|
Name |
Accession |
Description |
Interval |
E-value |
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-232 |
1.17e-165 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 456.35 E-value: 1.17e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 1 MLKLTDVTWLYQHLPMRFTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAKRPVSMLFQEN 80
Cdd:PRK10771 1 MLKLTDITWLYHHLPMRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 81 NLFTHLTVRQNIALGMHPGLRLNDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSAL 160
Cdd:PRK10771 81 NLFSHLTVAQNIGLGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 779793995 161 DPALRQEMLTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELLKGNAAASSLLGISA 232
Cdd:PRK10771 161 DPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKASASALLGIKS 232
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-230 |
1.34e-150 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 418.39 E-value: 1.34e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 1 MLKLTDVTWLYQHLPMRFTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAKRPVSMLFQEN 80
Cdd:COG3840 1 MLRLDDLTYRYGDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 81 NLFTHLTVRQNIALGMHPGLRLNDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSAL 160
Cdd:COG3840 81 NLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 779793995 161 DPALRQEMLTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELLKGN--AAASSLLGI 230
Cdd:COG3840 161 DPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEppPALAAYLGI 232
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
2-212 |
1.71e-117 |
|
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: 334.08 E-value: 1.71e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 2 LKLTDVTWLYQHLPMRFTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAKRPVSMLFQENN 81
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 82 LFTHLTVRQNIALGMHPGLRLNDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALD 161
Cdd:cd03298 81 LFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 779793995 162 PALRQEMLTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDG 212
Cdd:cd03298 161 PALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
2-214 |
5.97e-115 |
|
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: 327.59 E-value: 5.97e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 2 LKLTDVTWLYQHLPMRFTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAKRPVSMLFQENN 81
Cdd:TIGR01277 1 LALDKVRYEYEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 82 LFTHLTVRQNIALGMHPGLRLNDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALD 161
Cdd:TIGR01277 81 LFAHLTVRQNIGLGLHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 779793995 162 PALRQEMLTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVT 214
Cdd:TIGR01277 161 PLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSDC 213
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-212 |
3.34e-89 |
|
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: 262.46 E-value: 3.34e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 2 LKLTDVTWLY--QHLPMRFTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAKRPVSMLFQE 79
Cdd:cd03259 1 LELKGLSKTYgsVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 80 NNLFTHLTVRQNIALGMHPGLRLNDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSA 159
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 779793995 160 LDPALRQEMLTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDG 212
Cdd:cd03259 161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
18-217 |
2.14e-76 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 234.61 E-value: 2.14e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 18 FTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAKRPVSMLFQENNLFTHLTVRQNIALGmh 97
Cdd:COG3842 24 VSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMVFQDYALFPHLTVAENVAFG-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 98 pgLRL----NDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQ 173
Cdd:COG3842 102 --LRMrgvpKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELR 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 779793995 174 DVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEEL 217
Cdd:COG3842 180 RLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
18-209 |
9.33e-72 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 219.58 E-value: 9.33e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 18 FTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPakrPVSMLFQENNLFTHLTVRQNIALGMH 97
Cdd:COG1116 30 VSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP---DRGVVFQEPALLPWLTVLDNVALGLE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 98 PGLRLNDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQDVCQ 177
Cdd:COG1116 107 LRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQ 186
|
170 180 190
....*....|....*....|....*....|....
gi 779793995 178 RQQLTMLMVSHSIEDAARIAPRSVVIAE--GRIV 209
Cdd:COG1116 187 ETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIV 220
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
19-229 |
3.90e-70 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 218.48 E-value: 3.90e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQD-HTHTPPAKRPVSMLFQENNLFTHLTVRQNIALGMH 97
Cdd:COG1118 22 SLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDlFTNLPPRERRVGFVFQHYALFPHMTVAENIAFGLR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 98 PGLRLNDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQDVCQ 177
Cdd:COG1118 102 VRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 779793995 178 RQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELLK--GNAAASSLLG 229
Cdd:COG1118 182 ELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDrpATPFVARFLG 235
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
18-217 |
2.12e-69 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 216.48 E-value: 2.12e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 18 FTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAKRPVSMLFQENNLFTHLTVRQNIALGmh 97
Cdd:COG3839 22 IDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMVFQSYALYPHMTVYENIAFP-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 98 pgLRLN----DAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQ 173
Cdd:COG3839 100 --LKLRkvpkAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIK 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 779793995 174 DVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEEL 217
Cdd:COG3839 178 RLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-209 |
3.49e-67 |
|
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: 206.55 E-value: 3.49e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 2 LKLTDVTWLYQHLPMRFT------LSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQdhthtpPAKRP--- 72
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTaledisLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE------PVTGPgpd 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 73 VSMLFQENNLFTHLTVRQNIALGmhpgLRLNDAQRHKLEEIAAQM----GIAGFIDRLPGELSGGQRQRVALARCLVREQ 148
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALG----LELQGVPKAEARERAEELlelvGLSGFENAYPHQLSGGMRQRVALARALAVDP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 779793995 149 PMLLLDEPFSALDPALRQEMLTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAE--GRIV 209
Cdd:cd03293 151 DVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIV 213
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-207 |
2.47e-65 |
|
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: 200.49 E-value: 2.47e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 2 LKLTDVTWLY--QHLPMRFTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHT----HTPPAKRPVSM 75
Cdd:cd03229 1 LELKNVSKRYgqKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdledELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 76 LFQENNLFTHLTVRQNIALGmhpglrlndaqrhkleeiaaqmgiagfidrlpgeLSGGQRQRVALARCLVREQPMLLLDE 155
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 779793995 156 PFSALDPALRQEMLTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGR 207
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-218 |
1.76e-62 |
|
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: 195.65 E-value: 1.76e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 1 MLKLTDVTWLYQHLPM--RFTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPP---AKRpVSM 75
Cdd:COG1120 1 MLEAENLSVGYGGRPVldDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRrelARR-IAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 76 LFQENNLFTHLTVRQNIALGMHPGL----RLNDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPML 151
Cdd:COG1120 80 VPQEPPAPFGLTVRELVALGRYPHLglfgRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 779793995 152 LLDEPFSALDPALRQEMLTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELL 218
Cdd:COG1120 160 LLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
18-219 |
2.60e-62 |
|
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: 194.81 E-value: 2.60e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 18 FTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAK-----RPVSMLFQENNLFTHLTVRQNI 92
Cdd:COG1127 24 VSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyelrRRIGMLFQGGALFDSLTVFENV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 93 ALGMHPGLRLNDAQRHKL-EEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTL 171
Cdd:COG1127 104 AFPLREHTDLSEAEIRELvLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDEL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 779793995 172 VQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELLK 219
Cdd:COG1127 184 IRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
17-217 |
4.43e-61 |
|
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: 191.68 E-value: 4.43e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 17 RFTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAKRPVSMLFQENNLFTHLTVRQNIALGM 96
Cdd:cd03300 18 GVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQNYALFPHLTVFENIAFGL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 97 HPGLRLNDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQDVC 176
Cdd:cd03300 98 RLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQ 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 779793995 177 QRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEEL 217
Cdd:cd03300 178 KELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
19-219 |
2.21e-60 |
|
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: 189.47 E-value: 2.21e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAK--RPVSMLFQ--ENNLFtHLTVRQNIAL 94
Cdd:COG1122 21 SLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLVFQnpDDQLF-APTVEEDVAF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 95 GMHPgLRLNDAQ-RHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQ 173
Cdd:COG1122 100 GPEN-LGLPREEiRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLK 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 779793995 174 DVcQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELLK 219
Cdd:COG1122 179 RL-NKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFS 223
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
18-212 |
5.12e-60 |
|
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: 188.27 E-value: 5.12e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 18 FTLSV---LQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVI------DNQDHTHTPPAKRPVSMLFQENNLFTHLTV 88
Cdd:cd03297 13 FTLKIdfdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLngtvlfDSRKKINLPPQQRKIGLVFQQYALFPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 89 RQNIALGMhPGLRlNDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEM 168
Cdd:cd03297 93 RENLAFGL-KRKR-NREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 779793995 169 LTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDG 212
Cdd:cd03297 171 LPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
18-218 |
5.28e-60 |
|
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: 192.62 E-value: 5.28e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 18 FTLSV---LQGERI-AVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDN---QDHTHT---PPAKRPVSMLFQENNLFTHLT 87
Cdd:COG4148 14 FTLDVdftLPGRGVtALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSARGiflPPHRRRIGYVFQEARLFPHLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 88 VRQNIALGMHPGLRLNDAQRhkLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQE 167
Cdd:COG4148 94 VRGNLLYGRKRAPRAERRIS--FDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 779793995 168 MLTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELL 218
Cdd:COG4148 172 ILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVL 222
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
19-217 |
6.70e-60 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 189.11 E-value: 6.70e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAK-----RPVSMLFQENNLFTHLTVRQNI- 92
Cdd:COG3638 23 SLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrRRIGMIFQQFNLVPRLSVLTNVl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 93 --ALGMHPGLR-----LNDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALR 165
Cdd:COG3638 103 agRLGRTSTWRsllglFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTA 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 779793995 166 QEMLTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEEL 217
Cdd:COG3638 183 RQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
19-220 |
7.57e-60 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 188.35 E-value: 7.57e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQD-HTHTPPAKRPVSMLFQENNLFTHLTVRQNIAL--G 95
Cdd:COG1131 20 SLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDvARDPAEVRRRIGYVPQEPALYPDLTVRENLRFfaR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 96 MHpGLRLNDAQRhKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQDV 175
Cdd:COG1131 100 LY-GLPRKEARE-RIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLREL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 779793995 176 CqRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELLKG 220
Cdd:COG1131 178 A-AEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-209 |
6.94e-59 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 185.63 E-value: 6.94e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 1 MLKLTDVTWLYQHLPMRFT------LSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAKRP-- 72
Cdd:COG1136 4 LLELRNLTKSYGTGEGEVTalrgvsLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELArl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 73 ----VSMLFQENNLFTHLTVRQNIALGMHP-GLRLNDAqRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVRE 147
Cdd:COG1136 84 rrrhIGFVFQFFNLLPELTALENVALPLLLaGVSRKER-RERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 779793995 148 QPMLLLDEPFSALDPALRQEMLTLVQDVCQRQQLTMLMVSHSiEDAARIAPRSVVIAEGRIV 209
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRIV 223
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-208 |
1.39e-58 |
|
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: 184.62 E-value: 1.39e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 2 LKLTDVTWLYQHLPMRF------TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAKRP--- 72
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqalkgvSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 73 ---VSMLFQENNLFTHLTVRQNIALGMHPGLRLNDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQP 149
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 779793995 150 MLLLDEPFSALDPALRQEMLTLVQDVCQRQQLTMLMVSHSiEDAARIAPRSVVIAEGRI 208
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
19-219 |
4.99e-58 |
|
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: 183.86 E-value: 4.99e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAK-----RPVSMLFQENNLFTHLTVRQNIA 93
Cdd:cd03261 20 DLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMGMLFQSGALFDSLTVFENVA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 94 LGMHPGLRLNDAQ-----RHKLEEIaaqmGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEM 168
Cdd:cd03261 100 FPLREHTRLSEEEireivLEKLEAV----GLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVI 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 779793995 169 LTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELLK 219
Cdd:cd03261 176 DDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
20-219 |
7.88e-58 |
|
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: 183.31 E-value: 7.88e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 20 LSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAKRPVSMLFQENNLFTHLTVRQNIALGMHpg 99
Cdd:cd03299 20 LEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQNYALFPHMTVYKNIAYGLK-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 100 LRLND-AQRH-KLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQDVCQ 177
Cdd:cd03299 98 KRKVDkKEIErKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRK 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 779793995 178 RQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELLK 219
Cdd:cd03299 178 EFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFK 219
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
17-209 |
2.12e-57 |
|
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: 181.30 E-value: 2.12e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 17 RFTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAKRPVSMLFQENNLFTHLTVRQNIALGm 96
Cdd:cd03301 18 DLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQNYALYPHMTVYDNIAFG- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 97 hpgLRLNDAQR----HKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLV 172
Cdd:cd03301 97 ---LKLRKVPKdeidERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAEL 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 779793995 173 QDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIV 209
Cdd:cd03301 174 KRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-194 |
6.12e-57 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 180.37 E-value: 6.12e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 1 MLKLTDVTWLYQHLPM--RFTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQP---VSGSIVIDNQDHTHTPPAKRPVSM 75
Cdd:COG4136 1 MLSLENLTITLGGRPLlaPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQRRIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 76 LFQENNLFTHLTVRQNIALGMHPGLRLNdAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDE 155
Cdd:COG4136 81 LFQDDLLFPHLSVGENLAFALPPTIGRA-QRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDE 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 779793995 156 PFSALDPALRQEMLTLVQDVCQRQQLTMLMVSHSIEDAA 194
Cdd:COG4136 160 PFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAP 198
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-217 |
6.61e-57 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 185.42 E-value: 6.61e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 1 MLKLTDVTWLY--QHLPMRFTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAKRPVSMLFQ 78
Cdd:PRK11607 19 LLEIRNLTKSFdgQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 79 ENNLFTHLTVRQNIALGMHPGLRLNDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFS 158
Cdd:PRK11607 99 SYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 779793995 159 ALDPALRQEMLTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEEL 217
Cdd:PRK11607 179 ALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
20-217 |
8.38e-55 |
|
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: 175.61 E-value: 8.38e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 20 LSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAKRPVSMLFQENNLFTHLTVRQNIALGM--- 96
Cdd:cd03296 23 LDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQHYALFRHMTVFDNVAFGLrvk 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 97 HPGLRLNDAQ-RHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQDV 175
Cdd:cd03296 103 PRSERPPEAEiRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 779793995 176 CQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEEL 217
Cdd:cd03296 183 HDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
19-207 |
3.39e-54 |
|
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: 173.04 E-value: 3.39e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAK--RPVSMLFQ--ENNLFTHlTVRQNIAL 94
Cdd:cd03225 21 SLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrRKVGLVFQnpDDQFFGP-TVEEEVAF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 95 GM-HPGLRLNDAQRhKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQ 173
Cdd:cd03225 100 GLeNLGLPEEEIEE-RVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLK 178
|
170 180 190
....*....|....*....|....*....|....
gi 779793995 174 DVcQRQQLTMLMVSHSIEDAARIAPRSVVIAEGR 207
Cdd:cd03225 179 KL-KAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-233 |
5.83e-54 |
|
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: 173.84 E-value: 5.83e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 1 MLKLTDVTWLYQHLPMRFT------LSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAK--RP 72
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPvlkdvsLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 73 VSMLFQ--ENNLFTHLTVRQNIALGMHpGLRLNDAQRhKLEEIAAQMGI-AGFIDRLPGELSGGQRQRVALARCLVREQP 149
Cdd:COG1124 81 VQMVFQdpYASLHPRHTVDRILAEPLR-IHGLPDREE-RIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 150 MLLLDEPFSALDPALRQEMLTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELLKG--NAAASSL 227
Cdd:COG1124 159 LLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGpkHPYTREL 238
|
....*.
gi 779793995 228 LGISAP 233
Cdd:COG1124 239 LAASLA 244
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-216 |
8.39e-54 |
|
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: 173.69 E-value: 8.39e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 1 MLKLTDVTwlyqhlpMRF---------TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAKR 71
Cdd:COG0411 4 LLEVRGLT-------KRFgglvavddvSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 72 P---VSMLFQENNLFTHLTVRQNIALGMHPGLRLN---------------DAQRHKLEEIAAQMGIAGFIDRLPGELSGG 133
Cdd:COG0411 77 ArlgIARTFQNPRLFPELTVLENVLVAAHARLGRGllaallrlprarreeREARERAEELLERVGLADRADEPAGNLSYG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 134 QRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGV 213
Cdd:COG0411 157 QQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGT 236
|
...
gi 779793995 214 TEE 216
Cdd:COG0411 237 PAE 239
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
18-212 |
1.21e-53 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 176.68 E-value: 1.21e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 18 FTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAKRPVSMLFQENNLFTHLTVRQNIALgmh 97
Cdd:PRK09452 33 LDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQSYALFPHMTVFENVAF--- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 98 pGLRLndaQRHKLEEIAAQMGIA-------GFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEM-L 169
Cdd:PRK09452 110 -GLRM---QKTPAAEITPRVMEAlrmvqleEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMqN 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 779793995 170 TLVQdvCQRQ-QLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDG 212
Cdd:PRK09452 186 ELKA--LQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDG 227
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
19-218 |
1.80e-53 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 172.10 E-value: 1.80e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQD----HTHTPPAKRPVSMLFQENNLFTHLTVRQNIAL 94
Cdd:COG1126 21 SLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDltdsKKDINKLRRKVGMVFQQFNLFPHLTVLENVTL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 95 GMHPGLRLNDAQRHKL-EEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQ 173
Cdd:COG1126 101 APIKVKKMSKAEAEERaMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMR 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 779793995 174 DVcQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELL 218
Cdd:COG1126 181 DL-AKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFF 224
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
19-219 |
3.06e-53 |
|
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: 171.47 E-value: 3.06e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPP---AKRPVSMLFQENNLFTHLTVRQNIALG 95
Cdd:cd03219 20 SFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPheiARLGIGRTFQIPRLFPELTVLENVMVA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 96 MHPGLRLN----------DAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALR 165
Cdd:cd03219 100 AQARTGSGlllararreeREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEET 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 779793995 166 QEMLTLVQDVcQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELLK 219
Cdd:cd03219 180 EELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
19-218 |
3.72e-53 |
|
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: 178.94 E-value: 3.72e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAK-----RPVSMLFQ--ENNLFTHLTVRQN 91
Cdd:COG1123 285 SLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrelrRRVQMVFQdpYSSLNPRMTVGDI 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 92 IALGMHPGLRLNDAQRH-KLEEIAAQMGI-AGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEML 169
Cdd:COG1123 365 IAEPLRLHGLLSRAERReRVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQIL 444
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 779793995 170 TLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELL 218
Cdd:COG1123 445 NLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVF 493
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-218 |
4.97e-53 |
|
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: 170.84 E-value: 4.97e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 1 MLKLTDVTWLYQHLPMRFT------LSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAK---- 70
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTalkdvsLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 71 -RPVSMLFQENNLFTHLTVRQNIALGM-HPGLRLNDAQRhKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQ 148
Cdd:cd03258 81 rRRIGMIFQHFNLLSSRTVFENVALPLeIAGVPKAEIEE-RVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 149 PMLLLDEPFSALDPALRQEMLTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELL 218
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVF 229
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-208 |
5.79e-52 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 167.30 E-value: 5.79e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 2 LKLTDVTWLYQHLPM--RFTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAK--RPVSMLF 77
Cdd:COG4619 1 LELEGLSFRVGGKPIlsPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 78 QENNLFTHlTVRQNIALGMHpgLRLNDAQRHKLEEIAAQMGI-AGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEP 156
Cdd:COG4619 81 QEPALWGG-TVRDNLPFPFQ--LRERKFDRERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 779793995 157 FSALDPALRQEMLTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRI 208
Cdd:COG4619 158 TSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
19-217 |
5.96e-52 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 168.52 E-value: 5.96e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAK-----RPVSMLFQENNLFTHLTVRQNI- 92
Cdd:cd03256 21 SLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrRQIGMIFQQFNLIERLSVLENVl 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 93 --ALGMHPGLR-----LNDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALR 165
Cdd:cd03256 101 sgRLGRRSTWRslfglFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASS 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 779793995 166 QEMLTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEEL 217
Cdd:cd03256 181 RQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-209 |
1.05e-51 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 168.50 E-value: 1.05e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 1 MLKLTDVTWLY----QHLPM--RFTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHtPPAKRPVs 74
Cdd:COG4525 3 MLTVRHVSVRYpgggQPQPAlqDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGADRGV- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 75 mLFQENNLFTHLTVRQNIALGmhpgLRLN---DAQRHKL-EEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPM 150
Cdd:COG4525 81 -VFQKDALLPWLNVLDNVAFG----LRLRgvpKAERRARaEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRF 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 779793995 151 LLLDEPFSALDPALRQEMLTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIA--EGRIV 209
Cdd:COG4525 156 LLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSpgPGRIV 216
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
20-208 |
1.72e-51 |
|
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: 166.55 E-value: 1.72e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 20 LSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPA----KRPVSMLFQENNLFTHLTVRQNIALG 95
Cdd:cd03262 21 LTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelRQKVGMVFQQFNLFPHLTVLENITLA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 96 MHPGLRLNDAQ-RHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQD 174
Cdd:cd03262 101 PIKVKGMSKAEaEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKD 180
|
170 180 190
....*....|....*....|....*....|....
gi 779793995 175 VCQRQQlTMLMVSHSIEDAARIAPRSVVIAEGRI 208
Cdd:cd03262 181 LAEEGM-TMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
19-218 |
2.09e-51 |
|
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: 167.82 E-value: 2.09e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPA------KRPVSMLFQENNLFTHLTVRQNI 92
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKelrelrRKKISMVFQSFALLPHRTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 93 ALGMHpgLR-LNDAQRH-KLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLT 170
Cdd:cd03294 124 AFGLE--VQgVPRAEREeRAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQD 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 779793995 171 LVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELL 218
Cdd:cd03294 202 ELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-218 |
2.21e-51 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 167.09 E-value: 2.21e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 2 LKLTDVTWLYQHLPM---RFTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAK--RPVSML 76
Cdd:cd03295 1 IEFENVTKRYGGGKKavnNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 77 FQENNLFTHLTVRQNIALGmhpgLRLNDAQRHKLEEIAAQ------MGIAGFIDRLPGELSGGQRQRVALARCLVREQPM 150
Cdd:cd03295 81 IQQIGLFPHMTVEENIALV----PKLLKWPKEKIRERADEllalvgLDPAEFADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 779793995 151 LLLDEPFSALDP----ALRQEMLTLVQDVCQrqqlTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELL 218
Cdd:cd03295 157 LLMDEPFGALDPitrdQLQEEFKRLQQELGK----TIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-219 |
2.61e-51 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 166.96 E-value: 2.61e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 1 MLKLTDVTWLYQHLPM--RFTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPP-AKRPVSMLF 77
Cdd:COG4555 1 MIEVENLSKKYGKVPAlkDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPReARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 78 QENNLFTHLTVRQNIAL-----GMHPglrlnDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLL 152
Cdd:COG4555 81 DERGLYDRLTVRENIRYfaelyGLFD-----EELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 779793995 153 LDEPFSALDPALRQEMLTLVQDVCQrQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELLK 219
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRALKK-EGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELRE 221
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
30-217 |
1.61e-50 |
|
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: 167.29 E-value: 1.61e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 30 VLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAKRPVSMLFQENNLFTHLTVRQNIALGmhpgLRLNDAQRhk 109
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFG----LKMRKVPR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 110 lEEIAAQMGIA-------GFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQDVCQRQQLT 182
Cdd:TIGR01187 75 -AEIKPRVLEAlrlvqleEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGIT 153
|
170 180 190
....*....|....*....|....*....|....*
gi 779793995 183 MLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEEL 217
Cdd:TIGR01187 154 FVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
19-218 |
6.14e-50 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 163.34 E-value: 6.14e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHtppAKRPVSMLFQ--ENNLFTHLTVRQNIALGM 96
Cdd:COG1121 26 SLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR---ARRRIGYVPQraEVDWDFPITVRDVVLMGR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 97 HPGL----RLNDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLV 172
Cdd:COG1121 103 YGRRglfrRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 779793995 173 QDVcQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWdGVTEELL 218
Cdd:COG1121 183 REL-RREGKTILVVTHDLGAVREYFDRVLLLNRGLVAH-GPPEEVL 226
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
20-209 |
3.60e-49 |
|
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: 160.75 E-value: 3.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 20 LSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAKRP-----VSMLFQE--NNLFTHLTVRQNI 92
Cdd:cd03257 26 FSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKirrkeIQMVFQDpmSSLNPRMTIGEQI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 93 ALGMHPGLRLNDAQRHKLEEIAAQMGI---AGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEML 169
Cdd:cd03257 106 AEPLRIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQIL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 779793995 170 TLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIV 209
Cdd:cd03257 186 DLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
19-219 |
8.08e-49 |
|
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: 161.47 E-value: 8.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTP-----PAKRPVSMLFQ--ENNLFtHLTVRQN 91
Cdd:TIGR04521 25 SLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKkkklkDLRKKVGLVFQfpEHQLF-EETVYKD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 92 IALG-MHPGLRLNDAQRhKLEEIAAQMGI-AGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEML 169
Cdd:TIGR04521 104 IAFGpKNLGLSEEEAEE-RVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEIL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 779793995 170 TLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELLK 219
Cdd:TIGR04521 183 DLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFS 232
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
18-219 |
5.46e-48 |
|
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: 168.09 E-value: 5.46e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 18 FTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAK--RPVSMLFQENNLFtHLTVRQNIALG 95
Cdd:COG2274 494 ISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQIGVVLQDVFLF-SGTIRENITLG 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 96 mHPglrlnDAQRHKLEEIAAQMGIAGFIDRLP-------GE----LSGGQRQRVALARCLVREQPMLLLDEPFSALDPAL 164
Cdd:COG2274 573 -DP-----DATDEEIIEAARLAGLHDFIEALPmgydtvvGEggsnLSGGQRQRLAIARALLRNPRILILDEATSALDAET 646
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 779793995 165 RQEMLTLVQDVCQRQqlTMLMVSH---SIEDAARIaprsVVIAEGRIVWDGVTEELLK 219
Cdd:COG2274 647 EAIILENLRRLLKGR--TVIIIAHrlsTIRLADRI----IVLDKGRIVEDGTHEELLA 698
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-221 |
1.02e-47 |
|
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: 165.32 E-value: 1.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 2 LKLTDVTWLY---QHLPMRFTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPA--KRPVSML 76
Cdd:COG4988 337 IELEDVSFSYpggRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAswRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 77 FQENNLFtHLTVRQNIALGMHpglrlnDAQRHKLEEIAAQMGIAGFIDRLP-------GE----LSGGQRQRVALARCLV 145
Cdd:COG4988 417 PQNPYLF-AGTIRENLRLGRP------DASDEELEAALEAAGLDEFVAALPdgldtplGEggrgLSGGQAQRLALARALL 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 779793995 146 REQPMLLLDEPFSALDPALRQEMLTLVQDVCQRQqlTMLMVSHSIEDAARiAPRSVVIAEGRIVWDGVTEELLKGN 221
Cdd:COG4988 490 RDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
18-221 |
1.03e-47 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 165.72 E-value: 1.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 18 FTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAK--RPVSMLFQENNLFtHLTVRQNIALG 95
Cdd:COG1132 359 ISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIGVVPQDTFLF-SGTIRENIRYG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 96 mhpglrLNDAQRHKLEEIAAQMGIAGFIDRLP-------GE----LSGGQRQRVALARCLVREQPMLLLDEPFSALDP-- 162
Cdd:COG1132 438 ------RPDATDEEVEEAAKAAQAHEFIEALPdgydtvvGErgvnLSGGQRQRIAIARALLKDPPILILDEATSALDTet 511
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 779793995 163 --ALRQEMLTLVQDVcqrqqlTMLMVSH---SIEDAARIaprsVVIAEGRIVWDGVTEELLKGN 221
Cdd:COG1132 512 eaLIQEALERLMKGR------TTIVIAHrlsTIRNADRI----LVLDDGRIVEQGTHEELLARG 565
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-158 |
1.32e-47 |
|
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: 154.34 E-value: 1.32e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHT--PPAKRPVSMLFQENNLFTHLTVRQNIALGM 96
Cdd:pfam00005 5 SLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDerKSLRKEIGYVFQDPQLFPRLTVRENLRLGL 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 779793995 97 HPGLRLNDAQRHKLEEIAAQMGIAGFIDRL----PGELSGGQRQRVALARCLVREQPMLLLDEPFS 158
Cdd:pfam00005 85 LLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
19-218 |
7.24e-47 |
|
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: 154.90 E-value: 7.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAKRP---VSMLFQENNLFTHLTVRQNIALG 95
Cdd:cd03224 20 SLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERAragIGYVPEGRRIFPELTVEENLLLG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 96 MHPGLRLNDAQRH--------KLEEIAAQMGiagfidrlpGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQE 167
Cdd:cd03224 100 AYARRRAKRKARLervyelfpRLKERRKQLA---------GTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 779793995 168 MLTLVQDVCqRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELL 218
Cdd:cd03224 171 IFEAIRELR-DEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
19-218 |
8.59e-47 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 155.25 E-value: 8.59e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAKRPV----SMLFQENNLFTHLTVRQNIAL 94
Cdd:PRK09493 21 DLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGMVFQQFYLFPHLTALENVMF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 95 GmhPgLRLNDAQRHKLEEIA----AQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLT 170
Cdd:PRK09493 101 G--P-LRVRGASKEEAEKQArellAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLK 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 779793995 171 LVQDVCQrQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELL 218
Cdd:PRK09493 178 VMQDLAE-EGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLI 224
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
18-228 |
1.61e-46 |
|
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: 162.24 E-value: 1.61e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 18 FTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAK--RPVSMLFQENNLFTHlTVRQNIALG 95
Cdd:COG4987 354 LSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrRRIAVVPQRPHLFDT-TLRENLRLA 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 96 mhpglrLNDAQRHKLEEIAAQMGIAGFIDRLP-------GE----LSGGQRQRVALARCLVREQPMLLLDEPFSALDPAL 164
Cdd:COG4987 433 ------RPDATDEELWAALERVGLGDWLAALPdgldtwlGEggrrLSGGERRRLALARALLRDAPILLLDEPTEGLDAAT 506
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 779793995 165 RQEMLTLVQDVCQRQqlTMLMVSHSIEDAARiAPRSVVIAEGRIVWDGVTEELLKGNAAASSLL 228
Cdd:COG4987 507 EQALLADLLEALAGR--TVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEELLAQNGRYRQLY 567
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
19-212 |
1.90e-46 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 152.20 E-value: 1.90e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAKRpvsmlfqennlfthltvRQNIALgmhp 98
Cdd:cd03214 19 SLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL-----------------ARKIAY---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 99 glrlndaqrhkLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQDVCQR 178
Cdd:cd03214 78 -----------VPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARE 146
|
170 180 190
....*....|....*....|....*....|....
