP------SQLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499272610 150 AIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRA-HGTSVLIISHNLDHVFEVADDLLILRGGRVVAE 221
Cdd:COG1135 150 GIARALANNPKVLLCDEATSALDPETTRSILDLLKDINReLGLTIVLITHEMDVVRRICDRVAVLENGRIVEQ 222
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-237 |
8.01e-31 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 119.25 E-value: 8.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 20 VSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDALALGITAVYQD---LALVDQRNVIHN 96
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMLCPEDrkaEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 97 IslgNIPTK----WGGLVVDRKKMRETAENALSYMKAKLPSLDIPVSSMSGGQRQAVAIARACASGGQLVIMDEPTAALG 172
Cdd:PRK11288 352 I---NISARrhhlRAGCLINNRWEAENADRFIRSLNIKTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGID 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499272610 173 IREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAEVERNAVSHDEVVRLIL 237
Cdd:PRK11288 429 VGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGELAREQATERQALSLAL 493
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-222 |
8.46e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 114.80 E-value: 8.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGH-----VTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQV-HMDSARDAL 74
Cdd:COG1101 1 MLELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 75 ALGitAVYQD--------------LALVDQRNVIHNISLGNiptkwgglvvdRKKMRETAENALSYMKAKLPS-LDIPVS 139
Cdd:COG1101 81 YIG--RVFQDpmmgtapsmtieenLALAYRRGKRRGLRRGL-----------TKKRRELFRELLATLGLGLENrLDTKVG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 140 SMSGGQRQAVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDL-RAHGTSVLIISHNLDHVFEVADDLLILRGGRV 218
Cdd:COG1101 148 LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
....
gi 499272610 219 VAEV 222
Cdd:COG1101 228 ILDV 231
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
5-218 |
1.04e-30 |
|
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: 113.27 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 5 QNLTKRFGH-VTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHmDSARDALAL---GITA 80
Cdd:cd03292 4 INVTKTYPNgTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVS-DLRGRAIPYlrrKIGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 81 VYQDLALVDQRNVIHNISLGNIPTKWGGLVVDRKKMRETAENALSYMKAKLPsldipvSSMSGGQRQAVAIARACASGGQ 160
Cdd:cd03292 83 VFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALP------AELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499272610 161 LVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRV 218
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-220 |
2.04e-30 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 116.86 E-value: 2.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARdALALGITA 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSAR-AASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 81 VYQDLALVDQRNVIHNISLGNIP--TKWGGLVVDRKKMRETAENALSYMKAklpsLDIPVSSMSGGQRQAVAIARACASG 158
Cdd:PRK09536 82 VPQDTSLSFEFDVRQVVEMGRTPhrSRFDTWTETDRAAVERAMERTGVAQF----ADRPVTSLSGGERQRVLLARALAQA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499272610 159 GQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVA 220
Cdd:PRK09536 158 TPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRA 219
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-219 |
2.32e-30 |
|
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: 112.35 E-value: 2.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDAlalGITAV 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDR---DIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 82 YQDLALVDQRNVIHNISLGNIPTKWGGLVVDRkKMRETAEN-ALSYMkaklpsLDIPVSSMSGGQRQAVAIARACASGGQ 160
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLKLRKVPKDEIDE-RVREVAELlQIEHL------LDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499272610 161 LVIMDEPTAALG--IREQrMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVV 219
Cdd:cd03301 151 VFLMDEPLSNLDakLRVQ-MRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-220 |
3.01e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 113.55 E-value: 3.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFG--HVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSAR------- 71
Cdd:PRK13632 7 MIKVENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKeirkkig 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 72 ------DALALGITaVYQDLALvdqrnvihniSLGNIptkwgglVVDRKKMRETAENA------LSYMKaKLPSldipvs 139
Cdd:PRK13632 87 iifqnpDNQFIGAT-VEDDIAF----------GLENK-------KVPPKKMKDIIDDLakkvgmEDYLD-KEPQ------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 140 SMSGGQRQAVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLI-ISHNLDHVFeVADDLLILRGGRV 218
Cdd:PRK13632 142 NLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLIsITHDMDEAI-LADKVIVFSEGKL 220
|
..
gi 499272610 219 VA 220
Cdd:PRK13632 221 IA 222
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
2-236 |
4.01e-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: 112.23 E-value: 4.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDALALGITAV 81
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 82 YQDLALVDQRNVIHNISLGniptkwggLVVDRKKMRETAENALSYMKAKLPSLDIPVSSMSGGQRQAVAIARACASGGQL 161
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTG--------LAALPRRSRKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499272610 162 VIMDEPTAalGIREQ--RMVLDVVHDLRA-HGTSVLIISHNLDHVFEVADDLLILRGGRVVAEVERNAVSHDEVVRLI 236
Cdd:TIGR03410 153 LLLDEPTE--GIQPSiiKDIGRVIRRLRAeGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDKVRRYL 228
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
15-221 |
5.17e-30 |
|
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: 112.93 E-value: 5.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 15 TAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDalalgITAVYQDLALVDQ---- 90
Cdd:TIGR04521 19 KALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKK-----LKDLRKKVGLVFQfpeh 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 91 ----RNVIHNISLGniPTKWGglvVDRKKMRETAENALsymkaKLPSLDIPVS-----SMSGGQRQAVAIARACASGGQL 161
Cdd:TIGR04521 94 qlfeETVYKDIAFG--PKNLG---LSEEEAEERVKEAL-----ELVGLDEEYLerspfELSGGQMRRVAIAGVLAMEPEV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499272610 162 VIMDEPTAALGIREQRMVLDVVHDL-RAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAE 221
Cdd:TIGR04521 164 LILDEPTAGLDPKGRKEILDLFKRLhKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLD 224
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-219 |
6.14e-30 |
|
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: 111.56 E-value: 6.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHmdsARDALALGITAV 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT---NLPPHKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 82 YQDLALVDQRNVIHNISLGNIPTKwgglvVDRKKMRETAENALSYMK-----AKLPsldipvSSMSGGQRQAVAIARACA 156
Cdd:cd03300 78 FQNYALFPHLTVFENIAFGLRLKK-----LPKAEIKERVAEALDLVQlegyaNRKP------SQLSGGQQQRVAIARALV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499272610 157 SGGQLVIMDEPTAALGIR---EQRMVLDVVHdlRAHGTSVLIISHNLDHVFEVADDLLILRGGRVV 219
Cdd:cd03300 147 NEPKVLLLDEPLGALDLKlrkDMQLELKRLQ--KELGITFVFVTHDQEEALTMSDRIAVMNKGKIQ 210
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-218 |
3.75e-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: 108.29 E-value: 3.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRfghvTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDALALGITA 80
Cdd:cd03215 4 VLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 81 VYQD---LALVDQRNVIHNISLGNIptkwgglvvdrkkmretaenalsymkaklpsldipvssMSGGQRQAVAIARACAS 157
Cdd:cd03215 80 VPEDrkrEGLVLDLSVAENIALSSL--------------------------------------LSGGNQQKVVLARWLAR 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499272610 158 GGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRV 218
Cdd:cd03215 122 DPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-234 |
7.71e-29 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 108.96 E-value: 7.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVH---MDS-ARdalaL 76
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIThlpMHKrAR----L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 77 GI------TAVYQDLalvdqrNVIHNIslgniptkwggLVV------DRKKMRETAENALSYMK-AKLpsLDIPVSSMSG 143
Cdd:COG1137 79 GIgylpqeASIFRKL------TVEDNI-----------LAVlelrklSKKEREERLEELLEEFGiTHL--RKSKAYSLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 144 GQRQAVAIARACASGGQLVIMDEPTAA---LGIRE-QRMvldvVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVV 219
Cdd:COG1137 140 GERRRVEIARALATNPKFILLDEPFAGvdpIAVADiQKI----IRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVL 215
|
250
....*....|....*
gi 499272610 220 AEVERNAVSHDEVVR 234
Cdd:COG1137 216 AEGTPEEILNNPLVR 230
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-219 |
8.04e-29 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 111.32 E-value: 8.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDAlalGITA 80
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDR---NIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 81 VYQDLALVDQRNVIHNISLgniPTKWGGlvVDRKKMRETAENAlsymkAKL----PSLDIPVSSMSGGQRQAVAIARACA 156
Cdd:COG3839 80 VFQSYALYPHMTVYENIAF---PLKLRK--VPKAEIDRRVREA-----AELlgleDLLDRKPKQLSGGQRQRVALGRALV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499272610 157 SGGQLVIMDEPTAAL--GIREQ-RMVLDVVHdlRAHGTSVLIISHNLDHVFEVADDLLILRGGRVV 219
Cdd:COG3839 150 REPKVFLLDEPLSNLdaKLRVEmRAEIKRLH--RRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQ 213
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-219 |
8.89e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 110.71 E-value: 8.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGH-----VTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWV----NGKQVHMDSAR 71
Cdd:PRK13631 21 ILRVKNLYCVFDEkqeneLVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 72 DA-----------LALGITAVYQ--DLALVdQRNVIHNISLGNIptkwgGLVVDRKKMRETAENALSYMKAKLPSLDIPV 138
Cdd:PRK13631 101 TNpyskkiknfkeLRRRVSMVFQfpEYQLF-KDTIEKDIMFGPV-----ALGVKKSEAKKLAKFYLNKMGLDDSYLERSP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 139 SSMSGGQRQAVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRV 218
Cdd:PRK13631 175 FGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKI 254
|
.
gi 499272610 219 V 219
Cdd:PRK13631 255 L 255
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-217 |
9.27e-29 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 108.68 E-value: 9.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRF-----GHVT--AISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVN--GKQVHMDSA- 70
Cdd:COG4778 4 LLEVENLSKTFtlhlqGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdGGWVDLAQAs 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 71 -RDALAL---GITAVYQDLalvdqrNVIHNIS-----------LGniptkwgglvVDRKKMRETAENALSYMkaKLPSL- 134
Cdd:COG4778 84 pREILALrrrTIGYVSQFL------RVIPRVSaldvvaeplleRG----------VDREEARARARELLARL--NLPERl 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 135 -DIPVSSMSGGQRQAVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLIL 213
Cdd:COG4778 146 wDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDV 225
|
....
gi 499272610 214 RGGR 217
Cdd:COG4778 226 TPFS 229
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
16-220 |
9.64e-29 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 108.45 E-value: 9.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 16 AISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNG---KQVHMDSARDalalGITAVYQDLALVdQRN 92
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdiRQLDPADLRR----NIGYVPQDVTLF-YGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 93 VIHNISLGNiptkwggLVVDRKKMRETAENA-LSYMKAKLP-SLDIPVS----SMSGGQRQAVAIARACASGGQLVIMDE 166
Cdd:cd03245 94 LRDNITLGA-------PLADDERILRAAELAgVTDFVNKHPnGLDLQIGergrGLSGGQRQAVALARALLNDPPILLLDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499272610 167 PTAALGIREQRMVLDVVHDLRAHGTsVLIISHNLDhVFEVADDLLILRGGRVVA 220
Cdd:cd03245 167 PTSAMDMNSEERLKERLRQLLGDKT-LIIITHRPS-LLDLVDRIIVMDSGRIVA 218
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-234 |
2.23e-28 |
|
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: 112.55 E-value: 2.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRF--GHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGkqvhmdsaRDALALGIT 79
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGG--------VDLRDLDED 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 80 AVYQDLALVDQRNVI------HNISLGNiPTkwgglvVDRKKMRETAENA-LSYMKAKLP-SLDIPV----SSMSGGQRQ 147
Cdd:COG4987 406 DLRRRIAVVPQRPHLfdttlrENLRLAR-PD------ATDEELWAALERVgLGDWLAALPdGLDTWLgeggRRLSGGERR 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 148 AVAIARACASGGQLVIMDEPTAAL-GIREQRmvldVVHDLRAH--GTSVLIISHNLDHVfEVADDLLILRGGRVVAever 224
Cdd:COG4987 479 RLALARALLRDAPILLLDEPTEGLdAATEQA----LLADLLEAlaGRTVLLITHRLAGL-ERMDRILVLEDGRIVE---- 549
|
250
....*....|
gi 499272610 225 nAVSHDEVVR 234
Cdd:COG4987 550 -QGTHEELLA 558
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-234 |
3.44e-28 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 107.27 E-value: 3.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQV-HMDSARdALALGIT 79
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDItDWQTAK-IMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 80 AVYQDLALVDQRNVIHNISLGniptkwgGLVVDRKKMRETAENALSYMKAKLPSLDIPVSSMSGGQRQAVAIARACASGG 159
Cdd:PRK11614 84 IVPEGRRVFSRMTVEENLAMG-------GFFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499272610 160 QLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAEVERNAVSHDEVVR 234
Cdd:PRK11614 157 RLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVR 231
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-218 |
3.50e-28 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 107.49 E-value: 3.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHmDSARDALALGITA 80
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVN-DPKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 81 --VYQDLALVDQRNVIHNISLGNIPTKWGGLVVDRKKMRET-AENALSYMKAKLPSldipvsSMSGGQRQAVAIARACAS 157
Cdd:PRK09493 80 gmVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELlAKVGLAERAHHYPS------ELSGGQQQRVAIARALAV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499272610 158 GGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRV 218
Cdd:PRK09493 154 KPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
26-220 |
3.60e-28 |
|
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: 106.61 E-value: 3.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 26 KGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNG-------KQVHMDSARDALALgitaVYQDLALVDQRNVIHNIS 98
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrKKINLPPQQRKIGL----VFQQYALFPHLNVRENLA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 99 LGnipTKwgglVVDRKKMRETAENALSYMKAKlPSLDIPVSSMSGGQRQAVAIARACASGGQLVIMDEPTAAL--GIREQ 176
Cdd:cd03297 98 FG---LK----RKRNREDRISVDELLDLLGLD-HLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALdrALRLQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499272610 177 RMVLdvVHDLRAH-GTSVLIISHNLDHVFEVADDLLILRGGRVVA 220
Cdd:cd03297 170 LLPE--LKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQY 212
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
10-221 |
3.76e-28 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 112.18 E-value: 3.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 10 RFGHVT--------AISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNG---KQVHMDSARDALALgi 78
Cdd:COG1132 341 EFENVSfsypgdrpVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGvdiRDLTLESLRRQIGV-- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 79 taVYQDLALVDqRNVIHNISLGNIPtkwgglvVDRKKMRETAENA-LSYMKAKLPS-LDIPV----SSMSGGQRQAVAIA 152
Cdd:COG1132 419 --VPQDTFLFS-GTIRENIRYGRPD-------ATDEEVEEAAKAAqAHEFIEALPDgYDTVVgergVNLSGGQRQRIAIA 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499272610 153 RACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTsVLIISHNLDHVfEVADDLLILRGGRVVAE 221
Cdd:COG1132 489 RALLKDPPILILDEATSALDTETEALIQEALERLMKGRT-TIVIAHRLSTI-RNADRILVLDDGRIVEQ 555
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-223 |
4.84e-28 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 107.64 E-value: 4.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFG----HVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDALal 76
Cdd:COG4525 3 MLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRGV-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 77 gitaVYQDLALVDQRNVIHNISLGnipTKWGGlvVDRKKMRETAENALSymKAKLPSL-DIPVSSMSGGQRQAVAIARAC 155
Cdd:COG4525 81 ----VFQKDALLPWLNVLDNVAFG---LRLRG--VPKAERRARAEELLA--LVGLADFaRRRIWQLSGGMRQRVGIARAL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499272610 156 ASGGQLVIMDEPTAALG--IRE--QRMVLDVvhdLRAHGTSVLIISHNLDHVFEVADDLLILRG--GRVVAEVE 223
Cdd:COG4525 150 AADPRFLLMDEPFGALDalTREqmQELLLDV---WQRTGKGVFLITHSVEEALFLATRLVVMSPgpGRIVERLE 220
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-248 |
1.13e-27 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 110.53 E-value: 1.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDALALGITA 80
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 81 VYQDLALVDQRNVIHNISLGnIPTKWGglvvDRKKMretaENALSYMKAKLpSLDIPVSSMSGGQRQAVAIARACASGGQ 160
Cdd:PRK15439 91 VPQEPLLFPNLSVKENILFG-LPKRQA----SMQKM----KQLLAALGCQL-DLDSSAGSLEVADRQIVEILRGLMRDSR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 161 LVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAEVERNAVSHDEVVRLILAGQ 240
Cdd:PRK15439 161 ILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDIIQAITPAA 240
|
....*...
gi 499272610 241 pRDADLEE 248
Cdd:PRK15439 241 -REKSLSA 247
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-220 |
1.48e-27 |
|
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: 105.50 E-value: 1.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHVTaISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKqvhmdsarDALAL----- 76
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGK--------DITNLppekr 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 77 GITAVYQDLALVDQRNVIHNISLGNIPTKWGGLVVDRkKMRETAEN-ALSYMkaklpsLDIPVSSMSGGQRQAVAIARAC 155
Cdd:cd03299 72 DISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIER-KVLEIAEMlGIDHL------LNRKPETLSGGEQQRVAIARAL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499272610 156 ASGGQLVIMDEPTAALGIREQ---RMVLDVVHdlRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVA 220
Cdd:cd03299 145 VVNPKILLLDEPFSALDVRTKeklREELKKIR--KEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQ 210
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-233 |
1.69e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 106.36 E-value: 1.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 4 VQNLTKRFGHVT-AISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDaLALGITAVY 82
Cdd:PRK13647 7 VEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKW-VRSKVGLVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 83 QDLAlvDQ---RNVIHNISLGNIptkwgGLVVDRKKMRETAENALSYMKAKlPSLDIPVSSMSGGQRQAVAIARACASGG 159
Cdd:PRK13647 86 QDPD--DQvfsSTVWDDVAFGPV-----NMGLDKDEVERRVEEALKAVRMW-DFRDKPPYHLSYGQKKRVAIAGVLAMDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499272610 160 QLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAEVERNAVSHDEVV 233
Cdd:PRK13647 158 DVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIV 231
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-224 |
5.09e-27 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 108.55 E-value: 5.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKrfghvTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDALALGITAV 81
Cdd:PRK10762 258 LKVDNLSG-----PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIVYI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 82 YQDL---ALVDQRNVIHNIS---LGNIPTKWGGLvvDRKKMRETAENALSYMKAKLPSLDIPVSSMSGGQRQAVAIARAC 155
Cdd:PRK10762 333 SEDRkrdGLVLGMSVKENMSltaLRYFSRAGGSL--KHADEQQAVSDFIRLFNIKTPSMEQAIGLLSGGNQQKVAIARGL 410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499272610 156 ASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAEVER 224
Cdd:PRK10762 411 MTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTR 479
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-221 |
7.87e-27 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 108.09 E-value: 7.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLT---KRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYK-PTQGSVWVNGKQVHMDSARDALAL 76
Cdd:PRK13549 259 ILEVRNLTawdPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQAIAQ 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 77 GITAVYQDL---ALVDQRNVIHNISLGNIPTKWGGLVVDRKKMRETAENALSYMKAKLPSLDIPVSSMSGGQRQAVAIAR 153
Cdd:PRK13549 339 GIAMVPEDRkrdGIVPVMGVGKNITLAALDRFTGGSRIDDAAELKTILESIQRLKVKTASPELAIARLSGGNQQKAVLAK 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499272610 154 ACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAE 221
Cdd:PRK13549 419 CLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLKGD 486
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
4-221 |
1.44e-26 |
|
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: 103.18 E-value: 1.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 4 VQNLTKR-FGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNG----KQVHMDSARDALALGI 78
Cdd:cd03267 23 LKSLFKRkYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGlvpwKRRKKFLRRIGVVFGQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 79 -TAVYQDLALVDQRNVIHNIslgniptkwggLVVDRKKMRETAENaLSYMKAKLPSLDIPVSSMSGGQRQAVAIARACAS 157
Cdd:cd03267 103 kTQLWWDLPVIDSFYLLAAI-----------YDLPPARFKKRLDE-LSELLDLEELLDTPVRQLSLGQRMRAEIAAALLH 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499272610 158 GGQLVIMDEPTAALGIREQRMVLDVVHDL-RAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAE 221
Cdd:cd03267 171 EPEILFLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYD 235
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-221 |
2.49e-26 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 102.85 E-value: 2.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHmDSARDALAlgita 80
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVA-TTPSRELA----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 81 vyQDLALVDQRNVIHN-------ISLGNIPTKWGGLVV-DRKKMREtaenALSYMkaKLPSL-DIPVSSMSGGQRQAVAI 151
Cdd:COG4604 75 --KRLAILRQENHINSrltvrelVAFGRFPYSKGRLTAeDREIIDE----AIAYL--DLEDLaDRYLDELSGGQRQRAFI 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499272610 152 ARACASGGQLVIMDEPTAALGIREQRMVLDVVHDL-RAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAE 221
Cdd:COG4604 147 AMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLaDELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQ 217
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-229 |
2.59e-26 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 104.50 E-value: 2.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRF----GHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDALAL 76
Cdd:PRK11153 1 MIELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 77 --GITAVYQDLALVDQRNVIHNISLgniPTKWGGlvVDRKKMRETAEN-----ALSYMKAKLPsldipvSSMSGGQRQAV 149
Cdd:PRK11153 81 rrQIGMIFQHFNLLSSRTVFDNVAL---PLELAG--TPKAEIKARVTEllelvGLSDKADRYP------AQLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 150 AIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDL-RAHGTSVLIISHNLDHVFEVADDLLILRGGRVvaeVERNAVS 228
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALDPATTRSILELLKDInRELGLTIVLITHEMDVVKRICDRVAVIDAGRL---VEQGTVS 226
|
.
