|
Name |
Accession |
Description |
Interval |
E-value |
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-232 |
6.22e-169 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 464.44 E-value: 6.22e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 1 MLKLNDVTWLYQHLPMRFTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQRPVSMLFQEN 80
Cdd:PRK10771 1 MLKLTDITWLYHHLPMRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 81 NLFNHLTVRQNIGLGIHPGLKLNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSAL 160
Cdd:PRK10771 81 NLFSHLTVAQNIGLGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1994014911 161 DPALRQEMLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLSGNSSASALLGISA 232
Cdd:PRK10771 161 DPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKASASALLGIKS 232
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-230 |
4.68e-152 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 421.86 E-value: 4.68e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 1 MLKLNDVTWLYQHLPMRFTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQRPVSMLFQEN 80
Cdd:COG3840 1 MLRLDDLTYRYGDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 81 NLFNHLTVRQNIGLGIHPGLKLNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSAL 160
Cdd:COG3840 81 NLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1994014911 161 DPALRQEMLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLSGNSSA--SALLGI 230
Cdd:COG3840 161 DPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPalAAYLGI 232
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
2-214 |
1.92e-117 |
|
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: 333.75 E-value: 1.92e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 2 LKLNDVTWLYQHLPMRFTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQRPVSMLFQENN 81
Cdd:TIGR01277 1 LALDKVRYEYEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 82 LFNHLTVRQNIGLGIHPGLKLNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALD 161
Cdd:TIGR01277 81 LFAHLTVRQNIGLGLHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1994014911 162 PALRQEMLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGAT 214
Cdd:TIGR01277 161 PLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSDC 213
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
2-212 |
2.30e-116 |
|
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: 330.99 E-value: 2.30e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 2 LKLNDVTWLYQHLPMRFTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQRPVSMLFQENN 81
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 82 LFNHLTVRQNIGLGIHPGLKLNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALD 161
Cdd:cd03298 81 LFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1994014911 162 PALRQEMLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDG 212
Cdd:cd03298 161 PALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-212 |
2.48e-87 |
|
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: 257.45 E-value: 2.48e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 2 LKLNDVTWLY--QHLPMRFTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQRPVSMLFQE 79
Cdd:cd03259 1 LELKGLSKTYgsVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 80 NNLFNHLTVRQNIGLGIHPGLKLNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSA 159
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1994014911 160 LDPALRQEMLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDG 212
Cdd:cd03259 161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
18-217 |
4.60e-74 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 228.44 E-value: 4.60e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 18 FTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQRPVSMLFQENNLFNHLTVRQNIGLGIH 97
Cdd:COG3842 24 VSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMVFQDYALFPHLTVAENVAFGLR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 98 pGLKLNR-EQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVADVC 176
Cdd:COG3842 104 -MRGVPKaEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQ 182
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1994014911 177 QRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDL 217
Cdd:COG3842 183 RELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
18-217 |
8.50e-70 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 217.25 E-value: 8.50e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 18 FTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQRPVSMLFQENNLFNHLTVRQNIGLGih 97
Cdd:COG3839 22 IDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMVFQSYALYPHMTVYENIAFP-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 98 pgLKLNR----EQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVA 173
Cdd:COG3839 100 --LKLRKvpkaEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIK 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1994014911 174 DVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDL 217
Cdd:COG3839 178 RLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
18-209 |
1.58e-69 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 213.80 E-value: 1.58e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 18 FTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKhnTTPPAQRpVSMLFQENNLFNHLTVRQNIGLGIH 97
Cdd:COG1116 30 VSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKP--VTGPGPD-RGVVFQEPALLPWLTVLDNVALGLE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 98 PGLKLNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVADVCQ 177
Cdd:COG1116 107 LRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQ 186
|
170 180 190
....*....|....*....|....*....|....