gi 779793995 179 QQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDG 212
Cdd:cd03214 147 RGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
26-218 |
5.56e-46 |
|
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: 156.43 E-value: 5.56e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 26 ERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDN---QDHTH---TPPAKRPVSMLFQENNLFTHLTVRQNIALGMHpg 99
Cdd:TIGR02142 24 GVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDSRKgifLPPEKRRIGYVFQEARLFPHLSVRGNLRYGMK-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 100 lRLNDAQRH-KLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQDVCQR 178
Cdd:TIGR02142 102 -RARPSERRiSFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 779793995 179 QQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELL 218
Cdd:TIGR02142 181 FGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVW 220
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
19-218 |
5.80e-46 |
|
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: 159.68 E-value: 5.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQP---VSGSIVIDNQDHTHTPPAKRP--VSMLFQE-NNLFTHLTVRQNI 92
Cdd:COG1123 26 SLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGrrIGMVFQDpMTQLNPVTVGDQI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 93 ALGMHPGLRLNDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLV 172
Cdd:COG1123 106 AEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 779793995 173 QDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELL 218
Cdd:COG1123 186 RELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEIL 231
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
19-208 |
6.39e-46 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 150.63 E-value: 6.39e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQD-HTHTPPAKRPVSMLFQENNLFTHLTVRQNIalgmh 97
Cdd:cd03230 20 SLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDiKKEPEEVKRRIGYLPEEPSLYENLTVRENL----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 98 pglrlndaqrhkleeiaaqmgiagfidrlpgELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQDvCQ 177
Cdd:cd03230 95 -------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRE-LK 142
|
170 180 190
....*....|....*....|....*....|.
gi 779793995 178 RQQLTMLMVSHSIEDAARIAPRSVVIAEGRI 208
Cdd:cd03230 143 KEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
20-217 |
8.24e-45 |
|
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: 150.14 E-value: 8.24e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 20 LSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAK-----RPVSMLFQENNLFTHLTVRQNI-- 92
Cdd:TIGR02315 23 LNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrklrRRIGMIFQHYNLIERLTVLENVlh 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 93 -ALGMHPGLR-----LNDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQ 166
Cdd:TIGR02315 103 gRLGYKPTWRsllgrFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSK 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 779793995 167 EMLTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEEL 217
Cdd:TIGR02315 183 QVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
19-230 |
9.01e-45 |
|
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: 149.75 E-value: 9.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAKRP---VSMLFQENNLFTHLTVRQNIALG 95
Cdd:COG0410 23 SLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIArlgIGYVPEGRRIFPSLTVEENLLLG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 96 MHPGlRLNDAQRHKLEEI----------AAQMGiagfidrlpGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALR 165
Cdd:COG0410 103 AYAR-RDRAEVRADLERVyelfprlkerRRQRA---------GTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIV 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 779793995 166 QEMLTLVQDVcQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELLKGNAAASSLLGI 230
Cdd:COG0410 173 EEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEVREAYLGV 236
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-212 |
1.61e-44 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 148.66 E-value: 1.61e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 1 MLKLTDVTWLYQHLPMRF---TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAKRP----- 72
Cdd:COG2884 1 MIRFENVSKRYPGGREALsdvSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPylrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 73 VSMLFQENNLFTHLTVRQNIALGMH-PGLRLNDAQRhKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPML 151
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPLRvTGKSRKEIRR-RVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 779793995 152 LLDEPFSALDPALRQEMLTLVQDVCQRqQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDG 212
Cdd:COG2884 160 LADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
20-219 |
3.98e-44 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 151.41 E-value: 3.98e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 20 LSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAKRPVSMLFQENNLFTHLTVRQNIALGMHPG 99
Cdd:PRK11432 27 LTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQSYALFPHMSLGENVGYGLKML 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 100 LRLNDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQDVCQRQ 179
Cdd:PRK11432 107 GVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQF 186
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 779793995 180 QLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELLK 219
Cdd:PRK11432 187 NITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYR 226
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
20-208 |
5.48e-44 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 151.72 E-value: 5.48e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 20 LSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAKRPVSMLFQENNLFTHLTVRQNIALGMH-P 98
Cdd:PRK11000 24 LDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMVFQSYALYPHLSVAENMSFGLKlA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 99 GLRLNDAQRhKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQDVCQR 178
Cdd:PRK11000 104 GAKKEEINQ-RVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKR 182
|
170 180 190
....*....|....*....|....*....|
gi 779793995 179 QQLTMLMVSHSIEDAARIAPRSVVIAEGRI 208
Cdd:PRK11000 183 LGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-212 |
7.72e-44 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 146.91 E-value: 7.72e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 3 KLTDVTWLY-QHLPMR-FTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTP------PAKRPVS 74
Cdd:cd03235 1 EVEDLTVSYgGHPVLEdVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERkrigyvPQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 75 MLFQennlfthLTVRQNIALGM--HPGL--RLNDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPM 150
Cdd:cd03235 81 RDFP-------ISVRDVVLMGLygHKGLfrRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 779793995 151 LLLDEPFSALDPALRQEMLTLVQDVCQRqQLTMLMVSHSIEDAARIAPRSVVIAeGRIVWDG 212
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLN-RTVVASG 213
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
19-219 |
1.08e-43 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 147.61 E-value: 1.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAK--RPVSMLFQENNLFTHLTVRQNIALGM 96
Cdd:PRK13548 22 SLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAVLPQHSSLSFPFTVEEVVAMGR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 97 HPGLRLNDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVR------EQPMLLLDEPFSALDPALRQEMLT 170
Cdd:PRK13548 102 APHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepdgPPRWLLLDEPTSALDLAHQHHVLR 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 779793995 171 LVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDG-----VTEELLK 219
Cdd:PRK13548 182 LARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGtpaevLTPETLR 235
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
18-207 |
1.27e-43 |
|
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: 144.83 E-value: 1.27e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 18 FTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAKRP--VSMLFQENNLFtHLTVRQNIalg 95
Cdd:cd03228 21 VSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRknIAYVPQDPFLF-SGTIRENI--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 96 mhpglrlndaqrhkleeiaaqmgiagfidrlpgeLSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQDV 175
Cdd:cd03228 97 ----------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRAL 142
|
170 180 190
....*....|....*....|....*....|....*
gi 779793995 176 CQRQqlTMLMVSH---SIEDAARIaprsVVIAEGR 207
Cdd:cd03228 143 AKGK--TVIVIAHrlsTIRDADRI----IVLDDGR 171
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
19-217 |
1.39e-43 |
|
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: 146.56 E-value: 1.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFL-----QPVSGSIVIDNQDHTHTPPA----KRPVSMLFQENNLFtHLTVR 89
Cdd:cd03260 20 SLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVDvlelRRRVGMVFQKPNPF-PGSIY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 90 QNIALGmhpgLRLNDAQRHK-LEEIAAQ-MGIAG----FIDRL-PGELSGGQRQRVALARCLVREQPMLLLDEPFSALDP 162
Cdd:cd03260 99 DNVAYG----LRLHGIKLKEeLDERVEEaLRKAAlwdeVKDRLhALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDP 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 779793995 163 ALRQEMLTLVQDvcQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEEL 217
Cdd:cd03260 175 ISTAKIEELIAE--LKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-211 |
1.87e-43 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 147.15 E-value: 1.87e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 18 FTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAKRP--VSMLFQENNLFT--HLTVRQNIA 93
Cdd:COG1101 25 LNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAkyIGRVFQDPMMGTapSMTIEENLA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 94 L----GMHPGLR--LNDAQRHKLEEIAAQMGIaGFIDRLP---GELSGGQRQRVALARCLVREQPMLLLDEPFSALDPAL 164
Cdd:COG1101 105 LayrrGKRRGLRrgLTKKRRELFRELLATLGL-GLENRLDtkvGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKT 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 779793995 165 RQEMLTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWD 211
Cdd:COG1101 184 AALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIILD 230
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
17-217 |
2.18e-43 |
|
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: 145.73 E-value: 2.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 17 RFTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQD-HTHTPPAKRPVSMLFQENNLFTHLTVRQNIAL- 94
Cdd:cd03263 20 DLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSiRTDRKAARQSLGYCPQFDALFDELTVREHLRFy 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 95 GMHPGLRLNDAQRHkLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQD 174
Cdd:cd03263 100 ARLKGLPKSEIKEE-VELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 779793995 175 VcqRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEEL 217
Cdd:cd03263 179 V--RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-188 |
2.37e-43 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 145.31 E-value: 2.37e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 1 MLKLTDVT------WLYQHLpmrfTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQD-HTHTPPAKRPV 73
Cdd:COG4133 2 MLEAENLScrrgerLLFSGL----SFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPiRDAREDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 74 SMLFQENNLFTHLTVRQNIAL--GMHpGLRLNDAQrhkLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPML 151
Cdd:COG4133 78 AYLGHADGLKPELTVRENLRFwaALY-GLRADREA---IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLW 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 779793995 152 LLDEPFSALDPALRQEMLTLVQDVCQRQQLTmLMVSH 188
Cdd:COG4133 154 LLDEPFTALDAAGVALLAELIAAHLARGGAV-LLTTH 189
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
19-218 |
2.42e-43 |
|
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: 146.15 E-value: 2.42e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAKRP---VSMLFQENNLFTHLTVRQNI--A 93
Cdd:cd03218 20 SLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRArlgIGYLPQEASIFRKLTVEENIlaV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 94 LGMHPGLRlnDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQ 173
Cdd:cd03218 100 LEIRGLSK--KEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIK 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 779793995 174 DVCQRqQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELL 218
Cdd:cd03218 178 ILKDR-GIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
19-218 |
8.21e-43 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 149.10 E-value: 8.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGErIAVL-GPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAK------RPVSMLFQENNLFTHLTVRQN 91
Cdd:COG4175 47 SFDVEEGE-IFVImGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKElrelrrKKMSMVFQHFALLPHRTVLEN 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 92 IALGmhpgLRLNDAQRHKLEEIAAQM----GIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQE 167
Cdd:COG4175 126 VAFG----LEIQGVPKAERRERAREAlelvGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRRE 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 779793995 168 M----LTLvQdvcQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELL 218
Cdd:COG4175 202 MqdelLEL-Q---AKLKKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEIL 252
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
19-218 |
1.04e-42 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 147.53 E-value: 1.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPP-----AKRPVSMLFQENNLFTHLTVRQNIA 93
Cdd:COG1135 25 SLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSErelraARRKIGMIFQHFNLLSSRTVAENVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 94 LgmhPgLRLN----DAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEML 169
Cdd:COG1135 105 L---P-LEIAgvpkAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSIL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 779793995 170 TLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELL 218
Cdd:COG1135 181 DLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVF 229
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-206 |
1.18e-42 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 144.15 E-value: 1.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 20 LSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAKRPVsmlFQENNLFTHLTVRQNIALGMHPG 99
Cdd:TIGR01184 6 LTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVV---FQNYSLLPWLTVRENIALAVDRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 100 LR-LNDAQRHKL-EEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQDVCQ 177
Cdd:TIGR01184 83 LPdLSKSERRAIvEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQIWE 162
|
170 180
....*....|....*....|....*....
gi 779793995 178 RQQLTMLMVSHSIEDAARIAPRSVVIAEG 206
Cdd:TIGR01184 163 EHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
19-238 |
2.01e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 145.19 E-value: 2.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHT----PPAKRPVSMLFQ--ENNLFTHlTVRQNI 92
Cdd:PRK13637 27 NIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKkvklSDIRKKVGLVFQypEYQLFEE-TIEKDI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 93 ALGmhP-GLRLNDAQRHKleEIAAQMGIAG-----FIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQ 166
Cdd:PRK13637 106 AFG--PiNLGLSEEEIEN--RVKRAMNIVGldyedYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRD 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 779793995 167 EMLTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELLKgNAAASSLLGISAPPLYSL 238
Cdd:PRK13637 182 EILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFK-EVETLESIGLAVPQVTYL 252
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
20-218 |
5.35e-42 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 143.33 E-value: 5.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 20 LSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPA----KRPVsmLFQENNLFTHLTVRQNIALG 95
Cdd:COG4559 22 LTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWelarRRAV--LPQHSSLAFPFTVEEVVALG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 96 MHPGLRLNDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCL------VREQP-MLLLDEPFSALDPALRQEM 168
Cdd:COG4559 100 RAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqlwepVDGGPrWLFLDEPTSALDLAHQHAV 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 779793995 169 LTLVQDVCqRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELL 218
Cdd:COG4559 180 LRLARQLA-RRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVL 228
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-218 |
7.66e-42 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 142.91 E-value: 7.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 1 MLKLTDVTWLYQHLPM--RFTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPP---AKRpVSM 75
Cdd:COG4604 1 MIEIKNVSKRYGGKVVldDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSrelAKR-LAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 76 LFQENNLFTHLTVRQNIALGMHP---GlRLNDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLL 152
Cdd:COG4604 80 LRQENHINSRLTVRELVAFGRFPyskG-RLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 779793995 153 LDEPFSALDPALRQEMLTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELL 218
Cdd:COG4604 159 LDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEII 224
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
19-217 |
3.38e-41 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 144.07 E-value: 3.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAKRPVSMLFQENNLFTHLTVRQNIALG--M 96
Cdd:PRK10851 22 SLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQHYALFRHMTVFDNIAFGltV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 97 HPGL-RLNDAQ-RHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQD 174
Cdd:PRK10851 102 LPRReRPNAAAiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQ 181
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 779793995 175 VCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEEL 217
Cdd:PRK10851 182 LHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-209 |
2.28e-40 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 139.06 E-value: 2.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 1 MLKLTDVTWLYQHLPM--RFTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQdHTHTPPAKRPVsmLFQ 78
Cdd:PRK11248 1 MLQISHLYADYGGKPAleDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK-PVEGPGAERGV--VFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 79 ENNLFTHLTVRQNIALGmhpgLRLNDAQRHKLEEIAAQM----GIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLD 154
Cdd:PRK11248 78 NEGLLPWRNVQDNVAFG----LQLAGVEKMQRLEIAHQMlkkvGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 779793995 155 EPFSALDPALRQEMLTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIA--EGRIV 209
Cdd:PRK11248 154 EPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSpgPGRVV 210
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-218 |
2.91e-40 |
|
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: 138.68 E-value: 2.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 1 MLKLTDVTWLYQ--HLPMRFTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSG-SIVIDNQDHTHTPPAK-RP---- 72
Cdd:COG1119 3 LLELRNVTVRRGgkTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWElRKrigl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 73 VSMLFQENnLFTHLTVRQNIALGMH--PGL--RLNDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQ 148
Cdd:COG1119 83 VSPALQLR-FPRDETVLDVVLSGFFdsIGLyrEPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 779793995 149 PMLLLDEPFSALDPALRQEMLTLVQDVCQRQQLTMLMVSHSIEDaarIAP---RSVVIAEGRIVWDGVTEELL 218
Cdd:COG1119 162 ELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEE---IPPgitHVLLLKDGRVVAAGPKEEVL 231
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-207 |
3.01e-40 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 135.84 E-value: 3.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 3 KLTDVTWLY--QHLPMRFTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPP--AKRPVSMLFQ 78
Cdd:cd00267 1 EIENLSFRYggRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLeeLRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 79 ennlfthltvrqnialgmhpglrlndaqrhkleeiaaqmgiagfidrlpgeLSGGQRQRVALARCLVREQPMLLLDEPFS 158
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 779793995 159 ALDPALRQEMLTLVQDVCQRQQlTMLMVSHSIEDAARIAPRSVVIAEGR 207
Cdd:cd00267 110 GLDPASRERLLELLRELAEEGR-TVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
19-208 |
8.81e-40 |
|
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: 136.38 E-value: 8.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTH-----TPPAKRPVSMLFQENNLFTHLTVRQNIA 93
Cdd:cd03292 21 NISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrgraIPYLRRKIGVVFQDFRLLPDRNVYENVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 94 LGM----HPGlrlNDAQRhKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEML 169
Cdd:cd03292 101 FALevtgVPP---REIRK-RVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIM 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 779793995 170 TLVQDVCQRqQLTMLMVSHSIEDAARIAPRSVVIAEGRI 208
Cdd:cd03292 177 NLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
19-208 |
1.21e-39 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 139.98 E-value: 1.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAKRPVSMLFQENNLFTHLTVRQNIALgmhp 98
Cdd:PRK11650 24 DLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAMVFQNYALYPHMSVRENMAY---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 99 GLRL----NDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQD 174
Cdd:PRK11650 100 GLKIrgmpKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQR 179
|
170 180 190
....*....|....*....|....*....|....
gi 779793995 175 VCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRI 208
Cdd:PRK11650 180 LHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVA 213
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
18-221 |
1.35e-39 |
|
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: 136.59 E-value: 1.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 18 FTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQD--HTHTPPAKRPVSMLFQENNLFTHlTVRQNIALG 95
Cdd:cd03251 21 ISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDvrDYTLASLRRQIGLVSQDVFLFND-TVAENIAYG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 96 MHpglrlnDAQRHKLEEIAAQMGIAGFIDRLP-------GE----LSGGQRQRVALARCLVREQPMLLLDEPFSALDpaL 164
Cdd:cd03251 100 RP------GATREEVEEAARAANAHEFIMELPegydtviGErgvkLSGGQRQRIAIARALLKDPPILILDEATSALD--T 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 779793995 165 RQEMltLVQDVCQR--QQLTMLMVSH---SIEDAARIaprsVVIAEGRIVWDGVTEELLKGN 221
Cdd:cd03251 172 ESER--LVQAALERlmKNRTTFVIAHrlsTIENADRI----VVLEDGKIVERGTHEELLAQG 227
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
19-207 |
2.16e-39 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 135.45 E-value: 2.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTH-----TPPAKRPVSMLFQENNLFTHLTVRQNIA 93
Cdd:TIGR02673 22 SLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRlrgrqLPLLRRRIGVVFQDFRLLPDRTVYENVA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 94 LGMHPGLRLNDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQ 173
Cdd:TIGR02673 102 LPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLDPDLSERILDLLK 181
|
170 180 190
....*....|....*....|....*....|....
gi 779793995 174 DVCQRqQLTMLMVSHSIEDAARIAPRSVVIAEGR 207
Cdd:TIGR02673 182 RLNKR-GTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
25-224 |
4.11e-39 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 143.08 E-value: 4.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 25 GERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPA--KRPVSMLFQENNLFtHLTVRQNIALGMhpgLRL 102
Cdd:TIGR03375 491 GEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPAdlRRNIGYVPQDPRLF-YGTLRDNIALGA---PYA 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 103 NDAQrhkLEEIAAQMGIAGFIDRLP-------GE----LSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTL 171
Cdd:TIGR03375 567 DDEE---ILRAAELAGVTEFVRRHPdgldmqiGErgrsLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDR 643
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 779793995 172 VQDVCQRQqlTMLMVSHSIEdAARIAPRSVVIAEGRIVWDGVTEELLKGNAAA 224
Cdd:TIGR03375 644 LKRWLAGK--TLVLVTHRTS-LLDLVDRIIVMDNGRIVADGPKDQVLEALRKG 693
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
19-212 |
1.19e-38 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 134.37 E-value: 1.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTL---LNLVAGflqPVSGSIVIDNQ--DHTHTPPAK------RPVSMLFQENNLFTHLT 87
Cdd:PRK11124 22 TLDCPQGETLVLLGPSGAGKSSLlrvLNLLEM---PRSGTLNIAGNhfDFSKTPSDKairelrRNVGMVFQQYNLWPHLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 88 VRQNIALGMHPGLRLNDAQRHK-LEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQ 166
Cdd:PRK11124 99 VQQNLIEAPCRVLGLSKDQALArAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 779793995 167 EMLTLVQDVcQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDG 212
Cdd:PRK11124 179 QIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
25-212 |
2.15e-38 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 133.60 E-value: 2.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 25 GERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQ--DHTHTPPAK------RPVSMLFQENNLFTHLTVRQNIALGM 96
Cdd:COG4161 28 GETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSEKairllrQKVGMVFQQYNLWPHLTVMENLIEAP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 97 HPGLRLNDAQ-RHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQDV 175
Cdd:COG4161 108 CKVLGLSKEQaREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIREL 187
|
170 180 190
....*....|....*....|....*....|....*..
gi 779793995 176 CQrQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDG 212
Cdd:COG4161 188 SQ-TGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG 223
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
20-219 |
4.52e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 133.99 E-value: 4.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 20 LSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQ------DHTHTPPAKRPVSMLFQ--ENNLFTHlTVRQN 91
Cdd:PRK13634 28 VSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERvitagkKNKKLKPLRKKVGIVFQfpEHQLFEE-TVEKD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 92 IALG-MHPGLRLNDAQRhKLEEIAAQMGI-AGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEML 169
Cdd:PRK13634 107 ICFGpMNFGVSEEDAKQ-KAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMM 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 779793995 170 TLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELLK 219
Cdd:PRK13634 186 EMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFA 235
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
19-212 |
5.25e-38 |
|
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: 131.94 E-value: 5.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPA--KRPVSMLFQENNLFTHlTVRQNIALGM 96
Cdd:cd03245 24 SLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAdlRRNIGYVPQDVTLFYG-TLRDNITLGA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 97 hpglRLNDAQRhkLEEIAAQMGIAGFIDRLP-------GE----LSGGQRQRVALARCLVREQPMLLLDEPFSALDPALR 165
Cdd:cd03245 103 ----PLADDER--ILRAAELAGVTDFVNKHPngldlqiGErgrgLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 779793995 166 QEML-TLVQDVCQRqqlTMLMVSHSIEdAARIAPRSVVIAEGRIVWDG 212
Cdd:cd03245 177 ERLKeRLRQLLGDK---TLIIITHRPS-LLDLVDRIIVMDSGRIVADG 220
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-212 |
5.45e-38 |
|
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: 131.72 E-value: 5.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 1 MLKLTDVTWLYQHLPMRF------TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTP-PAKRPV 73
Cdd:cd03266 1 MITADALTKRFRDVKKTVqavdgvSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPaEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 74 SMLFQENNLFTHLTVRQNIAL--GMHpGLRlNDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPML 151
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYfaGLY-GLK-GDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 779793995 152 LLDEPFSALDPALRQEMLTLVQDVCqRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDG 212
Cdd:cd03266 159 LLDEPTTGLDVMATRALREFIRQLR-ALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
20-219 |
5.89e-38 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 133.32 E-value: 5.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 20 LSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDH---THTPPAKRPVSMLFQeN--NLFTHLTVRQNIAL 94
Cdd:TIGR04520 23 LSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTldeENLWEIRKKVGMVFQ-NpdNQFVGATVEDDVAF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 95 GMHpGLRLNDAQ-RHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQ 173
Cdd:TIGR04520 102 GLE-NLGVPREEmRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIR 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 779793995 174 DVCQRQQLTMLMVSHSIEDAARiAPRSVVIAEGRIVWDGVTEELLK 219
Cdd:TIGR04520 181 KLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFS 225
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
20-219 |
1.02e-37 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 131.69 E-value: 1.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 20 LSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPP---AKRPVSMLFQENNLFTHLTVRQNI--AL 94
Cdd:COG1137 24 LEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMhkrARLGIGYLPQEASIFRKLTVEDNIlaVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 95 GMHPglrLNDAQRH-KLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQ 173
Cdd:COG1137 104 ELRK---LSKKEREeRLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIR 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 779793995 174 DVCQRqQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELLK 219
Cdd:COG1137 181 HLKER-GIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILN 225
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
29-216 |
1.43e-37 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 134.23 E-value: 1.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 29 AVLGPSGAGKSTLLNLVAGFLQPVSGSIVI------DNQDHTHTPPAKRPVSMLFQENNLFTHLTVRQNIALGMHPGlrl 102
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLngrvlfDAEKGICLPPEKRRIGYVFQDARLFPHYKVRGNLRYGMAKS--- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 103 NDAQrhkLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQDVCQRQQLT 182
Cdd:PRK11144 105 MVAQ---FDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIP 181
|
170 180 190
....*....|....*....|....*....|....