gi 499272610 229 H 229
Cdd:PRK11153 227 E 227
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-227 |
2.61e-26 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 104.43 E-value: 2.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRF-----------GHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSA 70
Cdd:COG4608 8 LEVRDLKKHFpvrgglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 71 RDALAL--GITAVYQD-LALVDQRN----------VIHNIslgniptkwgglvVDRKKMRETAENALSymKAKLPSldip 137
Cdd:COG4608 88 RELRPLrrRMQMVFQDpYASLNPRMtvgdiiaeplRIHGL-------------ASKAERRERVAELLE--LVGLRP---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 138 vSSM-------SGGQRQAVAIARACASGGQLVIMDEPTAAL--GIREQrmVLDVVHDLRA-HGTSVLIISHNLDHVFEVA 207
Cdd:COG4608 149 -EHAdryphefSGGQRQRIGIARALALNPKLIVCDEPVSALdvSIQAQ--VLNLLEDLQDeLGLTYLFISHDLSVVRHIS 225
|
250 260
....*....|....*....|
gi 499272610 208 DDLLILRGGRVVAEVERNAV 227
Cdd:COG4608 226 DRVAVMYLGKIVEIAPRDEL 245
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-219 |
4.80e-26 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 104.53 E-value: 4.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQV-HMDSARDAlalgIT 79
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLsHVPPYQRP----IN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 80 AVYQDLALVDQRNVIHNISLGnipTKWGGLVVDRKKMRETAENALSYMK---AKLPsldipvSSMSGGQRQAVAIARACA 156
Cdd:PRK11607 95 MMFQSYALFPHMTVEQNIAFG---LKQDKLPKAEIASRVNEMLGLVHMQefaKRKP------HQLSGGQRQRVALARSLA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499272610 157 SGGQLVIMDEPTAALGIR-EQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVV 219
Cdd:PRK11607 166 KRPKLLLLDEPMGALDKKlRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-219 |
8.58e-26 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 101.31 E-value: 8.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDALalgita 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGV------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 81 VYQDLALVDQRNVIHNISLGnipTKWGGlvVDRKKMRETAENALSymKAKLPSLDI-PVSSMSGGQRQAVAIARACASGG 159
Cdd:PRK11248 75 VFQNEGLLPWRNVQDNVAFG---LQLAG--VEKMQRLEIAHQMLK--KVGLEGAEKrYIWQLSGGQRQRVGIARALAANP 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499272610 160 QLVIMDEPTAALG--IRE--QRMVLDVVHDlraHGTSVLIISHNLDHVFEVADDLLILR--GGRVV 219
Cdd:PRK11248 148 QLLLLDEPFGALDafTREqmQTLLLKLWQE---TGKQVLLITHDIEEAVFMATELVLLSpgPGRVV 210
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-221 |
1.73e-25 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 100.16 E-value: 1.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRF----------------------GHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSV 58
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 59 WVNGKQVHMdsardaLALGiTAVYQDLALVDqrNV-----IHNISLGNIptkwgglvvdRKKMRETAENA-LSymkaklP 132
Cdd:COG1134 84 EVNGRVSAL------LELG-AGFHPELTGRE--NIylngrLLGLSRKEI----------DEKFDEIVEFAeLG------D 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 133 SLDIPVSSMSGGQRQAVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLI 212
Cdd:COG1134 139 FIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIW 218
|
....*....
gi 499272610 213 LRGGRVVAE 221
Cdd:COG1134 219 LEKGRLVMD 227
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-221 |
2.34e-25 |
|
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: 99.19 E-value: 2.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHVTAISNVSANIRKGrVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQV--HMDSARDALALgit 79
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVlkQPQKLRRRIGY--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 80 aVYQDLALVDQRNVI----HNISLGNIPTkwgglvvdrKKMRETAENALSymKAKL-PSLDIPVSSMSGGQRQAVAIARA 154
Cdd:cd03264 77 -LPQEFGVYPNFTVRefldYIAWLKGIPS---------KEVKARVDEVLE--LVNLgDRAKKKIGSLSGGMRRRVGIAQA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499272610 155 CASGGQLVIMDEPTAALGIREQRMVLDVVHDLrAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAE 221
Cdd:cd03264 145 LVGDPSILIVDEPTAGLDPEERIRFRNLLSEL-GEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
10-213 |
2.45e-25 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 98.46 E-value: 2.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 10 RFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVwvngkqVHMDSARDALALGITAVYQDLALvd 89
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV------RRAGGARVAYVPQRSEVPDSLPL-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 90 qrNVIHNISLGNIPtKWGGLVVDRKKMRETAENALsyMKAKLPSL-DIPVSSMSGGQRQAVAIARACASGGQLVIMDEPT 168
Cdd:NF040873 73 --TVRDLVAMGRWA-RRGLWRRLTRDDRAAVDDAL--ERVGLADLaGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499272610 169 AALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEvADDLLIL 213
Cdd:NF040873 148 TGLDAESRERIIALLAEEHARGATVVVVTHDLELVRR-ADPCVLL 191
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-233 |
2.60e-25 |
|
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: 103.75 E-value: 2.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRF---GHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPT-QGSVWVNGKQVHMDSARDALAL 76
Cdd:TIGR02633 257 ILEARNLTCWDvinPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQAIRA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 77 GITAVYQDL---ALVDQRNVIHNISLGNIPTKWGGLVVDRKKMRETAENALSYMKAKLPSLDIPVSSMSGGQRQAVAIAR 153
Cdd:TIGR02633 337 GIAMVPEDRkrhGIVPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIGRLSGGNQQKAVLAK 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 154 ACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAEVERNAVSHDEVV 233
Cdd:TIGR02633 417 MLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDFVNHALTQEQVL 496
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-221 |
3.00e-25 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 100.45 E-value: 3.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQV-HMDSARDALALGITA 80
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIqHYASKEVARRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 81 vyQDLALVDQRNVIHNISLGNIP-----TKWgglvvdRKkmrETAENALSYMKAK-LPSL-DIPVSSMSGGQRQAVAIAR 153
Cdd:PRK10253 88 --QNATTPGDITVQELVARGRYPhqplfTRW------RK---EDEEAVTKAMQATgITHLaDQSVDTLSGGQRQRAWIAM 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499272610 154 ACASGGQLVIMDEPTAALGIREQRMVLDVVHDL-RAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAE 221
Cdd:PRK10253 157 VLAQETAIMLLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQ 225
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
3-236 |
3.55e-25 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 99.86 E-value: 3.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 3 RVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARdALALGITAVY 82
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK-AFARKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 83 QDLALVDQRNVIHNISLGNIPtkW-GGLVVDRKKMRETAENALSYMKAKlPSLDIPVSSMSGGQRQAVAIARACASGGQL 161
Cdd:PRK10575 92 QQLPAAEGMTVRELVAIGRYP--WhGALGRFGAADREKVEEAISLVGLK-PLAHRLVDSLSGGERQRAWIAMLVAQDSRC 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499272610 162 VIMDEPTAALGIREQRMVLDVVHDL-RAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAEVERNAVSHDEVVRLI 236
Cdd:PRK10575 169 LLLDEPTSALDIAHQVDVLALVHRLsQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQI 244
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-218 |
4.61e-25 |
|
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: 97.29 E-value: 4.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHVTA--ISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNG---KQVHMDSARDALAl 76
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGadiSQWDPNELGDHVG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 77 gitAVYQDLALVDqrnvihnislGNIptkwgglvvdrkkmretAENALsymkaklpsldipvssmSGGQRQAVAIARACA 156
Cdd:cd03246 80 ---YLPQDDELFS----------GSI-----------------AENIL-----------------SGGQRQRLGLARALY 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499272610 157 SGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDhVFEVADDLLILRGGRV 218
Cdd:cd03246 113 GNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPE-TLASADRILVLEDGRV 173
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-233 |
4.72e-25 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 99.29 E-value: 4.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDALALGITA 80
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 81 VYQDLALVDQRNVIHNISLG-------NIptkWGGLVVD---RKKMRETAENALSYMKaKLPSLDI---PVSSMSGGQRQ 147
Cdd:PRK11300 85 TFQHVRLFREMTVIENLLVAqhqqlktGL---FSGLLKTpafRRAESEALDRAATWLE-RVGLLEHanrQAGNLAYGQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 148 AVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLR-AHGTSVLIISHNLDHVFEVADDLLILRGGRVVAEVERNA 226
Cdd:PRK11300 161 RLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRnEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEE 240
|
....*..
gi 499272610 227 VSHDEVV 233
Cdd:PRK11300 241 IRNNPDV 247
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-219 |
6.53e-25 |
|
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: 102.87 E-value: 6.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFG--HVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNG---KQVHMDSARDALAL 76
Cdd:TIGR02203 331 VEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGhdlADYTLASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 77 gitaVYQDLALVDQrNVIHNISLGNIPTkwgglvVDRKKMRETAE--NALSYMKAKLPSLDIPV----SSMSGGQRQAVA 150
Cdd:TIGR02203 411 ----VSQDVVLFND-TIANNIAYGRTEQ------ADRAEIERALAaaYAQDFVDKLPLGLDTPIgengVLLSGGQRQRLA 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499272610 151 IARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSvLIISHNLDHVfEVADDLLILRGGRVV 219
Cdd:TIGR02203 480 IARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTT-LVIAHRLSTI-EKADRIVVMDDGRIV 546
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-234 |
9.21e-25 |
|
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: 98.33 E-value: 9.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 16 AISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHM-DSARDALALGItaVYQDLALVDqRNVI 94
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALaDPAWLRRQVGV--VLQENVLFN-RSIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 95 HNISLGNIPtkwgglvVDRKKMRETAENALSY-MKAKLP-SLDIPV----SSMSGGQRQAVAIARACASGGQLVIMDEPT 168
Cdd:cd03252 94 DNIALADPG-------MSMERVIEAAKLAGAHdFISELPeGYDTIVgeqgAGLSGGQRQRIAIARALIHNPRILIFDEAT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499272610 169 AALGIREQRMVLDVVHDLRAhGTSVLIISHNLDHVfEVADDLLILRGGRVVaeverNAVSHDEVVR 234
Cdd:cd03252 167 SALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTV-KNADRIIVMEKGRIV-----EQGSHDELLA 225
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-220 |
1.03e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 98.93 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMdSARDALAL--GI 78
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDY-SKRGLLALrqQV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 79 TAVYQDlalVDQRNVIHNISlGNIPTKWGGLVVDRKKMRETAENALSYMKAKLPSLDiPVSSMSGGQRQAVAIARACASG 158
Cdd:PRK13638 80 ATVFQD---PEQQIFYTDID-SDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQ-PIQCLSHGQKKRVAIAGALVLQ 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499272610 159 GQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVA 220
Cdd:PRK13638 155 ARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILT 216
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-218 |
1.23e-24 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 100.16 E-value: 1.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 4 VQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDAlalGITAVYQ 83
Cdd:PRK10851 5 IANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDR---KVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 84 DLALVDQRNVIHNISLG--NIP--TKWGGLVVDRKKMRETAENALSYMKAKLPsldipvSSMSGGQRQAVAIARACASGG 159
Cdd:PRK10851 82 HYALFRHMTVFDNIAFGltVLPrrERPNAAAIKAKVTQLLEMVQLAHLADRYP------AQLSGGQKQRVALARALAVEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499272610 160 QLVIMDEPTAALGI---REQRMVLDVVH-DLRAhgTSVLiISHNLDHVFEVADDLLILRGGRV 218
Cdd:PRK10851 156 QILLLDEPFGALDAqvrKELRRWLRQLHeELKF--TSVF-VTHDQEEAMEVADRVVVMSQGNI 215
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-219 |
1.42e-24 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 98.07 E-value: 1.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQ---------------- 64
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrdlyalseaerrr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 65 --------VHMDsARDALALGITA---VYQDLALVDQRNvihnisLGNIptkwgglvvdrkkmRETAENALSYMKAKLPS 133
Cdd:PRK11701 86 llrtewgfVHQH-PRDGLRMQVSAggnIGERLMAVGARH------YGDI--------------RATAGDWLERVEIDAAR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 134 LDIPVSSMSGGQRQAVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDL-RAHGTSVLIISHNLDHVFEVADDLLI 212
Cdd:PRK11701 145 IDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARLLAHRLLV 224
|
....*..
gi 499272610 213 LRGGRVV 219
Cdd:PRK11701 225 MKQGRVV 231
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
29-221 |
1.55e-24 |
|
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: 99.80 E-value: 1.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 29 VTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDAL-----ALGItaVYQDLALVDQRNVIHNISLGnip 103
Cdd:TIGR02142 25 VTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLppekrRIGY--VFQEARLFPHLSVRGNLRYG--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 104 tkwggLVVDRKKMRETAENALSYMKAKLPSLDIPVSSMSGGQRQAVAIARACASGGQLVIMDEPTAALGIREQRMVLDVV 183
Cdd:TIGR02142 100 -----MKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYL 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 499272610 184 HDLRAH-GTSVLIISHNLDHVFEVADDLLILRGGRVVAE 221
Cdd:TIGR02142 175 ERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAA 213
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
24-221 |
2.03e-24 |
|
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: 96.79 E-value: 2.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 24 IRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQV-HMDSARDAlalgITAVYQDLALVDQRNVIHNISLGNI 102
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVtAAPPADRP----VSMLFQENNLFAHLTVEQNVGLGLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 103 PtkwgGL---VVDRKKMRET-AENALSYMKAKLPSldipvsSMSGGQRQAVAIARACASGGQLVIMDEPTAALG-IREQR 177
Cdd:cd03298 97 P----GLkltAEDRQAIEVAlARVGLAGLEKRLPG------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDpALRAE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499272610 178 MvLDVVHDLRAH-GTSVLIISHNLDHVFEVADDLLILRGGRVVAE 221
Cdd:cd03298 167 M-LDLVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-219 |
2.37e-24 |
|
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: 101.03 E-value: 2.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRF-----GHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVN--------GKQVHM 67
Cdd:TIGR03269 279 IIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgdewvdmTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 68 DSARDALALGItaVYQDLALVDQRNVIHN----ISLgNIPTKWGGL--VVDRKKMRETAENALSYMKaKLPsldipvSSM 141
Cdd:TIGR03269 359 GRGRAKRYIGI--LHQEYDLYPHRTVLDNlteaIGL-ELPDELARMkaVITLKMVGFDEEKAEEILD-KYP------DEL 428
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499272610 142 SGGQRQAVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAH-GTSVLIISHNLDHVFEVADDLLILRGGRVV 219
Cdd:TIGR03269 429 SEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKIV 507
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-218 |
2.72e-24 |
|
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: 96.77 E-value: 2.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLT---KRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARdALALGI 78
Cdd:cd03248 12 VKFQNVTfayPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK-YLHSKV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 79 TAVYQDLALVdQRNVIHNISLGniptkWGGLVVDRKKMRETAENALSYMKAKLPSLDIPV----SSMSGGQRQAVAIARA 154
Cdd:cd03248 91 SLVGQEPVLF-ARSLQDNIAYG-----LQSCSFECVKEAAQKAHAHSFISELASGYDTEVgekgSQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499272610 155 CASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHgTSVLIISHNLDHVfEVADDLLILRGGRV 218
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYDWPER-RTVLVIAHRLSTV-ERADQILVLDGGRI 226
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-218 |
4.70e-24 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 97.01 E-value: 4.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTY---KPTQGSVWVNGKQVHMDS--ARDALA 75
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQREGrlARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 76 --LGITAVYQDLALVDQRNVIHNI---SLGNIP-----TKWGGLVVDRKKMRETAENALSYMKAKlpsldiPVSSMSGGQ 145
Cdd:PRK09984 84 srANTGYIFQQFNLVNRLSVLENVligALGSTPfwrtcFSWFTREQKQRALQALTRVGMVHFAHQ------RVSTLSGGQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499272610 146 RQAVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDL-RAHGTSVLIISHNLDHVFEVADDLLILRGGRV 218
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-219 |
7.83e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 99.37 E-value: 7.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKG-RVtALLGDNGAGKSTLVKMICGTYKPTQGSVWVnGKQVHMdsardalalgit 79
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGdRI-GLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVKI------------ 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 80 AVY-QDLA-LVDQRNVIHNISLGniptkwgglvvdRKKMRETaeNALSYMKAKLPS---LDIPVSSMSGGQRQAVAIARA 154
Cdd:COG0488 381 GYFdQHQEeLDPDKTVLDELRDG------------APGGTEQ--EVRGYLGRFLFSgddAFKPVGVLSGGEKARLALAKL 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499272610 155 CASGGQLVIMDEPTAALGIREQRMVLDVvhdLRAHGTSVLIISHnlDHVF--EVADDLLILRGGRVV 219
Cdd:COG0488 447 LLSPPNVLLLDEPTNHLDIETLEALEEA---LDDFPGTVLLVSH--DRYFldRVATRILEFEDGGVR 508
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-218 |
1.21e-23 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 95.64 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARD-----ALA 75
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDgelvpADR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 76 LGITAVYQDLALVDQ-------RNVIHNISLGNIPTkwggLVVDRKKMRETAEN-----ALSYMKAKLPSldipvsSMSG 143
Cdd:COG4598 88 RQLQRIRTRLGMVFQsfnlwshMTVLENVIEAPVHV----LGRPKAEAIERAEAllakvGLADKRDAYPA------HLSG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499272610 144 GQRQAVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRV 218
Cdd:COG4598 158 GQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRI 232
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
17-219 |
1.43e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 96.05 E-value: 1.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 17 ISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDALalgiTAVYQDLALVDQ------ 90
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNL----KKLRKKVSLVFQfpeaql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 91 --RNVIHNISLGniPTKWGGlvvdrkKMRETAENALSYMKAKLPSLDIPVSS---MSGGQRQAVAIARACASGGQLVIMD 165
Cdd:PRK13641 99 feNTVLKDVEFG--PKNFGF------SEDEAKEKALKWLKKVGLSEDLISKSpfeLSGGQMRRVAIAGVMAYEPEILCLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499272610 166 EPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVV 219
Cdd:PRK13641 171 EPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLI 224
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-201 |
2.13e-23 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 94.09 E-value: 2.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKP---TQGSVWVNGKQVHmdsARDALALG 77
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLT---ALPAEQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 78 ITAVYQDLALVDQRNVIHNISLGnIPTKWGglvvdRKKMRETAENALSymKAKLPSL-DIPVSSMSGGQRQAVAIARACA 156
Cdd:COG4136 78 IGILFQDDLLFPHLSVGENLAFA-LPPTIG-----RAQRRARVEQALE--EAGLAGFaDRDPATLSGGQRARVALLRALL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499272610 157 SGGQLVIMDEPTAAL--GIREQrmVLDVVHD-LRAHGTSVLIISHNLD 201
Cdd:COG4136 150 AEPRALLLDEPFSKLdaALRAQ--FREFVFEqIRQRGIPALLVTHDEE 195
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-219 |
2.36e-23 |
|
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: 98.22 E-value: 2.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRF-----------GHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYkPTQGSVWVNGKQVHMDSA 70
Cdd:COG4172 276 LEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 71 RDALAL--GITAVYQD-----------LALVDQRNVIHNISLgniptkwgglvvDRKKMRETAENALSymkaklpSLDIP 137
Cdd:COG4172 355 RALRPLrrRMQVVFQDpfgslsprmtvGQIIAEGLRVHGPGL------------SAAERRARVAEALE-------EVGLD 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 138 VSSM-------SGGQRQAVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDL-RAHGTSVLIISHNLDHVFEVADD 209
Cdd:COG4172 416 PAARhryphefSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLqREHGLAYLFISHDLAVVRALAHR 495
|
250
....*....|
gi 499272610 210 LLILRGGRVV 219
Cdd:COG4172 496 VMVMKDGKVV 505
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-220 |
3.54e-23 |
|
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: 96.32 E-value: 3.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVqNLTKRFGHVTAisNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGkQVHMDSARDaLAL---- 76
Cdd:COG4148 2 MLEV-DFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGG-EVLQDSARG-IFLpphr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 77 -GITAVYQDLALVDQRNVIHNISLGniptkwgglvvdrkkMRETAENAlsyMKAKLPS----------LDIPVSSMSGGQ 145
Cdd:COG4148 77 rRIGYVFQEARLFPHLSVRGNLLYG---------------RKRAPRAE---RRISFDEvvellgighlLDRRPATLSGGE 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499272610 146 RQAVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAH-GTSVLIISHNLDHVFEVADDLLILRGGRVVA 220
Cdd:COG4148 139 RQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVA 214
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-221 |
3.87e-23 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 94.75 E-value: 3.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHV---------TAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHM--DS 69
Cdd:PRK10419 3 LLNVSGLSHHYAHGglsgkhqhqTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlnRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 70 ARDALALGITAVYQD-LALVDQRNVI---------HNISLgniptkwgglvvDRKKMRETAENALSYMKAKLPSLDIPVS 139
Cdd:PRK10419 83 QRKAFRRDIQMVFQDsISAVNPRKTVreiireplrHLLSL------------DKAERLARASEMLRAVDLDDSVLDKRPP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 140 SMSGGQRQAVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAH-GTSVLIISHNLDHVFEVADDLLILRGGRV 218
Cdd:PRK10419 151 QLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
...
gi 499272610 219 VAE 221
Cdd:PRK10419 231 VET 233
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-221 |
4.16e-23 |
|
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: 93.83 E-value: 4.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFG--HVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNG---KQVHMDSARDALAL 76
Cdd:cd03251 1 VEFKNVTFRYPgdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 77 gitaVYQDLALVDQrNVIHNISLGNiptkwggLVVDRKKMRETAE--NALSYMKAKLPSLDIPV----SSMSGGQRQAVA 150
Cdd:cd03251 81 ----VSQDVFLFND-TVAENIAYGR-------PGATREEVEEAARaaNAHEFIMELPEGYDTVIgergVKLSGGQRQRIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499272610 151 IARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSvLIISHNLDHVfEVADDLLILRGGRVVAE 221
Cdd:cd03251 149 IARALLKDPPILILDEATSALDTESERLVQAALERLMKNRTT-FVIAHRLSTI-ENADRIVVLEDGKIVER 217
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
18-227 |
4.26e-23 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 94.14 E-value: 4.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 18 SNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYkPTQGSVWVNGKQV-HMDSARDA----------LALGITAVYQDLA 86
Cdd:COG4138 13 GPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLsDWSAAELArhraylsqqqSPPFAMPVFQYLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 87 LVDQRNVihnislgniptkwgglvvdrkkMRETAENALSYMKAKL---PSLDIPVSSMSGGQRQAVAIARACA------- 156
Cdd:COG4138 92 LHQPAGA----------------------SSEAVEQLLAQLAEALgleDKLSRPLTQLSGGEWQRVRLAAVLLqvwptin 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499272610 157 SGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAEVERNAV 227
Cdd:COG4138 150 PEGQLLLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEV 220
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-248 |
6.99e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 94.14 E-value: 6.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVT-AISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVhmdsarDALALGIT 79
Cdd:PRK13636 5 ILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI------DYSRKGLM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 80 AVYQDLALVDQR--------NVIHNISLGNIptkwgGLVVDRKKMRETAENALSYMKAKlPSLDIPVSSMSGGQRQAVAI 151
Cdd:PRK13636 79 KLRESVGMVFQDpdnqlfsaSVYQDVSFGAV-----NLKLPEDEVRKRVDNALKRTGIE-HLKDKPTHCLSFGQKKRVAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 152 ARACASGGQLVIMDEPTAAL---GIREqrMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAE-VERNAV 227
Cdd:PRK13636 153 AGVLVMEPKVLVLDEPTAGLdpmGVSE--IMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQgNPKEVF 230
|
250 260
....*....|....*....|.