gi 1994014911 178 RQQLTLLMVSHSVEDAARIAPRSIVVAE--GRIA 209
Cdd:COG1116 187 ETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIV 220
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-207 |
4.58e-67 |
|
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: 204.73 E-value: 4.58e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 2 LKLNDVTWLY--QHLPMRFTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNT----TPPAQRPVSM 75
Cdd:cd03229 1 LELKNVSKRYgqKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDledeLPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 76 LFQENNLFNHLTVRQNIGLGihpglklnreqraqvtaiagqmgmdtlldrlpgeLSGGQRQRAALARCLVRQQPVLLLDE 155
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1994014911 156 PFSALDPALRQEMLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGR 207
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-209 |
1.69e-65 |
|
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: 201.93 E-value: 1.69e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 2 LKLNDVTWLYQHLPMRFT------LSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAqrpVSM 75
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTaledisLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD---RGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 76 LFQENNLFNHLTVRQNIGLGihpgLKLNREQRAQVTAIAGQM----GMDTLLDRLPGELSGGQRQRAALARCLVRQQPVL 151
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALG----LELQGVPKAEARERAEELlelvGLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 152 LLDEPFSALDPALRQEMLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAE--GRIA 209
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIV 213
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
19-218 |
3.37e-64 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 203.07 E-value: 3.37e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNT-TPPAQRPVSMLFQENNLFNHLTVRQNIGLGIH 97
Cdd:COG1118 22 SLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTnLPPRERRVGFVFQHYALFPHMTVAENIAFGLR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 98 PGLKLNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVADVCQ 177
Cdd:COG1118 102 VRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHD 181
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1994014911 178 RQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLL 218
Cdd:COG1118 182 ELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVY 222
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-219 |
5.84e-61 |
|
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: 191.80 E-value: 5.84e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 1 MLKLNDVTWLYQHLPM--RFTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQ--RPVSML 76
Cdd:COG1120 1 MLEAENLSVGYGGRPVldDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaRRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 77 FQENNLFNHLTVRQNIGLGIHPGLK----LNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLL 152
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGRYPHLGlfgrPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1994014911 153 LDEPFSALDPALRQEMLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
19-219 |
1.44e-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: 189.85 E-value: 1.44e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQ--RPVSMLFQ--ENNLFNhLTVRQNIGL 94
Cdd:COG1122 21 SLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLVFQnpDDQLFA-PTVEEDVAF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 95 GIHPgLKLNREQ-RAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVA 173
Cdd:COG1122 100 GPEN-LGLPREEiRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLK 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1994014911 174 DVcQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:COG1122 179 RL-NKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFS 223
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
17-208 |
1.52e-58 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 184.75 E-value: 1.52e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 17 RFTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQRPVSMLFQENNLFNHLTVRQNIGLGi 96
Cdd:cd03300 18 GVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQNYALFPHLTVFENIAFG- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 97 hpgLKLNR----EQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:cd03300 97 ---LRLKKlpkaEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLEL 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 1994014911 173 ADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRI 208
Cdd:cd03300 174 KRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
13-212 |
2.29e-58 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 183.65 E-value: 2.29e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 13 HLPMRFTLSverGERIAVLGPSGAGKSTLLNLIAGFLPPASG------SLLIDGEKHNTTPPAQRPVSMLFQENNLFNHL 86
Cdd:cd03297 14 TLKIDFDLN---EEVTGIFGASGAGKSTLLRCIAGLEKPDGGtivlngTVLFDSRKKINLPPQQRKIGLVFQQYALFPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 87 TVRQNIGLGIHpgLKLNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQ 166
Cdd:cd03297 91 NVRENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1994014911 167 EMLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDG 212
Cdd:cd03297 169 QLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
19-217 |
3.99e-58 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 184.10 E-value: 3.99e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQ-----RPVSMLFQENNLFNHLTVRQNI- 92
Cdd:COG3638 23 SLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrRRIGMIFQQFNLVPRLSVLTNVl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 93 --GLGIHPGLK-----LNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVrQQP-VLLLDEPFSALDPAL 164
Cdd:COG3638 103 agRLGRTSTWRsllglFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARALV-QEPkLILADEPVASLDPKT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1994014911 165 RQEMLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDL 217
Cdd:COG3638 182 ARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-208 |
8.33e-58 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 182.55 E-value: 8.33e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 1 MLKLNDVTWLYQHLPMRFT------LSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQRP-- 72
Cdd:COG1136 4 LLELRNLTKSYGTGEGEVTalrgvsLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELArl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 73 ----VSMLFQENNLFNHLTVRQNIGLGIHPGLKLNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQ 148
Cdd:COG1136 84 rrrhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 149 PVLLLDEPFSALDPALRQEMLTLVADVCQRQQLTLLMVSHSvEDAARIAPRSIVVAEGRI 208
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRI 222
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
18-218 |
3.03e-57 |
|
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: 181.72 E-value: 3.03e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 18 FTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQ-----RPVSMLFQENNLFNHLTVRQNI 92
Cdd:COG1127 24 VSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyelrRRIGMLFQGGALFDSLTVFENV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 93 GLGIHPGLKLNREQ-RAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTL 171
Cdd:COG1127 104 AFPLREHTDLSEAEiRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDEL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1994014911 172 VADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLL 218
Cdd:COG1127 184 IRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELL 230
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-208 |
3.16e-57 |
|
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: 180.76 E-value: 3.16e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 2 LKLNDVTWLYQHLPMRF------TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQRP--- 72
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqalkgvSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 73 ---VSMLFQENNLFNHLTVRQNIGLGIHPGLKLNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQP 149
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1994014911 150 VLLLDEPFSALDPALRQEMLTLVADVCQRQQLTLLMVSHSvEDAARIAPRSIVVAEGRI 208
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
20-208 |
5.61e-57 |
|
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: 180.99 E-value: 5.61e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 20 LSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQRPVSMLFQENNLFNHLTVRQNIGLGIHPG 99
Cdd:cd03299 20 LEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQNYALFPHMTVYKNIAYGLKKR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 100 LKLNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVADVCQRQ 179
Cdd:cd03299 100 KVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEF 179
|
170 180
....*....|....*....|....*....