gi 779793995 183 MLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEE 216
Cdd:PRK11144 182 ILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
18-219 |
8.90e-37 |
|
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: 128.88 E-value: 8.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 18 FTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQD-HTHTPPAKRP-VSMLFQENNLFTHlTVRQNIALG 95
Cdd:cd03254 22 INFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDiRDISRKSLRSmIGVVLQDTFLFSG-TIMENIRLG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 96 MhpglrlNDAQRHKLEEIAAQMGIAGFIDRLP-----------GELSGGQRQRVALARCLVREQPMLLLDEPFSALDPal 164
Cdd:cd03254 101 R------PNATDEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKILILDEATSNIDT-- 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 165 rqEMLTLVQDVCQR--QQLTMLMVSH---SIEDAARIaprsVVIAEGRIVWDGVTEELLK 219
Cdd:cd03254 173 --ETEKLIQEALEKlmKGRTSIIIAHrlsTIKNADKI----LVLDDGKIIEEGTHDELLA 226
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-219 |
9.49e-37 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 130.52 E-value: 9.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTP--PAKRPVSMLFQE-NNLFTHLTVRQNIALG 95
Cdd:PRK13635 27 SFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETvwDVRRQVGMVFQNpDNQFVGATVQDDVAFG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 96 M-HPGLRLNDAQRhKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQD 174
Cdd:PRK13635 107 LeNIGVPREEMVE-RVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQ 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 779793995 175 VCQRQQLTMLMVSHSIEDAARiAPRSVVIAEGRIVWDGVTEELLK 219
Cdd:PRK13635 186 LKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFK 229
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
18-203 |
1.06e-36 |
|
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: 135.11 E-value: 1.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 18 FTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPA--KRPVSMLFQENNLFTHlTVRQNIALG 95
Cdd:TIGR02857 341 VSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADswRDQIAWVPQHPFLFAG-TIAENIRLA 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 96 mhpglrLNDAQRHKLEEIAAQMGIAGFIDRLPG-----------ELSGGQRQRVALARCLVREQPMLLLDEPFSALDPAL 164
Cdd:TIGR02857 420 ------RPDASDAEIREALERAGLDEFVAALPQgldtpigeggaGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAET 493
|
170 180 190
....*....|....*....|....*....|....*....
gi 779793995 165 RQEMLTLVQDVCQRQqlTMLMVSHSIEDAARiAPRSVVI 203
Cdd:TIGR02857 494 EAEVLEALRALAQGR--TVLLVTHRLALAAL-ADRIVVL 529
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
6-227 |
1.16e-36 |
|
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: 128.89 E-value: 1.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 6 DVTWLYQhlPMRFTL-----SVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHT--PPAKRPVSMLFQ 78
Cdd:cd03253 5 NVTFAYD--PGRPVLkdvsfTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVtlDSLRRAIGVVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 79 ENNLFtHLTVRQNIALGmhpglRLnDAQRHKLEEIAAQMGIAGFIDRLP-------GE----LSGGQRQRVALARCLVRE 147
Cdd:cd03253 83 DTVLF-NDTIGYNIRYG-----RP-DATDEEVIEAAKAAQIHDKIMRFPdgydtivGErglkLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 148 QPMLLLDEPFSALDPALRQEMLTLVQDVCQRQqlTMLMVSH---SIEDAARIaprsVVIAEGRIVWDGVTEELLKGNAAA 224
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRDVSKGR--TTIVIAHrlsTIVNADKI----IVLKDGRIVERGTHEELLAKGGLY 229
|
...
gi 779793995 225 SSL 227
Cdd:cd03253 230 AEM 232
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-216 |
3.97e-36 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 130.31 E-value: 3.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 1 MLKLTDVTWLYQHLPMRFT------LSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPP-----A 69
Cdd:PRK11153 1 MIELKNISKVFPQGGRTIHalnnvsLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEkelrkA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 70 KRPVSMLFQENNLFTHLTVRQNIALgmhPgLRLNDAQRH----KLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLV 145
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVAL---P-LELAGTPKAeikaRVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 779793995 146 REQPMLLLDEPFSALDPALRQEMLTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEE 216
Cdd:PRK11153 157 SNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSE 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-217 |
7.86e-36 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 132.45 E-value: 7.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPA---KRPVSMLFQENNLFTHLTVRQNIALG 95
Cdd:COG1129 24 SLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRdaqAAGIAIIHQELNLVPNLSVAENIFLG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 96 MHP--GLRLND-AQRHKLEEIAAQMGIAgfID--RLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLT 170
Cdd:COG1129 104 REPrrGGLIDWrAMRRRARELLARLGLD--IDpdTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 779793995 171 LVQDVcQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEEL 217
Cdd:COG1129 182 IIRRL-KAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
18-195 |
1.10e-35 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 125.42 E-value: 1.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 18 FTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDhTHTPPAKRPVSM-------LFQENNLFTHLTVRQ 90
Cdd:TIGR03608 17 LNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQE-TPPLNSKKASKFrreklgyLFQNFALIENETVEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 91 NIALGMhPGLRLNDAQ-RHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEML 169
Cdd:TIGR03608 96 NLDLGL-KYKKLSKKEkREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDPKNRDEVL 174
|
170 180
....*....|....*....|....*.
gi 779793995 170 TLVQDVCQRQQlTMLMVSHSIEDAAR 195
Cdd:TIGR03608 175 DLLLELNDEGK-TIIIVTHDPEVAKQ 199
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
19-227 |
1.14e-35 |
|
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: 126.45 E-value: 1.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPA--KRPVSMLFQENNLFTHlTVRQNIALGm 96
Cdd:cd03252 22 SLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQVGVVLQENVLFNR-SIRDNIALA- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 97 HPGlrlndAQRHKLEEIAAQMGIAGFIDRLP-------GE----LSGGQRQRVALARCLVREQPMLLLDEPFSALDPALR 165
Cdd:cd03252 100 DPG-----MSMERVIEAAKLAGAHDFISELPegydtivGEqgagLSGGQRQRIAIARALIHNPRILIFDEATSALDYESE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 779793995 166 QEMLTLVQDVCQRQqlTMLMVSHSIEdAARIAPRSVVIAEGRIVWDGVTEELLKGNAAASSL 227
Cdd:cd03252 175 HAIMRNMHDICAGR--TVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
19-217 |
5.83e-35 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 124.02 E-value: 5.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTP-PAKRPVSMLFQENNLFTHLTVRQNIAlgMH 97
Cdd:cd03265 20 SFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPrEVRRRIGIVFQDLSVDDELTGWENLY--IH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 98 PGLR--LNDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQDV 175
Cdd:cd03265 98 ARLYgvPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 779793995 176 CQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEEL 217
Cdd:cd03265 178 KEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-219 |
6.03e-35 |
|
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: 124.57 E-value: 6.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 18 FTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQD-HTHTPPAKRP-VSMLFQENNLFThLTVRQNIALG 95
Cdd:cd03249 22 LSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDiRDLNLRWLRSqIGLVSQEPVLFD-GTIAENIRYG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 96 mhpglrLNDAQRHKLEEIAAQMGIAGFIDRLP-----------GELSGGQRQRVALARCLVREQPMLLLDEPFSALDpal 164
Cdd:cd03249 101 ------KPDATDEEVEEAAKKANIHDFIMSLPdgydtlvgergSQLSGGQKQRIAIARALLRNPKILLLDEATSALD--- 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 165 rQEMLTLVQDVCQRQQL--TMLMVSH---SIEDAARIAprsvVIAEGRIVWDGVTEELLK 219
Cdd:cd03249 172 -AESEKLVQEALDRAMKgrTTIVIAHrlsTIRNADLIA----VLQNGQVVEQGTHDELMA 226
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
19-219 |
9.99e-35 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 124.36 E-value: 9.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAK--RPVSMLFQENNLFTHLTVRQNIALGM 96
Cdd:PRK11231 22 SLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlaRRLALLPQHHLTPEGITVRELVAYGR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 97 HPGL----RLNDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLV 172
Cdd:PRK11231 102 SPWLslwgRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLM 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 779793995 173 QDVcQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDG-----VTEELLK 219
Cdd:PRK11231 182 REL-NTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGtpeevMTPGLLR 232
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
20-218 |
1.13e-34 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 127.65 E-value: 1.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 20 LSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQD--HTHTPPAKRPVSMLFQENNLFTHLTVRQNIALGMH 97
Cdd:PRK09536 24 LSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDveALSARAASRRVASVPQDTSLSFEFDVRQVVEMGRT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 98 PGL----RLNDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQ 173
Cdd:PRK09536 104 PHRsrfdTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVR 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 779793995 174 DVCQRQQlTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELL 218
Cdd:PRK09536 184 RLVDDGK-TAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
19-222 |
2.65e-34 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 126.69 E-value: 2.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPA------KRPVSMLFQENNLFTHLTVRQNI 92
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAelrevrRKKIAMVFQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 93 ALGMHPGLRLNDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLV 172
Cdd:PRK10070 128 AFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDEL 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 779793995 173 QDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELLKGNA 222
Cdd:PRK10070 208 VKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPA 257
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
28-212 |
2.89e-34 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 121.92 E-value: 2.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 28 IAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAKRP-VSMLFQENNLFTHLTVRQ---NIAL--GMHPGlr 101
Cdd:cd03264 28 YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRrIGYLPQEFGVYPNFTVREfldYIAWlkGIPSK-- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 102 lndAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQDVCQRQql 181
Cdd:cd03264 106 ---EVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDR-- 180
|
170 180 190
....*....|....*....|....*....|.
gi 779793995 182 TMLMVSHSIEDAARIAPRSVVIAEGRIVWDG 212
Cdd:cd03264 181 IVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
20-211 |
4.04e-34 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 122.86 E-value: 4.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 20 LSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHtppAKRPVSMLFQENNLFTHLTVRQNIALGMHPG 99
Cdd:PRK11247 33 LHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE---AREDTRLMFQDARLLPWKKVIDNVGLGLKGQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 100 LRlnDAQRHKLEEIaaqmGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQDVCQRQ 179
Cdd:PRK11247 110 WR--DAALQALAAV----GLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQH 183
|
170 180 190
....*....|....*....|....*....|..
gi 779793995 180 QLTMLMVSHSIEDAARIAPRSVVIAEGRIVWD 211
Cdd:PRK11247 184 GFTVLLVTHDVSEAVAMADRVLLIEEGKIGLD 215
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
20-218 |
4.29e-34 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 122.94 E-value: 4.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 20 LSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSI-----VID-----NQDHTHTPPAKRPVSMLFQENNLFTHLTVR 89
Cdd:PRK11264 24 LEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDtarslSQQKGLIRQLRQHVGFVFQNFNLFPHRTVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 90 QNIALGmhPGLRLNDAQRHKLE---EIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQ 166
Cdd:PRK11264 104 ENIIEG--PVIVKGEPKEEATArarELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVG 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 779793995 167 EMLTLVQDVCQRQQlTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELL 218
Cdd:PRK11264 182 EVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALF 232
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
18-231 |
4.58e-34 |
|
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: 128.30 E-value: 4.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 18 FTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPA--KRPVSMLFQENNLFTHlTVRQNIALG 95
Cdd:TIGR02203 351 ISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLAslRRQVALVSQDVVLFND-TIANNIAYG 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 96 mhpglRLNDAQRHKLEEIAAQMGIAGFIDRLP-----------GELSGGQRQRVALARCLVREQPMLLLDEPFSALDpal 164
Cdd:TIGR02203 430 -----RTEQADRAEIERALAAAYAQDFVDKLPlgldtpigengVLLSGGQRQRLAIARALLKDAPILILDEATSALD--- 501
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 779793995 165 rQEMLTLVQDVCQR--QQLTMLMVSH---SIEDAARIaprsVVIAEGRIVWDGVTEELLKGNAAASSLLGIS 231
Cdd:TIGR02203 502 -NESERLVQAALERlmQGRTTLVIAHrlsTIEKADRI----VVMDDGRIVERGTHNELLARNGLYAQLHNMQ 568
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
19-199 |
4.80e-34 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 120.80 E-value: 4.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIdnqdhthtpPAKRPVSMLFQENNLFTHL--TVRQNIALGM 96
Cdd:NF040873 12 DLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRR---------AGGARVAYVPQRSEVPDSLplTVRDLVAMGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 97 --HPGL--RLNDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLV 172
Cdd:NF040873 83 waRRGLwrRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALL 162
|
170 180
....*....|....*....|....*..
gi 779793995 173 QDVCqRQQLTMLMVSHSIEDAARIAPR 199
Cdd:NF040873 163 AEEH-ARGATVVVVTHDLELVRRADPC 188
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
19-209 |
1.52e-33 |
|
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: 120.62 E-value: 1.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTH---TPPAK---RPVSMLFQENNLFTHLTVRQNI 92
Cdd:COG4181 32 SLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAldeDARARlraRHVGFVFQSFQLLPTLTALENV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 93 ALgmhPGLRLNDAQ-RHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTL 171
Cdd:COG4181 112 ML---PLELAGRRDaRARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDL 188
|
170 180 190
....*....|....*....|....*....|....*...
gi 779793995 172 VQDVCQRQQLTMLMVSHSIEDAARiAPRSVVIAEGRIV 209
Cdd:COG4181 189 LFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLV 225
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
19-217 |
2.08e-33 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 120.91 E-value: 2.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLL---N----LVAGFLqpVSGSIVIDNQD--HTHTPPAK--RPVSMLFQENNLFTHlT 87
Cdd:COG1117 31 NLDIPENKVTALIGPSGCGKSTLLrclNrmndLIPGAR--VEGEILLDGEDiyDPDVDVVElrRRVGMVFQKPNPFPK-S 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 88 VRQNIALGmhpgLRLN-DAQRHKLEEI-------AAqmgiagfI-----DRL--PG-ELSGGQRQRVALARCLVREQPML 151
Cdd:COG1117 108 IYDNVAYG----LRLHgIKSKSELDEIveeslrkAA-------LwdevkDRLkkSAlGLSGGQQQRLCIARALAVEPEVL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 152 LLDEPFSALDP--ALRQE--MLTLvqdvcqRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEEL 217
Cdd:COG1117 177 LMDEPTSALDPisTAKIEelILEL------KKDYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQI 240
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
19-219 |
2.30e-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: 122.47 E-value: 2.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQP---VSGSIVIDNQDHTHTPPAK------RPVSMLFQE-----NNLFT 84
Cdd:COG0444 25 SFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKElrkirgREIQMIFQDpmtslNPVMT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 85 hltVRQNIALGM--HPGLRLNDAqRHKLEEIAAQMGI---AGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSA 159
Cdd:COG0444 105 ---VGDQIAEPLriHGGLSKAEA-RERAIELLERVGLpdpERRLDRYPHELSGGMRQRVMIARALALEPKLLIADEPTTA 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 160 LDPALRQEMLTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELLK 219
Cdd:COG0444 181 LDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFE 240
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
19-217 |
2.30e-33 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 121.41 E-value: 2.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQD-----HTHTPPAKRPVSMLFQENNLFTHLTVRQNIA 93
Cdd:PRK11831 27 SLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENipamsRSRLYTVRKRMSMLFQSGALFTDMNVFDNVA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 94 LGMHPGLRLNDAQRH-----KLEEIaaqmGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEM 168
Cdd:PRK11831 107 YPLREHTQLPAPLLHstvmmKLEAV----GLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 779793995 169 LTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEEL 217
Cdd:PRK11831 183 VKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
19-209 |
4.98e-33 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 118.51 E-value: 4.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDhthTPPAKR--PVSMLFQENN--LFTHlTVRQNIAL 94
Cdd:cd03226 20 SLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP---IKAKERrkSIGYVMQDVDyqLFTD-SVREELLL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 95 GmhpgLRLNDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQD 174
Cdd:cd03226 96 G----LKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRE 171
|
170 180 190
....*....|....*....|....*....|....*
gi 779793995 175 vCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIV 209
Cdd:cd03226 172 -LAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
19-217 |
2.67e-32 |
|
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: 117.63 E-value: 2.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPP---AKRPVSMLFQENNLFTHLTVRQNIALG 95
Cdd:TIGR03410 20 SLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPherARAGIAYVPQGREIFPRLTVEENLLTG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 96 MHPglrLNDAQRHKLEEIAA------QMgiagfIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEML 169
Cdd:TIGR03410 100 LAA---LPRRSRKIPDEIYElfpvlkEM-----LGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDIG 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 779793995 170 TLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEEL 217
Cdd:TIGR03410 172 RVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-218 |
5.26e-32 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 122.10 E-value: 5.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTL-LNLVAgfLQPVSGSIVIDNQD-HTHTPPAKRP----VSMLFQE--NNLFTHLTVRQ 90
Cdd:COG4172 306 SLTLRRGETLGLVGESGSGKSTLgLALLR--LIPSEGEIRFDGQDlDGLSRRALRPlrrrMQVVFQDpfGSLSPRMTVGQ 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 91 NIALGMH---PGLrlNDAQRHKL-EEIAAQMGI-AGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALR 165
Cdd:COG4172 384 IIAEGLRvhgPGL--SAAERRARvAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQ 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 779793995 166 QEMLTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELL 218
Cdd:COG4172 462 AQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVF 514
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
19-217 |
5.30e-32 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 118.65 E-value: 5.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTP-PAKRPVSMLFQENNLFTHLTVRQNiaLGMH 97
Cdd:TIGR01188 13 NFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPrKVRRSIGIVPQYASVDEDLTGREN--LEMM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 98 PGLR--LNDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQDV 175
Cdd:TIGR01188 91 GRLYglPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDYIRAL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 779793995 176 cQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEEL 217
Cdd:TIGR01188 171 -KEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
19-216 |
5.34e-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: 5.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPA---KRPVSMLFQENNLFTHLTVRQNIALG 95
Cdd:COG3845 25 SLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRdaiALGIGMVHQHFMLVPNLTVAENIVLG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 96 MHP--GLRLNDAQ-RHKLEEIAAQMGIAgfID--RLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLT 170
Cdd:COG3845 105 LEPtkGGRLDRKAaRARIRELSERYGLD--VDpdAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFE 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 779793995 171 LVQDVCqRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEE 216
Cdd:COG3845 183 ILRRLA-AEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAE 227
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
15-217 |
5.69e-32 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 122.65 E-value: 5.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 15 PMRFTLSvlQGERIAVLGPSGAGKSTLLNLVAGFLqPVSGSIVIDNQDHTHTPPA--KRPVSMLFQENNLFtHLTVRQNI 92
Cdd:PRK11174 368 PLNFTLP--AGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPEswRKHLSWVGQNPQLP-HGTLRDNV 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 93 ALGMHpglrlnDAQRHKLEEIAAQMGIAGFIDRLP-------GE----LSGGQRQRVALARCLVREQPMLLLDEPFSALD 161
Cdd:PRK11174 444 LLGNP------DASDEQLQQALENAWVSEFLPLLPqgldtpiGDqaagLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 779793995 162 PALRQEMLTLVQDVCQRQqlTMLMVSHSIEDAARIaPRSVVIAEGRIVWDGVTEEL 217
Cdd:PRK11174 518 AHSEQLVMQALNAASRRQ--TTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAEL 570
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
25-218 |
1.02e-31 |
|
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: 121.85 E-value: 1.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 25 GERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPA--KRPVSMLFQENNLFTHlTVRQNIALGmhpglRL 102
Cdd:COG5265 384 GKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQAslRAAIGIVPQDTVLFND-TIAYNIAYG-----RP 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 103 nDAQRHKLEEiAAQMG-IAGFIDRLP-------GE----LSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLT 170
Cdd:COG5265 458 -DASEEEVEA-AARAAqIHDFIESLPdgydtrvGErglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQA 535
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 779793995 171 LVQDVCQRQqlTMLMVSH---SIEDAARIaprsVVIAEGRIVWDGVTEELL 218
Cdd:COG5265 536 ALREVARGR--TTLVIAHrlsTIVDADEI----LVLEAGRIVERGTHAELL 580
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
20-218 |
2.04e-31 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 116.05 E-value: 2.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 20 LSVLQGERIAVLGPSGAGKSTLL---NLVAgflQPVSGSIVIDNQD-------HTHTPPAKRP--------VSMLFQENN 81
Cdd:COG4598 29 LTARKGDVISIIGSSGSGKSTFLrciNLLE---TPDSGEIRVGGEEirlkpdrDGELVPADRRqlqrirtrLGMVFQSFN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 82 LFTHLTVRQNIALGMHPGLRLNDAQ-RHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSAL 160
Cdd:COG4598 106 LWSHMTVLENVIEAPVHVLGRPKAEaIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSAL 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 779793995 161 DPALRQEMLTLVQDVCQRQQlTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELL 218
Cdd:COG4598 186 DPELVGEVLKVMRDLAEEGR-TMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVF 242
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
19-208 |
2.81e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 115.98 E-value: 2.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTP--PAKRPVSMLFQE-NNLFTHLTVRQNIALG 95
Cdd:PRK13650 27 SFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENvwDIRHKIGMVFQNpDNQFVGATVEDDVAFG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 96 M-HPGLRLNDaQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQD 174
Cdd:PRK13650 107 LeNKGIPHEE-MKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKG 185
|
170 180 190
....*....|....*....|....*....|....
gi 779793995 175 VCQRQQLTMLMVSHSIEDAArIAPRSVVIAEGRI 208
Cdd:PRK13650 186 IRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQV 218
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-208 |
8.59e-31 |
|
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: 113.33 E-value: 8.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 2 LKLTDVTWLYQHLPMR-----FTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQ-----DHTHTppaKR 71
Cdd:cd03248 12 VKFQNVTFAYPTRPDTlvlqdVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpisqyEHKYL---HS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 72 PVSMLFQENNLFTHlTVRQNIALGmhpglrLNDAQRHKLEEIAAQMGIAGFIDRLP-----------GELSGGQRQRVAL 140
Cdd:cd03248 89 KVSLVGQEPVLFAR-SLQDNIAYG------LQSCSFECVKEAAQKAHAHSFISELAsgydtevgekgSQLSGGQKQRVAI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 779793995 141 ARCLVREQPMLLLDEPFSALDPALRQEMLTLVQDVCQRQqlTMLMVSHSIEDAARiAPRSVVIAEGRI 208
Cdd:cd03248 162 ARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-212 |
2.13e-30 |
|
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: 110.87 E-value: 2.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 2 LKLTDVTWLY----QHLPMRFTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQD-HTHTPPAKRPVSML 76
Cdd:cd03247 1 LSINNVSFSYpeqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPvSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 77 FQENNLFThLTVRQNIalgmhpGLRlndaqrhkleeiaaqmgiagfidrlpgeLSGGQRQRVALARCLVREQPMLLLDEP 156
Cdd:cd03247 81 NQRPYLFD-TTLRNNL------GRR----------------------------FSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 779793995 157 FSALDPALRQEMLTLVQDVCQRQqlTMLMVSH---SIEDAARIaprsVVIAEGRIVWDG 212
Cdd:cd03247 126 TVGLDPITERQLLSLIFEVLKDK--TLIWITHhltGIEHMDKI----LFLENGKIIMQG 178
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
27-217 |
2.34e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 113.74 E-value: 2.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 27 RIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHT--HTPPAKRPVSMLFQ--ENNLFTHlTVRQNIALG-MHPGLR 101
Cdd:PRK13652 32 RIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITkeNIREVRKFVGLVFQnpDDQIFSP-TVEQDIAFGpINLGLD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 102 lNDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQDVCQRQQL 181
Cdd:PRK13652 111 -EETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGM 189
|
170 180 190
....*....|....*....|....*....|....*.
gi 779793995 182 TMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEEL 217
Cdd:PRK13652 190 TVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-212 |
3.38e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 113.30 E-value: 3.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTP------PAKRPVSMLFQ--ENNLFTHlTVRQ 90
Cdd:PRK13649 27 NLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdikQIRKKVGLVFQfpESQLFEE-TVLK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 91 NIALG-MHPGLRLNDAQRHKLEEIAAqMGIA-GFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEM 168
Cdd:PRK13649 106 DVAFGpQNFGVSQEEAEALAREKLAL-VGISeSLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKEL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 779793995 169 LTLVQDVcQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDG 212
Cdd:PRK13649 185 MTLFKKL-HQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSG 227
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
9-228 |
4.48e-30 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 112.59 E-value: 4.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 9 WLYQHLPM--RFTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPA-----KRPVSMLFQE-- 79
Cdd:TIGR02769 19 GAKQRAPVltNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKqrrafRRDVQLVFQDsp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 80 NNLFTHLTVRQNIALGMHPGLRLNDAQRH-KLEEIAAQMGI-AGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPF 157
Cdd:TIGR02769 99 SAVNPRMTVRQIIGEPLRHLTSLDESEQKaRIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAV 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 779793995 158 SALDPALRQEMLTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELLKGNAAASSLL 228
Cdd:TIGR02769 179 SNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLSFKHPAGRNL 249
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
19-217 |
6.85e-30 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 113.67 E-value: 6.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAK-----RPVSMLFQenNLFTHL----TVR 89
Cdd:COG4608 38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRElrplrRRMQMVFQ--DPYASLnprmTVG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 90 QNIALGM--HpGLRLNDAQRHKLEEIAAQMGI-AGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQ 166
Cdd:COG4608 116 DIIAEPLriH-GLASKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQA 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 167 EMLTLVQDVCQRQQLTMLMVSHSIedaariaprSVV--IAE-------GRIVWDGVTEEL 217
Cdd:COG4608 195 QVLNLLEDLQDELGLTYLFISHDL---------SVVrhISDrvavmylGKIVEIAPRDEL 245
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
19-228 |
1.10e-29 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 111.70 E-value: 1.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPA-----KRPVSMLFQE--NNLFTHLTVRQN 91
Cdd:PRK10419 32 SLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAqrkafRRDIQMVFQDsiSAVNPRKTVREI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 92 IALGMHPGLRLNDAQR-HKLEEIAAQMGIA-GFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEML 169
Cdd:PRK10419 112 IREPLRHLLSLDKAERlARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVI 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 779793995 170 TLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELLKGNAAASSLL 228
Cdd:PRK10419 192 RLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLTFSSPAGRVL 250
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
19-227 |
1.96e-29 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 110.83 E-value: 1.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQ---------------DHTHTPPAKRPVSMLFQENNLF 83
Cdd:PRK10619 25 SLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQtinlvrdkdgqlkvaDKNQLRLLRTRLTMVFQHFNLW 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 84 THLTVRQNIALGMHPGLRLNDAQ-RHKLEEIAAQMGIAGFI-DRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALD 161
Cdd:PRK10619 105 SHMTVLENVMEAPIQVLGLSKQEaRERAVKYLAKVGIDERAqGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALD 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 779793995 162 PALRQEMLTLVQDVCQRQQlTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELLkGNAAASSL 227
Cdd:PRK10619 185 PELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLF-GNPQSPRL 248
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
2-228 |
2.13e-29 |
|
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: 115.43 E-value: 2.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 2 LKLTDVTWLY----QHLPMRFTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPA--KRPVSM 75
Cdd:TIGR03796 478 VELRNITFGYsplePPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREvlANSVAM 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 76 LFQENNLFTHlTVRQNIALGMHPglrLNDAQrhkLEEIAAQMGIAGFIDRLPGE-----------LSGGQRQRVALARCL 144
Cdd:TIGR03796 558 VDQDIFLFEG-TVRDNLTLWDPT---IPDAD---LVRACKDAAIHDVITSRPGGydaelaegganLSGGQRQRLEIARAL 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 145 VREQPMLLLDEPFSALDPALRQEmltlVQDVCQRQQLTMLMVSH---SIEDAARIaprsVVIAEGRIVWDGVTEELLKGN 221
Cdd:TIGR03796 631 VRNPSILILDEATSALDPETEKI----IDDNLRRRGCTCIIVAHrlsTIRDCDEI----IVLERGKVVQRGTHEELWAVG 702
|
....*..