gi 499272610 228 SHDEVVRLILAGQPRDADLEE 248
Cdd:PRK13636 231 AEKEMLRKVNLRLPRIGHLME 251
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
2-219 |
8.76e-23 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 94.65 E-value: 8.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRF----------GHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQV--HMDS 69
Cdd:PRK11308 6 LQAIDLKKHYpvkrglfkpeRLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkADPE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 70 ARDALALGITAVYQD-LALVDQRNVIHNIsLGN---IPTKwgglvVDRKKMRETAENalsyMKAKL----------PSLd 135
Cdd:PRK11308 86 AQKLLRQKIQIVFQNpYGSLNPRKKVGQI-LEEpllINTS-----LSAAERREKALA----MMAKVglrpehydryPHM- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 136 ipvssMSGGQRQAVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAH-GTSVLIISHNLDHVFEVADDLLILR 214
Cdd:PRK11308 155 -----FSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMY 229
|
....*
gi 499272610 215 GGRVV 219
Cdd:PRK11308 230 LGRCV 234
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-221 |
1.06e-22 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 93.11 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDA-------- 73
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGqlkvadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 74 ----LALGITAVYQDLALVDQRNVIHNISlgNIPTKWGGLvvDRKKMRETAENALSYMKAKLPSLDIPVSSMSGGQRQAV 149
Cdd:PRK10619 86 qlrlLRTRLTMVFQHFNLWSHMTVLENVM--EAPIQVLGL--SKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499272610 150 AIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAE 221
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEE 233
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-221 |
1.17e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 93.54 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHVT--AISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDALA-LGI 78
Cdd:PRK13635 6 IRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRqVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 79 -----------TAVYQDLALvdqrnvihniSLGNIPtkwgglvVDRKKMRETAENALSYMKAKlPSLDIPVSSMSGGQRQ 147
Cdd:PRK13635 86 vfqnpdnqfvgATVQDDVAF----------GLENIG-------VPREEMVERVDQALRQVGME-DFLNREPHRLSGGQKQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499272610 148 AVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGT-SVLIISHNLDHVFEvADDLLILRGGRVVAE 221
Cdd:PRK13635 148 RVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQ-ADRVIVMNKGEILEE 221
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-219 |
1.25e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 94.79 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDS--ARDalalgIT 79
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSiqQRD-----IC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 80 AVYQDLALVDQRNVIHNISLGnipTKWGGlvVDRKKMRETAENALsymkaKLPSL----DIPVSSMSGGQRQAVAIARAC 155
Cdd:PRK11432 82 MVFQSYALFPHMSLGENVGYG---LKMLG--VPKEERKQRVKEAL-----ELVDLagfeDRYVDQISGGQQQRVALARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499272610 156 ASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAH-GTSVLIISHNLDHVFEVADDLLILRGGRVV 219
Cdd:PRK11432 152 ILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIM 216
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
6-221 |
1.28e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 94.51 E-value: 1.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 6 NLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHmDSARDALAlGITAVYQDL 85
Cdd:PRK13536 46 GVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP-ARARLARA-RIGVVPQFD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 86 ALVDQRNVIHNIslgniptkwggLVVDRKKMRETAEnalsyMKAKLPSL----------DIPVSSMSGGQRQAVAIARAC 155
Cdd:PRK13536 124 NLDLEFTVRENL-----------LVFGRYFGMSTRE-----IEAVIPSLlefarleskaDARVSDLSGGMKRRLTLARAL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499272610 156 ASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAE 221
Cdd:PRK13536 188 INDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAE 253
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-240 |
1.29e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 96.01 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 4 VQNLTKR-FGHVtaiSNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDALALG---IT 79
Cdd:PRK09700 268 VRNVTSRdRKKV---RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGmayIT 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 80 AVYQDLALVDQRNVIHNISLGNI--PTKWGGLV--VDRKKMRETAENALSYMKAKLPSLDIPVSSMSGGQRQAVAIARAC 155
Cdd:PRK09700 345 ESRRDNGFFPNFSIAQNMAISRSlkDGGYKGAMglFHEVDEQRTAENQRELLALKCHSVNQNITELSGGNQQKVLISKWL 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 156 ASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAEVE-RNAVSHDEVVR 234
Cdd:PRK09700 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTnRDDMSEEEIMA 504
|
....*.
gi 499272610 235 LILAGQ 240
Cdd:PRK09700 505 WALPQE 510
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-219 |
1.38e-22 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 92.34 E-value: 1.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSanIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGkQVHMDSARDALALGIta 80
Cdd:PRK10771 1 MLKLTDITWLYHHLPMRFDLT--VERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG-QDHTTTPPSRRPVSM-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 81 VYQDLALVDQRNVIHNISLGNIPtkwgGLVVD---RKKMRETAEN-ALSYMKAKLPsldipvSSMSGGQRQAVAIARACA 156
Cdd:PRK10771 76 LFQENNLFSHLTVAQNIGLGLNP----GLKLNaaqREKLHAIARQmGIEDLLARLP------GQLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499272610 157 SGGQLVIMDEPTAAL--GIReQRMvLDVVHDL-RAHGTSVLIISHNLDHVFEVADDLLILRGGRVV 219
Cdd:PRK10771 146 REQPILLLDEPFSALdpALR-QEM-LTLVSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIA 209
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
16-232 |
1.99e-22 |
|
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: 91.90 E-value: 1.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 16 AISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHmDSARDALALGITAVYQDLALVdQRNVIH 95
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIR-DISRKSLRSMIGVVLQDTFLF-SGTIME 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 96 NISLGNIPTKwgglvvDRKKMRETAENALSYMKAKLPS-LDIPV----SSMSGGQRQAVAIARACASGGQLVIMDEPTAA 170
Cdd:cd03254 96 NIRLGRPNAT------DEEVIEAAKEAGAHDFIMKLPNgYDTVLgengGNLSQGERQLLAIARAMLRDPKILILDEATSN 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499272610 171 LGIREQRMVLDVVHDLRaHGTSVLIISHNLDHVFEvADDLLILRGGRVVAEvernaVSHDEV 232
Cdd:cd03254 170 IDTETEKLIQEALEKLM-KGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEE-----GTHDEL 224
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
13-221 |
2.41e-22 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 91.91 E-value: 2.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 13 HVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNG---KQVHMDSARDAlalgITAVYQDLALVD 89
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdiREVTLDSLRRA----IGVVPQDTVLFN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 90 QrNVIHNISLGniptkwgglvvdrkkmRETAENALSYMKAKLPSLDIPVSSM---------------SGGQRQAVAIARA 154
Cdd:cd03253 89 D-TIGYNIRYG----------------RPDATDEEVIEAAKAAQIHDKIMRFpdgydtivgerglklSGGEKQRVAIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499272610 155 CASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVlIISHNLDHVFEvADDLLILRGGRVVAE 221
Cdd:cd03253 152 ILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTI-VIAHRLSTIVN-ADKIIVLKDGRIVER 216
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-213 |
2.72e-22 |
|
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: 95.05 E-value: 2.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRF-GHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGkQVHMDSARDALALGITA 80
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNG-VPLADADADSWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 81 VYQDLALVDQrNVIHNISLGNiptkwggLVVDRKKMRETAENA-LSYMKAKLPS-LDIPV----SSMSGGQRQAVAIARA 154
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIRLAR-------PDASDAEIREALERAgLDEFVAALPQgLDTPIgeggAGLSGGQAQRLALARA 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499272610 155 CASGGQLVIMDEPTAALGIREQRMVLDVVHDLrAHGTSVLIISHNLdHVFEVADDLLIL 213
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRL-ALAALADRIVVL 529
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
2-219 |
3.30e-22 |
|
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: 90.30 E-value: 3.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLT-----KRFGHVTAI-SNVSANIRKGRVTALLGDNGAGKSTLVKMICG--TYKPTQGSVWVNGKQVHMDSARDA 73
Cdd:cd03213 4 LSFRNLTvtvksSPSKSGKQLlKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDKRSFRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 74 lalgitavyqdLALVDQRNVIHnislgniPTkwggLVVdrkkmRETAENAlsymkAKLPSLdipvssmSGGQRQAVAIAR 153
Cdd:cd03213 84 -----------IGYVPQDDILH-------PT----LTV-----RETLMFA-----AKLRGL-------SGGERKRVSIAL 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 154 ACASGGQLVIMDEPTAALgirEQRMVLDVVHDLRA---HGTSVLIISHNL-DHVFEVADDLLILRGGRVV 219
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGL---DSSSALQVMSLLRRladTGRTIICSIHQPsSEIFELFDKLLLLSQGRVI 191
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2-240 |
3.61e-22 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 94.73 E-value: 3.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRfghvtAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDALALGItaV 81
Cdd:PRK15439 269 LTVEDLTGE-----GFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGL--V 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 82 YqdlaLVDQRNViHNISLgNIPTKWG--GLVVDRKK--MRETAENAL--SYMKA---KLPSLDIPVSSMSGGQRQAVAIA 152
Cdd:PRK15439 342 Y----LPEDRQS-SGLYL-DAPLAWNvcALTHNRRGfwIKPARENAVleRYRRAlniKFNHAEQAARTLSGGNQQKVLIA 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 153 RACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAEVERNAVSHDEV 232
Cdd:PRK15439 416 KCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAINVDTI 495
|
....*...
gi 499272610 233 VRLILAGQ 240
Cdd:PRK15439 496 MRLAFGEH 503
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-221 |
4.70e-22 |
|
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: 89.68 E-value: 4.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGH--VTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHmdSARDALAlgit 79
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVS--DLEKALS---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 80 avyQDLALVDQRNVIHNISLGNiptkwgglvvdrkkmretaenalsymkaklpSLDIPvssMSGGQRQAVAIARACASGG 159
Cdd:cd03247 75 ---SLISVLNQRPYLFDTTLRN-------------------------------NLGRR---FSGGERQRLALARILLQDA 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499272610 160 QLVIMDEPTAALGIREQRMVLDVVHDLrAHGTSVLIISHNLDHVfEVADDLLILRGGRVVAE 221
Cdd:cd03247 118 PIVLLDEPTVGLDPITERQLLSLIFEV-LKDKTLIWITHHLTGI-EHMDKILFLENGKIIMQ 177
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
9-221 |
5.10e-22 |
|
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: 90.67 E-value: 5.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 9 KRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKqvhmDSARDALALGItavyqDLALV 88
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR----VSSLLGLGGGF-----NPELT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 89 DQRNVIHNISLGNIPTKwgglvVDRKKMRETAEnaLSYMKAklpSLDIPVSSMSGGQRQAVAIARACASGGQLVIMDEPT 168
Cdd:cd03220 101 GRENIYLNGRLLGLSRK-----EIDEKIDEIIE--FSELGD---FIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499272610 169 AALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAE 221
Cdd:cd03220 171 AVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-250 |
8.17e-22 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 90.89 E-value: 8.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNgkQVHMDSARDALALgitaV 81
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG--TAPLAEAREDTRL----M 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 82 YQDLALVDQRNVIHNISLGnIPTKWgglvvdrkkmRETAENALSYMKAKLPSLDIPvSSMSGGQRQAVAIARACASGGQL 161
Cdd:PRK11247 87 FQDARLLPWKKVIDNVGLG-LKGQW----------RDAALQALAAVGLADRANEWP-AALSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 162 VIMDEPTAALGIREQRMVLDVVHDL-RAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAEVernAVshdEVVRLILAGQ 240
Cdd:PRK11247 155 LLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDL---TV---DLPRPRRRGS 228
|
250
....*....|
gi 499272610 241 PRDADLEEEV 250
Cdd:PRK11247 229 ARLAELEAEV 238
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-250 |
1.22e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 91.69 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRF-------G--------------HVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVW 59
Cdd:COG4586 1 IIEVENLSKTYrvyekepGlkgalkglfrreyrEVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 60 VNGKQVHMDsaRDALALGITAV-------YQDLALVDQRNV---IHNISlgniptkwgglvvdrkkmRETAENALSYMKA 129
Cdd:COG4586 81 VLGYVPFKR--RKEFARRIGVVfgqrsqlWWDLPAIDSFRLlkaIYRIP------------------DAEYKKRLDELVE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 130 KL---PSLDIPVSSMSGGQRQAVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRA-HGTSVLIISHNLDHVFE 205
Cdd:COG4586 141 LLdlgELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNReRGTTILLTSHDMDDIEA 220
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 499272610 206 VADDLLILRGGRVV--AEVE--RNAVSHDEVVRLILAGQPRDADLEEEV 250
Cdd:COG4586 221 LCDRVIVIDHGRIIydGSLEelKERFGPYKTIVLELAEPVPPLELPRGG 269
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-216 |
1.69e-21 |
|
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: 89.45 E-value: 1.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 17 ISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMD-----------------SARDALALGIT 79
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPgpdrmvvfqnysllpwlTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 80 AVYQDLALVDQRNVI-HNISLGNiptkwgglvvdrkkMRETAENalsymkaklpsldiPVSSMSGGQRQAVAIARACASG 158
Cdd:TIGR01184 81 RVLPDLSKSERRAIVeEHIALVG--------------LTEAADK--------------RPGQLSGGMKQRVAIARALSIR 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499272610 159 GQLVIMDEPTAALG--IRE--QRMVLDVVHDlraHGTSVLIISHNLDHVFEVADDLLILRGG 216
Cdd:TIGR01184 133 PKVLLLDEPFGALDalTRGnlQEELMQIWEE---HRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
26-221 |
1.96e-21 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 89.14 E-value: 1.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 26 KGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQvhmdSARDALALGITAVYQDLAL---VDQRNVIHNISLGNI 102
Cdd:TIGR03771 5 KGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGAS----PGKGWRHIGYVPQRHEFAWdfpISVAHTVMSGRTGHI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 103 ptkwgGLVvDRKKMRETAENALSYMKAKLPSL-DIPVSSMSGGQRQAVAIARACASGGQLVIMDEPTAALGIREQRMVLD 181
Cdd:TIGR03771 81 -----GWL-RRPCVADFAAVRDALRRVGLTELaDRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499272610 182 VVHDLRAHGTSVLIISHNLDHVFEVADDLLILrGGRVVAE 221
Cdd:TIGR03771 155 LFIELAGAGTAILMTTHDLAQAMATCDRVVLL-NGRVIAD 193
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-242 |
2.92e-21 |
|
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: 92.12 E-value: 2.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRF--GHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHmDSARDALALGIT 79
Cdd:COG4618 331 LSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLS-QWDREELGRHIG 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 80 AVYQDLALVDQRnVIHNIS-LGNiptkwgglvVDRKKMRETAENA-LSYMKAKLPS-LDIPV----SSMSGGQRQAVAIA 152
Cdd:COG4618 410 YLPQDVELFDGT-IAENIArFGD---------ADPEKVVAAAKLAgVHEMILRLPDgYDTRIgeggARLSGGQRQRIGLA 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 153 RACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLdHVFEVADDLLILRGGRVVAEVERnavshDEV 232
Cdd:COG4618 480 RALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGPR-----DEV 553
|
250
....*....|
gi 499272610 233 VRLILAGQPR 242
Cdd:COG4618 554 LARLARPAAA 563
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-227 |
3.19e-21 |
|
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: 88.99 E-value: 3.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQG-SVWVNGKQVHMDSARDaL--ALG 77
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWE-LrkRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 78 ItaVYQDLAL---VDQ--RNVIhnISlGniptKWGGLVVDRK---KMRETAENALSYMK-AKLpsLDIPVSSMSGGQRQA 148
Cdd:COG1119 82 L--VSPALQLrfpRDEtvLDVV--LS-G----FFDSIGLYREptdEQRERARELLELLGlAHL--ADRPFGTLSQGEQRR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 149 VAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHG-TSVLIISHNLDHVFEVADDLLILRGGRVVAEVERNAV 227
Cdd:COG1119 151 VLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
17-219 |
5.11e-21 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 91.54 E-value: 5.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 17 ISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQvhmdsaRDALALGITAvyQDLALVDQR----- 91
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIP------REEIPREVLA--NSVAMVDQDiflfe 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 92 -NVIHNISLgniptkWGGLVVDRKKMRETAENALSYMKAKLP-SLDIPV----SSMSGGQRQAVAIARACASGGQLVIMD 165
Cdd:TIGR03796 567 gTVRDNLTL------WDPTIPDADLVRACKDAAIHDVITSRPgGYDAELaeggANLSGGQRQRLEIARALVRNPSILILD 640
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499272610 166 EPTAALGIREQRMVLDvvhDLRAHGTSVLIISHNLDHVFEvADDLLILRGGRVV 219
Cdd:TIGR03796 641 EATSALDPETEKIIDD---NLRRRGCTCIIVAHRLSTIRD-CDEIIVLERGKVV 690
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1-235 |
6.29e-21 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 90.94 E-value: 6.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRfgHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDALALGI-- 78
Cdd:PRK10982 250 ILEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHGFal 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 79 -------TAVYQDLAlVDQRNVIHNISlgNIPTKWGGLvvDRKKMRETAENALSYMKAKLPSLDIPVSSMSGGQRQAVAI 151
Cdd:PRK10982 328 vteerrsTGIYAYLD-IGFNSLISNIR--NYKNKVGLL--DNSRMKSDTQWVIDSMRVKTPGHRTQIGSLSGGNQQKVII 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 152 ARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAEVERNAVSHDE 231
Cdd:PRK10982 403 GRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGIVDTKTTTQNE 482
|
....
gi 499272610 232 VVRL 235
Cdd:PRK10982 483 ILRL 486
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-227 |
6.48e-21 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 88.27 E-value: 6.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNgkQVHMDSARD-------- 72
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVG--DITIDTARSlsqqkgli 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 73 -ALALGITAVYQDLALVDQRNVIHNISLGNiptkwgglVVDRKKMRETAENALSYMKAKLP---SLDIPVSSMSGGQRQA 148
Cdd:PRK11264 81 rQLRQHVGFVFQNFNLFPHRTVLENIIEGP--------VIVKGEPKEEATARARELLAKVGlagKETSYPRRLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499272610 149 VAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAEVERNAV 227
Cdd:PRK11264 153 VAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-222 |
8.66e-21 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 87.56 E-value: 8.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFG----HVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDALAL 76
Cdd:PRK11629 5 LLQCDNLCKRYQegsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 77 ---GITAVYQDLALVDQRNVIHNISLgniPTKWGGlvVDRKKMRETAENALSYMKAKLPSLDIPvSSMSGGQRQAVAIAR 153
Cdd:PRK11629 85 rnqKLGFIYQFHHLLPDFTALENVAM---PLLIGK--KKPAEINSRALEMLAAVGLEHRANHRP-SELSGGERQRVAIAR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499272610 154 ACASGGQLVIMDEPTAALGIREQRMVLDVVHDL-RAHGTSVLIISHNLdhvfEVADDL---LILRGGRVVAEV 222
Cdd:PRK11629 159 ALVNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDL----QLAKRMsrqLEMRDGRLTAEL 227
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-249 |
1.06e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 88.21 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVT-AISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSArdalalGIT 79
Cdd:PRK13639 1 ILETRDLKYSYPDGTeALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKK------SLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 80 AVYQDLALVDQR--------NVIHNISLGNIPTKWGGLVVDRKKMRETAENALSYMKAKLPSldipvsSMSGGQRQAVAI 151
Cdd:PRK13639 75 EVRKTVGIVFQNpddqlfapTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPH------HLSGGQKKRVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 152 ARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAE-VERNAVSHD 230
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEgTPKEVFSDI 228
|
250
....*....|....*....
gi 499272610 231 EVVRLILAGQPRDADLEEE 249
Cdd:PRK13639 229 ETIRKANLRLPRVAHLIEI 247
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-203 |
1.23e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.12 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 4 VQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGkqvhmdsardalalGITAVY- 82
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK--------------GLRIGYl 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 83 -QDLALVDQRNVIHNISLGNiptkwGGLVVDRKKMRE--------------------------------TAENALSYMKA 129
Cdd:COG0488 67 pQEPPLDDDLTVLDTVLDGD-----AELRALEAELEEleaklaepdedlerlaelqeefealggweaeaRAEEILSGLGF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 130 KLPSLDIPVSSMSGGQRQAVAIARACASGGQLVIMDEPTAAL---GIR--EQRmvldvvhdLRAHGTSVLIISHN---LD 201
Cdd:COG0488 142 PEEDLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLdleSIEwlEEF--------LKNYPGTVLVVSHDryfLD 213
|
..