gi 1994014911 180 QLTLLMVSHSVEDAARIAPRSIVVAEGRI 208
Cdd:cd03299 180 GVTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
19-220 |
5.93e-57 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 180.64 E-value: 5.93e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQRP-VSMLFQENNLFNHLTVRQNIGL--G 95
Cdd:COG1131 20 SLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRrIGYVPQEPALYPDLTVRENLRFfaR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 96 IHPGLKLNREQRAQvtAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVADV 175
Cdd:COG1131 100 LYGLPRKEARERID--ELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLREL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1994014911 176 CqRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLSG 220
Cdd:COG1131 178 A-AEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
17-208 |
6.16e-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: 180.14 E-value: 6.16e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 17 RFTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQRPVSMLFQENNLFNHLTVRQNIGLGi 96
Cdd:cd03301 18 DLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQNYALYPHMTVYDNIAFG- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 97 hpgLKLNREQR----AQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:cd03301 97 ---LKLRKVPKdeidERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAEL 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 1994014911 173 ADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRI 208
Cdd:cd03301 174 KRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-194 |
7.28e-57 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 179.60 E-value: 7.28e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 1 MLKLNDVTWLYQHLPM--RFTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPP---ASGSLLIDGEKHNTTPPAQRPVSM 75
Cdd:COG4136 1 MLSLENLTITLGGRPLlaPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQRRIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 76 LFQENNLFNHLTVRQNIGLGIHPGLKlNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDE 155
Cdd:COG4136 81 LFQDDLLFPHLSVGENLAFALPPTIG-RAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDE 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 1994014911 156 PFSALDPALRQEMLTLVADVCQRQQLTLLMVSHSVEDAA 194
Cdd:COG4136 160 PFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAP 198
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-219 |
5.10e-55 |
|
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: 179.53 E-value: 5.10e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 1 MLKLnDVTWLYQHLPMRFTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGE------KHNTTPPAQRPVS 74
Cdd:COG4148 2 MLEV-DFRLRRGGFTLDVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdsaRGIFLPPHRRRIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 75 MLFQENNLFNHLTVRQNIGLGIHPGLKLNReqRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLD 154
Cdd:COG4148 81 YVFQEARLFPHLSVRGNLLYGRKRAPRAER--RISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1994014911 155 EPFSALDPALRQEMLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:COG4148 159 EPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLS 223
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
19-217 |
6.92e-55 |
|
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: 175.38 E-value: 6.92e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEK-HNTTPPAQRP----VSMLFQENNLFNHLTVRQNIG 93
Cdd:cd03261 20 DLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDiSGLSEAELYRlrrrMGMLFQSGALFDSLTVFENVA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 94 LGIHPGLKLNREQ-RAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:cd03261 100 FPLREHTRLSEEEiREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLI 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1994014911 173 ADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDL 217
Cdd:cd03261 180 RSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
19-207 |
9.65e-55 |
|
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: 174.19 E-value: 9.65e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQ--RPVSMLFQ--ENNLFNHlTVRQNIGL 94
Cdd:cd03225 21 SLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrRKVGLVFQnpDDQFFGP-TVEEEVAF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 95 GIhPGLKLNREQRAQ-VTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVA 173
Cdd:cd03225 100 GL-ENLGLPEEEIEErVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLK 178
|
170 180 190
....*....|....*....|....*....|....