gi 779793995 222 AAASSLL 228
Cdd:TIGR03796 703 GAYARLI 709
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
19-212 |
2.34e-29 |
|
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: 110.11 E-value: 2.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSI-VIDNQDHTHTPPAKRPVSMLF-QENNLFTHLTVRQNIALgM 96
Cdd:cd03267 41 SFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVrVAGLVPWKRRKKFLRRIGVVFgQKTQLWWDLPVIDSFYL-L 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 97 HPGLRLNDAQ-RHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQDV 175
Cdd:cd03267 120 AAIYDLPPARfKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEY 199
|
170 180 190
....*....|....*....|....*....|....*..
gi 779793995 176 CQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDG 212
Cdd:cd03267 200 NRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-238 |
2.43e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 110.85 E-value: 2.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 1 MLKLTDVTWLY--QHLPM--RFTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHT--HTPPAKRPVS 74
Cdd:PRK13632 7 MIKVENVSFSYpnSENNAlkNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISkeNLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 75 MLFQE-NNLFTHLTVRQNIALGMHPGLRLNDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLL 153
Cdd:PRK13632 87 IIFQNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 154 DEPFSALDPALRQEMLTLVQDVCQRQQLTMLMVSHSIEDAArIAPRSVVIAEGRIVWDGVTEELLKgNAAASSLLGISAP 233
Cdd:PRK13632 167 DESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILN-NKEILEKAKIDSP 244
|
....*
gi 779793995 234 PLYSL 238
Cdd:PRK13632 245 FIYKL 249
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-218 |
2.48e-29 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 114.92 E-value: 2.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 2 LKLTDVTWLYQHLPM----RFTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPA--KRPVSM 75
Cdd:PRK11160 339 LTLNNVSFTYPDQPQpvlkGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAalRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 76 LFQENNLFTHlTVRQNIALGMHpglrlnDAQRHKLEEIAAQMGIAGFIDRLPG----------ELSGGQRQRVALARCLV 145
Cdd:PRK11160 419 VSQRVHLFSA-TLRDNLLLAAP------NASDEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGIARALL 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 779793995 146 REQPMLLLDEPFSALDPALRQEMLTLVQDVCQRQqlTMLMVSH---SIEDAARIaprsVVIAEGRIVWDGVTEELL 218
Cdd:PRK11160 492 HDAPLLLLDEPTEGLDAETERQILELLAEHAQNK--TVLMITHrltGLEQFDRI----CVMDNGQIIEQGTHQELL 561
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-218 |
2.71e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 111.09 E-value: 2.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 1 MLKLTDVTWLY---QHLPMRFTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPA----KRPV 73
Cdd:PRK13636 5 ILKVEELNYNYsdgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGlmklRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 74 SMLFQ--ENNLFThLTVRQNIALG-MHPGLRLNDAQRhKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPM 150
Cdd:PRK13636 85 GMVFQdpDNQLFS-ASVYQDVSFGaVNLKLPEDEVRK-RVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 779793995 151 LLLDEPFSALDPALRQEMLTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELL 218
Cdd:PRK13636 163 LVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
20-212 |
3.06e-29 |
|
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: 108.84 E-value: 3.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 20 LSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAKRPVSMLFQENNLFTHLTVRQNIALGMHpG 99
Cdd:cd03268 21 LHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEAPGFYPNLTARENLRLLAR-L 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 100 LRLNDAQRHKLEEIaaqMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQDVcQRQ 179
Cdd:cd03268 100 LGIRKKRIDEVLDV---VGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSL-RDQ 175
|
170 180 190
....*....|....*....|....*....|...
gi 779793995 180 QLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDG 212
Cdd:cd03268 176 GITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
20-217 |
3.17e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 110.55 E-value: 3.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 20 LSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQ----DHTHTPPAKRPVSMLFQ--ENNLFTHlTVRQNIA 93
Cdd:PRK13639 23 FKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpikyDKKSLLEVRKTVGIVFQnpDDQLFAP-TVEEDVA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 94 LG-MHPGLRLNDAQRhKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLV 172
Cdd:PRK13639 102 FGpLNLGLSKEEVEK-RVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 779793995 173 QDVcQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEEL 217
Cdd:PRK13639 181 YDL-NKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-211 |
3.41e-29 |
|
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: 107.51 E-value: 3.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPA---KRPVSMLFQennlfthltvrqnialg 95
Cdd:cd03216 20 SLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRdarRAGIAMVYQ----------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 96 mhpglrlndaqrhkleeiaaqmgiagfidrlpgeLSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQDV 175
Cdd:cd03216 83 ----------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRL 128
|
170 180 190
....*....|....*....|....*....|....*.
gi 779793995 176 cQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWD 211
Cdd:cd03216 129 -RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
19-189 |
4.30e-29 |
|
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: 113.99 E-value: 4.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPA--KRPVSMLFQENNLFtHLTVRQNIALGM 96
Cdd:TIGR02868 355 SLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDevRRRVSVCAQDAHLF-DTTVRENLRLAR 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 97 hpglrlNDAQRHKLEEIAAQMGIAGFIDRLPG-----------ELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALR 165
Cdd:TIGR02868 434 ------PDATDEELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPTEHLDAETA 507
|
170 180
....*....|....*....|....
gi 779793995 166 QEMLTLVQDVCQRqqLTMLMVSHS 189
Cdd:TIGR02868 508 DELLEDLLAALSG--RTVVLITHH 529
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-219 |
9.51e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 109.82 E-value: 9.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 1 MLKLTDVTWLYQ-HLPMR------FTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSI------VIDNQDHTHTP 67
Cdd:PRK13643 1 MIKFEKVNYTYQpNSPFAsralfdIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdivVSSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 68 PAKRPVSMLFQ--ENNLFTHlTVRQNIALG-MHPGLRLNDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCL 144
Cdd:PRK13643 81 PVRKKVGVVFQfpESQLFEE-TVLKDVAFGpQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 779793995 145 VREQPMLLLDEPFSALDPALRQEMLTLVQDVCQRQQlTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELLK 219
Cdd:PRK13643 160 AMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQ-TVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
19-229 |
1.37e-28 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 108.06 E-value: 1.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTP---PAKRPVSMLFQENNLFTHLTVRQNIALG 95
Cdd:PRK10895 23 SLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlhaRARRGIGYLPQEASIFRRLSVYDNLMAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 96 MHPGLRLNDAQRH-KLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQD 174
Cdd:PRK10895 103 LQIRDDLSAEQREdRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEH 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 779793995 175 VcQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELLKGNAAASSLLG 229
Cdd:PRK10895 183 L-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYLG 236
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
19-220 |
1.70e-28 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 108.34 E-value: 1.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQ--DHTHTPPAKRPVSMLFQENNLFTHLTVRQNIALGM 96
Cdd:PRK10575 31 SLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQplESWSSKAFARKVAYLPQQLPAAEGMTVRELVAIGR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 97 HP---GL-RLNDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLV 172
Cdd:PRK10575 111 YPwhgALgRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALV 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 779793995 173 QDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELLKG 220
Cdd:PRK10575 191 HRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRG 238
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
19-218 |
1.84e-28 |
|
type I secretion system ABC transporter, HlyB 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: 273831 [Multi-domain] Cd Length: 694 Bit Score: 112.91 E-value: 1.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPA--KRPVSMLFQENNLFTHlTVRQNIALGm 96
Cdd:TIGR01846 477 NLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAwlRRQMGVVLQENVLFSR-SIRDNIALC- 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 97 HPGLrlndaqrhKLEEIAAQMGIAG---FIDRLP-----------GELSGGQRQRVALARCLVREQPMLLLDEPFSALDP 162
Cdd:TIGR01846 555 NPGA--------PFEHVIHAAKLAGahdFISELPqgyntevgekgANLSGGQRQRIAIARALVGNPRILIFDEATSALDY 626
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 779793995 163 ALRQEMLTLVQDVCQRQqlTMLMVSHSIeDAARIAPRSVVIAEGRIVWDGVTEELL 218
Cdd:TIGR01846 627 ESEALIMRNMREICRGR--TVIIIAHRL-STVRACDRIIVLEKGQIAESGRHEELL 679
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
20-217 |
1.97e-28 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 108.18 E-value: 1.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 20 LSVLQGERIAVLGPSGAGKSTLLnlvagflQPVSGSIVIDNQDHTHTPPAKRPVS-----------------MLFQENNL 82
Cdd:PRK09984 25 LNIHHGEMVALLGPSGSGKSTLL-------RHLSGLITGDKSAGSHIELLGRTVQregrlardirksrantgYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 83 FTHLTVRQNI---ALGMHPGLR-----LNDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLD 154
Cdd:PRK09984 98 VNRLSVLENVligALGSTPFWRtcfswFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILAD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 779793995 155 EPFSALDPALRQEMLTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEEL 217
Cdd:PRK09984 178 EPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
20-209 |
2.32e-28 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 107.05 E-value: 2.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 20 LSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAKRP------VSMLFQENNLFTHLTVRQNIA 93
Cdd:TIGR02211 26 LSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAklrnkkLGFIYQFHHLLPDFTALENVA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 94 LgmhPGLrLNDAQRHKLEEIAAQM----GIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEML 169
Cdd:TIGR02211 106 M---PLL-IGKKSVKEAKERAYEMlekvGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNNAKIIF 181
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 779793995 170 TLVQDVCQRQQLTMLMVSHSIEDAARIaPRSVVIAEGRIV 209
Cdd:TIGR02211 182 DLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQLF 220
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
19-219 |
2.51e-28 |
|
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: 112.15 E-value: 2.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAK--RPVSMLFQENNLFTHlTVRQNIAlgm 96
Cdd:COG4618 352 SFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREElgRHIGYLPQDVELFDG-TIAENIA--- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 97 hpglRLNDAQRHKLEEiAAQM-GIAGFIDRLP-------GE----LSGGQRQRVALARCLVREQPMLLLDEPFSALDPAL 164
Cdd:COG4618 428 ----RFGDADPEKVVA-AAKLaGVHEMILRLPdgydtriGEggarLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEG 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 779793995 165 RQEMLTLVQDVCQRQQlTMLMVSHSIEdAARIAPRSVVIAEGRIVWDGVTEELLK 219
Cdd:COG4618 503 EAALAAAIRALKARGA-TVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
19-218 |
3.01e-28 |
|
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: 111.82 E-value: 3.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVI----DNQDHTHTPP-----AKRPVSMLFQENNLFTHLTVR 89
Cdd:TIGR03269 304 SLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPdgrgrAKRYIGILHQEYDLYPHRTVL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 90 QNIALGMhpGLRLNDaqrhkleEIAAQMGI-----AGF--------IDRLPGELSGGQRQRVALARCLVREQPMLLLDEP 156
Cdd:TIGR03269 384 DNLTEAI--GLELPD-------ELARMKAVitlkmVGFdeekaeeiLDKYPDELSEGERHRVALAQVLIKEPRIVILDEP 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 779793995 157 FSALDPALRQEMLTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELL 218
Cdd:TIGR03269 455 TGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
12-209 |
5.46e-28 |
|
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: 105.83 E-value: 5.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 12 QHLPMRF---------TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNqdHTHTPPAKRPVSMLFQENNL 82
Cdd:cd03269 4 ENVTKRFgrvtalddiSFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG--KPLDIAARNRIGYLPEERGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 83 FTHLTVR-QNIALGMHPGLRLNDAqRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALD 161
Cdd:cd03269 82 YPKMKVIdQLVYLAQLKGLKKEEA-RRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 779793995 162 PALRQEMLTLVQDVcQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIV 209
Cdd:cd03269 161 PVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
14-217 |
5.88e-28 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 106.61 E-value: 5.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 14 LPMRF---------TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPP---AKRPVSMLFQENN 81
Cdd:PRK11300 11 LMMRFggllavnnvNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGhqiARMGVVRTFQHVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 82 LFTHLTVRQNIALGMH--------------PGLRlnDAQRHKLEEIAA---QMGIAGFIDRLPGELSGGQRQRVALARCL 144
Cdd:PRK11300 91 LFREMTVIENLLVAQHqqlktglfsgllktPAFR--RAESEALDRAATwleRVGLLEHANRQAGNLAYGQQRRLEIARCM 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 779793995 145 VREQPMLLLDEPFSALDPALRQEMLTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEEL 217
Cdd:PRK11300 169 VTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 241
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
25-218 |
7.76e-28 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 111.20 E-value: 7.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 25 GERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTH--TPPAKRPVSMLFQENNLFTHlTVRQNIALGMhpGLRL 102
Cdd:TIGR03797 479 GEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGldVQAVRRQLGVVLQNGRLMSG-SIFENIAGGA--PLTL 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 103 NDAQRhkleeiAAQM-GIAGFIDRLP-----------GELSGGQRQRVALARCLVREQPMLLLDEPFSALDpalrQEMLT 170
Cdd:TIGR03797 556 DEAWE------AARMaGLAEDIRAMPmgmhtviseggGTLSGGQRQRLLIARALVRKPRILLFDEATSALD----NRTQA 625
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 779793995 171 LVQDVCQRQQLTMLMVSH---SIEDAARIaprsVVIAEGRIVWDGVTEELL 218
Cdd:TIGR03797 626 IVSESLERLKVTRIVIAHrlsTIRNADRI----YVLDAGRVVQQGTYDELM 672
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
19-228 |
1.13e-27 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 110.58 E-value: 1.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQD---------HTHtppakrpVSMLFQENNLFTHlTVR 89
Cdd:TIGR00958 501 TFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPlvqydhhylHRQ-------VALVGQEPVLFSG-SVR 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 90 QNIALGmhpglrLNDAQRHKLEEIAAQMGIAGFIDRLP-------GE----LSGGQRQRVALARCLVREQPMLLLDEPFS 158
Cdd:TIGR00958 573 ENIAYG------LTDTPDEEIMAAAKAANAHDFIMEFPngydtevGEkgsqLSGGQKQRIAIARALVRKPRVLILDEATS 646
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 779793995 159 ALDPALRQemltLVQDVCQRQQLTMLMVSH---SIEDAARIaprsVVIAEGRIVWDGVTEELLKGNAAASSLL 228
Cdd:TIGR00958 647 ALDAECEQ----LLQESRSRASRTVLLIAHrlsTVERADQI----LVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
18-163 |
1.14e-27 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 104.57 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 18 FTLSvlQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAKRpVSMLFQENNLFTHLTVRQNIALGMh 97
Cdd:PRK13539 23 FTLA--AGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA-CHYLGHRNAMKPALTVAENLEFWA- 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 779793995 98 pglRLNDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPA 163
Cdd:PRK13539 99 ---AFLGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA 161
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-227 |
1.24e-27 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 110.11 E-value: 1.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 2 LKLTDVTWLYQ---HLPMR-FTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDN---QDHTHTPpAKRPVS 74
Cdd:PRK11176 342 IEFRNVTFTYPgkeVPALRnINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlRDYTLAS-LRNQVA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 75 MLFQENNLFTHlTVRQNIALGmhpglRLNDAQRHKLEEiAAQMGIA-GFIDRLP-------GE----LSGGQRQRVALAR 142
Cdd:PRK11176 421 LVSQNVHLFND-TIANNIAYA-----RTEQYSREQIEE-AARMAYAmDFINKMDngldtviGEngvlLSGGQRQRIAIAR 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 143 CLVREQPMLLLDEPFSALDpalrQEMLTLVQ---DVCQRQQlTMLMVSH---SIEDAARIaprsVVIAEGRIVWDGVTEE 216
Cdd:PRK11176 494 ALLRDSPILILDEATSALD----TESERAIQaalDELQKNR-TSLVIAHrlsTIEKADEI----LVVEDGEIVERGTHAE 564
|
250
....*....|.
gi 779793995 217 LLKGNAAASSL 227
Cdd:PRK11176 565 LLAQNGVYAQL 575
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
19-218 |
1.64e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 106.33 E-value: 1.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHT--HTPPAKRPVSMLFQE-NNLFTHLTVRQNIALG 95
Cdd:PRK13642 27 SFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTaeNVWNLRRKIGMVFQNpDNQFVGATVEDDVAFG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 96 MHPGLRLNDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQDV 175
Cdd:PRK13642 107 MENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEI 186
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 779793995 176 CQRQQLTMLMVSHSIEDAARiAPRSVVIAEGRIVWDGVTEELL 218
Cdd:PRK13642 187 KEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
20-193 |
1.67e-27 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 104.04 E-value: 1.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 20 LSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPP----AKRPVSMLFQ--ENNLFTHlTVRQNIA 93
Cdd:TIGR01166 13 FAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKglleRRQRVGLVFQdpDDQLFAA-DVDQDVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 94 LG-MHPGLRLNDAQRhKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLV 172
Cdd:TIGR01166 92 FGpLNLGLSEAEVER-RVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGREQMLAIL 170
|
170 180
....*....|....*....|.
gi 779793995 173 QDVcQRQQLTMLMVSHSIEDA 193
Cdd:TIGR01166 171 RRL-RAEGMTVVISTHDVDLA 190
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-222 |
1.85e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 106.71 E-value: 1.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 2 LKLTDVTWLY-QHLPMRF------TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSI--VIDNQDHTHTPPAK-- 70
Cdd:PRK13651 3 IKVKNIVKIFnKKLPTELkaldnvSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewIFKDEKNKKKTKEKek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 71 ----------------------RPVSMLFQ--ENNLFTHlTVRQNIALG-MHPGLRLNDAqrhklEEIAAQM-GIAG--- 121
Cdd:PRK13651 83 vleklviqktrfkkikkikeirRRVGVVFQfaEYQLFEQ-TIEKDIIFGpVSMGVSKEEA-----KKRAAKYiELVGlde 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 122 -FIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQDVcQRQQLTMLMVSHSIEDAARIAPRS 200
Cdd:PRK13651 157 sYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNL-NKQGKTIILVTHDLDNVLEWTKRT 235
|
250 260
....*....|....*....|..
gi 779793995 201 VVIAEGRIVWDGVTEELLKGNA 222
Cdd:PRK13651 236 IFFKDGKIIKDGDTYDILSDNK 257
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
30-217 |
2.32e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 106.86 E-value: 2.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 30 VLGPSGAGKSTLLNLVAGFLQPVSGSIVI---------DNQDHTHTPPAK---------RPVSMLFQ--ENNLFTHlTVR 89
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkkNNHELITNPYSKkiknfkelrRRVSMVFQfpEYQLFKD-TIE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 90 QNIALG-MHPGLRLNDAqRHKLEEIAAQMGI-AGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQE 167
Cdd:PRK13631 136 KDIMFGpVALGVKKSEA-KKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHE 214
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 779793995 168 MLTLVQDvCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEEL 217
Cdd:PRK13631 215 MMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEI 263
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
19-208 |
2.51e-27 |
|
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: 103.06 E-value: 2.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQD-HTHTPPAKRP-VSMLFQENNLFTHlTVRQNIalgm 96
Cdd:cd03246 22 SFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADiSQWDPNELGDhVGYLPQDDELFSG-SIAENI---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 97 hpglrlndaqrhkleeiaaqmgiagfidrlpgeLSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQDVc 176
Cdd:cd03246 97 ---------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAAL- 142
|
170 180 190
....*....|....*....|....*....|..
gi 779793995 177 QRQQLTMLMVSHSIEdAARIAPRSVVIAEGRI 208
Cdd:cd03246 143 KAAGATRIVIAHRPE-TLASADRILVLEDGRV 173
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
19-188 |
4.52e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 108.23 E-value: 4.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIdnqdhthtPPAKRpVSMLFQENNLFTHLTVRQNIALGMHP 98
Cdd:COG0488 18 SLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI--------PKGLR-IGYLPQEPPLDDDLTVLDTVLDGDAE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 99 ---------------------GLRLNDAQ-----------RHKLEEIAAQMGIAGFI-DRLPGELSGGQRQRVALARCLV 145
Cdd:COG0488 89 lraleaeleeleaklaepdedLERLAELQeefealggweaEARAEEILSGLGFPEEDlDRPVSELSGGWRRRVALARALL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 779793995 146 REQPMLLLDEPFSALDpalrQEMLTLVQDVCQRQQLTMLMVSH 188
Cdd:COG0488 169 SEPDLLLLDEPTNHLD----LESIEWLEEFLKNYPGTVLVVSH 207
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
19-219 |
4.68e-27 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 104.01 E-value: 4.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDnqdhthtppaKRPVSML-----FQENnlfthLTVRQNIA 93
Cdd:COG1134 46 SFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVN----------GRVSALLelgagFHPE-----LTGRENIY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 94 LG--MHpGLRLNDAQRhKLEEIAAQMGIAGFIDrLP-GELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLT 170
Cdd:COG1134 111 LNgrLL-GLSRKEIDE-KFDEIVEFAELGDFID-QPvKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLA 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 779793995 171 LVQDVcQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELLK 219
Cdd:COG1134 188 RIREL-RESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
19-217 |
5.51e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 104.09 E-value: 5.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLV--AGFLQP---VSGSIVIDNQD----HTHTPPAKRPVSMLFQENNLFThLTVR 89
Cdd:PRK14239 25 SLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGHNiyspRTDTVDLRKEIGMVFQQPNPFP-MSIY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 90 QNIALGmhpgLRLNDAQ-RHKLEEIAAQMGIAGFI-----DRLPGE---LSGGQRQRVALARCLVREQPMLLLDEPFSAL 160
Cdd:PRK14239 104 ENVVYG----LRLKGIKdKQVLDEAVEKSLKGASIwdevkDRLHDSalgLSGGQQQRVCIARVLATSPKIILLDEPTSAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 779793995 161 DP----ALRQEMLTLvqdvcqRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEEL 217
Cdd:PRK14239 180 DPisagKIEETLLGL------KDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
19-209 |
5.85e-27 |
|
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: 103.34 E-value: 5.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAK--RPVSMLFQENNLFTHlTVRQNIA-LG 95
Cdd:cd03244 24 SFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDlrSRISIIPQDPVLFSG-TIRSNLDpFG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 96 MHPGLRLNDAqrhkLEeiaaQMGIAGFIDRLPGEL-----------SGGQRQRVALARCLVREQPMLLLDEPFSALDPAL 164
Cdd:cd03244 103 EYSDEELWQA----LE----RVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALLRKSKILVLDEATASVDPET 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 779793995 165 RQEMLTLVQDVCqrQQLTMLMVSHSIE---DAARIaprsVVIAEGRIV 209
Cdd:cd03244 175 DALIQKTIREAF--KDCTVLTIAHRLDtiiDSDRI----LVLDKGRVV 216
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-209 |
1.03e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 104.14 E-value: 1.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIdnQDHTHTPPA--------KRPVSMLFQ--ENNLFTHlTV 88
Cdd:PRK13641 27 SFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITI--AGYHITPETgnknlkklRKKVSLVFQfpEAQLFEN-TV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 89 RQNIALG-MHPGLRLNDAQRHKLEEIAaQMGIA-GFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQ 166
Cdd:PRK13641 104 LKDVEFGpKNFGFSEDEAKEKALKWLK-KVGLSeDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRK 182
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 779793995 167 EMLTLVQDVcQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIV 209
Cdd:PRK13641 183 EMMQLFKDY-QKAGHTVILVTHNMDDVAEYADDVLVLEHGKLI 224
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
19-219 |
1.18e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 104.01 E-value: 1.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDN---QDHTHTPPAKRPVSMLFQE-NNLFTHLTVRQNIA- 93
Cdd:PRK13633 30 NLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtSDEENLWDIRNKAGMVFQNpDNQIVATIVEEDVAf 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 94 ----LGMHPglrlnDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEML 169
Cdd:PRK13633 110 gpenLGIPP-----EEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVV 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 779793995 170 TLVQDVCQRQQLTMLMVSHSIEDAARiAPRSVVIAEGRIVWDGVTEELLK 219
Cdd:PRK13633 185 NTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFK 233
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
18-218 |
1.28e-26 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 103.00 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 18 FTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLqPVSGSIVIDNQDHTHTPPAK--RPVSMLFQENNLFTHLTVRQNIALG 95
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAElaRHRAYLSQQQSPPFAMPVFQYLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 96 MHPGLRLnDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQP-------MLLLDEPFSALDPALRQEM 168
Cdd:COG4138 94 QPAGASS-EAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQVWPtinpegqLLLLDEPMNSLDVAQQAAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 779793995 169 LTLVQDVCQrQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELL 218
Cdd:COG4138 173 DRLLRELCQ-QGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-219 |
6.40e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 102.86 E-value: 6.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNqdhtHTPPAKRP-----VSMLF-QENNLFTHLTVRQNi 92
Cdd:COG4586 42 SFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG----YVPFKRRKefarrIGVVFgQRSQLWWDLPAIDS- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 93 algmhpgLRLN-------DAQ-RHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPAL 164
Cdd:COG4586 117 -------FRLLkaiyripDAEyKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVS 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 779793995 165 RQEMLTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELLK 219
Cdd:COG4586 190 KEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKE 244
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
18-217 |
8.84e-26 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 102.35 E-value: 8.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 18 FTLSvlQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPA-----KRPVSMLFQenNLFTHLTVRQNI 92
Cdd:PRK11308 36 FTLE--RGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEaqkllRQKIQIVFQ--NPYGSLNPRKKV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 93 ALGMHPGLRLN-----DAQRHKLEEIAAQMGI-AGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQ 166
Cdd:PRK11308 112 GQILEEPLLINtslsaAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQA 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 779793995 167 EMLTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEEL 217
Cdd:PRK11308 192 QVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQI 242
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
25-184 |
9.77e-26 |
|
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: 99.36 E-value: 9.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 25 GERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDH-THTPPAKRPVSMLFQENNLFTHLTVRQNialgMHPGLRLN 103
Cdd:TIGR01189 26 GEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLaEQRDEPHENILYLGHLPGLKPELSALEN----LHFWAAIH 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 104 DAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQDVCQRQQLTM 183
Cdd:TIGR01189 102 GGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHLARGGIVL 181
|
.