gi 499272610 202 HV 203
Cdd:COG0488 214 RV 215
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-221 |
1.37e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 88.32 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDALALGITAV 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 82 YQDLAlvDQRNVIHNISlgnIPTKWGGLvvDRKKMRETAENALSYmkAKLPS-LDIPVSSMSGGQRQAVAIARACASGGQ 160
Cdd:PRK13537 88 FDNLD--PDFTVRENLL---VFGRYFGL--SAAAARALVPPLLEF--AKLENkADAKVGELSGGMKRRLTLARALVNDPD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499272610 161 LVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAE 221
Cdd:PRK13537 159 VLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAE 219
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-220 |
1.66e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 90.17 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRF----GHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQV-HMDSarDALA 75
Cdd:PRK10535 4 LLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVaTLDA--DALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 76 ------LGItaVYQDLALVDQRNVIHNISlgnIPTKWGGLvvDRKKMRETAENALSYMKAKlPSLDIPVSSMSGGQRQAV 149
Cdd:PRK10535 82 qlrrehFGF--IFQRYHLLSHLTAAQNVE---VPAVYAGL--ERKQRLLRAQELLQRLGLE-DRVEYQPSQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499272610 150 AIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNlDHVFEVADDLLILRGGRVVA 220
Cdd:PRK10535 154 SIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEIVR 223
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-219 |
1.67e-20 |
|
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: 90.13 E-value: 1.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGH----VTAISNVSANIRKGRVTALLGDNGAGKS----TLVKMICGTYKPTQGSVWVNGKQVHMDSARD 72
Cdd:COG4172 6 LLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 73 ALAL---GITAVYQD--LALvdqrNVIHNIS--LGNIPTKWGGLvvDRKKMRETAENALSymKAKLPSLDIPVSS----M 141
Cdd:COG4172 86 LRRIrgnRIAMIFQEpmTSL----NPLHTIGkqIAEVLRLHRGL--SGAAARARALELLE--RVGIPDPERRLDAyphqL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499272610 142 SGGQRQAVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRA-HGTSVLIISHNLDHVFEVADDLLILRGGRVV 219
Cdd:COG4172 158 SGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQReLGMALLLITHDLGVVRRFADRVAVMRQGEIV 236
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-250 |
2.39e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 87.35 E-value: 2.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVT-AISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGkqvhMDSARDALALGIT 79
Cdd:PRK13644 1 MIRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG----IDTGDFSKLQGIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 80 AVyqdLALVDQ--------RNVIHNISLG--NI---PTKWgglvvdRKKM-RETAENALSYMKAKLPsldipvSSMSGGQ 145
Cdd:PRK13644 77 KL---VGIVFQnpetqfvgRTVEEDLAFGpeNLclpPIEI------RKRVdRALAEIGLEKYRHRSP------KTLSGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 146 RQAVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVfEVADDLLILRGGRVVAEVERN 225
Cdd:PRK13644 142 GQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPE 220
|
250 260
....*....|....*....|....*
gi 499272610 226 AVSHDEVVRLILAGQPRDADLEEEV 250
Cdd:PRK13644 221 NVLSDVSLQTLGLTPPSLIELAENL 245
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-219 |
5.33e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 88.61 E-value: 5.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRF-----------GHVTAISNVSANIRKGRVTALLGDNGAGKST----LVKMIcgtykPTQGSVWVNGKQV 65
Cdd:PRK15134 275 LLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 66 HMDSARDALAL--GITAVYQD--LALVDQRNVIHNISLG---NIPTKWGGLVVDR--KKMRETAENALSymKAKLPSldi 136
Cdd:PRK15134 350 HNLNRRQLLPVrhRIQVVFQDpnSSLNPRLNVLQIIEEGlrvHQPTLSAAQREQQviAVMEEVGLDPET--RHRYPA--- 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 137 pvsSMSGGQRQAVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRA-HGTSVLIISHNLDHVFEVADDLLILRG 215
Cdd:PRK15134 425 ---EFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQkHQLAYLFISHDLHVVRALCHQVIVLRQ 501
|
....
gi 499272610 216 GRVV 219
Cdd:PRK15134 502 GEVV 505
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-219 |
6.12e-20 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 85.45 E-value: 6.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMD---SARDALAL-- 76
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSqkpSEKAIRLLrq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 77 GITAVYQDLALVDQRNVIHNisLGNIPTKWGGLVvdRKKMRETAENALSYMKAKLPSLDIPVSsMSGGQRQAVAIARACA 156
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMEN--LIEAPCKVLGLS--KEQAREKAMKLLARLRLTDKADRFPLH-LSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499272610 157 SGGQLVIMDEPTAAL--GIREQrmVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVV 219
Cdd:COG4161 158 MEPQVLLFDEPTAALdpEITAQ--VVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRII 220
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-219 |
6.47e-20 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 85.86 E-value: 6.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYK--P---TQGSVWVNGKQVHmDSARDalal 76
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDIY-DPDVD---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 77 gITAVYQDLALVDQR----------NV-----IHNISlgniptkwgglvvDRKKMRETAENALSymKAKLPS-----LDI 136
Cdd:COG1117 87 -VVELRRRVGMVFQKpnpfpksiydNVayglrLHGIK-------------SKSELDEIVEESLR--KAALWDevkdrLKK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 137 PVSSMSGGQRQAVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTsVLIISHNLDHVFEVADDLLILRGG 216
Cdd:COG1117 151 SALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYT-IVIVTHNMQQAARVSDYTAFFYLG 229
|
...
gi 499272610 217 RVV 219
Cdd:COG1117 230 ELV 232
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-226 |
7.47e-20 |
|
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: 85.18 E-value: 7.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRF----GHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVH-MDsaRDALA 75
Cdd:COG4181 8 IIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFaLD--EDARA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 76 ------LGItaVYQDLALVDQRNVIHNISLgniPTKWGGlvvdRKKMRETAENALSYM--KAKL---PSldipvsSMSGG 144
Cdd:COG4181 86 rlrarhVGF--VFQSFQLLPTLTALENVML---PLELAG----RRDARARARALLERVglGHRLdhyPA------QLSGG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 145 QRQAVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDL-RAHGTSVLIISHNLdhvfEVA---DDLLILRGGRVVA 220
Cdd:COG4181 151 EQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELnRERGTTLVLVTHDP----ALAarcDRVLRLRAGRLVE 226
|
....*.
gi 499272610 221 EVERNA 226
Cdd:COG4181 227 DTAATA 232
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
16-222 |
9.03e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 85.99 E-value: 9.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 16 AISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHmDSARDALalgITAVYQDLALVDQ----- 90
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIT-HKTKDKY---IRPVRKRIGMVFQfpesq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 91 ---RNVIHNISLGniPTKWGglvVDRKKMRETAENALsyMKAKLPSlDIPVSS---MSGGQRQAVAIARACASGGQLVIM 164
Cdd:PRK13646 98 lfeDTVEREIIFG--PKNFK---MNLDEVKNYAHRLL--MDLGFSR-DVMSQSpfqMSGGQMRKIAIVSILAMNPDIIVL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499272610 165 DEPTAALGIREQRMVLDVVHDLRA-HGTSVLIISHNLDHVFEVADDLLILRGGRVVAEV 222
Cdd:PRK13646 170 DEPTAGLDPQSKRQVMRLLKSLQTdENKTIILVSHDMNEVARYADEVIVMKEGSIVSQT 228
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
16-219 |
1.05e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 85.57 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 16 AISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDAlalgITAVYQDLALVDQ----- 90
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKD----IKQIRKKVGLVFQfpesq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 91 ---RNVIHNISLGniPTKWGglvVDRKKMRETAENALSYMKAKLPSLDIPVSSMSGGQRQAVAIARACASGGQLVIMDEP 167
Cdd:PRK13649 98 lfeETVLKDVAFG--PQNFG---VSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499272610 168 TAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVV 219
Cdd:PRK13649 173 TAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
17-236 |
1.12e-19 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 87.54 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 17 ISNVSANIRKGRVTALLGDNGAGKSTLVKMICG-TY-KPTQGSVWVNGKQVHMDSARDALALGITAVYQD---LALVDQR 91
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGrSYgRNISGTVFKDGKEVDVSTVSDAIDAGLAYVTEDrkgYGLNLID 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 92 NVIHNISLGNIPTKWGGLVVDRKKMRETAENALSYMKAKLPSLDIPVSSMSGGQRQAVAIARACASGGQLVIMDEPTAal 171
Cdd:NF040905 356 DIKRNITLANLGKVSRRGVIDENEEIKVAEEYRKKMNIKTPSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTR-- 433
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499272610 172 GIreqrmvlDV---------VHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAEVERNAVSHDEVVRLI 236
Cdd:NF040905 434 GI-------DVgakyeiytiINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRITGELPREEASQERIMRLI 500
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-226 |
1.12e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 85.48 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTkrfgHV---------TAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNG-----KQVHM 67
Cdd:PRK13637 3 IKIENLT----HIymegtpfekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdKKVKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 68 DSARDALalGITAVYQDLALVDQrNVIHNISLGniPTKWGgLVVD--RKKMRETAEN-ALSY--MKAKLPSldipvsSMS 142
Cdd:PRK13637 79 SDIRKKV--GLVFQYPEYQLFEE-TIEKDIAFG--PINLG-LSEEeiENRVKRAMNIvGLDYedYKDKSPF------ELS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 143 GGQRQAVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDL-RAHGTSVLIISHNLDHVFEVADDLLILRGGRVV-- 219
Cdd:PRK13637 147 GGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELhKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCElq 226
|
250
....*....|
gi 499272610 220 ---AEVERNA 226
Cdd:PRK13637 227 gtpREVFKEV 236
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
32-219 |
1.34e-19 |
|
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: 86.01 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 32 LLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVhmdSARDALALGITAVYQDLALVDQRNVIHNISLgniPTKWGGlvV 111
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDV---TNVPPHLRHINMVFQSYALFPHMTVEENVAF---GLKMRK--V 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 112 DRKKMRETAENALSY-----MKAKLPSldipvsSMSGGQRQAVAIARACASGGQLVIMDEPTAALG--IREQrMVLDVVH 184
Cdd:TIGR01187 73 PRAEIKPRVLEALRLvqleeFADRKPH------QLSGGQQQRVALARALVFKPKILLLDEPLSALDkkLRDQ-MQLELKT 145
|
170 180 190
....*....|....*....|....*....|....*
gi 499272610 185 DLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVV 219
Cdd:TIGR01187 146 IQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIA 180
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-219 |
1.37e-19 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 84.16 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRF-GHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDA--LALG 77
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVpfLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 78 ITAVYQDLALVDQRNVIHNISlgnIPTKWGGLVVDRKKMRETAenALSYMKAKLPSLDIPVsSMSGGQRQAVAIARACAS 157
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVA---IPLIIAGASGDDIRRRVSA--ALDKVGLLDKAKNFPI-QLSGGEQQRVGIARAVVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499272610 158 GGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVV 219
Cdd:PRK10908 155 KPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
16-220 |
1.45e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 85.56 E-value: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 16 AISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWV-------NGKQVHMDSARDALalGITAVYQDLALV 88
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvssTSKQKEIKPVRKKV--GVVFQFPESQLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 89 DQrNVIHNISLGniPTKWGglvVDRKKMRETAENALSYMKAKLPSLDIPVSSMSGGQRQAVAIARACASGGQLVIMDEPT 168
Cdd:PRK13643 99 EE-TVLKDVAFG--PQNFG---IPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499272610 169 AALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVA 220
Cdd:PRK13643 173 AGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIIS 224
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
21-218 |
1.89e-19 |
|
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: 83.76 E-value: 1.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 21 SANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQvHMDSArdALALGITAVYQDLALVDQRNVIHNISLG 100
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQS-HTGLA--PYQRPVSMLFQENNLFAHLTVRQNIGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 101 NIPtkwgGL---VVDRKKMRETAEN-ALSYMKAKLPSldipvsSMSGGQRQAVAIARACASGGQLVIMDEPTAAL--GIR 174
Cdd:TIGR01277 95 LHP----GLklnAEQQEKVVDAAQQvGIADYLDRLPE------QLSGGQRQRVALARCLVRPNPILLLDEPFSALdpLLR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499272610 175 EQRMVLdVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRV 218
Cdd:TIGR01277 165 EEMLAL-VKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
24-219 |
2.57e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 86.70 E-value: 2.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 24 IRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVhmdSARDALALgitavYQDLALVDQ------RNVIHNI 97
Cdd:TIGR00958 504 LHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPL---VQYDHHYL-----HRQVALVGQepvlfsGSVRENI 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 98 SLGniptkwgglvVDRKKMRET-----AENALSYMKAKLPSLDIPV----SSMSGGQRQAVAIARACASGGQLVIMDEPT 168
Cdd:TIGR00958 576 AYG----------LTDTPDEEImaaakAANAHDFIMEFPNGYDTEVgekgSQLSGGQKQRIAIARALVRKPRVLILDEAT 645
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499272610 169 AALGIREQRMVLDvvhDLRAHGTSVLIISHNLdHVFEVADDLLILRGGRVV 219
Cdd:TIGR00958 646 SALDAECEQLLQE---SRSRASRTVLLIAHRL-STVERADQILVLKKGSVV 692
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-198 |
2.70e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 82.69 E-value: 2.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSArdalalgitA 80
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLC---------T 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 81 VYQDLALVDQRNVIH-NISLG-----NIPTKWGGLVVDRkkmretaenaLSYMKAKLPSLDIPVSSMSGGQRQAVAIARA 154
Cdd:PRK13540 72 YQKQLCFVGHRSGINpYLTLRenclyDIHFSPGAVGITE----------LCRLFSLEHLIDYPCGLLSSGQKRQVALLRL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499272610 155 CASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISH 198
Cdd:PRK13540 142 WMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-221 |
3.43e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 84.08 E-value: 3.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRF-GHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDALALgIT 79
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKF-VG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 80 AVYQDLAlvDQ---RNVIHNISLGniPTKWGglvVDRKKMRETAENALSYMKAKLPSLDIPvSSMSGGQRQAVAIARACA 156
Cdd:PRK13652 82 LVFQNPD--DQifsPTVEQDIAFG--PINLG---LDEETVAHRVSSALHMLGLEELRDRVP-HHLSGGEKKRVAIAGVIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499272610 157 SGGQLVIMDEPTAALGIREQRMVLDVVHDL-RAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAE 221
Cdd:PRK13652 154 MEPQVLVLDEPTAGLDPQGVKELIDFLNDLpETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAY 219
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
10-219 |
3.78e-19 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 86.17 E-value: 3.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 10 RFGHVT--------AISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHmDSARDALALGITAV 81
Cdd:PRK13657 336 EFDDVSfsydnsrqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIR-TVTRASLRRNIAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 82 YQDLALVDqRNVIHNISLGNiPTkwgglvVDRKKMRETAE--NALSYMKAKLPSLDIPV----SSMSGGQRQAVAIARAC 155
Cdd:PRK13657 415 FQDAGLFN-RSIEDNIRVGR-PD------ATDEEMRAAAEraQAHDFIERKPDGYDTVVgergRQLSGGERQRLAIARAL 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499272610 156 ASGGQLVIMDEPTAALGIREQRMVLDVVHDLRaHGTSVLIISHNLDHVFEvADDLLILRGGRVV 219
Cdd:PRK13657 487 LKDPPILILDEATSALDVETEAKVKAALDELM-KGRTTFIIAHRLSTVRN-ADRILVFDNGRVV 548
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-221 |
4.37e-19 |
|
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: 82.19 E-value: 4.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICG--TYKPTQGSVWVNGKQVHMDSARDALALGIT 79
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGEDITDLPPEERARLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 80 AVYQDlalvdqrnvihnislgniPTKWGGLvvdrkkmreTAENALSYMKAKLpsldipvssmSGGQRQAVAIARACASGG 159
Cdd:cd03217 81 LAFQY------------------PPEIPGV---------KNADFLRYVNEGF----------SGGEKKRNEILQLLLLEP 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499272610 160 QLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHN---LDHVfeVADDLLILRGGRVVAE 221
Cdd:cd03217 124 DLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYqrlLDYI--KPDRVHVLYDGRIVKS 186
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
15-221 |
7.49e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 83.21 E-value: 7.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 15 TAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGkqvhMDSARDALALGITA----VYQ--DLALV 88
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG----LDTSDEENLWDIRNkagmVFQnpDNQIV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 89 dQRNVIHNISLGniPTKWGglvVDRKKMRETAENAL-----SYMKAKLPSLdipvssMSGGQRQAVAIARACASGGQLVI 163
Cdd:PRK13633 100 -ATIVEEDVAFG--PENLG---IPPEEIRERVDESLkkvgmYEYRRHAPHL------LSGGQKQRVAIAGILAMRPECII 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499272610 164 MDEPTAALGIREQRMVLDVVHDL-RAHGTSVLIISHNLDHVFEvADDLLILRGGRVVAE 221
Cdd:PRK13633 168 FDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVME 225
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-219 |
7.86e-19 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 82.37 E-value: 7.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDALAlgITAV 81
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDKA--IREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 82 YQDLALVDQR-------NVIHNisLGNIPTKWGGLvvDRKKMRETAENALSYMKAKLPSLDIPVSsMSGGQRQAVAIARA 154
Cdd:PRK11124 81 RRNVGMVFQQynlwphlTVQQN--LIEAPCRVLGL--SKDQALARAEKLLERLRLKPYADRFPLH-LSGGQQQRVAIARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499272610 155 CASGGQLVIMDEPTAALG--IREQrmVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVV 219
Cdd:PRK11124 156 LMMEPQVLLFDEPTAALDpeITAQ--IVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIV 220
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-208 |
8.94e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 82.91 E-value: 8.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVK-------MICGTYkpTQGSVWVNGKQVHmDSARDAL 74
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFR--VEGKVTFHGKNLY-APDVDPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 75 AlgitaVYQDLALVDQR------NVIHNISLGnipTKWGGLVVDrkkMRETAENALSY------MKAKLPSLDIpvsSMS 142
Cdd:PRK14243 88 E-----VRRRIGMVFQKpnpfpkSIYDNIAYG---ARINGYKGD---MDELVERSLRQaalwdeVKDKLKQSGL---SLS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499272610 143 GGQRQAVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTsVLIISHNLDHVFEVAD 208
Cdd:PRK14243 154 GGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYT-IIIVTHNMQQAARVSD 218
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
16-218 |
1.01e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 82.88 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 16 AISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDalalgitaVYQDLALVDQRNviH 95
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEK--------LRKHIGIVFQNP--D 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 96 NISLGNIpTKWG---GL---VVDRKKMRETAENALSYMKAkLPSLDIPVSSMSGGQRQAVAIARACASGGQLVIMDEPTA 169
Cdd:PRK13648 94 NQFVGSI-VKYDvafGLenhAVPYDEMHRRVSEALKQVDM-LERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATS 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499272610 170 ALGIREQRMVLDVVHDLRA-HGTSVLIISHNLDHVFEvADDLLILRGGRV 218
Cdd:PRK13648 172 MLDPDARQNLLDLVRKVKSeHNITIISITHDLSEAME-ADHVIVMNKGTV 220
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-203 |
1.27e-18 |
|
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: 84.60 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVnGKQVHM---DSARDALAlgi 78
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKLayvDQSRDALD--- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 79 tavyqdlalvDQRNVIHNISLGNIPTKWGGlvvdrkkmRETAENA-LSYMKAKLPSLDIPVSSMSGGQRQAVAIARACAS 157
Cdd:TIGR03719 399 ----------PNKTVWEEISGGLDIIKLGK--------REIPSRAyVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKS 460
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499272610 158 GGQLVIMDEPTAALGIREQRMVLDVvhdLRAHGTSVLIISHN---LDHV 203
Cdd:TIGR03719 461 GGNVLLLDEPTNDLDVETLRALEEA---LLNFAGCAVVISHDrwfLDRI 506
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
19-219 |
1.31e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 84.51 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 19 NVSANIRKGRVTALLGDNGAGKSTLVKMICGtYKPTQGSVWVNG---KQVHMDSARDALA-LGitavyQDLALVDQrNVI 94
Cdd:PRK11174 368 PLNFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKINGielRELDPESWRKHLSwVG-----QNPQLPHG-TLR 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 95 HNISLGNIPtkwgglvVDRKKMRETAENA-LSYMKAKLPS-LDIPVS----SMSGGQRQAVAIARACASGGQLVIMDEPT 168
Cdd:PRK11174 441 DNVLLGNPD-------ASDEQLQQALENAwVSEFLPLLPQgLDTPIGdqaaGLSVGQAQRLALARALLQPCQLLLLDEPT 513
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499272610 169 AALGIREQRMVLDVVHDLrAHGTSVLIISHNLDHVFEVaDDLLILRGGRVV 219
Cdd:PRK11174 514 ASLDAHSEQLVMQALNAA-SRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIV 562
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-213 |
2.22e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 81.31 E-value: 2.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKqvhmdsardalaLGITA 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK------------LRIGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 81 VYQDLALvdqrnvihNISLgniptkwgGLVVDRKKM------RETAENALSYMKAKlPSLDIPVSSMSGGQRQAVAIARA 154
Cdd:PRK09544 72 VPQKLYL--------DTTL--------PLTVNRFLRlrpgtkKEDILPALKRVQAG-HLIDAPMQKLSGGETQRVLLARA 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 155 CASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAH-GTSVLIISHNLDHVFEVADDLLIL 213
Cdd:PRK09544 135 LLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCL 194
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
2-221 |
2.72e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 80.88 E-value: 2.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICG--TYKPTQGSVWVNGKQV-HMDS---ARDALA 75
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSILLDGEDIlELSPderARAGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 76 L---------GITAvyqdlalvdqRNVIHnISLGNIPTKWGGLVVDRKKMRETAEnALSyMKAKLpsLDIPV-SSMSGGQ 145
Cdd:COG0396 81 LafqypveipGVSV----------SNFLR-TALNARRGEELSAREFLKLLKEKMK-ELG-LDEDF--LDRYVnEGFSGGE 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499272610 146 RQAVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHN---LDHVfeVADDLLILRGGRVVAE 221
Cdd:COG0396 146 KKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYqriLDYI--KPDFVHVLVDGRIVKS 222
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-240 |
3.07e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 81.09 E-value: 3.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDALALGITAV 81
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 82 YQDLALVDQRNVIHNisLGNIPTKWGGLVVDRKKMRET---AENALSYMKAKLPSldipvsSMSGGQRQAVAIARACASG 158
Cdd:PRK10895 84 PQEASIFRRLSVYDN--LMAVLQIRDDLSAEQREDRANelmEEFHIEHLRDSMGQ------SLSGGERRRVEIARALAAN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 159 GQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAEVERNAVSHDEVVRLILA 238
Cdd:PRK10895 156 PKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYL 235
|
..