gi 779793995 184 L 184
Cdd:TIGR01189 182 L 182
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
17-193 |
1.17e-25 |
|
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: 99.49 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 17 RFTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQ-DHTHTPPAKRPVSMLFQENNLFTHLTVRQNIALg 95
Cdd:cd03231 18 GLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGpLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRF- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 96 MHPglrlnDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQDV 175
Cdd:cd03231 97 WHA-----DHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGH 171
|
170
....*....|....*...
gi 779793995 176 CQRQQLTMLMVSHSIEDA 193
Cdd:cd03231 172 CARGGMVVLTTHQDLGLS 189
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-197 |
1.63e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 100.50 E-value: 1.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLL------NLVAGFLQpVSGSIVIDNQD----HTHTPPAKRPVSMLFQENNLFThLTV 88
Cdd:PRK14258 27 SMEIYQSKVTAIIGPSGCGKSTFLkclnrmNELESEVR-VEGRVEFFNQNiyerRVNLNRLRRQVSMVHPKPNLFP-MSV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 89 RQNIA-----LGMHPGLRLNDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPA 163
Cdd:PRK14258 105 YDNVAygvkiVGWRPKLEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPI 184
|
170 180 190
....*....|....*....|....*....|....
gi 779793995 164 LRQEMLTLVQDVCQRQQLTMLMVSHSIEDAARIA 197
Cdd:PRK14258 185 ASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLS 218
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
19-228 |
1.73e-25 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 104.27 E-value: 1.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPA--KRPVSMLFQENNLFTHlTVRQNIALGM 96
Cdd:PRK13657 355 SFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAslRRNIAVVFQDAGLFNR-SIEDNIRVGR 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 97 hpglrlNDAQRHKLEEIAAQMGIAGFIDRLP-------GE----LSGGQRQRVALARCLVREQPMLLLDEPFSALDpALR 165
Cdd:PRK13657 434 ------PDATDEEMRAAAERAQAHDFIERKPdgydtvvGErgrqLSGGERQRLAIARALLKDPPILILDEATSALD-VET 506
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 779793995 166 QEMLTLVQDvCQRQQLTMLMVSH---SIEDAARIaprsVVIAEGRIVWDGVTEELLKGNAAASSLL 228
Cdd:PRK13657 507 EAKVKAALD-ELMKGRTTFIIAHrlsTVRNADRI----LVFDNGRVVESGSFDELVARGGRFAALL 567
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
25-209 |
1.86e-25 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 99.56 E-value: 1.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 25 GERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQD-----HTHTPPAKRPVSMLFQENNLFTHLTVRQNIALGMH-P 98
Cdd:PRK10908 28 GEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDitrlkNREVPFLRRQIGMIFQDHHLLMDRTVYDNVAIPLIiA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 99 GLRLNDAQRhkleEIAAQMGIAGFIDR---LPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQDV 175
Cdd:PRK10908 108 GASGDDIRR----RVSAALDKVGLLDKaknFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEF 183
|
170 180 190
....*....|....*....|....*....|....
gi 779793995 176 cQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIV 209
Cdd:PRK10908 184 -NRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-219 |
1.99e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 101.01 E-value: 1.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 2 LKLTDVTWLYQH-LPMRF------TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTP------P 68
Cdd:PRK13646 3 IRFDNVSYTYQKgTPYEHqaihdvNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyirP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 69 AKRPVSMLFQ--ENNLFTHlTVRQNIALGmhP---GLRLNDAqRHKLEEIAAQMGIAGFIDRL-PGELSGGQRQRVALAR 142
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFED-TVEREIIFG--PknfKMNLDEV-KNYAHRLLMDLGFSRDVMSQsPFQMSGGQMRKIAIVS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 779793995 143 CLVREQPMLLLDEPFSALDPALRQEMLTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELLK 219
Cdd:PRK13646 159 ILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
18-218 |
2.23e-25 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 100.45 E-value: 2.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 18 FTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQ--DHTHTPPAKRPVSMLFQENNLFTHLTVRQNIALG 95
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEhiQHYASKEVARRIGLLAQNATTPGDITVQELVARG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 96 MHPGLRLNDAQRHKLEE-IAAQM---GIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTL 171
Cdd:PRK10253 106 RYPHQPLFTRWRKEDEEaVTKAMqatGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLEL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 779793995 172 VQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELL 218
Cdd:PRK10253 186 LSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
20-218 |
3.83e-25 |
|
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: 98.77 E-value: 3.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 20 LSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDhthTPPAKRPVSMLFQENNlFT---HLTVRQNIALGM 96
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGAS---PGKGWRHIGYVPQRHE-FAwdfPISVAHTVMSGR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 97 --------HPGLRLNDAQRHKLEeiaaQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEM 168
Cdd:TIGR03771 77 tghigwlrRPCVADFAAVRDALR----RVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 779793995 169 LTLVQDVCQrQQLTMLMVSHSIEDAARIAPRsVVIAEGRIVWDGVTEELL 218
Cdd:TIGR03771 153 TELFIELAG-AGTAILMTTHDLAQAMATCDR-VVLLNGRVIADGTPQQLQ 200
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
19-228 |
5.78e-25 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 102.88 E-value: 5.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQD-HTHTPPA-----KRPVSMLFQENNLFTHLTVRQNI 92
Cdd:PRK10535 28 SLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDvATLDADAlaqlrREHFGFIFQRYHLLSHLTAAQNV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 93 AL-GMHPGLRLNdAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTL 171
Cdd:PRK10535 108 EVpAVYAGLERK-QRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAI 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 779793995 172 VQDVCQRQQlTMLMVSHSIEDAARiAPRSVVIAEGRIVWDGVTEELLKGNAAASSLL 228
Cdd:PRK10535 187 LHQLRDRGH-TVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPPAQEKVNVAGGTEPVV 241
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
19-208 |
6.28e-25 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 98.35 E-value: 6.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQD-HTHTPPAK-----RPVSMLFQENNLFTHLTVRQNI 92
Cdd:PRK11629 29 SFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPmSKLSSAAKaelrnQKLGFIYQFHHLLPDFTALENV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 93 ALGMHPG-LRLNDAQRHKLEEIAAqMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTL 171
Cdd:PRK11629 109 AMPLLIGkKKPAEINSRALEMLAA-VGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQL 187
|
170 180 190
....*....|....*....|....*....|....*..
gi 779793995 172 VQDVCQRQQLTMLMVSHSIEDAARIApRSVVIAEGRI 208
Cdd:PRK11629 188 LGELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRL 223
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
20-218 |
6.56e-25 |
|
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: 102.07 E-value: 6.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 20 LSVLQGERIAVLGPSGAGKS----TLLNLVAGFLQPVSGSIVIDNQDHTHTPPAK------RPVSMLFQE-----NNLFT 84
Cdd:COG4172 31 FDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERElrrirgNRIAMIFQEpmtslNPLHT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 85 hltVRQNIA--LGMHPGLRLNDAQRHKLEeIAAQMGI---AGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSA 159
Cdd:COG4172 111 ---IGKQIAevLRLHRGLSGAAARARALE-LLERVGIpdpERRLDAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTA 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 779793995 160 LDPALRQEMLTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELL 218
Cdd:COG4172 187 LDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELF 245
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
4-238 |
8.08e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 99.31 E-value: 8.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 4 LTDVTWLY-QHLPMRF------TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNqdhtHTPPA------- 69
Cdd:PRK13645 9 LDNVSYTYaKKTPFEFkalnntSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGD----YAIPAnlkkike 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 70 ----KRPVSMLFQ--ENNLFTHlTVRQNIALG-MHPGLRLNDAQRhKLEEIAAQMGIA-GFIDRLPGELSGGQRQRVALA 141
Cdd:PRK13645 85 vkrlRKEIGLVFQfpEYQLFQE-TIEKDIAFGpVNLGENKQEAYK-KVPELLKLVQLPeDYVKRSPFELSGGQKRRVALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 142 RCLVREQPMLLLDEPFSALDPALRQEMLTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELLKgN 221
Cdd:PRK13645 163 GIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS-N 241
|
250
....*....|....*..
gi 779793995 222 AAASSLLGISAPPLYSL 238
Cdd:PRK13645 242 QELLTKIEIDPPKLYQL 258
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-217 |
1.12e-24 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 101.67 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 20 LSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAKRP---VSMLFQENNLFTHLTVRQNIALGM 96
Cdd:PRK15439 32 FTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHqlgIYLVPQEPLLFPNLSVKENILFGL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 97 HpglRLNDAQRhKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQDVc 176
Cdd:PRK15439 112 P---KRQASMQ-KMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIREL- 186
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 779793995 177 QRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEEL 217
Cdd:PRK15439 187 LAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
19-212 |
1.20e-24 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 97.22 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNqdhthtppakRPVSML-----FQENnlfthLTVRQNIA 93
Cdd:cd03220 42 SFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG----------RVSSLLglgggFNPE-----LTGRENIY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 94 L-GMHPGLRLNDAQRhKLEEIAAQMGIAGFIDRLPGELSGGQRQRV--ALARCLvrEQPMLLLDEPFSALDPALRQEMLT 170
Cdd:cd03220 107 LnGRLLGLSRKEIDE-KIDEIIEFSELGDFIDLPVKTYSSGMKARLafAIATAL--EPDILLIDEVLAVGDAAFQEKCQR 183
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 779793995 171 LVQDVCQrQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDG 212
Cdd:cd03220 184 RLRELLK-QGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
19-219 |
1.44e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 98.33 E-value: 1.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGS---IVIDNQDHTHTP--PAKRPVSMLFQE-NNLFTHLTVRQNI 92
Cdd:PRK13640 27 SFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTvwDIREKVGIVFQNpDNQFVGATVGDDV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 93 ALGmhpgLRLNDAQRHKLEEIA----AQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEM 168
Cdd:PRK13640 107 AFG----LENRAVPRPEMIKIVrdvlADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQI 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 779793995 169 LTLVQDVCQRQQLTMLMVSHSIEDAArIAPRSVVIAEGRIVWDGVTEELLK 219
Cdd:PRK13640 183 LKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPVEIFS 232
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-219 |
2.20e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 97.51 E-value: 2.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 1 MLKLTDVTWLYQHlPMRFTL-----SVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQ--DHTHTPPAKRPV 73
Cdd:PRK13648 7 IIVFKNVSFQYQS-DASFTLkdvsfNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQaiTDDNFEKLRKHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 74 SMLFQE-NNLFTHLTVRQNIALGMHPGLRLNDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLL 152
Cdd:PRK13648 86 GIVFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVII 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 779793995 153 LDEPFSALDPALRQEMLTLVQDVCQRQQLTMLMVSHSIEDAARiAPRSVVIAEGRIVWDGVTEELLK 219
Cdd:PRK13648 166 LDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-217 |
2.48e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 97.87 E-value: 2.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 1 MLKLTDVTwlyqhlpMRF---------TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAKr 71
Cdd:COG4152 1 MLELKGLT-------KRFgdktavddvSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRR- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 72 pVSMLFQENNLFTHLTVRQNIA-LGMHPGLRLNDAqRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPM 150
Cdd:COG4152 73 -IGYLPEERGLYPKMKVGEQLVyLARLKGLSKAEA-KRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPEL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 779793995 151 LLLDEPFSALDPALRQEMLTLVQDVcQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEEL 217
Cdd:COG4152 151 LILDEPFSGLDPVNVELLKDVIREL-AAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
29-218 |
2.87e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 96.91 E-value: 2.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 29 AVLGPSGAGKSTLLN----LVAGFLQP-VSGSIVIDNQDHTHTPPA--KRPVSMLFQENNLFTHLTVRQNIALGmhpgLR 101
Cdd:PRK14247 33 ALMGPSGSGKSTLLRvfnrLIELYPEArVSGEVYLDGQDIFKMDVIelRRRVQMVFQIPNPIPNLSIFENVALG----LK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 102 LNDAQRHKLEEIA--------AQM--GIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTL 171
Cdd:PRK14247 109 LNRLVKSKKELQErvrwalekAQLwdEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESL 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 779793995 172 VQDVcqRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELL 218
Cdd:PRK14247 189 FLEL--KKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVF 233
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
19-218 |
2.88e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 97.95 E-value: 2.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVI-DNQDHTHTPPAKRPVSMLFQENNLFTHLTVRQNI-ALGM 96
Cdd:PRK13537 27 SFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcGEPVPSRARHARQRVGVVPQFDNLDPDFTVRENLlVFGR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 97 HPGLRLNDAQRH--KLEEIAAQMGIAgfiDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQD 174
Cdd:PRK13537 107 YFGLSAAAARALvpPLLEFAKLENKA---DAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRS 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 779793995 175 VCQRQQlTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELL 218
Cdd:PRK13537 184 LLARGK-TILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALI 226
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-238 |
3.17e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 97.37 E-value: 3.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 1 MLKLTDVTWLY-QHLPM--RFTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIV---IDNQDHTHTPPAKRPVS 74
Cdd:PRK13644 1 MIRLENVSYSYpDGTPAleNINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLvsgIDTGDFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 75 MLFQE-NNLFTHLTVRQNIALGMHpGLRLNDAQRHKLEEIA-AQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLL 152
Cdd:PRK13644 81 IVFQNpETQFVGRTVEEDLAFGPE-NLCLPPIEIRKRVDRAlAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 153 LDEPFSALDPALRQEMLTLVQDVcQRQQLTMLMVSHSIEDaARIAPRSVVIAEGRIVWDGVTEELLkgNAAASSLLGISA 232
Cdd:PRK13644 160 FDEVTSMLDPDSGIAVLERIKKL-HEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVL--SDVSLQTLGLTP 235
|
....*.
gi 779793995 233 PPLYSL 238
Cdd:PRK13644 236 PSLIEL 241
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
19-227 |
6.96e-24 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 99.81 E-value: 6.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIV-----IDNQDHTHTppaKRPVSMLFQENNLFTHlTVRQNIA 93
Cdd:TIGR01193 494 SLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILlngfsLKDIDRHTL---RQFINYLPQEPYIFSG-SILENLL 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 94 LGMHPGLRLNDAQRH-KLEEIAA-----QMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQE 167
Cdd:TIGR01193 570 LGAKENVSQDEIWAAcEIAEIKDdienmPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKK 649
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 168 mltLVQDVCQRQQLTMLMVSHSIEDAARiAPRSVVIAEGRIVWDGVTEELLKGNAAASSL 227
Cdd:TIGR01193 650 ---IVNNLLNLQDKTIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDELLDRNGFYASL 705
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-229 |
7.43e-24 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 95.72 E-value: 7.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 1 MLKLTDVTWLYQHLPM--RFTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAK---RPVSM 75
Cdd:PRK11614 5 MLSFDKVSAHYGKIQAlhEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKimrEAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 76 LFQENNLFTHLTVRQNIALGMHPGLRLNDAQR--------HKLEEIAAQMGiagfidrlpGELSGGQRQRVALARCLVRE 147
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLAMGGFFAERDQFQERikwvyelfPRLHERRIQRA---------GTMSGGEQQMLAIGRALMSQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 148 QPMLLLDEPFSALDPALRQEMLTLVQDVcQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELLKGNAAASSL 227
Cdd:PRK11614 156 PRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAY 234
|
..
gi 779793995 228 LG 229
Cdd:PRK11614 235 LG 236
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
29-219 |
7.58e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 96.06 E-value: 7.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 29 AVLGPSGAGKSTLLNLVAGFLQ-----PVSGSIVIDNQDhTHTP-----PAKRPVSMLFQENNLFTHLTVRQNIALGmhp 98
Cdd:PRK14267 34 ALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRN-IYSPdvdpiEVRREVGMVFQYPNPFPHLTIYDNVAIG--- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 99 gLRLNDAQRHKlEEIAAQMGIA--------GFIDRL---PGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQE 167
Cdd:PRK14267 110 -VKLNGLVKSK-KELDERVEWAlkkaalwdEVKDRLndyPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAK 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 779793995 168 MLTLVQDVcqRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELLK 219
Cdd:PRK14267 188 IEELLFEL--KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFE 237
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
18-210 |
9.77e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 98.98 E-value: 9.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 18 FTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVI-DN-------QDHTHTPPAKRPVSMLFQENNLFTHLTVR 89
Cdd:COG0488 334 LSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLgETvkigyfdQHQEELDPDKTVLDELRDGAPGGTEQEVR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 90 QnialgmhpglrlndaqrhkleeIAAQMGIAG-FIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPalrqEM 168
Cdd:COG0488 414 G----------------------YLGRFLFSGdDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDI----ET 467
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 779793995 169 LTLVQDVCQRQQLTMLMVSHsieD---AARIAPRSVVIAEGRIVW 210
Cdd:COG0488 468 LEALEEALDDFPGTVLLVSH---DryfLDRVATRILEFEDGGVRE 509
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
29-226 |
1.08e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 95.93 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 29 AVLGPSGAGKSTLL-------NLVAGFlqPVSGSIVIDNQ---DHTHTPPAKRPVSMLFQENNLFThLTVRQNIALGMH- 97
Cdd:PRK14271 51 SLMGPTGSGKTTFLrtlnrmnDKVSGY--RYSGDVLLGGRsifNYRDVLEFRRRVGMLFQRPNPFP-MSIMDNVLAGVRa 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 98 ----PGLRLNDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQ 173
Cdd:PRK14271 128 hklvPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIR 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 779793995 174 DVCQRqqLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELLKGNAAASS 226
Cdd:PRK14271 208 SLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAET 258
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
18-189 |
2.93e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 93.63 E-value: 2.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 18 FTLSvlQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPA--KRPVSMLFQENNLFTHlTVRQNIAL- 94
Cdd:PRK10247 28 FSLR--AGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEiyRQQVSYCAQTPTLFGD-TVYDNLIFp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 95 ----GMHPGLR--LNDAQRHKLEEIAAQMGIAgfidrlpgELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEM 168
Cdd:PRK10247 105 wqirNQQPDPAifLDDLERFALPDTILTKNIA--------ELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNV 176
|
170 180
....*....|....*....|.
gi 779793995 169 LTLVQDVCQRQQLTMLMVSHS 189
Cdd:PRK10247 177 NEIIHRYVREQNIAVLWVTHD 197
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
19-228 |
6.65e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 93.65 E-value: 6.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQD-HTHTPPAKRP-VSMLFQE--NNLFThLTVRQNIAL 94
Cdd:PRK13647 25 SLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREvNAENEKWVRSkVGLVFQDpdDQVFS-STVWDDVAF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 95 G-MHPGLRLNDAQRhKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPAlRQEMLTLVQ 173
Cdd:PRK13647 104 GpVNMGLDKDEVER-RVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPR-GQETLMEIL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 779793995 174 DVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELLKGNAAASSLL 228
Cdd:PRK13647 182 DRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIVEQAGL 236
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
6-212 |
7.99e-23 |
|
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: 91.84 E-value: 7.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 6 DVTWLYQHLPMRFTLSVLQ--------GERIAVLGPSGAGKSTLLNLVAGFLQP--VSGSIVIDNQDHTHTPPAKRpVSM 75
Cdd:cd03213 8 NLTVTVKSSPSKSGKQLLKnvsgkakpGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDKRSFRKI-IGY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 76 LFQENNLFTHLTVRQNIalgmhpglrlndaqrhkleEIAAQM-GIagfidrlpgelSGGQRQRVALARCLVREQPMLLLD 154
Cdd:cd03213 87 VPQDDILHPTLTVRETL-------------------MFAAKLrGL-----------SGGERKRVSIALELVSNPSLLFLD 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 779793995 155 EPFSALDPALRQEMLTLVQDVCQrQQLTMLMVSHSiedaariaPRS---------VVIAEGRIVWDG 212
Cdd:cd03213 137 EPTSGLDSSSALQVMSLLRRLAD-TGRTIICSIHQ--------PSSeifelfdklLLLSQGRVIYFG 194
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
19-212 |
1.19e-22 |
|
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: 91.95 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQP---VSGSIVIDNQD-HTHTppAKRPVSMLFQENNLFTHLTVRQNIAL 94
Cdd:cd03234 27 SLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPrKPDQ--FQKCVAYVRQDDILLPGLTVRETLTY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 95 GMHPGLR--LNDAQRHKLEEIAA--QMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLT 170
Cdd:cd03234 105 TAILRLPrkSSDAIRKKRVEDVLlrDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVS 184
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 779793995 171 LVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDG 212
Cdd:cd03234 185 TLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-218 |
1.25e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 92.80 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQD--------HTHTPPAKRPVSMLFQENNLFTHLTVRQ 90
Cdd:PRK14246 30 TIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVlyfgkdifQIDAIKLRKEVGMVFQQPNPFPHLSIYD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 91 NIALGMHP-GLRLNDAQRHKLEEIAAQMGIAGFI-DRL---PGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALR 165
Cdd:PRK14246 110 NIAYPLKShGIKEKREIKKIVEECLRKVGLWKEVyDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNS 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 779793995 166 QEMLTLVQDVcqRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELL 218
Cdd:PRK14246 190 QAIEKLITEL--KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIF 240
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-217 |
2.34e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 95.16 E-value: 2.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 16 MRFTLSvlQGERIAVLGPSGAGKST----LLNLVAGflqpvSGSIVIDNQD-HTHTP----PAKRPVSMLFQENN--LFT 84
Cdd:PRK15134 305 ISFTLR--PGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQPlHNLNRrqllPVRHRIQVVFQDPNssLNP 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 85 HLTVRQNIALGM---HPglRLNDAQRHklEEIAAQMGIAGfID-----RLPGELSGGQRQRVALARCLVREQPMLLLDEP 156
Cdd:PRK15134 378 RLNVLQIIEEGLrvhQP--TLSAAQRE--QQVIAVMEEVG-LDpetrhRYPAEFSGGQRQRIAIARALILKPSLIILDEP 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 779793995 157 FSALDPALRQEMLTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEEL 217
Cdd:PRK15134 453 TSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERV 513
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-217 |
2.98e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 94.47 E-value: 2.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDH---THTPPAKRPVSMLFQENNLFTHLTVRQNIALG 95
Cdd:PRK09700 25 NLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYnklDHKLAAQLGIGIIYQELSVIDELTVLENLYIG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 96 MHP-----GLRLND--AQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPAlRQEM 168
Cdd:PRK09700 105 RHLtkkvcGVNIIDwrEMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNK-EVDY 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 779793995 169 LTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEEL 217
Cdd:PRK09700 184 LFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
17-212 |
3.11e-22 |
|
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: 95.08 E-value: 3.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 17 RFTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQD-HTHTPPAKRPVSMLFQENNLFTHLTVRQNIALG 95
Cdd:TIGR01257 948 RLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDiETNLDAVRQSLGMCPQHNILFHHLTVAEHILFY 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 96 MHPGLRLNDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVqdV 175
Cdd:TIGR01257 1028 AQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--L 1105
|
170 180 190
....*....|....*....|....*....|....*..
gi 779793995 176 CQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDG 212
Cdd:TIGR01257 1106 KYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
19-219 |
4.42e-22 |
|
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: 94.34 E-value: 4.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAK--RPVSMLFQENNLFTHlTVRQNIAlgm 96
Cdd:TIGR01842 338 SFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfgKHIGYLPQDVELFPG-TVAENIA--- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 97 hpglRLND-AQRHKLEEIAAQMGIAGFIDRLP-----------GELSGGQRQRVALARCLVREQPMLLLDEPFSALDPAL 164
Cdd:TIGR01842 414 ----RFGEnADPEKIIEAAKLAGVHELILRLPdgydtvigpggATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEG 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 779793995 165 RQEMLTLVQDVcQRQQLTMLMVSHSIEdAARIAPRSVVIAEGRIVWDGVTEELLK 219
Cdd:TIGR01842 490 EQALANAIKAL-KARGITVVVITHRPS-LLGCVDKILVLQDGRIARFGERDEVLA 542
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
25-236 |
4.75e-22 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 94.34 E-value: 4.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 25 GERIAVLGPSGAGKSTLLNLVAGFLQP---VSGSIVIDNqdHTHTPPAKRPVSMLFQENNLFT-HLTVRQNIALGMHpgL 100
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNG--MPIDAKEMRAISAYVQQDDLFIpTLTVREHLMFQAH--L 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 101 RL-----NDAQRHKLEEIAAQMG-------IAGFIDRLPGeLSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEM 168
Cdd:TIGR00955 127 RMprrvtKKEKRERVDEVLQALGlrkcantRIGVPGRVKG-LSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSV 205
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 779793995 169 LTLVQDVCQRQQlTMLMVSHSiedaariaPRS---------VVIAEGRIVWDGVTEELLKgnaaASSLLGISAPPLY 236
Cdd:TIGR00955 206 VQVLKGLAQKGK-TIICTIHQ--------PSSelfelfdkiILMAEGRVAYLGSPDQAVP----FFSDLGHPCPENY 269
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
18-219 |
4.88e-22 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 90.76 E-value: 4.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 18 FTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLqPVSGSIVIDNQDHTHTPPAK--RPVSMLFQENNLFTHLTVRQNIALG 95
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAElaRHRAYLSQQQTPPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 96 MHPGLRLnDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQP-------MLLLDEPFSALDPALRQEM 168
Cdd:PRK03695 94 QPDKTRT-EAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWPdinpagqLLLLDEPMNSLDVAQQAAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 779793995 169 LTLVQDVCQrQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELLK 219
Cdd:PRK03695 173 DRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLT 222
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
12-212 |
1.15e-21 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 89.38 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 12 QHLPMRFTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNqdHTHTPPAKRPVSMLFQENNLFTHLTVRQN 91
Cdd:TIGR03740 13 QTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDG--HPWTRKDLHKIGSLIESPPLYENLTAREN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 92 iaLGMHPGLRLNDAQRhkLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTL 171
Cdd:TIGR03740 91 --LKVHTTLLGLPDSR--IDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLDPIGIQELREL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 779793995 172 VQDVCQrQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDG 212
Cdd:TIGR03740 167 IRSFPE-QGITVILSSHILSEVQQLADHIGIISEGVLGYQG 206
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
18-202 |
1.35e-21 |
|
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: 89.77 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 18 FTLSVLQG-----ERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPpakrpvsmlfQENNLFTHLTVRQNI 92
Cdd:cd03237 13 FTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKP----------QYIKADYEGTVRDLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 93 A-----LGMHPGLRlndaqrhklEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQE 167
Cdd:cd03237 83 SsitkdFYTHPYFK---------TEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLM 153
|
170 180 190
....*....|....*....|....*....|....*
gi 779793995 168 MLTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVV 202
Cdd:cd03237 154 ASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
18-207 |
1.37e-21 |
|
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: 89.42 E-value: 1.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 18 FTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDhthtppakRPVSMlfqennlfTHLTVRQNIAL--- 94
Cdd:COG4778 30 VSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDG--------GWVDL--------AQASPREILALrrr 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 95 --G------------------MHPGLRLN---DAQRHKLEEIAAQMGIAgfiDRL----PGELSGGQRQRVALARCLVRE 147
Cdd:COG4778 94 tiGyvsqflrviprvsaldvvAEPLLERGvdrEEARARARELLARLNLP---ERLwdlpPATFSGGEQQRVNIARGFIAD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 148 QPMLLLDEPFSALDPALRQEMLTLVQDvCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGR 207
Cdd:COG4778 171 PPLLLLDEPTASLDAANRAVVVELIEE-AKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-217 |
1.94e-21 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 90.92 E-value: 1.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAKR-----PVSMLFQE--NNLFTHLTVRQN 91
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravrsDIQMIFQDplASLNPRMTIGEI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 92 IALGM---HPGLRlNDAQRHKLEEIAAQMGI-AGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQE 167
Cdd:PRK15079 121 IAEPLrtyHPKLS-RQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQ 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 779793995 168 MLTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEEL 217
Cdd:PRK15079 200 VVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 249
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
25-218 |
3.41e-21 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 88.83 E-value: 3.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 25 GERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAKRPVS---MLFQENNLFthltVRQNIALGMHP--- 98
Cdd:PRK11701 32 GEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEAerrRLLRTEWGF----VHQHPRDGLRMqvs 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 99 -----GLRLNDA-QRH--KLEEIAAQ----MGI-AGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALR 165
Cdd:PRK11701 108 aggniGERLMAVgARHygDIRATAGDwlerVEIdAARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQ 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 779793995 166 QEMLTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELL 218
Cdd:PRK11701 188 ARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVL 240
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
19-161 |
3.61e-21 |
|
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: 91.54 E-value: 3.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDnqdhthtPPAKrpVSMLFQENNLFTHLTVRQNIALGMHP 98
Cdd:TIGR03719 25 SLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ-------PGIK--VGYLPQEPQLDPTKTVRENVEEGVAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 99 GL----RLN---------DAQRHKL--------EEIAA--------QMGIAGFIDRLP------GELSGGQRQRVALARC 143
Cdd:TIGR03719 96 IKdaldRFNeisakyaepDADFDKLaaeqaelqEIIDAadawdldsQLEIAMDALRCPpwdadvTKLSGGERRRVALCRL 175
|
170
....*....|....*...
gi 779793995 144 LVREQPMLLLDEPFSALD 161
Cdd:TIGR03719 176 LLSKPDMLLLDEPTNHLD 193
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
10-161 |
5.57e-21 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 87.17 E-value: 5.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 10 LYQHLpmrfTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAkrpvsmlFQENNLF------ 83
Cdd:PRK13538 16 LFSGL----SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE-------YHQDLLYlghqpg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 84 --THLTVRQN--IALGMHpglrlNDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSA 159
Cdd:PRK13538 85 ikTELTALENlrFYQRLH-----GPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTA 159
|
..
gi 779793995 160 LD 161
Cdd:PRK13538 160 ID 161
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
12-218 |
7.54e-21 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 88.31 E-value: 7.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 12 QHL----PMRFTLSvlQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAKRP--VSMLFQENNlfTH 85
Cdd:PRK15112 24 QTVeavkPLSFTLR--EGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSqrIRMIFQDPS--TS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 86 LTVRQNIALGMHPGLRLN-----DAQRHKLEEIAAQMGI-AGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSA 159
Cdd:PRK15112 100 LNPRQRISQILDFPLRLNtdlepEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALAS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 779793995 160 LDPALRQEMLTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELL 218
Cdd:PRK15112 180 LDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVL 238
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-219 |
8.45e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 89.12 E-value: 8.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 2 LKLTDVTWLYQHLPM--RFTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSI-VIDNQDHTHTPPAKRPVSMLFQ 78
Cdd:PRK13536 42 IDLAGVSKSYGDKAVvnGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItVLGVPVPARARLARARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 79 ENNLFTHLTVRQNIAL-----GMHPglRLNDAQRHKLEEIAAQMGIAgfiDRLPGELSGGQRQRVALARCLVREQPMLLL 153
Cdd:PRK13536 122 FDNLDLEFTVRENLLVfgryfGMST--REIEAVIPSLLEFARLESKA---DARVSDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 779793995 154 DEPFSALDPALRQEMLTLVQDVCQRQQlTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELLK 219
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALID 261
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
19-219 |
1.58e-20 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 87.57 E-value: 1.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQP--------VSGSIVIDNQDHTHTPPAK--RPVSMLFQENNLFTHLTV 88
Cdd:PRK13547 21 SLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGggaprgarVTGDVTLNGEPLAAIDAPRlaRLRAVLPQAAQPAFAFSA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 89 RQNIALGMHPGLRLNDAQRHKLEEIA----AQMGIAGFIDRLPGELSGGQRQRVALARCLVREQP---------MLLLDE 155
Cdd:PRK13547 101 REIVLLGRYPHARRAGALTHRDGEIAwqalALAGATALVGRDVTTLSGGELARVQFARVLAQLWPphdaaqpprYLLLDE 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 779793995 156 PFSALDPALRQEMLTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELLK 219
Cdd:PRK13547 181 PTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLT 244
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-208 |
5.44e-20 |
|
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: 84.02 E-value: 5.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 1 MLKLTDVTWLYQHLPmrFTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPA---KRPVSML- 76
Cdd:cd03215 4 VLEVRGLSVKGAVRD--VSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRdaiRAGIAYVp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 77 --FQENNLFTHLTVRQNIALGMHpglrlndaqrhkleeiaaqmgiagfidrlpgeLSGGQRQRVALARCLVREQPMLLLD 154
Cdd:cd03215 82 edRKREGLVLDLSVAENIALSSL--------------------------------LSGGNQQKVVLARWLARDPRVLILD 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 779793995 155 EPFSALDPALRQEMLTLVQDvCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRI 208
Cdd:cd03215 130 EPTRGVDVGAKAEIYRLIRE-LADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
19-161 |
5.68e-20 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 88.25 E-value: 5.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVidnqdhtHTPPAKrpVSMLFQENNLFTHLTVRQNIALGMHP 98
Cdd:PRK11819 27 SLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEAR-------PAPGIK--VGYLPQEPQLDPEKTVRENVEEGVAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 99 GLRLNDaqrhKLEEIAAQMG--IAGF-------------ID------------------RLP------GELSGGQRQRVA 139
Cdd:PRK11819 98 VKAALD----RFNEIYAAYAepDADFdalaaeqgelqeiIDaadawdldsqleiamdalRCPpwdakvTKLSGGERRRVA 173
|
170 180
....*....|....*....|..
gi 779793995 140 LARCLVREQPMLLLDEPFSALD 161
Cdd:PRK11819 174 LCRLLLEKPDMLLLDEPTNHLD 195
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
20-195 |
1.95e-19 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 83.67 E-value: 1.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 20 LSVLQG--------ERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAKRP------VSMLFQENNLFTH 85
Cdd:PRK10584 23 LSILTGvelvvkrgETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAklrakhVGFVFQSFMLIPT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 86 LTVRQNIALgmhPGLRLNDAQRHKLE---EIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDP 162
Cdd:PRK10584 103 LNALENVEL---PALLRGESSRQSRNgakALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR 179
|
170 180 190
....*....|....*....|....*....|...
gi 779793995 163 ALRQEMLTLVQDVCQRQQLTMLMVSHSIEDAAR 195
Cdd:PRK10584 180 QTGDKIADLLFSLNREHGTTLILVTHDLQLAAR 212
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
20-207 |
2.62e-19 |
|
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: 82.52 E-value: 2.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 20 LSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIdnqdhthtppakrPVSMLF--QENNLFThLTVRQNIALGmH 97
Cdd:cd03250 26 LEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV-------------PGSIAYvsQEPWIQN-GTIRENILFG-K 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 98 PglrlNDAQRHK-------LEEIAAQM--GIAGFIdrlpGE----LSGGQRQRVALARCLVREQPMLLLDEPFSALDPAL 164
Cdd:cd03250 91 P----FDEERYEkvikacaLEPDLEILpdGDLTEI----GEkginLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 779793995 165 RQemlTLVQDvCQRQQL----TMLMVSHSIE---DAARIaprsVVIAEGR 207
Cdd:cd03250 163 GR---HIFEN-CILGLLlnnkTRILVTHQLQllpHADQI----VVLDNGR 204
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
18-188 |
3.55e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 86.01 E-value: 3.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 18 FTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIdnqdhthtPPAKRpvsMLF--QENNLFTHlTVRQNIALG 95
Cdd:COG4178 382 LSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR--------PAGAR---VLFlpQRPYLPLG-TLREALLYP 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 96 mHPGLRLNDAQrhkLEEIAAQMGIAGFIDRL------PGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEML 169
Cdd:COG4178 450 -ATAEAFSDAE---LREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALY 525
|
170
....*....|....*....
gi 779793995 170 TLVQDvcQRQQLTMLMVSH 188
Cdd:COG4178 526 QLLRE--ELPGTTVISVGH 542
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
19-197 |
6.54e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 82.91 E-value: 6.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLL-------NLVAGFlqPVSGSIVIDNQD--HTHTPPA--KRPVSMLFQENNLFTHlT 87
Cdd:PRK14243 30 WLDIPKNQITAFIGPSGCGKSTILrcfnrlnDLIPGF--RVEGKVTFHGKNlyAPDVDPVevRRRIGMVFQKPNPFPK-S 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 88 VRQNIALGMhpglRLNDAQRHKLEEIAAQMGIAGFIDRLPGEL-------SGGQRQRVALARCLVREQPMLLLDEPFSAL 160
Cdd:PRK14243 107 IYDNIAYGA----RINGYKGDMDELVERSLRQAALWDEVKDKLkqsglslSGGQQQRLCIARAIAVQPEVILMDEPCSAL 182
|
170 180 190
....*....|....*....|....*....|....*....
gi 779793995 161 DP--ALRQEmlTLVQDVcqRQQLTMLMVSHSIEDAARIA 197
Cdd:PRK14243 183 DPisTLRIE--ELMHEL--KEQYTIIIVTHNMQQAARVS 217
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-209 |
1.73e-18 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 83.72 E-value: 1.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 20 LSVLQGERIAVLGPSGAGKSTLLNLVAGfLQP---VSGSIVIDNQD--HTHTPPAKRP-VSMLFQENNLFTHLTVRQNIA 93
Cdd:TIGR02633 22 LEVRPGECVGLCGENGAGKSTLMKILSG-VYPhgtWDGEIYWSGSPlkASNIRDTERAgIVIIHQELTLVPELSVAENIF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 94 LG---MHPGLRLN-DAQRHKLEEIAAQMGIAGFIDRLP-GELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEM 168
Cdd:TIGR02633 101 LGneiTLPGGRMAyNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEIL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 779793995 169 LTLVQDVcQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIV 209
Cdd:TIGR02633 181 LDIIRDL-KAHGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
20-209 |
2.10e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 83.53 E-value: 2.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 20 LSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAK------------RpvsmlfQENNLFTHLT 87
Cdd:COG1129 273 FSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairagiayvpedR------KGEGLVLDLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 88 VRQNIALG----MHPGLRLNDAQRHKL-EEIAAQMGI-AGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALD 161
Cdd:COG1129 347 IRENITLAsldrLSRGGLLDRRRERALaEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGID 426
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 779793995 162 PALRQEMLTLVQDVCqRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIV 209
Cdd:COG1129 427 VGAKAEIYRLIRELA-AEGKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
19-209 |
3.52e-18 |
|
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: 79.76 E-value: 3.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTP--PAKRPVSMLFQENNLFTHlTVRQNialgm 96
Cdd:cd03369 28 SFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPleDLRSSLTIIPQDPTLFSG-TIRSN----- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 97 hpglrLNDAQRHKLEEIAAQMGIAGfidrlPGE-LSGGQRQRVALARCLVREQPMLLLDEPFSALD---PALRQEML-TL 171
Cdd:cd03369 102 -----LDPFDEYSDEEIYGALRVSE-----GGLnLSQGQRQLLCLARALLKRPRVLVLDEATASIDyatDALIQKTIrEE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 779793995 172 VQDVcqrqqlTMLMVSH---SIEDAARIaprsVVIAEGRIV 209
Cdd:cd03369 172 FTNS------TILTIAHrlrTIIDYDKI----LVMDAGEVK 202
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
19-207 |
1.05e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 81.51 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGfLQPV---SGSIVIDNQD---HTHTPPAKRPVSMLFQENNLFTHLTVRQNI 92
Cdd:PRK13549 25 SLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFEGEElqaSNIRDTERAGIAIIHQELALVKELSVLENI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 93 ALG--MHPGLRLN-DAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEML 169
Cdd:PRK13549 104 FLGneITPGGIMDyDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLL 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 779793995 170 TLVQDVcQRQQLTMLMVSHSIEDAARIAPRSVVIAEGR 207
Cdd:PRK13549 184 DIIRDL-KAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
20-219 |
1.45e-17 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 78.96 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 20 LSVLQGERIAVLGPSGAGKSTLLNLVAGF--LQPVSGSIVIDNQDHTHTPP---AKRPVSMLFQ---EnnlFTHLTVRQ- 90
Cdd:COG0396 21 LTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPderARAGIFLAFQypvE---IPGVSVSNf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 91 -NIALGMHPGLRLNDAQRHK-LEEIAAQMGI-AGFIDR-LPGELSGGQRQRVALARCLVREQPMLLLDEPFSALD-PALR 165
Cdd:COG0396 98 lRTALNARRGEELSAREFLKlLKEKMKELGLdEDFLDRyVNEGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDiDALR 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 779793995 166 qemltLVQDVCQR---QQLTMLMVSHSiedaAR----IAPRSV-VIAEGRIVWDGvTEELLK 219
Cdd:COG0396 178 -----IVAEGVNKlrsPDRGILIITHY----QRildyIKPDFVhVLVDGRIVKSG-GKELAL 229
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
25-239 |
3.66e-17 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 79.92 E-value: 3.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 25 GERIAVLGPSGAGKSTLLNLVAGFLQP--VSGSIVIDNQDHTHtpPAKRPVSMLFQENNLFTHLTVRQNI---ALGMHPG 99
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGnnFTGTILANNRKPTK--QILKRTGFVTQDDILYPHLTVRETLvfcSLLRLPK 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 100 LRLNDAQRHKLEEIAAQMGIAGFIDRLPGE-----LSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQD 174
Cdd:PLN03211 172 SLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGS 251
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 779793995 175 VCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGvteellKGNAAASSLLGISAPPLYSLD 239
Cdd:PLN03211 252 LAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFG------KGSDAMAYFESVGFSPSFPMN 310
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
19-217 |
6.40e-17 |
|
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: 79.08 E-value: 6.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGF--LQPVSGSIV---------------------------------ID--NQ 61
Cdd:TIGR03269 20 SFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpskvgepcpvcggtlepeeVDfwNL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 62 DHTHTPPAKRPVSMLFQEN-NLFTHLTVRQNIALGMHP-GLRLNDAQRHKLEEIAaQMGIAGFIDRLPGELSGGQRQRVA 139
Cdd:TIGR03269 100 SDKLRRRIRKRIAIMLQRTfALYGDDTVLDNVLEALEEiGYEGKEAVGRAVDLIE-MVQLSHRITHIARDLSGGEKQRVV 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 779793995 140 LARCLVREQPMLLLDEPFSALDPALRQEMLTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEEL 217
Cdd:TIGR03269 179 LARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIKEEGTPDEV 256
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
7-215 |
2.54e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 76.07 E-value: 2.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 7 VTWLYQHLPMR-FTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVI----DNQDHTHTPPAKRPVSmlfQENN 81
Cdd:PRK15056 14 VTWRNGHTALRdASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISIlgqpTRQALQKNLVAYVPQS---EEVD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 82 LFTHLTVRQNIALGM--HPGL--RLNDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPF 157
Cdd:PRK15056 91 WSFPVLVEDVVMMGRygHMGWlrRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPF 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 779793995 158 SALDPALRQEMLTLVQDVcQRQQLTMLMVSHSIEDAARIAPRSVVIaEGRIVWDGVTE 215
Cdd:PRK15056 171 TGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYTVMV-KGTVLASGPTE 226
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
18-188 |
3.63e-16 |
|
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: 72.87 E-value: 3.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 18 FTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIvidnqdhthtppakrpvsmlfqennlfthltvrqnialgmh 97
Cdd:cd03221 19 ISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV----------------------------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 98 pglrlndaQRHKLEEIA--AQmgiagfidrlpgeLSGGQRQRVALARCLVREQPMLLLDEPFSALDPalrqEMLTLVQDV 175
Cdd:cd03221 58 --------TWGSTVKIGyfEQ-------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDL----ESIEALEEA 112
|
170
....*....|...
gi 779793995 176 CQRQQLTMLMVSH 188
Cdd:cd03221 113 LKEYPGTVILVSH 125
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-209 |
3.72e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 76.87 E-value: 3.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 20 LSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDH--THTPPA-KRPVSMLFQENNLFTHLTVRQNIALGM 96
Cdd:PRK11288 25 FDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfASTTAAlAAGVAIIYQELHLVPEMTVAENLYLGQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 97 HPG----LRLNDAQRHKLEEIAAqMGIAgfID-RLP-GELSGGQRQRVALARCLVREQPMLLLDEPFSALDpALRQEMLT 170
Cdd:PRK11288 105 LPHkggiVNRRLLNYEAREQLEH-LGVD--IDpDTPlKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLS-AREIEQLF 180
|
170 180 190
....*....|....*....|....*....|....*....
gi 779793995 171 LVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIV 209
Cdd:PRK11288 181 RVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYV 219
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
15-172 |
5.01e-16 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 74.11 E-value: 5.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 15 PMRFTLSVlqGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQdHTHTPPAKRPVSMLFQENNLFTHLTVRQNiaL 94
Cdd:PRK13543 29 PLDFHVDA--GEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK-TATRGDRSRFMAYLGHLPGLKADLSTLEN--L 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 779793995 95 GMHPGLRLNDAQRHKLEEIAAqMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPalrqEMLTLV 172
Cdd:PRK13543 104 HFLCGLHGRRAKQMPGSALAI-VGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL----EGITLV 176
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-240 |
5.13e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 75.04 E-value: 5.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 1 MLKLTDVTWLYQHLP------MRFTLSVLQGeriaVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPA----K 70
Cdd:PRK13638 1 MLATSDLWFRYQDEPvlkglnLDFSLSPVTG----LVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGllalR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 71 RPVSMLFQ--ENNLFtHLTVRQNIALGMH--------------PGLRLNDAQRHKLEEIAAqmgiagfidrlpgeLSGGQ 134
Cdd:PRK13638 77 QQVATVFQdpEQQIF-YTDIDSDIAFSLRnlgvpeaeitrrvdEALTLVDAQHFRHQPIQC--------------LSHGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 135 RQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQDVCQrQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVT 214
Cdd:PRK13638 142 KKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVA-QGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAP 220
|
250 260
....*....|....*....|....*.
gi 779793995 215 EELLkGNAAASSLLGISAPPLYSLDS 240
Cdd:PRK13638 221 GEVF-ACTEAMEQAGLTQPWLVKLHT 245
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
25-209 |
6.34e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 76.43 E-value: 6.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 25 GERIAVLGPSGAGKST----LLNLVagflQPVSGSIV-----IDNQDHTHTPPAKRPVSMLFQENnlFTHLTVRQNIALG 95
Cdd:PRK10261 350 GETLSLVGESGSGKSTtgraLLRLV----ESQGGEIIfngqrIDTLSPGKLQALRRDIQFIFQDP--YASLDPRQTVGDS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 96 -MHP----GLRLNDAQRHKLEEIAAQMGI-AGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEML 169
Cdd:PRK10261 424 iMEPlrvhGLLPGKAAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQII 503
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 779793995 170 TLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIV 209
Cdd:PRK10261 504 NLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
24-161 |
7.00e-16 |
|
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: 76.36 E-value: 7.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 24 QGERIAVLGPSGAGKSTLLNLVAGFLQPvsgsividNQDHTHTPPAKRPVSMLFQENNLFTHL------TVR-----QNI 92
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKP--------NLGDYDEEPSWDEVLKRFRGTELQDYFkklangEIKvahkpQYV 169
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 779793995 93 AL--GMHPG-----LRLNDaQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALD 161
Cdd:COG1245 170 DLipKVFKGtvrelLEKVD-ERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-234 |
8.41e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 76.17 E-value: 8.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 1 MLKLTDVTWLYQ-HLP---MRFTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTH--TPPAKRPVS 74
Cdd:PLN03232 1234 SIKFEDVHLRYRpGLPpvlHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfgLTDLRRVLS 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 75 MLFQENNLFTHlTVRQNIalgmHPGLRLNDAQrhkLEEIAAQMGIAGFIDRLP----------GE-LSGGQRQRVALARC 143
Cdd:PLN03232 1314 IIPQSPVLFSG-TVRFNI----DPFSEHNDAD---LWEALERAHIKDVIDRNPfgldaevsegGEnFSVGQRQLLSLARA 1385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 144 LVREQPMLLLDEPFSALDpaLRQEmlTLVQDVCQRQ--QLTMLMVSH---SIEDAARIaprsVVIAEGRIVWDGVTEELL 218
Cdd:PLN03232 1386 LLRRSKILVLDEATASVD--VRTD--SLIQRTIREEfkSCTMLVIAHrlnTIIDCDKI----LVLSSGQVLEYDSPQELL 1457
|
250
....*....|....*.
gi 779793995 219 KGNAAASSLLGISAPP 234
Cdd:PLN03232 1458 SRDTSAFFRMVHSTGP 1473
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
18-188 |
8.58e-16 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 76.14 E-value: 8.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 18 FTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIvidnqdHTHTppaKRPVSMLFQ-ENNLFTHLTVRQNIALGM 96
Cdd:PRK11147 338 FSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI------HCGT---KLEVAYFDQhRAELDPEKTVMDNLAEGK 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 97 HPgLRLNDAQRHKLeeiaaqmgiaGFID---------RLP-GELSGGQRQRVALARCLVREQPMLLLDEPFSALDpalrQ 166
Cdd:PRK11147 409 QE-VMVNGRPRHVL----------GYLQdflfhpkraMTPvKALSGGERNRLLLARLFLKPSNLLILDEPTNDLD----V 473
|
170 180
....*....|....*....|..
gi 779793995 167 EMLTLVQDVCQRQQLTMLMVSH 188
Cdd:PRK11147 474 ETLELLEELLDSYQGTVLLVSH 495
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-218 |
2.29e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 74.74 E-value: 2.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQ--PV---SGSIVIDNQDHTHTPPAK------RPVSMLFQE-----NNL 82
Cdd:PRK15134 29 SLQIEAGETLALVGESGSGKSVTALSILRLLPspPVvypSGDIRFHGESLLHASEQTlrgvrgNKIAMIFQEpmvslNPL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 83 FThLTVRQNIALGMHPGLRlNDAQRHKLEEIAAQMGIAGFIDRL---PGELSGGQRQRVALARCLVREQPMLLLDEPFSA 159
Cdd:PRK15134 109 HT-LEKQLYEVLSLHRGMR-REAARGEILNCLDRVGIRQAAKRLtdyPHQLSGGERQRVMIAMALLTRPELLIADEPTTA 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 779793995 160 LDPALRQEMLTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELL 218
Cdd:PRK15134 187 LDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLF 245
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
17-219 |
2.44e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 73.62 E-value: 2.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 17 RFTLSVLQGERIAVLGPSGAGKSTLLNLVAGFL----QPVSGSIVIDNQDHTHTPPAKR------PVSMLFQE--NNLFT 84
Cdd:PRK11022 25 RISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDLQRISEKERrnlvgaEVAMIFQDpmTSLNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 85 HLTVRQNI--ALGMHPGLRlNDAQRHKLEEIAAQMGIAGFIDRL---PGELSGGQRQRVALARCLVREQPMLLLDEPFSA 159
Cdd:PRK11022 105 CYTVGFQImeAIKVHQGGN-KKTRRQRAIDLLNQVGIPDPASRLdvyPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTA 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 160 LDPALRQEMLTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELLK 219
Cdd:PRK11022 184 LDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFR 243
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
19-208 |
2.47e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 74.70 E-value: 2.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAKRPVSMLF------QENNLFTHLTVRQNI 92
Cdd:PRK15439 283 SLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVylpedrQSSGLYLDAPLAWNV 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 93 ALGMH--PGLRLNDAQ-RHKLEEIAAQMGIA-GFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEM 168
Cdd:PRK15439 363 CALTHnrRGFWIKPAReNAVLERYRRALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDI 442
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 779793995 169 LTLVQDVCQrQQLTMLMVSHSIEDAARIAPRSVVIAEGRI 208
Cdd:PRK15439 443 YQLIRSIAA-QNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-217 |
3.61e-15 |
|
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: 74.66 E-value: 3.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 1 MLKLTDVTWLYQHLPM----RFTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQD-HTHTPPAKRPVSM 75
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSSpavdRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTNISDVHQNMGY 2016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 76 LFQENNLFTHLTVRQNIALGMhpglRLNDAQRHKLEEIA----AQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPML 151
Cdd:TIGR01257 2017 CPQFDAIDDLLTGREHLYLYA----RLRGVPAEEIEKVAnwsiQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLV 2092
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 779793995 152 LLDEPFSALDPALRQEMLTLVQDVCqRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEEL 217
Cdd:TIGR01257 2093 LLDEPTTGMDPQARRMLWNTIVSII-REGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
18-161 |
3.83e-15 |
|
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: 74.05 E-value: 3.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 18 FTLSV-----LQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIvidnqdhthtpPAKRPVSMLFQENNLFTHLTVRQNi 92
Cdd:COG1245 354 FSLEVeggeiREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-----------DEDLKISYKPQYISPDYDGTVEEF- 421
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 779793995 93 aLGMHPGLRLNDAQRHklEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALD 161
Cdd:COG1245 422 -LRSANTDDFGSSYYK--TEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
18-209 |
4.32e-15 |
|
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: 71.02 E-value: 4.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 18 FTLSVLQGERIAVLGPSGAGKSTLLNLVAGF--LQPVSGSIVIDNQDHTHTPP---AKRPVSMLFQENNLFthltvrqni 92
Cdd:cd03217 19 VNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPeerARLGIFLAFQYPPEI--------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 93 algmhPGLRLNDAQRHKLEeiaaqmgiaGFidrlpgelSGGQRQRVALARCLVREQPMLLLDEPFSALD-PALRqemltL 171
Cdd:cd03217 90 -----PGVKNADFLRYVNE---------GF--------SGGEKKRNEILQLLLLEPDLAILDEPDSGLDiDALR-----L 142
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 779793995 172 VQDVCQR---QQLTMLMVSHSIEDAARIAPRSV-VIAEGRIV 209
Cdd:cd03217 143 VAEVINKlreEGKSVLIITHYQRLLDYIKPDRVhVLYDGRIV 184
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-188 |
5.29e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 71.13 E-value: 5.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 1 MLKLTDVTWLYQHLPM--RFTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPA-KRPVSMLF 77
Cdd:PRK13540 1 MLDVIELDFDYHDQPLlqQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTyQKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 78 QENNLFTHLTVRQNIALGMHpglrlNDAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPF 157
Cdd:PRK13540 81 HRSGINPYLTLRENCLYDIH-----FSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170 180 190
....*....|....*....|....*....|.