gi 499272610 239 GQ 240
Cdd:PRK10895 236 GE 237
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
7-215 |
3.13e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 81.47 E-value: 3.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 7 LTKRFGHvTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVhmdsaRDALALGITAVYQDLA 86
Cdd:PRK15056 14 VTWRNGH-TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT-----RQALQKNLVAYVPQSE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 87 LVDQR--NVIHNISLGNIPTKWGGLVVDRKKMRETAENALsymkAKLPSLDI---PVSSMSGGQRQAVAIARACASGGQL 161
Cdd:PRK15056 88 EVDWSfpVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAAL----ARVDMVEFrhrQIGELSGGQKKRVFLARAIAQQGQV 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499272610 162 VIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRG 215
Cdd:PRK15056 164 ILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKG 217
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-221 |
3.27e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 81.11 E-value: 3.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKM---ICGTYKPTQ--GSVWVNGKQV-HMDSARdaLA 75
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrLIELYPEARvsGEVYLDGQDIfKMDVIE--LR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 76 LGITAVYQDLALVDQRNVIHNISLGnipTKWGGLVVDRKKMRETAENALSymKAKL-----PSLDIPVSSMSGGQRQAVA 150
Cdd:PRK14247 82 RRVQMVFQIPNPIPNLSIFENVALG---LKLNRLVKSKKELQERVRWALE--KAQLwdevkDRLDAPAGKLSGGQQQRLC 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499272610 151 IARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLiISHNLDHVFEVADDLLILRGGRVVAE 221
Cdd:PRK14247 157 IARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVL-VTHFPQQAARISDYVAFLYKGQIVEW 226
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
13-231 |
3.94e-18 |
|
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: 80.66 E-value: 3.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 13 HVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNG---KQVHMDSARDALALgitaVYQDLALVD 89
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGvdiRDLNLRWLRSQIGL----VSQEPVLFD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 90 qRNVIHNISLGniptKWGGLVVDRKKMRETAeNALSYMkAKLP-SLDIPV----SSMSGGQRQAVAIARACASGGQLVIM 164
Cdd:cd03249 91 -GTIAENIRYG----KPDATDEEVEEAAKKA-NIHDFI-MSLPdGYDTLVgergSQLSGGQKQRIAIARALLRNPKILLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499272610 165 DEPTAALGIREQRMVLDVVHDLRAhGTSVLIISHNLDHVfEVADDLLILRGGRVvaeVERNavSHDE 231
Cdd:cd03249 164 DEATSALDAESEKLVQEALDRAMK-GRTTIVIAHRLSTI-RNADLIAVLQNGQV---VEQG--THDE 223
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-218 |
4.10e-18 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 82.30 E-value: 4.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSA--RDalalgIT 79
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAenRH-----VN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 80 AVYQDLALVDQRNVIHNISLGNIPTKwgglvVDRKKMRETAENALSYMkaKLPSL-DIPVSSMSGGQRQAVAIARACASG 158
Cdd:PRK09452 90 TVFQSYALFPHMTVFENVAFGLRMQK-----TPAAEITPRVMEALRMV--QLEEFaQRKPHQLSGGQQQRVAIARAVVNK 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499272610 159 GQLVIMDEPTAALG--IREQrMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRV 218
Cdd:PRK09452 163 PKVLLLDESLSALDykLRKQ-MQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRI 223
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
16-220 |
7.22e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 80.83 E-value: 7.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 16 AISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWV-------NGKQVHMDSARDALalGITAVYQDLALV 88
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitaGKKNKKLKPLRKKV--GIVFQFPEHQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 89 DQrNVIHNISLGniPTKWGglvVDRKKMRETAENALsymkaKLPSLDIPVSS-----MSGGQRQAVAIARACASGGQLVI 163
Cdd:PRK13634 100 EE-TVEKDICFG--PMNFG---VSEEDAKQKAREMI-----ELVGLPEELLArspfeLSGGQMRRVAIAGVLAMEPEVLV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499272610 164 MDEPTAALGIREQRMVLDVVHDL-RAHGTSVLIISHNLDHVFEVADDLLILRGGRVVA 220
Cdd:PRK13634 169 LDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFL 226
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-221 |
7.38e-18 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 80.26 E-value: 7.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKM----ICGTYKP----TQGSVWVNGKQVHmdsARD 72
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKAlagdLTGGGAPrgarVTGDVTLNGEPLA---AID 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 73 ALALG-ITAVyqdLALVDQR----NVIHNISLGNIPTKWGGLVVDRKKmRETAENALSYMKAKlPSLDIPVSSMSGGQRQ 147
Cdd:PRK13547 78 APRLArLRAV---LPQAAQPafafSAREIVLLGRYPHARRAGALTHRD-GEIAWQALALAGAT-ALVGRDVTTLSGGELA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 148 AVAIARACA---------SGGQLVIMDEPTAALGIREQRMVLDVVHDL-RAHGTSVLIISHNLDHVFEVADDLLILRGGR 217
Cdd:PRK13547 153 RVQFARVLAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLaRDWNLGVLAIVHDPNLAARHADRIAMLADGA 232
|
....
gi 499272610 218 VVAE 221
Cdd:PRK13547 233 IVAH 236
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-245 |
7.42e-18 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 80.22 E-value: 7.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRF---------GHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMD--- 68
Cdd:PRK15112 4 LLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGdys 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 69 --SARdalalgITAVYQDLAL-VDQRNVIHNISlgNIPTKwggLVVDRKKM-RETAENALSYMKAKLPSLDIPVSSM-SG 143
Cdd:PRK15112 84 yrSQR------IRMIFQDPSTsLNPRQRISQIL--DFPLR---LNTDLEPEqREKQIIETLRQVGLLPDHASYYPHMlAP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 144 GQRQAVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRA-HGTSVLIISHNLDHVFEVADDLLILRGGRVvaeV 222
Cdd:PRK15112 153 GQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHLGMMKHISDQVLVMHQGEV---V 229
|
250 260 270
....*....|....*....|....*....|..
gi 499272610 223 ERNAVS-------HDEVVRLILA--GQPRDAD 245
Cdd:PRK15112 230 ERGSTAdvlasplHELTKRLIAGhfGEALTAD 261
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
2-227 |
7.95e-18 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 82.40 E-value: 7.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKR--FGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNG---KQVHmdsaRDALAL 76
Cdd:TIGR01842 317 LSVENVTIVppGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGadlKQWD----RETFGK 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 77 GITAVYQDLALVDQrNVIHNISLGniptkwgGLVVDRKKMRETAENALSY-MKAKLPS---LDIPV--SSMSGGQRQAVA 150
Cdd:TIGR01842 393 HIGYLPQDVELFPG-TVAENIARF-------GENADPEKIIEAAKLAGVHeLILRLPDgydTVIGPggATLSGGQRQRIA 464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499272610 151 IARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDhVFEVADDLLILRGGRVVAEVERNAV 227
Cdd:TIGR01842 465 LARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPS-LLGCVDKILVLQDGRIARFGERDEV 540
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1-220 |
1.24e-17 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 80.69 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVqNLTKRFGHVTAisNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGkQVHMDSARDaLAL---- 76
Cdd:PRK11144 1 MLEL-NFKQQLGDLCL--TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNG-RVLFDAEKG-ICLppek 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 77 -GITAVYQDLALVDQRNVIHNISLGNiptkwgglvvdRKKMRETAENALSYMKAKlPSLDIPVSSMSGGQRQAVAIARAC 155
Cdd:PRK11144 76 rRIGYVFQDARLFPHYKVRGNLRYGM-----------AKSMVAQFDKIVALLGIE-PLLDRYPGSLSGGEKQRVAIGRAL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499272610 156 ASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAH-GTSVLIISHNLDHVFEVADDLLILRGGRVVA 220
Cdd:PRK11144 144 LTAPELLLMDEPLASLDLPRKRELLPYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKVKA 209
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-199 |
1.56e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 78.38 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDALA-LGit 79
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHyLG-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 80 avYQDlALVDQRNVIHNISLgniptkWGGLVVDRKKMRETAENALsymkaKL-PSLDIPVSSMSGGQRQAVAIARACASG 158
Cdd:PRK13539 80 --HRN-AMKPALTVAENLEF------WAAFLGGEELDIAAALEAV-----GLaPLAHLPFGYLSAGQKRRVALARLLVSN 145
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499272610 159 GQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHN 199
Cdd:PRK13539 146 RPIWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATHI 186
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
2-219 |
1.73e-17 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 80.85 E-value: 1.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDS---ARDALALGI 78
Cdd:PRK10070 29 LSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaeLREVRRKKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 79 TAVYQDLALVDQRNVIHNISLGnipTKWGGLVVDRKkmRETAENALSYMKAKLPSLDIPvSSMSGGQRQAVAIARACASG 158
Cdd:PRK10070 109 AMVFQSFALMPHMTVLDNTAFG---MELAGINAEER--REKALDALRQVGLENYAHSYP-DELSGGMRQRVGLARALAIN 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499272610 159 GQLVIMDEPTAALGIREQRMVLDVVHDLRA-HGTSVLIISHNLDHVFEVADDLLILRGGRVV 219
Cdd:PRK10070 183 PDILLMDEAFSALDPLIRTEMQDELVKLQAkHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-217 |
2.46e-17 |
|
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: 75.95 E-value: 2.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGkqvhmdsardalalGITAV 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS--------------TVKIG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 82 YqdlalVDQrnvihnislgniptkwgglvvdrkkmretaenalsymkaklpsldipvssMSGGQRQAVAIARACASGGQL 161
Cdd:cd03221 67 Y-----FEQ--------------------------------------------------LSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499272610 162 VIMDEPTAALGIrEQRMVLDVVhdLRAHGTSVLIISHNLDHVFEVADDLLILRGGR 217
Cdd:cd03221 92 LLLDEPTNHLDL-ESIEALEEA--LKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
16-231 |
3.39e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 80.45 E-value: 3.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 16 AISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNG---KQVHMDSARDALALgitaVYQDLALVDQrN 92
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlRDYTLASLRNQVAL----VSQNVHLFND-T 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 93 VIHNISLGniptkwgglvVDRKKMRETAENALSYMKA-----KLPS-LDIPV----SSMSGGQRQAVAIARACASGGQLV 162
Cdd:PRK11176 433 IANNIAYA----------RTEQYSREQIEEAARMAYAmdfinKMDNgLDTVIgengVLLSGGQRQRIAIARALLRDSPIL 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499272610 163 IMDEPTAALGIREQRMVLDVVHDLRAHGTSvLIISHNLDHVfEVADDLLILRGGRVvaeVERNavSHDE 231
Cdd:PRK11176 503 ILDEATSALDTESERAIQAALDELQKNRTS-LVIAHRLSTI-EKADEILVVEDGEI---VERG--THAE 564
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
20-227 |
3.48e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 78.05 E-value: 3.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 20 VSANIRKGRVTALLGDNGAGKSTLVKMICGTYkPTQGSVWVNGKQVHMDSARDaLA------------LGITAVYQDLAL 87
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAE-LArhraylsqqqtpPFAMPVFQYLTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 88 vdqrnviHNISLGNIptkwgglvvdrkkmrETAENALSYMKAKL---PSLDIPVSSMSGGQRQAVAIARACA-------S 157
Cdd:PRK03695 93 -------HQPDKTRT---------------EAVASALNEVAEALgldDKLGRSVNQLSGGEWQRVRLAAVVLqvwpdinP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 158 GGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAEVERNAV 227
Cdd:PRK03695 151 AGQLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
16-221 |
3.61e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 78.69 E-value: 3.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 16 AISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKP---TQGSVWVNGKQVHMDSARDAL-ALGItaVYQ--DLALVD 89
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIReKVGI--VFQnpDNQFVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 90 QrNVIHNISLGniptkWGGLVVDRKKMRETAENALSYMkAKLPSLDIPVSSMSGGQRQAVAIARACASGGQLVIMDEPTA 169
Cdd:PRK13640 100 A-TVGDDVAFG-----LENRAVPRPEMIKIVRDVLADV-GMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499272610 170 ALGIREQRMVLDVVHDLRA-HGTSVLIISHNLDHVfEVADDLLILRGGRVVAE 221
Cdd:PRK13640 173 MLDPAGKEQILKLIRKLKKkNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQ 224
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-235 |
4.63e-17 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 80.02 E-value: 4.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHVT-AISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDALALgITA 80
Cdd:PRK10522 323 LELRNVTFAYQDNGfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKL-FSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 81 VYQDLALVDQrnvihniSLGN--------IPTKWgglvVDRKKMREtaenalsymKAKLPSLDIPVSSMSGGQRQAVAIA 152
Cdd:PRK10522 402 VFTDFHLFDQ-------LLGPegkpanpaLVEKW----LERLKMAH---------KLELEDGRISNLKLSKGQKKRLALL 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 153 RACASGGQLVIMDEPTAalgirEQ----RMV--LDVVHDLRAHGTSVLIISHNlDHVFEVADDLLILRGGRvVAEV---E 223
Cdd:PRK10522 462 LALAEERDILLLDEWAA-----DQdphfRREfyQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQ-LSELtgeE 534
|
250
....*....|..
gi 499272610 224 RNAVSHDEVVRL 235
Cdd:PRK10522 535 RDAASRDAVART 546
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-208 |
4.82e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 77.89 E-value: 4.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMI--CGTYKP---TQGSVWVNGKQVHmdSAR-DAL 74
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGHNIY--SPRtDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 75 AL--GITAVYQD---LALVDQRNVIHNISLGNIPtkwgglvvDRKKMRETAENAL------SYMKAKLPSLDIpvsSMSG 143
Cdd:PRK14239 83 DLrkEIGMVFQQpnpFPMSIYENVVYGLRLKGIK--------DKQVLDEAVEKSLkgasiwDEVKDRLHDSAL---GLSG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499272610 144 GQRQAVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRaHGTSVLIISHNLDHVFEVAD 208
Cdd:PRK14239 152 GQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLK-DDYTMLLVTRSMQQASRISD 215
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-232 |
5.99e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 78.21 E-value: 5.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRF---GHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDaLALG 77
Cdd:PRK13642 4 ILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWN-LRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 78 ITAVYQD-----LALVDQRNVIHNISLGNIPTKWgglVVDRKKMRETAENALSYmKAKLPsldipvSSMSGGQRQAVAIA 152
Cdd:PRK13642 83 IGMVFQNpdnqfVGATVEDDVAFGMENQGIPREE---MIKRVDEALLAVNMLDF-KTREP------ARLSGGQKQRVAVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 153 RACASGGQLVIMDEPTAALGIREQRMVLDVVHDLR-AHGTSVLIISHNLDHVFEvADDLLILRGGRVVAEV---ERNAVS 228
Cdd:PRK13642 153 GIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKeKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAapsELFATS 231
|
....
gi 499272610 229 HDEV 232
Cdd:PRK13642 232 EDMV 235
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-218 |
7.48e-17 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 79.67 E-value: 7.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 4 VQNLTKRFGHV--TAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDsardalalgITAV 81
Cdd:TIGR01257 931 VKNLVKIFEPSgrPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETN---------LDAV 1001
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 82 YQDLALVDQrnviHNISLGNIPTKWGGLVVDRKKMRETAENALSyMKAKLPSLDI------PVSSMSGGQRQAVAIARAC 155
Cdd:TIGR01257 1002 RQSLGMCPQ----HNILFHHLTVAEHILFYAQLKGRSWEEAQLE-MEAMLEDTGLhhkrneEAQDLSGGMQRKLSVAIAF 1076
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499272610 156 ASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAhGTSVLIISHNLDHVFEVADDLLILRGGRV 218
Cdd:TIGR01257 1077 VGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-219 |
1.41e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 76.62 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 17 ISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMdsARDALALGITAVYQDLALV-DQRNVIH 95
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYF--GKDIFQIDAIKLRKEVGMVfQQPNPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 96 NISL-GNI--PTKWGGLVVDR--KKMRETAENALSYMKAKLPSLDIPVSSMSGGQRQAVAIARACASGGQLVIMDEPTAA 170
Cdd:PRK14246 104 HLSIyDNIayPLKSHGIKEKReiKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499272610 171 LGIREQRMVLDVVHDLRAHgTSVLIISHNLDHVFEVADDLLILRGGRVV 219
Cdd:PRK14246 184 IDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELV 231
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-239 |
5.12e-16 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 75.19 E-value: 5.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQV------HMDSARDAL 74
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsrsRLYTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 75 ALgitaVYQDLALVDQRNVIHNISLgniPTKwgglvvDRKKMRETAENALSYMKAKLPSL----DIPVSSMSGGQRQAVA 150
Cdd:PRK11831 87 SM----LFQSGALFTDMNVFDNVAY---PLR------EHTQLPAPLLHSTVMMKLEAVGLrgaaKLMPSELSGGMARRAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 151 IARACASGGQLVIMDEPTAALGIREQRMVLDVVHDL-RAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAEVERNAVSH 229
Cdd:PRK11831 154 LARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELnSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQA 233
|
250
....*....|..
gi 499272610 230 --DEVVRLILAG 239
Cdd:PRK11831 234 npDPRVRQFLDG 245
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-219 |
5.72e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 75.51 E-value: 5.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFG-----HVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSV-WV------NGKQVHMDS 69
Cdd:PRK13651 3 IKVKNIVKIFNkklptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIeWIfkdeknKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 70 ARDALALGIT---------------------AVYQDLALVDQRNVIHN-ISLGniptkwgglvVDRKkmrETAENALSYM 127
Cdd:PRK13651 83 VLEKLVIQKTrfkkikkikeirrrvgvvfqfAEYQLFEQTIEKDIIFGpVSMG----------VSKE---EAKKRAAKYI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 128 K-AKLPSLDIPVS--SMSGGQRQAVAIARACASGGQLVIMDEPTAAL---GIREqrmVLDVVHDLRAHGTSVLIISHNLD 201
Cdd:PRK13651 150 ElVGLDESYLQRSpfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLdpqGVKE---ILEIFDNLNKQGKTIILVTHDLD 226
|
250
....*....|....*...
gi 499272610 202 HVFEVADDLLILRGGRVV 219
Cdd:PRK13651 227 NVLEWTKRTIFFKDGKII 244
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-218 |
1.02e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 74.77 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVT---AISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDaLALG 77
Cdd:PRK13650 4 IIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWD-IRHK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 78 ITAVYQ--DLALVDQrNVIHNISLGnIPTKWgglvVDRKKMRETAENALSYM-----KAKLPSldipvsSMSGGQRQAVA 150
Cdd:PRK13650 83 IGMVFQnpDNQFVGA-TVEDDVAFG-LENKG----IPHEEMKERVNEALELVgmqdfKEREPA------RLSGGQKQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499272610 151 IARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLR-AHGTSVLIISHNLDHVfEVADDLLILRGGRV 218
Cdd:PRK13650 151 IAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRdDYQMTVISITHDLDEV-ALSDRVLVMKNGQV 218
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-231 |
1.18e-15 |
|
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: 76.01 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHV--------TAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNG---KQVHMDSA 70
Cdd:COG5265 351 LVVGGGEVRFENVsfgydperPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGqdiRDVTQASL 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 71 RDALalGItaVYQDLALVdqrnvihNISLG-NIptKWGGLVVDRKKMRETAENA-LSYMKAKLPS-LDIPVSS----MSG 143
Cdd:COG5265 431 RAAI--GI--VPQDTVLF-------NDTIAyNI--AYGRPDASEEEVEAAARAAqIHDFIESLPDgYDTRVGErglkLSG 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 144 GQRQAVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLrAHGTSVLIISHNLDHVFEvADDLLILRGGRVvaeVE 223
Cdd:COG5265 498 GEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREV-ARGRTTLVIAHRLSTIVD-ADEILVLEAGRI---VE 572
|
....*...
gi 499272610 224 RNavSHDE 231
Cdd:COG5265 573 RG--THAE 578
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-219 |
2.60e-15 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 74.17 E-value: 2.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRF----GHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTqgsvWvngkQVHMDSAR----D 72
Cdd:COG4170 3 LLDIRNLTIEIdtpqGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDN----W----HVTADRFRwngiD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 73 ALALG-----------ITAVYQD-LALVDQRNVIHNISLGNIPTK-WGGLVVDRKKMRETAENAL----------SYMKA 129
Cdd:COG4170 75 LLKLSprerrkiigreIAMIFQEpSSCLDPSAKIGDQLIEAIPSWtFKGKWWQRFKWRKKRAIELlhrvgikdhkDIMNS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 130 kLPsldipvSSMSGGQRQAVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDL-RAHGTSVLIISHNLDHVFEVAD 208
Cdd:COG4170 155 -YP------HELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLnQLQGTSILLISHDLESISQWAD 227
|
250
....*....|.
gi 499272610 209 DLLILRGGRVV 219
Cdd:COG4170 228 TITVLYCGQTV 238
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
16-219 |
3.28e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 73.50 E-value: 3.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 16 AISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWV-------NGKQVHmDSARDALALGITAVYQDLALV 88
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgdyaipaNLKKIK-EVKRLRKEIGLVFQFPEYQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 89 dQRNVIHNISLGNIptkwgGLVVDRKKMRETAENALSYMKakLPSLDIPVS--SMSGGQRQAVAIARACASGGQLVIMDE 166
Cdd:PRK13645 105 -QETIEKDIAFGPV-----NLGENKQEAYKKVPELLKLVQ--LPEDYVKRSpfELSGGQKRRVALAGIIAMDGNTLVLDE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499272610 167 PTAALGIREQRMVLDVVHDL-RAHGTSVLIISHNLDHVFEVADDLLILRGGRVV 219
Cdd:PRK13645 177 PTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVI 230
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
16-230 |
3.65e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 73.59 E-value: 3.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 16 AISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDALAL--GITAVYQD-LALVDQRn 92
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVrsDIQMIFQDpLASLNPR- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 93 vihnISLGNI---PtkwggLVVDRKKM-RETAENALSYMKAK---LPSL--DIPvSSMSGGQRQAVAIARACASGGQLVI 163
Cdd:PRK15079 115 ----MTIGEIiaeP-----LRTYHPKLsRQEVKDRVKAMMLKvglLPNLinRYP-HEFSGGQCQRIGIARALILEPKLII 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499272610 164 MDEPTAALGIREQRMVLDVVHDL-RAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAEVERNAVSHD 230
Cdd:PRK15079 185 CDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHN 252
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-203 |
4.09e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 74.38 E-value: 4.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVnGKQVHM---DSARDALAlgi 78
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVKLayvDQSRDALD--- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 79 tavyqdlalvDQRNVIHNISLGNIPTKWGGlvvdrkkmRETaeNALSYMKA---KLPSLDIPVSSMSGGQRQAVAIARAC 155
Cdd:PRK11819 401 ----------PNKTVWEEISGGLDIIKVGN--------REI--PSRAYVGRfnfKGGDQQKKVGVLSGGERNRLHLAKTL 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499272610 156 ASGGQLVIMDEPTAAlgireqrmvLDvVHDLRA-------HGTSVLIISHN---LDHV 203
Cdd:PRK11819 461 KQGGNVLLLDEPTND---------LD-VETLRAleealleFPGCAVVISHDrwfLDRI 508
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
16-217 |
8.66e-15 |
|
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: 70.58 E-value: 8.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 16 AISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKqvhmdsardalalgitavyqdLALVDQRNVIH 95
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS---------------------IAYVSQEPWIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 96 NISL-GNIptkWGGLVVDRKKMRETAEN-ALSYMKAKLPSLDIPV-----SSMSGGQRQAVAIARACASGGQLVIMDEPT 168
Cdd:cd03250 79 NGTIrENI---LFGKPFDEERYEKVIKAcALEPDLEILPDGDLTEigekgINLSGGQKQRISLARAVYSDADIYLLDDPL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499272610 169 AALGIR-EQRMVLDVVHDLRAHGTSVLIISHNLDHVFEvADDLLILRGGR 217
Cdd:cd03250 156 SAVDAHvGRHIFENCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-200 |
9.18e-15 |
|
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: 73.16 E-value: 9.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRF-GHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHmDSARDALALGITA 80
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVS-SLDQDEVRRRVSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 81 VYQDLALVDQrNVIHNISLGNiPTkwgglvVDRKKMRETAENA-LSYMKAKLPS-LDIPV----SSMSGGQRQAVAIARA 154
Cdd:TIGR02868 414 CAQDAHLFDT-TVRENLRLAR-PD------ATDEELWAALERVgLADWLRALPDgLDTVLgeggARLSGGERQRLALARA 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499272610 155 CASGGQLVIMDEPTAALgirEQRMVLDVVHDLRA--HGTSVLIISHNL 200
Cdd:TIGR02868 486 LLADAPILLLDEPTEHL---DAETADELLEDLLAalSGRTVVLITHHL 530
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-200 |
1.43e-14 |
|
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: 72.51 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 25 RKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVwvnGKQVHMDSARDALAlGiTAVYQDL-ALVDQR-NVIHNIS-LGN 101
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDY---DEEPSWDEVLKRFR-G-TELQDYFkKLANGEiKVAHKPQyVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 102 IPTKWGGLV------VD-RKKMRETAEnalsymkaKL---PSLDIPVSSMSGGQRQAVAIARACASGGQLVIMDEPTAAL 171
Cdd:COG1245 172 IPKVFKGTVrellekVDeRGKLDELAE--------KLgleNILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYL 243
|
170 180 190
....*....|....*....|....*....|
gi 499272610 172 GIReQRM-VLDVVHDLRAHGTSVLIISHNL 200
Cdd:COG1245 244 DIY-QRLnVARLIRELAEEGKYVLVVEHDL 272
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
6-218 |
2.76e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 71.21 E-value: 2.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 6 NLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVH--MDSARdalalGITAVYQ 83
Cdd:PRK11000 8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNdvPPAER-----GVGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 84 DLALVDQRNVIHNISLGnipTKWGGlvVDRKKMRETAENALSYMK-AKLpsLDIPVSSMSGGQRQAVAIARACASGGQLV 162
Cdd:PRK11000 83 SYALYPHLSVAENMSFG---LKLAG--AKKEEINQRVNQVAEVLQlAHL--LDRKPKALSGGQRQRVAIGRTLVAEPSVF 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499272610 163 IMDEPTAAL--GIREQ-RMVLDVVHdlRAHGTSVLIISHNLDHVFEVADDLLILRGGRV 218
Cdd:PRK11000 156 LLDEPLSNLdaALRVQmRIEISRLH--KRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
17-219 |
3.04e-14 |
|
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: 69.61 E-value: 3.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 17 ISNVSANIRKGRVTALLGDNGAGKSTLVKMICG---TYKPTQGSVWVNGKQVHMDSAR---------DALALGITaVYQD 84
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQPRKPDQFQkcvayvrqdDILLPGLT-VRET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 85 LALVDQrNVIHNISLGNIPTKwgglVVDRKKMRETAENALSYMKaklpsldipVSSMSGGQRQAVAIARACASGGQLVIM 164
Cdd:cd03234 102 LTYTAI-LRLPRKSSDAIRKK----RVEDVLLRDLALTRIGGNL---------VKGISGGERRRVSIAVQLLWDPKVLIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499272610 165 DEPTAALgirEQRMVLDVVHDLR--AHGTSVLIISHnldH-----VFEVADDLLILRGGRVV 219
Cdd:cd03234 168 DEPTSGL---DSFTALNLVSTLSqlARRNRIVILTI---HqprsdLFRLFDRILLLSSGEIV 223
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-200 |
3.25e-14 |
|
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: 70.09 E-value: 3.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 25 RKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSvwvNGKQVHMDSARDALALGITAVYQDLALVDQRNVIHNIS-LGNIP 103
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGK---FDDPPDWDEILDEFRGSELQNYFTKLLEGDVKVIVKPQyVDLIP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 104 TKWGGLVVDR-KKMRETaeNALSYMKAKL---PSLDIPVSSMSGGQRQAVAIARACASGGQLVIMDEPTAALGIREQRMV 179
Cdd:cd03236 101 KAVKGKVGELlKKKDER--GKLDELVDQLelrHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNA 178
|
170 180
....*....|....*....|.
gi 499272610 180 LDVVHDLRAHGTSVLIISHNL 200
Cdd:cd03236 179 ARLIRELAEDDNYVLVVEHDL 199
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
113-221 |
3.36e-14 |
|
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: 71.58 E-value: 3.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 113 RKKMRETAENALSYMKaklpsLDIPVSSMSGGQRQAVAIAR---ACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAH 189
Cdd:TIGR00630 807 SRKLQTLCDVGLGYIR-----LGQPATTLSGGEAQRIKLAKelsKRSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDK 881
|
90 100 110
....*....|....*....|....*....|....*...
gi 499272610 190 GTSVLIISHNLDhVFEVADDLLIL------RGGRVVAE 221
Cdd:TIGR00630 882 GNTVVVIEHNLD-VIKTADYIIDLgpeggdGGGTVVAS 918
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-227 |
3.73e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 71.42 E-value: 3.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFG-----------HVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHM-- 67
Cdd:PRK10261 313 ILQVRNLVTRFPlrsgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTls 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 68 DSARDALALGITAVYQD-LALVDQRNVI----------HNISLGNIPTKWGGLVVDRKKMRetAENALSYMKAklpsldi 136
Cdd:PRK10261 393 PGKLQALRRDIQFIFQDpYASLDPRQTVgdsimeplrvHGLLPGKAAAARVAWLLERVGLL--PEHAWRYPHE------- 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 137 pvssMSGGQRQAVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDL-RAHGTSVLIISHNLDHVFEVADDLLILRG 215
Cdd:PRK10261 464 ----FSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLqRDFGIAYLFISHDMAVVERISHRVAVMYL 539
|
250
....*....|..
gi 499272610 216 GRVVAEVERNAV 227
Cdd:PRK10261 540 GQIVEIGPRRAV 551
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-199 |
6.90e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 68.65 E-value: 6.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGH----VTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVH-MDS-ARDAL 74
Cdd:PRK10584 6 IVEVHHLKKSVGQgeheLSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHqMDEeARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 75 -ALGITAVYQDLALVDQRNVIHNISLgniPTKWGGlvVDRKKMRETAENALSYMKAKLPSLDIPvSSMSGGQRQAVAIAR 153
Cdd:PRK10584 86 rAKHVGFVFQSFMLIPTLNALENVEL---PALLRG--ESSRQSRNGAKALLEQLGLGKRLDHLP-AQLSGGEQQRVALAR 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499272610 154 ACASGGQLVIMDEPTAALGIREQRMVLDVVHDL-RAHGTSVLIISHN 199
Cdd:PRK10584 160 AFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHD 206
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
24-200 |
7.59e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 70.61 E-value: 7.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 24 IRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVwvnGKQVHMDSARDALAlGiTAVYQDLALVDQRN--VIHNIS-LG 100
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDY---EEEPSWDEVLKRFR-G-TELQNYFKKLYNGEikVVHKPQyVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 101 NIPTKWGGLVVD-------RKKMRETAEnalsymkaKL---PSLDIPVSSMSGGQRQAVAIARACASGGQLVIMDEPTAA 170
Cdd:PRK13409 171 LIPKVFKGKVREllkkvdeRGKLDEVVE--------RLgleNILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSY 242
|
170 180 190
....*....|....*....|....*....|.
gi 499272610 171 LGIReQRM-VLDVVHDLrAHGTSVLIISHNL 200
Cdd:PRK13409 243 LDIR-QRLnVARLIREL-AEGKYVLVVEHDL 271
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-216 |
1.15e-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: 70.43 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVT--AISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDsardalalgI 78
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTN---------I 2007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 79 TAVYQDLALVDQRNVIHNISLGN----IPTKWGGlvVDRKKMRETAENALSYMKAKLPSlDIPVSSMSGGQRQAVAIARA 154
Cdd:TIGR01257 2008 SDVHQNMGYCPQFDAIDDLLTGRehlyLYARLRG--VPAEEIEKVANWSIQSLGLSLYA-DRLAGTYSGGNKRKLSTAIA 2084
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499272610 155 CASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGG 216
Cdd:TIGR01257 2085 LIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-208 |
2.96e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 67.37 E-value: 2.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMIcGTYKPTQGSVWVNGKQVHMDSARDALALGITAV 81
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGRVEFFNQNIYERRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 82 YQDLALVDQR------NVIHNISLGNIPTKWGGLVvdrkKMRETAENALS------YMKAKL--PSLDipvssMSGGQRQ 147
Cdd:PRK14258 87 RRQVSMVHPKpnlfpmSVYDNVAYGVKIVGWRPKL----EIDDIVESALKdadlwdEIKHKIhkSALD-----LSGGQQQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499272610 148 AVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGT-SVLIISHNLDHVFEVAD 208
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNLHQVSRLSD 219
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-244 |
3.44e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 67.43 E-value: 3.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 6 NLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMI------CGTYKPTqGSVWVNGKQVHmdSARDALALgit 79
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkVSGYRYS-GDVLLGGRSIF--NYRDVLEF--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 80 avYQDLALVDQR------NVIHNISLGNIPTKwgglVVDRKKMRETAENALS------YMKAKLPslDIPVSsMSGGQRQ 147
Cdd:PRK14271 100 --RRRVGMLFQRpnpfpmSIMDNVLAGVRAHK----LVPRKEFRGVAQARLTevglwdAVKDRLS--DSPFR-LSGGQQQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 148 AVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLrAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAE--VER- 224
Cdd:PRK14271 171 LLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSL-ADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEgpTEQl 249
|
250 260
....*....|....*....|...
gi 499272610 225 -NAVSHDEVVRLI--LAGQPRDA 244
Cdd:PRK14271 250 fSSPKHAETARYVagLSGDVKDA 272
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
17-219 |
4.10e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 68.21 E-value: 4.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 17 ISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARdALALGITAVYQD-LALVDqrNVIH 95
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS-VLRQGVAMVQQDpVVLAD--TFLA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 96 NISLG-NIPTK--WGGLvvdrkkmrETAEnaLSYMKAKLPS-----LDIPVSSMSGGQRQAVAIARACASGGQLVIMDEP 167
Cdd:PRK10790 434 NVTLGrDISEEqvWQAL--------ETVQ--LAELARSLPDglytpLGEQGNNLSVGQKQLLALARVLVQTPQILILDEA 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499272610 168 TAALGIREQRMVLDVVHDLRAHgTSVLIISHNLDHVFEvADDLLILRGGRVV 219
Cdd:PRK10790 504 TANIDSGTEQAIQQALAAVREH-TTLVVIAHRLSTIVE-ADTILVLHRGQAV 553
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-220 |
4.73e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 68.31 E-value: 4.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRF--GHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHmDSARDALALGIT 79
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIA-DYSEAALRQAIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 80 avyqdlaLVDQRNVIHNISLGN-----IPTKwgglvvDRKKMRETAEN-ALSYMKAKLPSLDIPVSS----MSGGQRQAV 149
Cdd:PRK11160 418 -------VVSQRVHLFSATLRDnlllaAPNA------SDEALIEVLQQvGLEKLLEDDKGLNAWLGEggrqLSGGEQRRL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499272610 150 AIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTsVLIISHNLdHVFEVADDLLILRGGRVVA 220
Cdd:PRK11160 485 GIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKT-VLMITHRL-TGLEQFDRICVMDNGQIIE 553
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
6-224 |
6.49e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 65.75 E-value: 6.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 6 NLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDalalGITAVYQDL 85
Cdd:COG2401 35 GVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGREAS----LIDAIGRKG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 86 ALVDQRNVIHNISLGNIPTkWgglvvdRKKMREtaenalsymkaklpsldipvssMSGGQRQAVAIARACASGGQLVIMD 165
Cdd:COG2401 111 DFKDAVELLNAVGLSDAVL-W------LRRFKE----------------------LSTGQKFRFRLALLLAERPKLLVID 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 166 EPTAALGIREQRMVLDVVHDL-RAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAEVER 224
Cdd:COG2401 162 EFCSHLDRQTAKRVARNLQKLaRRAGITLVVATHHYDVIDDLQPDLLIFVGYGGVPEEKR 221
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-217 |
6.78e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 65.89 E-value: 6.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKqvhmdsarDALALGITA 80
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGE--------DISTLKPEI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 81 VYQDLALVDQrnvihnislgnIPTKWGGLVVD--------RKKMRETAENALSYMKAKLPS--LDIPVSSMSGGQRQAVA 150
Cdd:PRK10247 79 YRQQVSYCAQ-----------TPTLFGDTVYDnlifpwqiRNQQPDPAIFLDDLERFALPDtiLTKNIAELSGGEKQRIS 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 151 IARACASGGQLVIMDEPTAALGIREQRMVLDVVHDL-RAHGTSVLIISHNLDHVFEvADDLLIL--RGGR 217
Cdd:PRK10247 148 LIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYvREQNIAVLWVTHDKDEINH-ADKVITLqpHAGE 216
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-226 |
7.25e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 67.42 E-value: 7.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRF---GHV-TAISNVSANIRKGRVTALLGDNGAGKS-TLVKMICGTYKP----TQGSVWVNGKQV-HMDSA 70
Cdd:PRK15134 5 LLAIENLSVAFrqqQTVrTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLlHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 71 RDALALG--ITAVYQD--LALvdqrNVIHNI--SLGNIptkwggLVVDRKKMRETAE-NALSYM------KAKLPSLDIP 137
Cdd:PRK15134 85 TLRGVRGnkIAMIFQEpmVSL----NPLHTLekQLYEV------LSLHRGMRREAARgEILNCLdrvgirQAAKRLTDYP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 138 vSSMSGGQRQAVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAH-GTSVLIISHNLDHVFEVADDLLILRGG 216
Cdd:PRK15134 155 -HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNG 233
|
250
....*....|
gi 499272610 217 RVvaeVERNA 226
Cdd:PRK15134 234 RC---VEQNR 240
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
2-238 |
8.22e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 66.26 E-value: 8.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRfGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKP----TQGSVWVNGKQVHMDSARdalalG 77
Cdd:PRK10418 5 IELRNIALQ-AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALR-----G 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 78 ITAvyqdlALVDQR-----NVIHNISLGNIPT-KWGGLVVDRKKMRETAENALSYMKAKLPSLdIPVSsMSGGQRQAVAI 151
Cdd:PRK10418 79 RKI-----ATIMQNprsafNPLHTMHTHARETcLALGKPADDATLTAALEAVGLENAARVLKL-YPFE-MSGGMLQRMMI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 152 ARACASGGQLVIMDEPTAALGIREQRMVLDVVHDL-RAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAEVERNAVSH- 229
Cdd:PRK10418 152 ALALLCEAPFIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNa 231
|
250
....*....|.
gi 499272610 230 --DEVVRLILA 238
Cdd:PRK10418 232 pkHAVTRSLVS 242
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-219 |
8.88e-13 |
|
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: 65.59 E-value: 8.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRF--GHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGkqvhmdsaRDALALGIT 79
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDG--------VDISKIGLH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 80 AVYQDLALVDQRNVI------HNISLGNIPTK---WGglVVDRKKMREtaenalsYMKAKLPSLDIPVSSM----SGGQR 146
Cdd:cd03244 75 DLRSRISIIPQDPVLfsgtirSNLDPFGEYSDeelWQ--ALERVGLKE-------FVESLPGGLDTVVEEGgenlSVGQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499272610 147 QAVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTsVLIISHNLDHVFEvADDLLILRGGRVV 219
Cdd:cd03244 146 QLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCT-VLTIAHRLDTIID-SDRILVLDKGRVV 216
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
113-221 |
1.09e-12 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 65.71 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 113 RKKMRETAENALSYMKaklpsLDIPVSSMSGGQRQAVAIARAC---ASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAH 189
Cdd:cd03271 147 ARKLQTLCDVGLGYIK-----LGQPATTLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDK 221
|
90 100 110
....*....|....*....|....*....|....*...
gi 499272610 190 GTSVLIISHNLDhVFEVADDLLIL------RGGRVVAE 221
Cdd:cd03271 222 GNTVVVIEHNLD-VIKCADWIIDLgpeggdGGGQVVAS 258
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
2-198 |
2.56e-12 |
|
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: 63.92 E-value: 2.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDS---ARDALALG- 77
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRdepHENILYLGh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 78 ITAVYQDLALVDQRNVIHNISLGNiptkwgglvvdrkkmRETAENALSymKAKLPSL-DIPVSSMSGGQRQAVAIARACA 156
Cdd:TIGR01189 81 LPGLKPELSALENLHFWAAIHGGA---------------QRTIEDALA--AVGLTGFeDLPAAQLSAGQQRRLALARLWL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499272610 157 SGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISH 198
Cdd:TIGR01189 144 SRRPLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-219 |
3.14e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 64.48 E-value: 3.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMI-----CGTYKPTQGSVWVNGKQVH---MDSARDA 73
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYspdVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 74 LALGItaVYQDLALVDQRNVIHNISLGnipTKWGGLVVDRKKMRETAENALSymKAKL-----PSLDIPVSSMSGGQRQA 148
Cdd:PRK14267 85 REVGM--VFQYPNPFPHLTIYDNVAIG---VKLNGLVKSKKELDERVEWALK--KAALwdevkDRLNDYPSNLSGGQRQR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499272610 149 VAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLiISHNLDHVFEVADDLLILRGGRVV 219
Cdd:PRK14267 158 LVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVL-VTHSPAQAARVSDYVAFLYLGKLI 227
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-65 |
5.41e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 65.15 E-value: 5.41e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499272610 5 QNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQV 65
Cdd:NF033858 270 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV 330
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
2-171 |
5.47e-12 |
|
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: 62.90 E-value: 5.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHmdSARDALALGITAV 81
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLD--FQRDSIARGLLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 82 YQDLALVDQRNVIHNISLgniptkWGGLVVDrkkmrETAENALSymKAKLPSL-DIPVSSMSGGQRQAVAIARACASGGQ 160
Cdd:cd03231 79 GHAPGIKTTLSVLENLRF------WHADHSD-----EQVEEALA--RVGLNGFeDRPVAQLSAGQQRRVALARLLLSGRP 145
|
170
....*....|.
gi 499272610 161 LVIMDEPTAAL 171
Cdd:cd03231 146 LWILDEPTTAL 156
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-217 |
5.73e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 64.36 E-value: 5.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRF----GHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKP---TQGSVWVNGKQV------HM 67
Cdd:PRK09473 12 LLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREIlnlpekEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 68 DSARdalALGITAVYQDLAlvdqrnvihnISLgNIPTKWGGLVVD----RKKM--RETAENALSYMKA-KLPS----LDI 136
Cdd:PRK09473 92 NKLR---AEQISMIFQDPM----------TSL-NPYMRVGEQLMEvlmlHKGMskAEAFEESVRMLDAvKMPEarkrMKM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 137 PVSSMSGGQRQAVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDL-RAHGTSVLIISHNLDHVFEVADDLLILRG 215
Cdd:PRK09473 158 YPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELkREFNTAIIMITHDLGVVAGICDKVLVMYA 237
|
..
gi 499272610 216 GR 217
Cdd:PRK09473 238 GR 239
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-250 |
6.31e-12 |
|
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: 64.82 E-value: 6.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGT--YKPTQGSV-----------WVN-----GK 63
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgYVErpskvGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 64 QVHM----------------DSARDALALGITAVYQ-DLALVDQRNVIHNI--SLGNIPTKwGGLVVDRkkmretAENAL 124
Cdd:TIGR03269 81 PCPVcggtlepeevdfwnlsDKLRRRIRKRIAIMLQrTFALYGDDTVLDNVleALEEIGYE-GKEAVGR------AVDLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 125 SYMKAKLPSLDIpVSSMSGGQRQAVAIARACASGGQLVIMDEPTAALgireQRMVLDVVHD-----LRAHGTSVLIISHN 199
Cdd:TIGR03269 154 EMVQLSHRITHI-ARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTL----DPQTAKLVHNaleeaVKASGISMVLTSHW 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 499272610 200 LDHVFEVADDLLILRGGRVVAEVERnavshDEVVRLILAGQPrDADLEEEV 250
Cdd:TIGR03269 229 PEVIEDLSDKAIWLENGEIKEEGTP-----DEVVAVFMEGVS-EVEKECEV 273
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-219 |
1.32e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 62.74 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICG--TYKPTQGSVWVNGKQVHMDSARDALALGI 78
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERAHLGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 79 TAVYQ---DLALVDQRN---VIHNislgnipTKwgglvvdRKKMRETAENALS---YMKAKLPSLDIPVS--------SM 141
Cdd:CHL00131 87 FLAFQypiEIPGVSNADflrLAYN-------SK-------RKFQGLPELDPLEfleIINEKLKLVGMDPSflsrnvneGF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 142 SGGQRQAVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHN---LDHVfeVADDLLILRGGRV 218
Cdd:CHL00131 153 SGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYqrlLDYI--KPDYVHVMQNGKI 230
|
.