gi 779793995 158 SALDPALRQEMLTLVQDvCQRQQLTMLMVSH 188
Cdd:PRK13540 156 VALDELSLLTIITKIQE-HRAKGGAVLLTSH 185
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-218 |
9.74e-15 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 72.74 E-value: 9.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 1 MLKLTDVTW-LYQHLPMRFT-LSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAK--RPVSML 76
Cdd:PRK10938 3 SLQISQGTFrLSDTKTLQLPsLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQlqKLVSDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 77 FQENNLF--------THLTVRQNIALGMHpglrlnDAQRhkLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQ 148
Cdd:PRK10938 83 WQRNNTDmlspgeddTGRTTAEIIQDEVK------DPAR--CEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 149 PMLLLDEPFSALDPALRQEMLTLVQDVcQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELL 218
Cdd:PRK10938 155 DLLILDEPFDGLDVASRQQLAELLASL-HQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEIL 223
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
12-195 |
1.10e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 72.85 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 12 QHLPMRF---------TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSI-----VIDNQDHThtppAKRPVSMLF 77
Cdd:NF033858 270 RGLTMRFgdftavdhvSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwlfgqPVDAGDIA----TRRRVGYMS 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 78 QENNLFTHLTVRQNIALgmHPGL-RLNDAQRHK-LEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDE 155
Cdd:NF033858 346 QAFSLYGELTVRQNLEL--HARLfHLPAAEIAArVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDE 423
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 779793995 156 PFSALDPALRQEMLTLVQDVCQRQQLTMLMVSHSIEDAAR 195
Cdd:NF033858 424 PTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAER 463
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
19-191 |
1.76e-14 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 70.05 E-value: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPA------KRPVSMLFQENNLFtHLTVRQNI 92
Cdd:cd03290 21 NIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEatrsrnRYSVAYAAQKPWLL-NATVEENI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 93 ALGmHPglrlNDAQRHKLeeIAAQMGIAGFIDRLP-------GE----LSGGQRQRVALARCLVREQPMLLLDEPFSALD 161
Cdd:cd03290 100 TFG-SP----FNKQRYKA--VTDACSLQPDIDLLPfgdqteiGErginLSGGQRQRICVARALYQNTNIVFLDDPFSALD 172
|
170 180 190
....*....|....*....|....*....|.
gi 779793995 162 PALRQEMLTL-VQDVCQRQQLTMLMVSHSIE 191
Cdd:cd03290 173 IHLSDHLMQEgILKFLQDDKRTLVLVTHKLQ 203
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
18-161 |
1.78e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 72.15 E-value: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 18 FTLSVL-----QGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQdhthtppakrpVSMLFQENNLFTHLTVRQNi 92
Cdd:PRK13409 353 FSLEVEggeiyEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK-----------ISYKPQYIKPDYDGTVEDL- 420
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 779793995 93 aLGMHPGlRLNDAQrHKlEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALD 161
Cdd:PRK13409 421 -LRSITD-DLGSSY-YK-SEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
20-228 |
4.89e-14 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 69.50 E-value: 4.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 20 LSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIvidnqDHTHTPPAKRPVSMLFQEnnlfthlTVRQNIALGMHpg 99
Cdd:cd03291 58 LKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-----KHSGRISFSSQFSWIMPG-------TIKENIIFGVS-- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 100 lrlNDAQRHKLEEIAAQM--GIAGFIDR---LPGE----LSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLT 170
Cdd:cd03291 124 ---YDEYRYKSVVKACQLeeDITKFPEKdntVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFE 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 779793995 171 lvQDVCQ-RQQLTMLMVSHSIEDaARIAPRSVVIAEGRIVWDGVTEELLKGNAAASSLL 228
Cdd:cd03291 201 --SCVCKlMANKTRILVTSKMEH-LKKADKILILHEGSSYFYGTFSELQSLRPDFSSKL 256
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
16-218 |
5.33e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 70.51 E-value: 5.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 16 MRFTLSvlQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHT--PPAKRPVSMLFQENNLFTHlTVRQNIA 93
Cdd:PRK10789 334 VNFTLK--PGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLqlDSWRSRLAVVSQTPFLFSD-TVANNIA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 94 LGmHPglrlnDAQRHKLEEIAAQMGIAGFIDRLP-------GE----LSGGQRQRVALARCLVREQPMLLLDEPFSALDP 162
Cdd:PRK10789 411 LG-RP-----DATQQEIEHVARLASVHDDILRLPqgydtevGErgvmLSGGQKQRISIARALLLNAEILILDDALSAVDG 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 163 ALRQEMLtlvQDVCQ-RQQLTMLMVSH---SIEDAARIaprsVVIAEGRIVWDGVTEELL 218
Cdd:PRK10789 485 RTEHQIL---HNLRQwGEGRTVIISAHrlsALTEASEI----LVMQHGHIAQRGNHDQLA 537
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-188 |
5.83e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 70.39 E-value: 5.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 2 LKLTDVTWLYQHL-----PMRFTLSvlQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPA--KRPVS 74
Cdd:PRK10522 323 LELRNVTFAYQDNgfsvgPINLTIK--RGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEdyRKLFS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 75 MLFQENNLFTHLTVRQNIA------------LGMHPGLRLNDaqrHKLEEIaaqmgiagfidrlpgELSGGQRQRVALAR 142
Cdd:PRK10522 401 AVFTDFHLFDQLLGPEGKPanpalvekwlerLKMAHKLELED---GRISNL---------------KLSKGQKKRLALLL 462
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 779793995 143 CLVREQPMLLLDEPFSALDPALRQEMLTLVQDVCQRQQLTMLMVSH 188
Cdd:PRK10522 463 ALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISH 508
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
17-188 |
6.67e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 68.45 E-value: 6.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 17 RFTLSVLQGERIAVLGPSGAGKSTLLNLVAGFL--QPVSGSIVIDNQDhthtppakrpvsmLFQENNLFTHLTVRQNIAL 94
Cdd:COG2401 48 DLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQ-------------FGREASLIDAIGRKGDFKD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 95 GMhpglrlndaqrhkleEIAAQMGI--AGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLV 172
Cdd:COG2401 115 AV---------------ELLNAVGLsdAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNL 179
|
170
....*....|....*.
gi 779793995 173 QDVCQRQQLTMLMVSH 188
Cdd:COG2401 180 QKLARRAGITLVVATH 195
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-160 |
7.40e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 70.03 E-value: 7.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAKRP---VSMLFQENNLFTHLTVRQNIALG 95
Cdd:PRK10762 24 ALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQeagIGIIHQELNLIPQLTIAENIFLG 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 779793995 96 MHPGLRLNDAQRHKLEEIA----AQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSAL 160
Cdd:PRK10762 104 REFVNRFGRIDWKKMYAEAdkllARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDAL 172
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
20-217 |
2.24e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 67.42 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 20 LSVLQGERIAVLGPSGAGKSTLLNLVAGFLQP----VSGSIVIDNQDHTHTPPAKRPVSMLFQE-----NNLFT--HLTV 88
Cdd:PRK10418 24 LTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALRGRKIATIMQNprsafNPLHTmhTHAR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 89 RQNIALGMHPglrlNDAQ-RHKLEEIAAQmGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQE 167
Cdd:PRK10418 104 ETCLALGKPA----DDATlTAALEAVGLE-NAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQAR 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 779793995 168 MLTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEEL 217
Cdd:PRK10418 179 ILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
28-218 |
3.01e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 68.59 E-value: 3.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 28 IAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNqdhthtppakRPVSMLfqennlfTHLTVRQNIAL----------GMH 97
Cdd:PRK10790 370 VALVGHTGSGKSTLASLLMGYYPLTEGEIRLDG----------RPLSSL-------SHSVLRQGVAMvqqdpvvladTFL 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 98 PGLRL-NDAQRHKLEEIAAQMGIAGFIDRLP-------GE----LSGGQRQRVALARCLVREQPMLLLDEPFSALDPALR 165
Cdd:PRK10790 433 ANVTLgRDISEEQVWQALETVQLAELARSLPdglytplGEqgnnLSVGQKQLLALARVLVQTPQILILDEATANIDSGTE 512
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 779793995 166 QEMLTLVQDVcqRQQLTMLMVSH---SIEDAARIaprsVVIAEGRIVWDGVTEELL 218
Cdd:PRK10790 513 QAIQQALAAV--REHTTLVVIAHrlsTIVEADTI----LVLHRGQAVEQGTHQQLL 562
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
20-217 |
3.52e-13 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 67.84 E-value: 3.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 20 LSVLQGERIAVLGPSGAG--KSTLLNLVAGflqPVSG-------SIVIDNQDHTHTPPAKRPVSMLFQENnlfthLTVRQ 90
Cdd:NF000106 34 LDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGrrpwrf*TWCANRRALRRTIG*HRPVR*GRRES-----FSGRE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 91 NI-ALGMHPGLRLNDAqRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEML 169
Cdd:NF000106 106 NLyMIGR*LDLSRKDA-RARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVW 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 779793995 170 TLVQDVCqRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEEL 217
Cdd:NF000106 185 DEVRSMV-RDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-188 |
3.94e-13 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 66.62 E-value: 3.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 25 GERIAVLGPSGAGKSTLLNLVAGFLQPvsgsividNQDHTHTPPAKRPVSMLFQENNL---FTHLtVRQNIALGMHP--- 98
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKP--------NLGKFDDPPDWDEILDEFRGSELqnyFTKL-LEGDVKVIVKPqyv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 99 -----------GLRLNDA-QRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQ 166
Cdd:cd03236 97 dlipkavkgkvGELLKKKdERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRL 176
|
170 180
....*....|....*....|..
gi 779793995 167 EMLTLVQDVCQRQQlTMLMVSH 188
Cdd:cd03236 177 NAARLIRELAEDDN-YVLVVEH 197
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-233 |
4.00e-13 |
|
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: 68.43 E-value: 4.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIvidnqdHTHTPPAKRPVSMLFQENNLfthltvRQNIALGmHP 98
Cdd:TIGR00957 658 TFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV------HMKGSVAYVPQQAWIQNDSL------RENILFG-KA 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 99 glrLNDAQRHKLEEIAAQMGIagfIDRLPG-----------ELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQE 167
Cdd:TIGR00957 725 ---LNEKYYQQVLEACALLPD---LEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKH 798
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 168 ML-TLVQDVCQRQQLTMLMVSHSIEdaarIAPRS---VVIAEGRIVWDGVTEELLKGNAAASSLLGISAP 233
Cdd:TIGR00957 799 IFeHVIGPEGVLKNKTRILVTHGIS----YLPQVdviIVMSGGKISEMGSYQELLQRDGAFAEFLRTYAP 864
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
53-195 |
5.17e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 68.13 E-value: 5.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 53 SGSIVIDNQD--HTHTPPAKRPVSMLFQENNLFtHLTVRQNIALGMHpglrlnDAQRHKLEEIAAQMGIAGFIDRLPGE- 129
Cdd:PTZ00265 1276 SGKILLDGVDicDYNLKDLRNLFSIVSQEPMLF-NMSIYENIKFGKE------DATREDVKRACKFAAIDEFIESLPNKy 1348
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 779793995 130 ----------LSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQDVCQRQQLTMLMVSHSIEDAAR 195
Cdd:PTZ00265 1349 dtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR 1424
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
27-188 |
5.43e-13 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 67.96 E-value: 5.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 27 RIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVidnqdhthtPPAKRPVSMLFQENnlFTHLTVRQNIALGM---HPGlrln 103
Cdd:PLN03073 537 RIAMVGPNGIGKSTILKLISGELQPSSGTVF---------RSAKVRMAVFSQHH--VDGLDLSSNPLLYMmrcFPG---- 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 104 dAQRHKLEEIAAQMGIAGFIDRLPG-ELSGGQRQRVALARCLVREQPMLLLDEPFSALD----PALRQEMLTLvqdvcqr 178
Cdd:PLN03073 602 -VPEQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDldavEALIQGLVLF------- 673
|
170
....*....|
gi 779793995 179 qQLTMLMVSH 188
Cdd:PLN03073 674 -QGGVLMVSH 682
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
22-208 |
5.64e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 67.73 E-value: 5.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 22 VLQGERIAVLGPSGAGKSTLLNLVAG------------F-LQPVSGSIVIDNQDHTHTppakrpVSmlfqeNNLftHL-- 86
Cdd:PRK10938 283 VNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndltlFgRRRGSGETIWDIKKHIGY------VS-----SSL--HLdy 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 87 ----TVRQNIALGMHPGLRL----NDAQRHKLEEIAAQMGIAGFIDRLP-GELSGGQrQRVAL-ARCLVREQPMLLLDEP 156
Cdd:PRK10938 350 rvstSVRNVILSGFFDSIGIyqavSDRQQKLAQQWLDILGIDKRTADAPfHSLSWGQ-QRLALiVRALVKHPTLLILDEP 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 779793995 157 FSALDPALRQEMLTLVQDVCQRQQLTMLMVSHSIEDAAR-IAPRSVVIAEGRI 208
Cdd:PRK10938 429 LQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDAPAcITHRLEFVPDGDI 481
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
19-225 |
6.16e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 67.84 E-value: 6.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVI---DNQDHTHtppaKRPVS-----M---LfqENNLFTHLT 87
Cdd:NF033858 21 SLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVlggDMADARH----RRAVCpriayMpqgL--GKNLYPTLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 88 VRQNIAL-GmhpglRL---NDAQRH-KLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDP 162
Cdd:NF033858 95 VFENLDFfG-----RLfgqDAAERRrRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 779793995 163 ALRQEMLTLVQDVC-QRQQLTMLMVSHSIEDAARIApRSVVIAEGRIVWDGVTEELLKGNAAAS 225
Cdd:NF033858 170 LSRRQFWELIDRIRaERPGMSVLVATAYMEEAERFD-WLVAMDAGRVLATGTPAELLARTGADT 232
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-216 |
8.03e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.12 E-value: 8.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPP---AKRPVSMLFQ---ENNLFTHLTVRQNI 92
Cdd:PRK09700 283 SFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPldaVKKGMAYITEsrrDNGFFPNFSIAQNM 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 93 A------LGMHPGL----------RLNDAQRHKLEEIAAQmgiagfIDRLPGELSGGQRQRVALARCLVREQPMLLLDEP 156
Cdd:PRK09700 363 AisrslkDGGYKGAmglfhevdeqRTAENQRELLALKCHS------VNQNITELSGGNQQKVLISKWLCCCPEVIIFDEP 436
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 779793995 157 FSALDPALRQEMLTLVQDVCQrQQLTMLMVSHSIEDAARIAPRSVVIAEGRIV-----WDGVTEE 216
Cdd:PRK09700 437 TRGIDVGAKAEIYKVMRQLAD-DGKVILMVSSELPEIITVCDRIAVFCEGRLTqiltnRDDMSEE 500
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
18-217 |
8.76e-13 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 66.67 E-value: 8.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 18 FTLSvlQGERIAVLGPSGAGKSTLLNLVAGFLQP---VSGSIVIDNQDHTHTPPAK------RPVSMLFQE--NNLFTHL 86
Cdd:PRK09473 37 FSLR--AGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPEKElnklraEQISMIFQDpmTSLNPYM 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 87 TVRQNIA--LGMHPGL----------RLNDAQrhKLEEIAAQMGIagfidrLPGELSGGQRQRVALARCLVREQPMLLLD 154
Cdd:PRK09473 115 RVGEQLMevLMLHKGMskaeafeesvRMLDAV--KMPEARKRMKM------YPHEFSGGMRQRVMIAMALLCRPKLLIAD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 779793995 155 EPFSALDPALRQEMLTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEEL 217
Cdd:PRK09473 187 EPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
19-188 |
1.19e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 65.52 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAKrpvsmLFQENNLftHLTVRQNIALgmHP 98
Cdd:PRK09544 24 SLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQK-----LYLDTTL--PLTVNRFLRL--RP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 99 GLRLNDAQRhKLEEIAAqmgiAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQDVCQR 178
Cdd:PRK09544 95 GTKKEDILP-ALKRVQA----GHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRE 169
|
170
....*....|
gi 779793995 179 QQLTMLMVSH 188
Cdd:PRK09544 170 LDCAVLMVSH 179
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
24-168 |
1.67e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 66.37 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 24 QGERIAVLGPSGAGKSTLLNLVAGFLQPvsgsividNQDHTHTPPAKRPVSMLFQENNLFTHL----------------- 86
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIP--------NLGDYEEEPSWDEVLKRFRGTELQNYFkklyngeikvvhkpqyv 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 87 ---------TVRQniaLgmhpgLRLNDaQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPF 157
Cdd:PRK13409 170 dlipkvfkgKVRE---L-----LKKVD-ERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPT 240
|
170
....*....|.
gi 779793995 158 SALDpaLRQEM 168
Cdd:PRK13409 241 SYLD--IRQRL 249
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
18-234 |
3.26e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 65.32 E-value: 3.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 18 FTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQD-HTHTPP-AKRPVSMLFQENN----LFTHLTVRQN 91
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPiDIRSPRdAIRAGIMLCPEDRkaegIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 92 IALG-----MHPGLRLNDAQRhklEEIAAQmgiagFIDRLP----------GELSGGQRQRVALARCLVREQPMLLLDEP 156
Cdd:PRK11288 352 INISarrhhLRAGCLINNRWE---AENADR-----FIRSLNiktpsreqliMNLSGGNQQKAILGRWLSEDMKVILLDEP 423
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 779793995 157 FSALDPALRQEMLTLVQDVCQrQQLTMLMVSHSIEDAARIAPRSVVIAEGRIvwdgvTEELLKGNAAASSLLGISAPP 234
Cdd:PRK11288 424 TRGIDVGAKHEIYNVIYELAA-QGVAVLFVSSDLPEVLGVADRIVVMREGRI-----AGELAREQATERQALSLALPR 495
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-219 |
3.81e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 65.26 E-value: 3.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSI-------------VIDNQDHTHTPPAK---RPVSMLFQE--N 80
Cdd:PRK10261 36 SFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqVIELSEQSAAQMRHvrgADMAMIFQEpmT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 81 NLFTHLTVRQNIA--LGMHPGLRLNDAQRhKLEEIAAQMGIA---GFIDRLPGELSGGQRQRVALARCLVREQPMLLLDE 155
Cdd:PRK10261 116 SLNPVFTVGEQIAesIRLHQGASREEAMV-EAKRMLDQVRIPeaqTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADE 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 779793995 156 PFSALDPALRQEMLTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELLK 219
Cdd:PRK10261 195 PTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFH 258
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
18-209 |
4.36e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 65.05 E-value: 4.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 18 FTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAKRPVSMLF------QENNLFTHLTVRQN 91
Cdd:COG3845 277 VSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVAyipedrLGRGLVPDMSVAEN 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 92 IALGMH------PGLRLNDAQRHKL-EEIAAQMGI-AGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDP- 162
Cdd:COG3845 357 LILGRYrrppfsRGGFLDRKAIRAFaEELIEEFDVrTPGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVg 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 779793995 163 ---ALRQEMLTLvqdvcqRQQ-LTMLMVSHSIEDAARIAPRSVVIAEGRIV 209
Cdd:COG3845 437 aieFIHQRLLEL------RDAgAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-219 |
5.19e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 65.19 E-value: 5.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVidnqdhthtppAKRPVSMLFQENNLFtHLTVRQNIaLGMHP 98
Cdd:PTZ00243 680 SVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-----------AERSIAYVPQQAWIM-NATVRGNI-LFFDE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 99 --GLRLNDAQR-HKLEEIAAQMGiaGFIDRLPGE----LSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEmltL 171
Cdd:PTZ00243 747 edAARLADAVRvSQLEADLAQLG--GGLETEIGEkgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGER---V 821
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 779793995 172 VQDvCQRQQL---TMLMVSHSIEDAARiAPRSVVIAEGRIVWDGVTEELLK 219
Cdd:PTZ00243 822 VEE-CFLGALagkTRVLATHQVHVVPR-ADYVVALGDGRVEFSGSSADFMR 870
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
20-219 |
5.41e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 65.14 E-value: 5.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 20 LSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPakrpVSMLFQEnnlfthlTVRQNIALGmhpg 99
Cdd:PLN03130 638 LDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVIRGTVAYVPQ----VSWIFNA-------TVRDNILFG---- 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 100 lrlNDAQRHKLEEIAAQMGIAGFIDRLPG-----------ELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEm 168
Cdd:PLN03130 703 ---SPFDPERYERAIDVTALQHDLDLLPGgdlteigergvNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQ- 778
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 779793995 169 ltlVQDVCQRQQL---TMLMVS---HSIEDAARIaprsVVIAEGRIVWDGVTEELLK 219
Cdd:PLN03130 779 ---VFDKCIKDELrgkTRVLVTnqlHFLSQVDRI----ILVHEGMIKEEGTYEELSN 828
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
19-189 |
9.67e-12 |
|
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: 61.40 E-value: 9.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIdnqdhthtpPAKRPVSMLFQENnLFTHLTVRQNIAlgmHP 98
Cdd:cd03223 21 SFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------PEGEDLLFLPQRP-YLPLGTLREQLI---YP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 99 GLRlndaqrhkleeiaaqmgiagfidrlpgELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQDVCqr 178
Cdd:cd03223 88 WDD---------------------------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELG-- 138
|
170
....*....|.
gi 779793995 179 qqLTMLMVSHS 189
Cdd:cd03223 139 --ITVISVGHR 147
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-219 |
1.00e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 64.23 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 20 LSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPakrpVSMLFQEnnlfthlTVRQNIALGmhpg 99
Cdd:PLN03232 638 LEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRGSVAYVPQ----VSWIFNA-------TVRENILFG---- 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 100 lrlNDAQRHKLEEIAAQMGIAGFIDRLPGE-----------LSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEm 168
Cdd:PLN03232 703 ---SDFESERYWRAIDVTALQHDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQ- 778
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 779793995 169 ltlVQDVCQRQQL---TMLMVSHSIEDAARIaPRSVVIAEGRIVWDGVTEELLK 219
Cdd:PLN03232 779 ---VFDSCMKDELkgkTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELSK 828
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
17-161 |
1.21e-11 |
|
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: 63.80 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 17 RFTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVID--------NQDHTHTPPAKrpvsmlfqennlfthlTV 88
Cdd:TIGR03719 340 DLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGetvklayvDQSRDALDPNK----------------TV 403
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 779793995 89 RQNIALGmHPGLRLNDAqrhkleEIAAQMGIAGF------IDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALD 161
Cdd:TIGR03719 404 WEEISGG-LDIIKLGKR------EIPSRAYVGRFnfkgsdQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
18-212 |
2.55e-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: 60.74 E-value: 2.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 18 FTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQP---VSGSIVIDNQD-HTHTPPAKRPVSMLFQENNLFTHLTVRQNI- 92
Cdd:cd03233 26 FSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGnvsVEGDIHYNGIPyKEFAEKYPGEIIYVSEEDVHFPTLTVRETLd 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 93 -ALgmhpGLRLNDAQRhkleeiaaqmGIagfidrlpgelSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTL 171
Cdd:cd03233 106 fAL----RCKGNEFVR----------GI-----------SGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKC 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 779793995 172 VQDVCQRQQLTMLM-VSHSIEDAARIAPRSVVIAEGRIVWDG 212
Cdd:cd03233 161 IRTMADVLKTTTFVsLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
18-208 |
3.20e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.33 E-value: 3.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 18 FTLSvlQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQD-HTHTPpakrpvsmlfQE---------------NN 81
Cdd:PRK10762 273 FTLR--KGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEvVTRSP----------QDglangivyisedrkrDG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 82 LFTHLTVRQNIALGM-----HPGLRLndaqRHKLEEIAAQMGIAGF------IDRLPGELSGGQRQRVALARCLVREQPM 150
Cdd:PRK10762 341 LVLGMSVKENMSLTAlryfsRAGGSL----KHADEQQAVSDFIRLFniktpsMEQAIGLLSGGNQQKVAIARGLMTRPKV 416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 779793995 151 LLLDEPFSALDPALRQEMLTLVQDVCQrQQLTMLMVSHSIEDAARIAPRSVVIAEGRI 208
Cdd:PRK10762 417 LILDEPTRGVDVGAKKEIYQLINQFKA-EGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
24-228 |
7.24e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 61.85 E-value: 7.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 24 QGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIvidnqDHTHTPPAKRPVSMLFQEnnlfthlTVRQNIALGMHpglrlN 103
Cdd:TIGR01271 451 KGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-----KHSGRISFSPQTSWIMPG-------TIKDNIIFGLS-----Y 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 104 DAQRHKLEEIAAQM--GIAGFI--DRLP-GE----LSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTlvQD 174
Cdd:TIGR01271 514 DEYRYTSVIKACQLeeDIALFPekDKTVlGEggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFE--SC 591
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 779793995 175 VCQ-RQQLTMLMVSHSIEDAARiAPRSVVIAEGRIVWDGVTEELLKGNAAASSLL 228
Cdd:TIGR01271 592 LCKlMSNKTRILVTSKLEHLKK-ADKILLLHEGVCYFYGTFSELQAKRPDFSSLL 645
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-227 |
7.52e-11 |
|
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: 61.38 E-value: 7.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAG-FLQPVSGSIVIDNQDHTHTPPAK---RPVSMLFQE---NNLFTHLTVRQN 91
Cdd:TIGR02633 280 SFSLRRGEILGVAGLVGAGRTELVQALFGaYPGKFEGNVFINGKPVDIRNPAQairAGIAMVPEDrkrHGIVPILGVGKN 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 92 IALGMhpglrLND-AQRHKLEEIAAQMGIAGFIDRLP----------GELSGGQRQRVALARCLVREQPMLLLDEPFSAL 160
Cdd:TIGR02633 360 ITLSV-----LKSfCFKMRIDAAAELQIIGSAIQRLKvktaspflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGV 434
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 779793995 161 DPALRQEMLTLVQDVCQrQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELLKGNAAASSL 227
Cdd:TIGR02633 435 DVGAKYEIYKLINQLAQ-EGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDFVNHALTQEQVLAAAL 500
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
17-218 |
8.14e-11 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 60.97 E-value: 8.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 17 RFTLSVLQGERIAVLGPSGAGKSTLLNLVAGF----LQPVSGSIVIDNQDHTH-TPPAKRP-----VSMLFQE------- 79
Cdd:PRK15093 25 RVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnWRVTADRMRFDDIDLLRlSPRERRKlvghnVSMIFQEpqscldp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 80 -NNLFTHLTvrQNIALGMHPG---LRLNDAQRHKLEeIAAQMGIAGFIDRL---PGELSGGQRQRVALARCLVREQPMLL 152
Cdd:PRK15093 105 sERVGRQLM--QNIPGWTYKGrwwQRFGWRKRRAIE-LLHRVGIKDHKDAMrsfPYELTEGECQKVMIAIALANQPRLLI 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 779793995 153 LDEPFSALDPALRQEMLTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELL 218
Cdd:PRK15093 182 ADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELV 247
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-219 |
1.16e-10 |
|
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: 61.11 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVID--NQDHTHTPPAKRPVSMLFQENNLFTHlTVRQNialgm 96
Cdd:TIGR00957 1306 NVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDglNIAKIGLHDLRFKITIIPQDPVLFSG-SLRMN----- 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 97 hpglrLNDAQRHKLEEIAAQMGIA---GFIDRLP----------GE-LSGGQRQRVALARCLVREQPMLLLDEPFSALDp 162
Cdd:TIGR00957 1380 -----LDPFSQYSDEEVWWALELAhlkTFVSALPdkldhecaegGEnLSVGQRQLVCLARALLRKTKILVLDEATAAVD- 1453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 779793995 163 alrQEMLTLVQDVCQRQ--QLTMLMVSH---SIEDAARIaprsVVIAEGRIVWDGVTEELLK 219
Cdd:TIGR00957 1454 ---LETDNLIQSTIRTQfeDCTVLTIAHrlnTIMDYTRV----IVLDKGEVAEFGAPSNLLQ 1508
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-191 |
1.23e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 61.08 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLnlvAGFLQPVS--GSIVID--NQDHTHTPPAKRPVSMLFQENNLFTHlTVRQNial 94
Cdd:TIGR01271 1239 SFSVEGGQRVGLLGRTGSGKSTLL---SALLRLLSteGEIQIDgvSWNSVTLQTWRKAFGVIPQKVFIFSG-TFRKN--- 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 95 gMHPGLRLNDAQrhkLEEIAAQMGIAGFIDRLPGEL-----------SGGQRQRVALARCLVREQPMLLLDEPFSALDPA 163
Cdd:TIGR01271 1312 -LDPYEQWSDEE---IWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKILLLDEPSAHLDPV 1387
|
170 180
....*....|....*....|....*....