gi 499272610 219 V 219
Cdd:CHL00131 231 I 231
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-221 |
1.38e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 63.22 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVT----AISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTY----KPTQGSVWVNGKQVHMDSA-- 70
Cdd:PRK11022 3 LLNVDKLSVHFGDESapfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDLQRISEke 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 71 -RDALALGITAVYQD--LALVDQRNVIHNIsLGNIPTKWGGlvvDRKKMRETAENALSYMKAKLPS--LDIPVSSMSGGQ 145
Cdd:PRK11022 83 rRNLVGAEVAMIFQDpmTSLNPCYTVGFQI-MEAIKVHQGG---NKKTRRQRAIDLLNQVGIPDPAsrLDVYPHQLSGGM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499272610 146 RQAVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDL-RAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAE 221
Cdd:PRK11022 159 SQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMYAGQVVET 235
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-198 |
2.02e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.43 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 4 VQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKqvhmdsardalaLGITAVYQ 83
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTK------------LEVAYFDQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 84 DLALVD-QRNVIHNISLGNIPTKWGGlvVDRkkmretaeNALSY--------MKAKlpsldIPVSSMSGGQRQAVAIARA 154
Cdd:PRK11147 390 HRAELDpEKTVMDNLAEGKQEVMVNG--RPR--------HVLGYlqdflfhpKRAM-----TPVKALSGGERNRLLLARL 454
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499272610 155 CASGGQLVIMDEPTAALGIReqrmVLDVVHDLRA--HGTsVLIISH 198
Cdd:PRK11147 455 FLKPSNLLILDEPTNDLDVE----TLELLEELLDsyQGT-VLLVSH 495
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
14-221 |
2.55e-11 |
|
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: 60.41 E-value: 2.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 14 VTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTykptqgsvwvngkqvhmdSARDALALGITAVYQDLAL-VDQRN 92
Cdd:cd03238 8 VHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYA------------------SGKARLISFLPKFSRNKLIfIDQLQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 93 VIHNISLGNIPtkwgglvvdrkkmretaenalsymkaklpsLDIPVSSMSGGQRQAVAIARACASG--GQLVIMDEPTAA 170
Cdd:cd03238 70 FLIDVGLGYLT------------------------------LGQKLSTLSGGELQRVKLASELFSEppGTLFILDEPSTG 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499272610 171 LGIREQRMVLDVVHDLRAHGTSVLIISHNLDhVFEVADDLLIL------RGGRVVAE 221
Cdd:cd03238 120 LHQQDINQLLEVIKGLIDLGNTVILIEHNLD-VLSSADWIIDFgpgsgkSGGKVVFS 175
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
6-215 |
2.90e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 62.88 E-value: 2.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 6 NLTKRFGHVTAISNvSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGK-----QVhmdsardalalgITA 80
Cdd:COG1245 346 DLTKSYGGFSLEVE-GGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKisykpQY------------ISP 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 81 VYQDLalVDQrnVIHNISLGNIPTKWG-GLVVDR---KKMretaenalsymkaklpsLDIPVSSMSGGQRQAVAIARACA 156
Cdd:COG1245 413 DYDGT--VEE--FLRSANTDDFGSSYYkTEIIKPlglEKL-----------------LDKNVKDLSGGELQRVAIAACLS 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499272610 157 SGGQLVIMDEPTAALGIrEQRMVLDVV--HDLRAHGTSVLIISHNLDHVFEVADDLLILRG 215
Cdd:COG1245 472 RDADLYLLDEPSAHLDV-EQRLAVAKAirRFAENRGKTAMVVDHDIYLIDYISDRLMVFEG 531
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
17-219 |
3.30e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 62.76 E-value: 3.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 17 ISNVSANIRKGRVTALLGDNGAGKSTLVKMICGtYKPT----QGSVWVNG-----KQVHMDSA---RDALALGITAVYQD 84
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAF-RSPKgvkgSGSVLLNGmpidaKEMRAISAyvqQDDLFIPTLTVREH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 85 LalvdqrNVIHNISLGNIPTKwgglvVDRKKMRETAENALSYMKAKLPSLDIP--VSSMSGGQRQAVAIARACASGGQLV 162
Cdd:TIGR00955 120 L------MFQAHLRMPRRVTK-----KEKRERVDEVLQALGLRKCANTRIGVPgrVKGLSGGERKRLAFASELLTDPPLL 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499272610 163 IMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHN-LDHVFEVADDLLILRGGRVV 219
Cdd:TIGR00955 189 FCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQpSSELFELFDKIILMAEGRVA 246
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
23-215 |
3.84e-11 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 61.27 E-value: 3.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 23 NIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGsvwvngkqvhmdsarDALALGITAVYQdlalvDQRnvihnislgnI 102
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEG---------------DIEIELDTVSYK-----PQY----------I 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 103 PTKWGGLVVD--RKKMRETAENalSYMKAKL-------PSLDIPVSSMSGGQRQAVAIARACASGGQLVIMDEPTAALGI 173
Cdd:cd03237 71 KADYEGTVRDllSSITKDFYTH--PYFKTEIakplqieQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499272610 174 rEQR-MVLDVVHDLRAHGTS-VLIISHNLDHVFEVADDLLILRG 215
Cdd:cd03237 149 -EQRlMASKVIRRFAENNEKtAFVVEHDIIMIDYLADRLIVFEG 191
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
124-229 |
5.59e-11 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 62.35 E-value: 5.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 124 LSYMKaklpsLDIPVSSMSGGQRQAVAIARACA---SGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNL 200
Cdd:COG0178 815 LGYIK-----LGQPATTLSGGEAQRVKLASELSkrsTGKTLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHNL 889
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 499272610 201 DhVFEVADDLLIL------RGGRVVA-----EVERNAVSH 229
Cdd:COG0178 890 D-VIKTADWIIDLgpeggdGGGEIVAegtpeEVAKVKASY 928
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
9-219 |
5.95e-11 |
|
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: 59.97 E-value: 5.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 9 KRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTykpTQGSVWVNGKqVHMDsardalalGITavYQDLALV 88
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR---TEGNVSVEGD-IHYN--------GIP--YKEFAEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 89 DQRNVIHNiSLGN--IPTkwggLVVdrkkmRETAENALSyMKAklpslDIPVSSMSGGQRQAVAIARACASGGQLVIMDE 166
Cdd:cd03233 81 YPGEIIYV-SEEDvhFPT----LTV-----RETLDFALR-CKG-----NEFVRGISGGERKRVSIAEALVSRASVLCWDN 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499272610 167 PTAALgirEQRMVLDVVHDLR-----AHGTSVLIISHNLDHVFEVADDLLILRGGRVV 219
Cdd:cd03233 145 STRGL---DSSTALEILKCIRtmadvLKTTTFVSLYQASDEIYDLFDKVLVLYEGRQI 199
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-219 |
1.37e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.02 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGH----VTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVwVNGKQVHMDSARDALAL 76
Cdd:PRK10261 12 VLAVENLNIAFMQeqqkIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLV-QCDKMLLRRRSRQVIEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 77 GITAVYQ-------DLALVDQRNVIhniSLGNIPTKwGGLVVDRKKMRETA--ENALSYMKAKLPSLDIPVSSM------ 141
Cdd:PRK10261 91 SEQSAAQmrhvrgaDMAMIFQEPMT---SLNPVFTV-GEQIAESIRLHQGAsrEEAMVEAKRMLDQVRIPEAQTilsryp 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 142 ---SGGQRQAVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAH-GTSVLIISHNLDHVFEVADDLLILRGGR 217
Cdd:PRK10261 167 hqlSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGE 246
|
..
gi 499272610 218 VV 219
Cdd:PRK10261 247 AV 248
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
24-215 |
1.66e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.59 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 24 IRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNgkqvhmdsardalalgITAVYQDLALVDQRNVIHNISLGNIP 103
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE----------------LKISYKPQYIKPDYDGTVEDLLRSIT 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 104 TKWGGlvvdrkkmretaenalSYMKAKL-------PSLDIPVSSMSGGQRQAVAIARACASGGQLVIMDEPTAALGIrEQ 176
Cdd:PRK13409 426 DDLGS----------------SYYKSEIikplqleRLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV-EQ 488
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499272610 177 RMVLDVV--HDLRAHGTSVLIISHNLDHVFEVADDLLILRG 215
Cdd:PRK13409 489 RLAVAKAirRIAEEREATALVVDHDIYMIDYISDRLMVFEG 529
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-211 |
2.17e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 60.18 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSV---------WVNGKQVHMD-SA 70
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYtfpgnwqlaWVNQETPALPqPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 71 RDALALG---ITAVYQDLALVDQRNVIHNISlgnipTKWGGL-VVDRKKMRETAENALSYMKAKLPSLDIPVSSMSGGQR 146
Cdd:PRK10636 81 LEYVIDGdreYRQLEAQLHDANERNDGHAIA-----TIHGKLdAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGGWR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499272610 147 QAVAIARACASGGQLVIMDEPTAALGireqrmvLDVV----HDLRAHGTSVLIISHNLDHVFEVADDLL 211
Cdd:PRK10636 156 MRLNLAQALICRSDLLLLDEPTNHLD-------LDAViwleKWLKSYQGTLILISHDRDFLDPIVDKII 217
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
17-219 |
2.41e-10 |
|
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: 58.02 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 17 ISNVSANIRKGRVTALLGDNGAGKSTLVKMICG--TYKPTQGSVWVNGKQVHMDSARdalalgiTAVYqdlalVDQrNVI 94
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLDKNFQR-------STGY-----VEQ-QDV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 95 HNISLgniptkwgglvvdrkKMRETAEnalsyMKAKLPSLdipvssmSGGQRQAVAIARACASGGQLVIMDEPTAALGIR 174
Cdd:cd03232 90 HSPNL---------------TVREALR-----FSALLRGL-------SVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQ 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499272610 175 EQRMVLDVVHDLRAHGTSVLI-ISHNLDHVFEVADDLLIL-RGGRVV 219
Cdd:cd03232 143 AAYNIVRFLKKLADSGQAILCtIHQPSASIFEKFDRLLLLkRGGKTV 189
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-233 |
2.64e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 59.43 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRF----GHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTqgsvWvngkQVHMDSARdalal 76
Cdd:PRK15093 3 LLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDN----W----RVTADRMR----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 77 gitavYQDLALV-----DQRNVI-HNISL--------------------GNIPT-KWGGLVVDRKKMRETAENALSYMKA 129
Cdd:PRK15093 70 -----FDDIDLLrlsprERRKLVgHNVSMifqepqscldpservgrqlmQNIPGwTYKGRWWQRFGWRKRRAIELLHRVG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 130 KLPSLDIPVS---SMSGGQRQAVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDL-RAHGTSVLIISHNLDHVFE 205
Cdd:PRK15093 145 IKDHKDAMRSfpyELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQ 224
|
250 260
....*....|....*....|....*...
gi 499272610 206 VADDLLILRGGRVVaeveRNAVSHDEVV 233
Cdd:PRK15093 225 WADKINVLYCGQTV----ETAPSKELVT 248
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
19-230 |
5.23e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 59.27 E-value: 5.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 19 NVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNG----KQVHM------------------DSARDALAL 76
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDINLkwwrskigvvsqdpllfsNSIKNNIKY 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 77 GITAVYQDLALVDQRNVIHNISLGNI------PTKWGGLVVDrkKMRETAENALSYMKAKLPSLD--------------- 135
Cdd:PTZ00265 483 SLYSLKDLEALSNYYNEDGNDSQENKnkrnscRAKCAGDLND--MSNTTDSNELIEMRKNYQTIKdsevvdvskkvlihd 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 136 ----IP----------VSSMSGGQRQAVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSV-LIISHNL 200
Cdd:PTZ00265 561 fvsaLPdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRItIIIAHRL 640
|
250 260 270
....*....|....*....|....*....|....
gi 499272610 201 DHVfEVADDLLIL----RGGRVVAEVERNAVSHD 230
Cdd:PTZ00265 641 STI-RYANTIFVLsnreRGSTVDVDIIGEDPTKD 673
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
14-216 |
6.18e-10 |
|
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: 57.34 E-value: 6.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 14 VTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDALALGITAVyqdlALVDQR-- 91
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSV----AYAAQKpw 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 92 ----NVIHNISLGNIPTKwgglvvDRKKMretAENALSYMkaklPSLDI-PVS----------SMSGGQRQAVAIARACA 156
Cdd:cd03290 90 llnaTVEENITFGSPFNK------QRYKA---VTDACSLQ----PDIDLlPFGdqteigergiNLSGGQRQRICVARALY 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499272610 157 SGGQLVIMDEPTAALGIR--EQRMVLDVVHDLRAHGTSVLIISHNLDHVFEvADDLLILRGG 216
Cdd:cd03290 157 QNTNIVFLDDPFSALDIHlsDHLMQEGILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-219 |
6.30e-10 |
|
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: 57.42 E-value: 6.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFG-HV-TAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKqvhmdsarDALALGIT 79
Cdd:cd03369 7 IEVENLSVRYApDLpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGI--------DISTIPLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 80 AVYQDLALVDQRnvihnislgniPTKWGGLV---VDRKKMRETAE--NALSYMKAKLpsldipvsSMSGGQRQAVAIARA 154
Cdd:cd03369 79 DLRSSLTIIPQD-----------PTLFSGTIrsnLDPFDEYSDEEiyGALRVSEGGL--------NLSQGQRQLLCLARA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499272610 155 CASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAhGTSVLIISHNLDHVFEVaDDLLILRGGRVV 219
Cdd:cd03369 140 LLKRPRVLVLDEATASIDYATDALIQKTIREEFT-NSTILTIAHRLRTIIDY-DKILVMDAGEVK 202
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-219 |
1.23e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 58.25 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 19 NVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNgkqvhmdsardalalgitavyQDLALVDQRNVIHNIS 98
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE---------------------RSIAYVPQQAWIMNAT 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 99 L-GNIptkwggLVVDRKKMRETAENA-LSYMKAKLPSLDIPVSS--------MSGGQRQAVAIARACASGGQLVIMDEPT 168
Cdd:PTZ00243 737 VrGNI------LFFDEEDAARLADAVrVSQLEADLAQLGGGLETeigekgvnLSGGQKARVSLARAVYANRDVYLLDDPL 810
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499272610 169 AALGIR-EQRMVLDVVHDLRAHGTSVLiISHNLdHVFEVADDLLILRGGRVV 219
Cdd:PTZ00243 811 SALDAHvGERVVEECFLGALAGKTRVL-ATHQV-HVVPRADYVVALGDGRVE 860
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
17-216 |
1.41e-09 |
|
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: 57.17 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 17 ISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKqVHMDSARDALALGITavyqdlalvdQRNVIHN 96
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-ISFSSQFSWIMPGTI----------KENIIFG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 97 ISLGNIPTKwggLVVDRKKMRETAenalsymkAKLPSLDIPVS-----SMSGGQRQAVAIARACASGGQLVIMDEPTAAL 171
Cdd:cd03291 122 VSYDEYRYK---SVVKACQLEEDI--------TKFPEKDNTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYL 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499272610 172 GIREQRMVLD-VVHDLRAHGTSVLIIShNLDHVfEVADDLLILRGG 216
Cdd:cd03291 191 DVFTEKEIFEsCVCKLMANKTRILVTS-KMEHL-KKADKILILHEG 234
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
124-229 |
2.71e-09 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 57.00 E-value: 2.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 124 LSYMKaklpsLDIPVSSMSGGQRQAVAIARAC---ASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNL 200
Cdd:PRK00349 819 LGYIK-----LGQPATTLSGGEAQRVKLAKELskrSTGKTLYILDEPTTGLHFEDIRKLLEVLHRLVDKGNTVVVIEHNL 893
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 499272610 201 DhVFEVADDLLIL------RGGRVVA-----EVERNAVSH 229
Cdd:PRK00349 894 D-VIKTADWIIDLgpeggdGGGEIVAtgtpeEVAKVEASY 932
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-171 |
4.96e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 54.81 E-value: 4.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHM---DSARDALALG 77
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRqrdEYHQDLLYLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 78 -ITAVYQDL-ALvdqRNVIHNISLGNIPTkwgglvvdrkkmRETAENALSYMkaklpSL----DIPVSSMSGGQRQAVAI 151
Cdd:PRK13538 81 hQPGIKTELtAL---ENLRFYQRLHGPGD------------DEALWEALAQV-----GLagfeDVPVRQLSAGQQRRVAL 140
|
170 180
....*....|....*....|
gi 499272610 152 ARACASGGQLVIMDEPTAAL 171
Cdd:PRK13538 141 ARLWLTRAPLWILDEPFTAI 160
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
13-216 |
5.49e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 56.46 E-value: 5.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 13 HVTAI-SNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGK--------QVHMDSARDALALGITavYQ 83
Cdd:TIGR01271 437 YVTPVlKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRisfspqtsWIMPGTIKDNIIFGLS--YD 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 84 DLALvdqRNVIHNISLGNiptkwgglvvDRKKMREtaenalsymKAKLPSLDIPVsSMSGGQRQAVAIARACASGGQLVI 163
Cdd:TIGR01271 515 EYRY---TSVIKACQLEE----------DIALFPE---------KDKTVLGEGGI-TLSGGQRARISLARAVYKDADLYL 571
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499272610 164 MDEPTAALGIREQRMVLD-VVHDLRAHGTSVLIIShNLDHVfEVADDLLILRGG 216
Cdd:TIGR01271 572 LDSPFTHLDVVTEKEIFEsCLCKLMSNKTRILVTS-KLEHL-KKADKILLLHEG 623
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
13-219 |
5.52e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 55.87 E-value: 5.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 13 HVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNG---KQVHMDSARDALALgitaVYQDLALVD 89
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDiplTKLQLDSWRSRLAV----VSQTPFLFS 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 90 QrNVIHNISLGNiPTKWGGLVVDRKKMRETAENALsymkaKLPS-LDIPVSS----MSGGQRQAVAIARACASGGQLVIM 164
Cdd:PRK10789 403 D-TVANNIALGR-PDATQQEIEHVARLASVHDDIL-----RLPQgYDTEVGErgvmLSGGQKQRISIARALLLNAEILIL 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499272610 165 DEPTAALGIREQRMVLdvvHDLR--AHGTSVLIISHNLDHVFEvADDLLILRGGRVV 219
Cdd:PRK10789 476 DDALSAVDGRTEHQIL---HNLRqwGEGRTVIISAHRLSALTE-ASEILVMQHGHIA 528
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-167 |
8.25e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 55.23 E-value: 8.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRF-GHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQV-HMDSA-RDalalg 77
Cdd:PRK11650 3 GLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVnELEPAdRD----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 78 ITAVYQDLALVDQRNVIHNISLGnipTKWGGlvVDRKKMRETAENAlsymkAKL----PSLDIPVSSMSGGQRQAVAIAR 153
Cdd:PRK11650 78 IAMVFQNYALYPHMSVRENMAYG---LKIRG--MPKAEIEERVAEA-----ARIlelePLLDRKPRELSGGQRQRVAMGR 147
|
170
....*....|....
gi 499272610 154 ACASGGQLVIMDEP 167
Cdd:PRK11650 148 AIVREPAVFLFDEP 161
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
32-203 |
9.42e-09 |
|
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: 55.33 E-value: 9.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 32 LLGDNGAGKSTLVKMICGTYKPTQGSVWVN-GKQV-------HMDSARDALALGITAVYQDLALVDQRNVIHNI------ 97
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVDKDFNGEARPQpGIKVgylpqepQLDPTKTVRENVEEGVAEIKDALDRFNEISAKyaepda 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 98 ----------SLGNIPTKWGGLVVDRKkmRETAENALsymkaKLPSLDIPVSSMSGGQRQAVAIARACASGGQLVIMDEP 167
Cdd:TIGR03719 116 dfdklaaeqaELQEIIDAADAWDLDSQ--LEIAMDAL-----RCPPWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEP 188
|
170 180 190
....*....|....*....|....*....|....*....
gi 499272610 168 TAALgirEQRMVLDVVHDLRAHGTSVLIISHN---LDHV 203
Cdd:TIGR03719 189 TNHL---DAESVAWLERHLQEYPGTVVAVTHDryfLDNV 224
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
16-218 |
1.17e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 54.90 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 16 AISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKqvhmdsardALALGITAvyqdlALVDQRNVIH 95
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS---------AALIAISS-----GLNGQLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 96 NISLgniptkwGGLV--VDRKKMRETAENALSYMK-AKLpsLDIPVSSMSGGQRQAVAIARACASGGQLVIMDEptaALG 172
Cdd:PRK13545 105 NIEL-------KGLMmgLTKEKIKEIIPEIIEFADiGKF--IYQPVKTYSSGMKSRLGFAISVHINPDILVIDE---ALS 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499272610 173 IREQRMV---LDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRV 218
Cdd:PRK13545 173 VGDQTFTkkcLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQV 221
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
16-218 |
1.29e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 54.05 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 16 AISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGkqvhmdsarDALALGITAvyqdlALVDQRNVIH 95
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG---------EVSVIAISA-----GLSGQLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 96 NISLgniptKWGGLVVDRKKMRETAENALSYmkAKLPS-LDIPVSSMSGGQRQAVAIARACASGGQLVIMDEptaALGIR 174
Cdd:PRK13546 105 NIEF-----KMLCMGFKRKEIKAMTPKIIEF--SELGEfIYQPVKKYSSGMRAKLGFSINITVNPDILVIDE---ALSVG 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499272610 175 EQRMV---LDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRV 218
Cdd:PRK13546 175 DQTFAqkcLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-221 |
1.88e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 53.97 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAG--KSTLVKMICGT---YKPTQGSVWVNGKQvhmdsardalAL 76
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPdagRRPWRF*TWCANRR----------AL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 77 GITAVYQDLALVDQRNVIHNISlgNIPTKWGGLVVDRKKMRETAENALSYMKAKlPSLDIPVSSMSGGQRQAVAIARACA 156
Cdd:NF000106 84 RRTIG*HRPVR*GRRESFSGRE--NLYMIGR*LDLSRKDARARADELLERFSLT-EAAGRAAAKYSGGMRRRLDLAASMI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499272610 157 SGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAE 221
Cdd:NF000106 161 GRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIAD 225
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-221 |
2.22e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.60 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 17 ISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQ-------GSV-------WVNGKQVH--------MDSARDAL 74
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAEtssvvirGSVayvpqvsWIFNATVRenilfgsdFESERYWR 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 75 ALGITAVYQDLALVDQRnvihnislgniptkwgglvvDRKKMRETAENalsymkaklpsldipvssMSGGQRQAVAIARA 154
Cdd:PLN03232 713 AIDVTALQHDLDLLPGR--------------------DLTEIGERGVN------------------ISGGQKQRVSMARA 754
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499272610 155 CASGGQLVIMDEPTAALGIREQRMVLD--VVHDLRahGTSVLIISHNLdHVFEVADDLLILRGGRVVAE 221
Cdd:PLN03232 755 VYSNSDIYIFDDPLSALDAHVAHQVFDscMKDELK--GKTRVLVTNQL-HFLPLMDRIILVSEGMIKEE 820
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
26-214 |
3.61e-08 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 51.59 E-value: 3.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 26 KGRVTALLGDNGAGKSTLVKMICgtykptqgsvWVNGKQVHMDSARDALALGITAVYQDLALVdqrnvihnislgniptk 105
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDAIG----------LALGGAQSATRRRSGVKAGCIVAAVSAELI----------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 106 wgglvvdrkkmretaenalsymkaklpsldIPVSSMSGGQRQAVAIARACAS----GGQLVIMDEPTAALGIREQRMVLD 181
Cdd:cd03227 73 ------------------------------FTRLQLSGGEKELSALALILALaslkPRPLYILDEIDRGLDPRDGQALAE 122
|
170 180 190
....*....|....*....|....*....|...