gi 779793995 164 LRQEML-TLVQDVcqrQQLTMLMVSHSIE 191
Cdd:TIGR01271 1388 TLQIIRkTLKQSF---SNCTVILSEHRVE 1413
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
19-166 |
1.29e-10 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 59.87 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNlvaGFLQPVS--GSIVIDNQDHTHTPPAK--RPVSMLFQENNLFTHlTVRQNial 94
Cdd:cd03289 24 SFSISPGQRVGLLGRTGSGKSTLLS---AFLRLLNteGDIQIDGVSWNSVPLQKwrKAFGVIPQKVFIFSG-TFRKN--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 95 gmhpglrLNDAQRHKLEEI---AAQMGIAGFIDRLPGEL-----------SGGQRQRVALARCLVREQPMLLLDEPFSAL 160
Cdd:cd03289 97 -------LDPYGKWSDEEIwkvAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDEPSAHL 169
|
....*.
gi 779793995 161 DPALRQ 166
Cdd:cd03289 170 DPITYQ 175
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
25-228 |
2.00e-10 |
|
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: 59.15 E-value: 2.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 25 GERIAVLGPSGAGKSTL----LNLVAGFlqpvSGSIVIDNQDHTHTP--PAKRPVSMLFQENNLFThltvrQNIALGMHP 98
Cdd:cd03288 47 GQKVGICGRTGSGKSSLslafFRMVDIF----DGKIVIDGIDISKLPlhTLRSRLSIILQDPILFS-----GSIRFNLDP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 99 GLRLNDAQRHKLEEIAAqmgIAGFIDRLPGEL-----------SGGQRQRVALARCLVREQPMLLLDEPFSALDPA---- 163
Cdd:cd03288 118 ECKCTDDRLWEALEIAQ---LKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASIDMAteni 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 779793995 164 LRQEMLTLVQDvcqRQQLTMLMVSHSIEDAARIaprsVVIAEGRIV-WDGVTEELLKGNAAASSLL 228
Cdd:cd03288 195 LQKVVMTAFAD---RTVVTIAHRVSTILDADLV----LVLSRGILVeCDTPENLLAQEDGVFASLV 253
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
24-203 |
2.46e-10 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 57.00 E-value: 2.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 24 QGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDhthtppakrpvsmlfqennlfthltvrqnialgmhpglrln 103
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGE----------------------------------------- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 104 daqrhKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQDVCQRQQ--- 180
Cdd:smart00382 40 -----DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLkse 114
|
170 180
....*....|....*....|....*....
gi 779793995 181 ------LTMLMVSHSIEDAARIAPRSVVI 203
Cdd:smart00382 115 knltviLTTNDEKDLGPALLRRRFDRRIV 143
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-216 |
3.78e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 59.03 E-value: 3.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGflqpV------SGSIVIDNQ--------DHTHtppakRPVSMLFQENNLFT 84
Cdd:NF040905 21 NLSVREGEIHALCGENGAGKSTLMKVLSG----VyphgsyEGEILFDGEvcrfkdirDSEA-----LGIVIIHQELALIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 85 HLTVRQNIALGMHPGLR--LN-DAQRHKLEEIAAQMGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALD 161
Cdd:NF040905 92 YLSIAENIFLGNERAKRgvIDwNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALN 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 779793995 162 PALRQEMLTLVQDVcQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVW------DGVTEE 216
Cdd:NF040905 172 EEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRTIEtldcraDEVTED 231
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
26-218 |
4.00e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 59.37 E-value: 4.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 26 ERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPA--KRPVSMLFQENNLFTHlTVRQNialgMHPGLRLN 103
Cdd:PLN03130 1266 EKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMdlRKVLGIIPQAPVLFSG-TVRFN----LDPFNEHN 1340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 104 DA------QRHKLEEIAAQ--MGIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALD---PALRQEMLTLV 172
Cdd:PLN03130 1341 DAdlweslERAHLKDVIRRnsLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDvrtDALIQKTIREE 1420
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 779793995 173 QDVCqrqqlTMLMVSH---SIEDAARIaprsVVIAEGRIVWDGVTEELL 218
Cdd:PLN03130 1421 FKSC-----TMLIIAHrlnTIIDCDRI----LVLDAGRVVEFDTPENLL 1460
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
19-209 |
6.02e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.59 E-value: 6.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQD---HTHTPPAKRPVSMLFQENNLFTHLTVRQNIALG 95
Cdd:PRK10982 18 NLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEidfKSSKEALENGISMVHQELNLVLQRSVMDNMWLG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 96 MHP--GLRLNDAQRHK-LEEIAAQMGIAgfIDrlP----GELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEM 168
Cdd:PRK10982 98 RYPtkGMFVDQDKMYRdTKAIFDELDID--ID--PrakvATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 779793995 169 LTLVQDVCQRqQLTMLMVSHSIEDAARIAPRSVVIAEGRIV 209
Cdd:PRK10982 174 FTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
21-217 |
8.74e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 58.02 E-value: 8.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 21 SVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVS-GSIVIDNQDHTHTPPA---KRPVSMLFQE---NNLFTHLTVRQNIA 93
Cdd:PRK13549 284 SLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGKPVKIRNPQqaiAQGIAMVPEDrkrDGIVPVMGVGKNIT 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 94 LGMHP----GLRLNDA--QRHKLEEIAaQMGIAGFIDRLP-GELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQ 166
Cdd:PRK13549 364 LAALDrftgGSRIDDAaeLKTILESIQ-RLKVKTASPELAiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKY 442
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 779793995 167 EMLTLVQDVCQrQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEEL 217
Cdd:PRK13549 443 EIYKLINQLVQ-QGVAIIVISSELPEVLGLSDRVLVMHEGKLKGDLINHNL 492
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
30-161 |
2.23e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.05 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 30 VLGPSGAGKSTLLNLVAGFLQPVSGSIVI---------DnQDHTHTPPAKrpvsmlfqennlfthlTVRQNIALGmHPGL 100
Cdd:PRK11819 355 IIGPNGAGKSTLFKMITGQEQPDSGTIKIgetvklayvD-QSRDALDPNK----------------TVWEEISGG-LDII 416
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 779793995 101 RLNDAqrhkleEIAAQMGIAGF----ID--RLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALD 161
Cdd:PRK11819 417 KVGNR------EIPSRAYVGRFnfkgGDqqKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
17-219 |
1.23e-08 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 54.53 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 17 RFTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQP---VSGS-IVIDNQDHTHTPPAKR------PVSMLFQE------- 79
Cdd:COG4170 25 RVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhVTADrFRWNGIDLLKLSPRERrkiigrEIAMIFQEpsscldp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 80 -NNLFTHLTvrQNIALGMHPGLRLNDAQRHKLEEIAA--QMGIAG---FIDRLPGELSGGQRQRVALARCLVReQPMLLL 153
Cdd:COG4170 105 sAKIGDQLI--EAIPSWTFKGKWWQRFKWRKKRAIELlhRVGIKDhkdIMNSYPHELTEGECQKVMIAMAIAN-QPRLLI 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 779793995 154 -DEPFSALDPALRQEMLTLVQDVCQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELLK 219
Cdd:COG4170 182 aDEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILK 248
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
25-212 |
1.80e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.34 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 25 GERIAVLGPSGAGKSTLLNLVA----GFLQPVSGSIVIDNQDHTHTPPAKRPVSMLFQENNL-FTHLTVRQNI---ALGM 96
Cdd:TIGR00956 87 GELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVhFPHLTVGETLdfaARCK 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 97 HPGLRLNDAQR-----HKLEEIAAQMGIAGFIDRLPGE-----LSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQ 166
Cdd:TIGR00956 167 TPQNRPDGVSReeyakHIADVYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATAL 246
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 779793995 167 EMLTLVQDVCQRQQLTMLM-VSHSIEDAARIAPRSVVIAEGRIVWDG 212
Cdd:TIGR00956 247 EFIRALKTSANILDTTPLVaIYQCSQDAYELFDKVIVLYEGYQIYFG 293
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
3-190 |
2.21e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 54.13 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 3 KLTDVTW-----LYQHLPMRFTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIdnqdhthtppaKRPVSMLF 77
Cdd:PRK13545 23 KLKDLFFrskdgEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI-----------KGSAALIA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 78 QENNLFTHLTVRQNIAL-GMHPGLRlndaqRHKLEEIAAQM----GIAGFIDRLPGELSGGQRQRVALARCLVREQPMLL 152
Cdd:PRK13545 92 ISSGLNGQLTGIENIELkGLMMGLT-----KEKIKEIIPEIiefaDIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILV 166
|
170 180 190
....*....|....*....|....*....|....*...
gi 779793995 153 LDEPFSALDPALRQEMLTLVQDVcQRQQLTMLMVSHSI 190
Cdd:PRK13545 167 IDEALSVGDQTFTKKCLDKMNEF-KEQGKTIFFISHSL 203
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
16-161 |
2.24e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 54.26 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 16 MRFTLSvlQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQDHTHTPPAK---RPVSMLFQENNLFTHlTVRQNI 92
Cdd:PTZ00265 404 LNFTLT--EGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDINLKwwrSKIGVVSQDPLLFSN-SIKNNI 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 93 ALGMHpGLRLNDAQRHKLEE----------------------------------------------------IAAQMGIA 120
Cdd:PTZ00265 481 KYSLY-SLKDLEALSNYYNEdgndsqenknkrnscrakcagdlndmsnttdsneliemrknyqtikdsevvdVSKKVLIH 559
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 779793995 121 GFIDRLP-----------GELSGGQRQRVALARCLVREQPMLLLDEPFSALD 161
Cdd:PTZ00265 560 DFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
24-203 |
2.45e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 52.19 E-value: 2.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 24 QGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNqdhthTPPAKRPvsmlfqennlfthltvrQNIalgmhpglrln 103
Cdd:cd03222 24 EGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG-----ITPVYKP-----------------QYI----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 104 daqrhkleeiaaqmgiagfidrlpgELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQDVCQRQQLTM 183
Cdd:cd03222 71 -------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTA 125
|
170 180
....*....|....*....|
gi 779793995 184 LMVSHSIEDAARIAPRSVVI 203
Cdd:cd03222 126 LVVEHDLAVLDYLSDRIHVF 145
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
20-166 |
3.00e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 53.64 E-value: 3.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 20 LSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIdnqdhthtppAKRPVSMLFQENNLfthltvrqnialgmhPG 99
Cdd:PRK10636 333 LNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL----------AKGIKLGYFAQHQL---------------EF 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 100 LRLNDAQRHKLEEIAAQ---------MGIAGF----IDRLPGELSGGQRQRVALArCLVREQP-MLLLDEPFSALDPALR 165
Cdd:PRK10636 388 LRADESPLQHLARLAPQeleqklrdyLGGFGFqgdkVTEETRRFSGGEKARLVLA-LIVWQRPnLLLLDEPTNHLDLDMR 466
|
.
gi 779793995 166 Q 166
Cdd:PRK10636 467 Q 467
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
18-65 |
3.12e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.36 E-value: 3.12e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 779793995 18 FTLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIV-IDN-------QDHTH 65
Cdd:PRK15064 338 LNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKwSENanigyyaQDHAY 393
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-155 |
6.67e-08 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 52.49 E-value: 6.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 2 LKLTDVTWLYQHL--PMRFT-----LSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQD-HTHTPPAKRP- 72
Cdd:COG4615 328 LELRGVTYRYPGEdgDEGFTlgpidLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPvTADNREAYRQl 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 73 VSMLFQENNLFTHLtvrqniaLGMhPGLRLNDAQRHKLE--EIAAQMGIAG--FIDRlpgELSGGQRQRVALARCLVREQ 148
Cdd:COG4615 408 FSAVFSDFHLFDRL-------LGL-DGEADPARARELLErlELDHKVSVEDgrFSTT---DLSQGQRKRLALLVALLEDR 476
|
....*..
gi 779793995 149 PMLLLDE 155
Cdd:COG4615 477 PILVFDE 483
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
20-161 |
9.10e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 52.26 E-value: 9.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 20 LSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDnQDHThtppakrpVSMLFQENNLFTHLTVRQNIALGM--- 96
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE-QDLI--------VARLQQDPPRNVEGTVYDFVAEGIeeq 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 97 -------HPGLRL-----NDAQRHKLEEIAAQMGIAG---FIDR---------LPG-----ELSGGQRQRVALARCLVRE 147
Cdd:PRK11147 95 aeylkryHDISHLvetdpSEKNLNELAKLQEQLDHHNlwqLENRinevlaqlgLDPdaalsSLSGGWLRKAALGRALVSN 174
|
170
....*....|....
gi 779793995 148 QPMLLLDEPFSALD 161
Cdd:PRK11147 175 PDVLLLDEPTNHLD 188
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
17-188 |
4.65e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 50.13 E-value: 4.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 17 RFTLSVLQGERIAVLGPSGAGKSTLLNLVAGfLQPVSGSividnqdhTHTPPAKRPVSMLFQENnLFTHLTVRQNIALGM 96
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFRILGE-LWPVYGG--------RLTKPAKGKLFYVPQRP-YMTLGTLRDQIIYPD 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 97 HP------GLRLNDaqrhkLEEIAAQMGIAGFIDRLPG---------ELSGGQRQRVALARCLVREQPMLLLDEPFSALD 161
Cdd:TIGR00954 540 SSedmkrrGLSDKD-----LEQILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTSAVS 614
|
170 180
....*....|....*....|....*..
gi 779793995 162 PALRQEMLTLvqdvCQRQQLTMLMVSH 188
Cdd:TIGR00954 615 VDVEGYMYRL----CREFGITLFSVSH 637
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
29-161 |
8.12e-07 |
|
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: 48.01 E-value: 8.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 29 AVLGPSGAGKSTLLNLVAG--FLQPVSGSIVIDNQDHTHTPPakRPVSMLFQENNLFTHLTVRQniALGMHPGLRlndaq 106
Cdd:cd03232 37 ALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLDKNFQ--RSTGYVEQQDVHSPNLTVRE--ALRFSALLR----- 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 779793995 107 rhkleeiaaqmgiagfidrlpgELSGGQRQRVALARCLVREQPMLLLDEPFSALD 161
Cdd:cd03232 108 ----------------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-219 |
1.77e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 47.50 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 19 TLSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQdhthtppakrpVSMLFQENNLFTHLTVRQNIALGMhp 98
Cdd:PRK13546 44 SLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-----------VSVIAISAGLSGQLTGIENIEFKM-- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 99 glRLNDAQRHKLEEIAAQM----GIAGFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQD 174
Cdd:PRK13546 111 --LCMGFKRKEIKAMTPKIiefsELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYE 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 779793995 175 VcQRQQLTMLMVSHSIEDAARIAPRSVVIAEGRIVWDGVTEELLK 219
Cdd:PRK13546 189 F-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLP 232
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
25-166 |
9.46e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 46.31 E-value: 9.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 25 GERIAVLGPSGAGKSTLLNLVAGFLQPVSGSIVIDNQD--HTHTPPAKRPVSMLFQENNLFTHlTVRQNIalgmHPGLRL 102
Cdd:PTZ00243 1336 REKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREigAYGLRELRRQFSMIPQDPVLFDG-TVRQNV----DPFLEA 1410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 103 NDAqrhkleEIAAQMGIAGFIDRLPGELSG--------------GQRQRVALARCLV-REQPMLLLDEPFSALDPAL-RQ 166
Cdd:PTZ00243 1411 SSA------EVWAALELVGLRERVASESEGidsrvleggsnysvGQRQLMCMARALLkKGSGFILMDEATANIDPALdRQ 1484
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
32-172 |
1.66e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 44.09 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 32 GPSGAGKSTLLNLVAGFLQPVSGSIVIDNqdhTHTPPAKRPVSMLFQEN-NLFTHLTVRQNIAL--GMHPGLRLNDAQRH 108
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKN---CNINNIAKPYCTYIGHNlGLKLEMTVFENLKFwsEIYNSAETLYAAIH 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 779793995 109 --KLEEiaaqmgiagFIDRLPGELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLV 172
Cdd:PRK13541 110 yfKLHD---------LLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLI 166
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
128-208 |
1.83e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.11 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 128 GELSGGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQDVCQRQQlTMLMVSHSIEDAARIAPRSVVIAEGR 207
Cdd:PRK10982 390 GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDK-GIIIISSEMPELLGITDRILVMSNGL 468
|
.
gi 779793995 208 I 208
Cdd:PRK10982 469 V 469
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
21-47 |
5.59e-05 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 42.77 E-value: 5.59e-05
10 20
....*....|....*....|....*..
gi 779793995 21 SVLQGERIAVLGPSGAGKSTLLNLVAG 47
Cdd:cd01854 81 ELLKGKTSVLVGQSGVGKSTLLNALLP 107
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
20-212 |
5.93e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 43.09 E-value: 5.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 20 LSVLQGERIAVLGPSGAGKSTLLNLVAGF--LQPVSGSIVIDNQDHTHTPPAKRpvsmlfqennlfTHLtvrqNIALGMH 97
Cdd:CHL00131 28 LSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPEER------------AHL----GIFLAFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 98 -----PG------LRLNDAQRHK------------LEEIAAQMGIAG----FIDRLPGE-LSGGQRQRVALARCLVREQP 149
Cdd:CHL00131 92 ypieiPGvsnadfLRLAYNSKRKfqglpeldplefLEIINEKLKLVGmdpsFLSRNVNEgFSGGEKKRNEILQMALLDSE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 779793995 150 MLLLDEPFSALD-PALRQ--EMLTLVQDVCQrqqlTMLMVSHSIEDAARIAPRSV-VIAEGRIVWDG 212
Cdd:CHL00131 172 LAILDETDSGLDiDALKIiaEGINKLMTSEN----SIILITHYQRLLDYIKPDYVhVMQNGKIIKTG 234
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
116-188 |
9.30e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 42.21 E-value: 9.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 116 QMGIAGFIDRLPGELSGGQRQ------RVALARCLVREQPMLLLDEPFSALDPA-LRQEMLTLVQDVCQRQQLTMLMVSH 188
Cdd:cd03240 102 QGESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEnIEESLAEIIEERKSQKNFQLIVITH 181
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
20-212 |
1.36e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 42.09 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 20 LSVLQGERIAVLGPSGAGKSTLLNLVAGF--LQPVSGSIVIDNQDHTHTPPAKRP---VSMLFQ--------ENNLFTHL 86
Cdd:PRK09580 22 LEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAgegIFMAFQypveipgvSNQFFLQT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 87 TVrqnialgmhpglrlNDAQRHKLEEIAAQMGIAGFID------RLPGEL---------SGGQRQRVALARCLVREQPML 151
Cdd:PRK09580 102 AL--------------NAVRSYRGQEPLDRFDFQDLMEekiallKMPEDLltrsvnvgfSGGEKKRNDILQMAVLEPELC 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 779793995 152 LLDEPFSALD-PALR--QEMLTLVQDvcqrQQLTMLMVSHSIEDAARIAPRSV-VIAEGRIVWDG 212
Cdd:PRK09580 168 ILDESDSGLDiDALKivADGVNSLRD----GKRSFIIVTHYQRILDYIKPDYVhVLYQGRIVKSG 228
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
20-47 |
3.90e-04 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 39.83 E-value: 3.90e-04
10 20
....*....|....*....|....*...
gi 779793995 20 LSVLQGERIAVLGPSGAGKSTLLNLVAG 47
Cdd:pfam03193 101 KELLKGKTTVLAGQSGVGKSTLLNALLP 128
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
131-161 |
5.70e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.61 E-value: 5.70e-04
10 20 30
....*....|....*....|....*....|.
gi 779793995 131 SGGQRQRVALARCLVREQPMLLLDEPFSALD 161
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
124-219 |
6.64e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.58 E-value: 6.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 124 DRLPGELSGGQRQRVALARCLVREQP--MLLLDEPFSALDPALRQEMLTLVQDVcQRQQLTMLMVSHS---IEDAAR--- 195
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKL-RDQGNTVLLVEHDeqmISLADRiid 549
|
90 100
....*....|....*....|....
gi 779793995 196 IAPRSVVIAeGRIVWDGVTEELLK 219
Cdd:PRK00635 550 IGPGAGIFG-GEVLFNGSPREFLA 572
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
15-218 |
9.50e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 40.21 E-value: 9.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 15 PMRFTLsvlqgeriaVLGPSGAGKSTLLNLVAGFLQP---VSGSIVIDNQDHTHTPPAKrpVSMLFQENNLFT-HLTVRQ 90
Cdd:PLN03140 190 PSRMTL---------LLGPPSSGKTTLLLALAGKLDPslkVSGEITYNGYRLNEFVPRK--TSAYISQNDVHVgVMTVKE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 91 NI-------ALGMHPGLRLNDAQRHK-------------LEEIAAQ--------------MGIAGFIDRLPGE-----LS 131
Cdd:PLN03140 259 TLdfsarcqGVGTRYDLLSELARREKdagifpeaevdlfMKATAMEgvksslitdytlkiLGLDICKDTIVGDemirgIS 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 132 GGQRQRVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQDVCQRQQLTMLMvshsieDAARIAPRS-------VVIA 204
Cdd:PLN03140 339 GGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLM------SLLQPAPETfdlfddiILLS 412
|
250
....*....|....
gi 779793995 205 EGRIVWDGVTEELL 218
Cdd:PLN03140 413 EGQIVYQGPRDHIL 426
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
129-162 |
1.80e-03 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 38.43 E-value: 1.80e-03
10 20 30
....*....|....*....|....*....|....*...
gi 779793995 129 ELSGGQRQRVAL----ARCLVREQPMLLLDEPFSALDP 162
Cdd:cd03273 166 ELSGGQRSLVALslilALLLFKPAPMYILDEVDAALDL 203
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
28-190 |
2.01e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 38.07 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 28 IAVLGPSGAGKSTLLNLV--AGFLQPVSGSIVIDNQDHTHTPPAKrpVSMLFQENNLFTHLTVRQ--------------- 90
Cdd:COG0419 26 NLIVGPNGAGKSTILEAIryALYGKARSRSKLRSDLINVGSEEAS--VELEFEHGGKRYRIERRQgefaefleakpserk 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 91 ---NIALGMHPGLRLNDAQRHKLEEIAAQMGIAGFIDRL-------------PGELSGGQRQRVALARCLvreqpMLLLD 154
Cdd:COG0419 104 ealKRLLGLEIYEELKERLKELEEALESALEELAELQKLkqeilaqlsgldpIETLSGGERLRLALADLL-----SLILD 178
|
170 180 190
....*....|....*....|....*....|....*.
gi 779793995 155 epFSALDPALRQEMLTLVQDvcqrqqltMLMVSHSI 190
Cdd:COG0419 179 --FGSLDEERLERLLDALEE--------LAIITHVI 204
|
|
| COG4928 |
COG4928 |
Predicted P-loop ATPase, KAP-like [General function prediction only]; |
28-59 |
3.46e-03 |
|
Predicted P-loop ATPase, KAP-like [General function prediction only];
Pssm-ID: 443956 Cd Length: 386 Bit Score: 37.97 E-value: 3.46e-03
10 20 30
....*....|....*....|....*....|..
gi 779793995 28 IAVLGPSGAGKSTLLNLVAGFLQPVSGSIVID 59
Cdd:COG4928 32 IGLDGEWGSGKTSFLNLIEKELESNEKVIVVY 63
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
27-53 |
3.73e-03 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 36.06 E-value: 3.73e-03
10 20
....*....|....*....|....*..
gi 779793995 27 RIAVLGPSGAGKSTLLNLVAGFLQPVS 53
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALTGAKAIVS 27
|
|
| VirB4 |
COG3451 |
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ... |
28-58 |
3.87e-03 |
|
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442674 [Multi-domain] Cd Length: 546 Bit Score: 38.00 E-value: 3.87e-03
10 20 30
....*....|....*....|....*....|.
gi 779793995 28 IAVLGPSGAGKSTLLNLVAGFLQPVSGSIVI 58
Cdd:COG3451 207 TLILGPSGSGKSFLLKLLLLQLLRYGARIVI 237
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
130-194 |
4.22e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 38.12 E-value: 4.22e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 779793995 130 LSGGQRQ------RVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQdvcqrQQL----TMLMVSHSIE--DAA 194
Cdd:PRK03918 789 LSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDEERRRKLVDIME-----RYLrkipQVIIVSHDEElkDAA 860
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
127-180 |
4.45e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 37.82 E-value: 4.45e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 779793995 127 PGELSGGQR-Q-----RVALARCLVREQPMLLLDEPFSALDPALRQEMLTLVQDVCQRQQ 180
Cdd:COG4717 556 VEELSRGTReQlylalRLALAELLAGEPLPLILDDAFVNFDDERLRAALELLAELAKGRQ 615
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
20-56 |
6.19e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 37.11 E-value: 6.19e-03
10 20 30
....*....|....*....|....*....|....*..
gi 779793995 20 LSVLQGERIAVLGPSGAGKSTLLNLVAGFLQPVSGSI 56
Cdd:PRK00098 159 KPLLAGKVTVLAGQSGVGKSTLLNALAPDLELKTGEI 195
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
24-43 |
6.75e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 37.22 E-value: 6.75e-03
|
| |