gi 499272610 182 VVHDLRAHGTSVLIISHNLDhVFEVADDLLILR 214
Cdd:cd03227 123 AILEHLVKGAQVIVITHLPE-LAELADKLIHIK 154
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-218 |
3.79e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 53.80 E-value: 3.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 17 ISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKqvhmdsardalalgitavyqdLALVDQRNVIHN 96
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS---------------------VAYVPQQAWIQN 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 97 ISLG-NIptkWGGLVVDRKKMRETAENAlsymkAKLPSLDIPVS-----------SMSGGQRQAVAIARACASGGQLVIM 164
Cdd:TIGR00957 713 DSLReNI---LFGKALNEKYYQQVLEAC-----ALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLF 784
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499272610 165 DEPTAALGIREQRMVLDVV---HDLRAHGTSVLiISHNLDHVFEVaDDLLILRGGRV 218
Cdd:TIGR00957 785 DDPLSAVDAHVGKHIFEHVigpEGVLKNKTRIL-VTHGISYLPQV-DVIIVMSGGKI 839
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
17-198 |
3.79e-08 |
|
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: 51.39 E-value: 3.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 17 ISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKptqgsvWVNGKqVHMDSARDALalgitavyqdlaLVDQRnvihn 96
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWP------WGSGR-IGMPEGEDLL------------FLPQR----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 97 islGNIPTkwGGLvvdrkkmREtaenALSYmkaklPSLDIpvssMSGGQRQAVAIARACASGGQLVIMDEPTAALGIREQ 176
Cdd:cd03223 73 ---PYLPL--GTL-------RE----QLIY-----PWDDV----LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESE 127
|
170 180
....*....|....*....|..
gi 499272610 177 RMVLDVvhdLRAHGTSVLIISH 198
Cdd:cd03223 128 DRLYQL---LKELGITVISVGH 146
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-71 |
5.29e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.20 E-value: 5.29e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499272610 3 RVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQvhMDSAR 71
Cdd:NF033858 3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGD--MADAR 69
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-219 |
9.90e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 51.33 E-value: 9.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGT--YKPTQGSVWVNGKQVHMDSARDALALGI 78
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 79 TAVYQ---DLALVDQRNVIhNISLGNIPTKWGGLVVDRKKMRETAEN--ALSYMKAKLPSLDIPVsSMSGGQRQAVAIAR 153
Cdd:PRK09580 81 FMAFQypvEIPGVSNQFFL-QTALNAVRSYRGQEPLDRFDFQDLMEEkiALLKMPEDLLTRSVNV-GFSGGEKKRNDILQ 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499272610 154 ACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHN---LDHVfeVADDLLILRGGRVV 219
Cdd:PRK09580 159 MAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYqriLDYI--KPDYVHVLYQGRIV 225
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
24-215 |
1.45e-07 |
|
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: 50.26 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 24 IRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSvwvngkqvhmdsardalalgitavyqdlalvdqrnvihnislgnip 103
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDN---------------------------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 104 TKWGGLVVdrkkmretaenalSYMKAKLpsldipvsSMSGGQRQAVAIARACASGGQLVIMDEPTAALGIREQRMVLDVV 183
Cdd:cd03222 56 DEWDGITP-------------VYKPQYI--------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAI 114
|
170 180 190
....*....|....*....|....*....|...
gi 499272610 184 HDLRAHGT-SVLIISHNLDHVFEVADDLLILRG 215
Cdd:cd03222 115 RRLSEEGKkTALVVEHDLAVLDYLSDRIHVFEG 147
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
131-220 |
1.75e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 51.75 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 131 LPsLDIPVSSMSGGQRQAVAIAR---ACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLdHVFEVA 207
Cdd:PRK00635 801 LP-LGRPLSSLSGGEIQRLKLAYellAPSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNM-HVVKVA 878
|
90
....*....|....*....
gi 499272610 208 DDLLIL------RGGRVVA 220
Cdd:PRK00635 879 DYVLELgpeggnLGGYLLA 897
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-59 |
1.81e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 51.43 E-value: 1.81e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 499272610 2 LRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSV-W 59
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkW 378
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
51-221 |
2.57e-07 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 51.17 E-value: 2.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 51 YKPTQGSVWVNGKQVHmdsarDALALGITAVY---QDLALVDQRNVIHNISLGNIPTKWGGLVvdrkkmretaENALSYM 127
Cdd:TIGR00630 416 LKPEALAVTVGGKSIA-----DVSELSIREAHeffNQLTLTPEEKKIAEEVLKEIRERLGFLI----------DVGLDYL 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 128 kaklpSLDIPVSSMSGGQRQAVAIARACASG--GQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDHVfE 205
Cdd:TIGR00630 481 -----SLSRAAGTLSGGEAQRIRLATQIGSGltGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTI-R 554
|
170 180
....*....|....*....|..
gi 499272610 206 VADDLLIL------RGGRVVAE 221
Cdd:TIGR00630 555 AADYVIDIgpgageHGGEVVAS 576
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
32-219 |
5.04e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 50.36 E-value: 5.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 32 LLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKqvhmdsarDALALGITAVYQDLALVDQRNV---------IHNISLGNI 102
Cdd:PLN03232 1267 VVGRTGAGKSSMLNALFRIVELEKGRIMIDDC--------DVAKFGLTDLRRVLSIIPQSPVlfsgtvrfnIDPFSEHND 1338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 103 PTKWGGLvvDRKKMRETAENAlSYmkaklpSLDIPVS----SMSGGQRQAVAIARACASGGQLVIMDEPTAALGIREQRM 178
Cdd:PLN03232 1339 ADLWEAL--ERAHIKDVIDRN-PF------GLDAEVSeggeNFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSL 1409
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499272610 179 VLDVVHDlRAHGTSVLIISHNLDHVFEvADDLLILRGGRVV 219
Cdd:PLN03232 1410 IQRTIRE-EFKSCTMLVIAHRLNTIID-CDKILVLSSGQVL 1448
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
20-219 |
7.10e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.84 E-value: 7.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 20 VSANIRKGRVTALLGDNGAGKSTLVKMICG--TYKPTQGSVWVNGKQVHMDS-ARDALALGITAVYQDLALVdQRNVIHN 96
Cdd:PLN03140 899 VTGAFRPGVLTALMGVSGAGKTTLMDVLAGrkTGGYIEGDIRISGFPKKQETfARISGYCEQNDIHSPQVTV-RESLIYS 977
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 97 ISLgNIPTKwgglVVDRKKMR---ETAE----NALSYMKAKLPSldipVSSMSGGQRQAVAIARACASGGQLVIMDEPTA 169
Cdd:PLN03140 978 AFL-RLPKE----VSKEEKMMfvdEVMElvelDNLKDAIVGLPG----VTGLSTEQRKRLTIAVELVANPSIIFMDEPTS 1048
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499272610 170 ALGIREQRMVLDVVHDLRAHGTSVLIISH--NLDhVFEVADDLLIL-RGGRVV 219
Cdd:PLN03140 1049 GLDARAAAIVMRTVRNTVDTGRTVVCTIHqpSID-IFEAFDELLLMkRGGQVI 1100
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
29-198 |
1.49e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.56 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 29 VTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHmdsarDALALGITAVYQDLALVDQRNVIHNISLgniptkWGG 108
Cdd:PRK13541 28 ITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNIN-----NIAKPYCTYIGHNLGLKLEMTVFENLKF------WSE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 109 LVvdrkKMRETAENALSYMKAKlPSLDIPVSSMSGGQRQAVAIARACASGGQLVIMDEPTAALGiREQRMVLDVVHDLRA 188
Cdd:PRK13541 97 IY----NSAETLYAAIHYFKLH-DLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS-KENRDLLNNLIVMKA 170
|
170
....*....|.
gi 499272610 189 H-GTSVLIISH 198
Cdd:PRK13541 171 NsGGIVLLSSH 181
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
3-233 |
1.79e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 48.34 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 3 RVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPT--QGSVWVNGKQVHMDSARDalalgITA 80
Cdd:PLN03211 70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQILKR-----TGF 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 81 VYQDLALVDQ---RNVIHNISLGNIPTKwgglvVDRKKMRETAENALSYMK-AKLPSLDIP---VSSMSGGQRQAVAIAR 153
Cdd:PLN03211 145 VTQDDILYPHltvRETLVFCSLLRLPKS-----LTKQEKILVAESVISELGlTKCENTIIGnsfIRGISGGERKRVSIAH 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 154 ACASGGQLVIMDEPTAAL-GIREQRMVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRVVAEVE-RNAVSHDE 231
Cdd:PLN03211 220 EMLINPSLLILDEPTSGLdATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKgSDAMAYFE 299
|
..
gi 499272610 232 VV 233
Cdd:PLN03211 300 SV 301
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
26-219 |
2.36e-06 |
|
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: 46.21 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 26 KGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVwvngkqvhmdsardalalgitavyqdlalvdqrnVIHNISLGNIPTK 105
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV----------------------------------IYIDGEDILEEVL 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 106 WGGLVVDRkkmretaenalsymkaklpslDIPVSSMSGGQRQAVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHD 185
Cdd:smart00382 47 DQLLLIIV---------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEEL 105
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499272610 186 ------LRAHGTSVLIISHNLDHVFevaDDLLILRGGRVV 219
Cdd:smart00382 106 rlllllKSEKNLTVILTTNDEKDLG---PALLRRRFDRRI 142
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-58 |
2.36e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.24 E-value: 2.36e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSV 58
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI 369
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
17-221 |
3.39e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.81 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 17 ISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQ-GSVWVNGK-----QVH----------------MDSARDAL 74
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRGTvayvpQVSwifnatvrdnilfgspFDPERYER 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 75 ALGITAVYQDLALvdqrnvihnislgnIPtkwGGlvvDRKKMRETAENalsymkaklpsldipvssMSGGQRQAVAIARA 154
Cdd:PLN03130 713 AIDVTALQHDLDL--------------LP---GG---DLTEIGERGVN------------------ISGGQKQRVSMARA 754
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 155 CASGGQLVIMDEPTAALGIREQRMVLD-VVHDLRAHGTSVLIIS--HNLDHVfevaDDLLILRGGRVVAE 221
Cdd:PLN03130 755 VYSNSDVYIFDDPLSALDAHVGRQVFDkCIKDELRGKTRVLVTNqlHFLSQV----DRIILVHEGMIKEE 820
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
20-219 |
5.48e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.04 E-value: 5.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 20 VSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKqvhmdsarDALALGITAVYQDLALVDQRNVIHNISL 99
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGC--------DISKFGLMDLRKVLGIIPQAPVLFSGTV 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 100 ---------GNIPTKWGGLvvDRKKMRETAE-NALSymkaklpsLDIPVS----SMSGGQRQAVAIARACASGGQLVIMD 165
Cdd:PLN03130 1330 rfnldpfneHNDADLWESL--ERAHLKDVIRrNSLG--------LDAEVSeageNFSVGQRQLLSLARALLRRSKILVLD 1399
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499272610 166 EPTAALGIREQRMVLDVV-HDLRAhgTSVLIISHNLDHVFEvADDLLILRGGRVV 219
Cdd:PLN03130 1400 EATAAVDVRTDALIQKTIrEEFKS--CTMLIIAHRLNTIID-CDRILVLDAGRVV 1451
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
31-218 |
8.78e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.39 E-value: 8.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 31 ALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKqVHMdsardalalgitavyqdlALVDQRNVihnislgniptkwGGLv 110
Cdd:PLN03073 539 AMVGPNGIGKSTILKLISGELQPSSGTVFRSAK-VRM------------------AVFSQHHV-------------DGL- 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 111 vdrkkmrETAENALSYM------------KAKLPSLDI-------PVSSMSGGQRQAVAIARACASGGQLVIMDEPTAAL 171
Cdd:PLN03073 586 -------DLSSNPLLYMmrcfpgvpeqklRAHLGSFGVtgnlalqPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHL 658
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499272610 172 GIREqrmVLDVVHDLRAHGTSVLIISHNLDHVFEVADDLLILRGGRV 218
Cdd:PLN03073 659 DLDA---VEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-198 |
9.07e-06 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 46.34 E-value: 9.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 1 MLRVQNLTKRF--GHVTaISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHM----------D 68
Cdd:COG4178 362 ALALEDLTLRTpdGRPL-LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLflpqrpylplG 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 69 SARDALAL-GITAVYQDLALvdqRNVIHNISLGNIptkwgglvVDRkkmretaenalsymkaklpsLDIPVS---SMSGG 144
Cdd:COG4178 441 TLREALLYpATAEAFSDAEL---REALEAVGLGHL--------AER--------------------LDEEADwdqVLSLG 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499272610 145 QRQAVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDlRAHGTSVLIISH 198
Cdd:COG4178 490 EQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGH 542
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
31-171 |
1.14e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 45.22 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 31 ALL--GDNGAGKSTLVKMICGTYKPTQGSVWVNGKQV-HMDSARDALALG-ITAVYQDLALVDQRNVIHNISlgniptkw 106
Cdd:PRK13543 39 ALLvqGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAtRGDRSRFMAYLGhLPGLKADLSTLENLHFLCGLH-------- 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499272610 107 gglvvdRKKMRETAENALSYMkAKLPSLDIPVSSMSGGQRQAVAIARACASGGQLVIMDEPTAAL 171
Cdd:PRK13543 111 ------GRRAKQMPGSALAIV-GLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANL 168
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-58 |
1.36e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.65 E-value: 1.36e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 499272610 1 MLRVQNLTKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSV 58
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNV 58
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
32-168 |
1.62e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.49 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 32 LLGDNGAGKSTLVKMICGTYKPTQGSVWvngkqvhmdsardaLALGITAVY--QDLALVDQRNVIHNISLGNIPTK---- 105
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEAR--------------PAPGIKVGYlpQEPQLDPEKTVRENVEEGVAEVKaald 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 106 --------------------------------WGGLVVDRKkmRETAENALsymkaKLPSLDIPVSSMSGGQRQAVAIAR 153
Cdd:PRK11819 104 rfneiyaayaepdadfdalaaeqgelqeiidaADAWDLDSQ--LEIAMDAL-----RCPPWDAKVTKLSGGERRRVALCR 176
|
170
....*....|....*
gi 499272610 154 ACASGGQLVIMDEPT 168
Cdd:PRK11819 177 LLLEKPDMLLLDEPT 191
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
124-208 |
2.84e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.20 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 124 LSYMkaklpSLDIPVSSMSGGQRQAVAIARACasGGQLV----IMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHN 199
Cdd:PRK00635 465 LPYL-----TPERALATLSGGEQERTALAKHL--GAELIgityILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD 537
|
....*....
gi 499272610 200 lDHVFEVAD 208
Cdd:PRK00635 538 -EQMISLAD 545
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-246 |
6.23e-05 |
|
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: 44.17 E-value: 6.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 17 ISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKQVHMDSARDaLALGITAVYQDLALVDQ--RNVI 94
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHD-LRFKITIIPQDPVLFSGslRMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 95 HNISLGNIPTKWGGLVVDRKKmretaenalSYMKAKLPSLDIPVS----SMSGGQRQAVAIARACASGGQLVIMDEPTAA 170
Cdd:TIGR00957 1381 DPFSQYSDEEVWWALELAHLK---------TFVSALPDKLDHECAeggeNLSVGQRQLVCLARALLRKTKILVLDEATAA 1451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499272610 171 LGIREQRMVLDVVHDlRAHGTSVLIISHNLDHVFEVADDLLILRGgrVVAEVerNAVSHDEVVRLILAGQPRDADL 246
Cdd:TIGR00957 1452 VDLETDNLIQSTIRT-QFEDCTVLTIAHRLNTIMDYTRVIVLDKG--EVAEF--GAPSNLLQQRGIFYSMAKDAGL 1522
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
2-219 |
9.99e-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: 42.59 E-value: 9.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 2 LRVQNLTKRFGHV--TAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGTYKPTQGSVWVNGKqvhmdsarDALALGIT 79
Cdd:cd03288 20 IKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGI--------DISKLPLH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 80 AVYQDLALVDQRNVIHN--ISLGNIPTKwgglVVDRKKMRETAENA-LSYMKAKLPS-LDIPVS----SMSGGQRQAVAI 151
Cdd:cd03288 92 TLRSRLSIILQDPILFSgsIRFNLDPEC----KCTDDRLWEALEIAqLKNMVKSLPGgLDAVVTeggeNFSVGQRQLFCL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499272610 152 ARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTsVLIISHNLDHVFEvADDLLILRGGRVV 219
Cdd:cd03288 168 ARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRT-VVTIAHRVSTILD-ADLVLVLSRGILV 233
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
140-200 |
1.08e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.09 E-value: 1.08e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499272610 140 SMSGGQRQAVAIARACASGGQLVIMDEPTAALGIREQRMVLDVVHDLRAHGTSVLI-ISHNL 200
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIItIAHRI 1419
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
14-219 |
1.08e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.17 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 14 VTAISNVSANIRKGRVTALLGDNGAGKSTLVKMICGT----YKPTQGSVWVNG-------KQVHMDSARDALA---LGIT 79
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNtdgfHIGVEGVITYDGitpeeikKHYRGDVVYNAETdvhFPHL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 80 AVYQDLALVDQRNVIHNISLGniptkwgglvVDR----KKMRETAENA--LSYMKAKLPSLDIpVSSMSGGQRQAVAIAR 153
Cdd:TIGR00956 154 TVGETLDFAARCKTPQNRPDG----------VSReeyaKHIADVYMATygLSHTRNTKVGNDF-VRGVSGGERKRVSIAE 222
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499272610 154 ACASGGQLVIMDEPTAALgirEQRMVLDVVHDLRA-----HGTSVLIISHNLDHVFEVADDLLILRGGRVV 219
Cdd:TIGR00956 223 ASLGGAKIQCWDNATRGL---DSATALEFIRALKTsanilDTTPLVAIYQCSQDAYELFDKVIVLYEGYQI 290
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
2-45 |
8.16e-04 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 40.03 E-value: 8.16e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 499272610 2 LRVQNLtKRFGHVTAISNVSANIRKGRVTALLGDNGAGKSTLVK 45
Cdd:COG1106 5 FSIENF-RSFKDELTLSMVASGLRLLRVNLIYGANASGKSNLLE 47
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
32-198 |
1.19e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 39.61 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 32 LLGDNGAGKSTLVKMICGTYKptQG----------------SVW--------VNGkQVHMD-----SARDALALGI---T 79
Cdd:PRK10938 291 IVGPNGAGKSTLLSLITGDHP--QGysndltlfgrrrgsgeTIWdikkhigyVSS-SLHLDyrvstSVRNVILSGFfdsI 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 80 AVYQDlalvdqrnvihnislgniptkwgglVVDRKKMRETAENALSYMKAKLPslDIPVSSMSGGQRQAVAIARACASGG 159
Cdd:PRK10938 368 GIYQA-------------------------VSDRQQKLAQQWLDILGIDKRTA--DAPFHSLSWGQQRLALIVRALVKHP 420
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499272610 160 QLVIMDEPTAALGIREQRMVLDVVHDLRAHG-TSVLIISH 198
Cdd:PRK10938 421 TLLILDEPLQGLDPLNRQLVRRFVDVLISEGeTQLLFVSH 460
|
|
| HSP70 |
pfam00012 |
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ... |
114-206 |
1.45e-03 |
|
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves repeated cycles of substrate binding and release. Hsp70 activity is ATP dependent. Hsp70 proteins are made up of two regions: the amino terminus is the ATPase domain and the carboxyl terminus is the substrate binding region.
Pssm-ID: 394970 [Multi-domain] Cd Length: 598 Bit Score: 39.55 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 114 KKMRETAEnalSYMKAKLPSLDIPVSS-MSGGQRQAVAIARACASGGQLVIMDEPTA---ALGIREQ---RMVLdvVHDL 186
Cdd:pfam00012 119 QKLKETAE---AYLGKPVTDAVITVPAyFNDAQRQATKDAGQIAGLNVLRIVNEPTAaalAYGLDKTdkeRNIA--VYDL 193
|
90 100
....*....|....*....|...
gi 499272610 187 rAHGT---SVLIIShnlDHVFEV 206
Cdd:pfam00012 194 -GGGTfdvSILEIG---RGVFEV 212
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
133-221 |
3.80e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.47 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 133 SLDIPVSSMSGG--QRqavaIARACASGGQLV----IMDEPTAALGIREQRMVLDVVHDLRAHGTSVLIISHNLDhVFEV 206
Cdd:COG0178 478 TLDRSAGTLSGGeaQR----IRLATQIGSGLVgvlyVLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHDED-TIRA 552
|
90 100
....*....|....*....|.
gi 499272610 207 ADDLLIL------RGGRVVAE 221
Cdd:COG0178 553 ADYIIDIgpgageHGGEVVAQ 573
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
135-173 |
3.87e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 38.39 E-value: 3.87e-03
10 20 30
....*....|....*....|....*....|....*....
gi 499272610 135 DIPVSSMSGGQRQAVAIARACASGGQLVIMDEPTAALGI 173
Cdd:PRK11147 151 DAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDI 189
|
|
| ASKHA_NBD_HSP70_Ssc1_3 |
cd11734 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein ... |
103-206 |
9.25e-03 |
|
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein Ssc1p and Ssc3p and similar proteins; This subgroup includes Saccharomyces cerevisiae Stress-Seventy subfamily C proteins, Ssc1p (also called import motor subunit, mitochondrial; endonuclease SceI 75 kDa subunit; mtHSP70; ENS1; endonuclease SceI 75 kDa subunit) and sc3p (also called extracellular mutant protein 10/Ecm10). Ssc1p is an essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. It constitutes the ATP-driven core of the motor and binds the precursor preprotein. It is required for the import of the processed frataxin homolog YFH1 into the mitochondrion. Ssc1p also acts as a non-catalytic component of endonuclease SceI (endo.SceI), which cleaves specifically at multiple sites on mitochondrial DNA and produces double-stranded breaks. Ssc1p confers broader sequence specificity, greater stability, and higher activity on the catalytic subunit. Ssc3p plays a role in facilitating the assembly of some protein complexes inside the mitochondria. It may initiate the events that lead to refolding of imported precursors in the matrix space.
Pssm-ID: 466840 [Multi-domain] Cd Length: 378 Bit Score: 37.04 E-value: 9.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499272610 103 PTKWGGLVVDrkKMRETAENALSyMKAKLPSLDIPvSSMSGGQRQAVAIARACASGGQLVIMDEPTAA-----LGIREQR 177
Cdd:cd11734 111 PSQIGAFVLG--KMKETAEGYLG-KPVKNAVVTVP-AYFNDSQRQATKDAGQIAGLNVLRVINEPTAAalaygLDKSGDK 186
|
90 100 110
....*....|....*....|....*....|..
gi 499272610 178 MVldVVHDLrAHGT---SVLIISHNldhVFEV 206
Cdd:cd11734 187 VI--AVYDL-GGGTfdiSILEIQKG---VFEV 212
|
|
| |