gi 1994014911 174 DVcQRQQLTLLMVSHSVEDAARIAPRSIVVAEGR 207
Cdd:cd03225 179 KL-KAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-224 |
1.41e-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: 174.99 E-value: 1.41e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 1 MLKLNDVTWLYQHLPMRFT------LSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGE--KHNTTPPAQRP 72
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPvlkdvsLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRpvTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 73 VSMLFQ--ENNLFNHLTVRQNIG--LGIHpGLklnREQRAQVTAIAGQMGMD-TLLDRLPGELSGGQRQRAALARCLVRQ 147
Cdd:COG1124 81 VQMVFQdpYASLHPRHTVDRILAepLRIH-GL---PDREERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARALILE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1994014911 148 QPVLLLDEPFSALDPALRQEMLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLSGNSSA 224
Cdd:COG1124 157 PELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHP 233
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-208 |
6.37e-54 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 172.31 E-value: 6.37e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 2 LKLNDVTWLYQHLPM--RFTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQ--RPVSMLF 77
Cdd:COG4619 1 LELEGLSFRVGGKPIlsPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 78 QENNLFNHlTVRQNIGLGIHpgLKLNREQRAQVTAIAGQMGMDT-LLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEP 156
Cdd:COG4619 81 QEPALWGG-TVRDNLPFPFQ--LRERKFDRERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1994014911 157 FSALDPALRQEMLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRI 208
Cdd:COG4619 158 TSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
19-217 |
3.66e-53 |
|
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: 171.21 E-value: 3.66e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPP-----AQRPVSMLFQENNLFNHLTVRQNI- 92
Cdd:cd03256 21 SLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGkalrqLRRQIGMIFQQFNLIERLSVLENVl 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 93 --GLGIHPGLK-----LNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVrQQPVLLL-DEPFSALDPAL 164
Cdd:cd03256 101 sgRLGRRSTWRslfglFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM-QQPKLILaDEPVASLDPAS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1994014911 165 RQEMLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDL 217
Cdd:cd03256 180 SRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-219 |
1.15e-52 |
|
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: 170.04 E-value: 1.15e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 1 MLKLNDVTWLYQHLPM--RFTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGE-KHNTTPPAQRPVSMLF 77
Cdd:COG4555 1 MIEVENLSKKYGKVPAlkDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEdVRKEPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 78 QENNLFNHLTVRQNIGL--GIHPGLKLNREQRAQvtAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDE 155
Cdd:COG4555 81 DERGLYDRLTVRENIRYfaELYGLFDEELKKRIE--ELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1994014911 156 PFSALDPALRQEMLTLVADVCQrQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:COG4555 159 PTNGLDVMARRLLREILRALKK-EGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELRE 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
19-219 |
3.89e-52 |
|
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: 175.86 E-value: 3.89e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGE-----KHNTTPPAQRPVSMLFQ--ENNLFNHLTVRQN 91
Cdd:COG1123 285 SLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKdltklSRRSLRELRRRVQMVFQdpYSSLNPRMTVGDI 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 92 I--GLGIHPGLKlNREQRAQVTAIAGQMGMDT-LLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEM 168
Cdd:COG1123 365 IaePLRLHGLLS-RAERRERVAELLERVGLPPdLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQI 443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1994014911 169 LTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:COG1123 444 LNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFA 494
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
19-219 |
6.50e-52 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 167.86 E-value: 6.50e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEK---HNTTPPAQRP-VSMLFQENNLFNHLTVRQNIGL 94
Cdd:COG1126 21 SLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDltdSKKDINKLRRkVGMVFQQFNLFPHLTVLENVTL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 95 GihPgLKLNREQRAQVTAIA----GQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLT 170
Cdd:COG1126 101 A--P-IKVKKMSKAEAEERAmellERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1994014911 171 LVADVcQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:COG1126 178 VMRDL-AKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFE 225
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-207 |
9.37e-52 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 171.94 E-value: 9.37e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 1 MLKLNDVTWLY--QHLPMRFTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQRPVSMLFQ 78
Cdd:PRK11607 19 LLEIRNLTKSFdgQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 79 ENNLFNHLTVRQNIGLgihpGLKLNREQRAQVTAIAGQM----GMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLD 154
Cdd:PRK11607 99 SYALFPHMTVEQNIAF----GLKQDKLPKAEIASRVNEMlglvHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1994014911 155 EPFSALDPALRQEMLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGR 207
Cdd:PRK11607 175 EPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-219 |
5.42e-51 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 166.03 E-value: 5.42e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 1 MLKLNDVTWLYQHLPM--RFTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKhnttPPAQRP----VS 74
Cdd:COG1121 6 AIELENLTVSYGGRPVleDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP----PRRARRrigyVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 75 MLFQENNLFnHLTVRQNIGLGIHPGLKL----NREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPV 150
Cdd:COG1121 82 QRAEVDWDF-PITVRDVVLMGRYGRRGLfrrpSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1994014911 151 LLLDEPFSALDPALRQEMLTLVADVcQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWdGATDDLLS 219
Cdd:COG1121 161 LLLDEPFAGVDAATEEALYELLREL-RREGKTILVVTHDLGAVREYFDRVLLLNRGLVAH-GPPEEVLT 227
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
20-224 |
1.34e-50 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 164.82 E-value: 1.34e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 20 LSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQRPVSMLFQENNLFNHLTVRQNI--GLGIH 97
Cdd:cd03296 23 LDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQHYALFRHMTVFDNVafGLRVK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 98 PGLKLNREQ--RAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVADV 175
Cdd:cd03296 103 PRSERPPEAeiRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1994014911 176 CQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLSGNSSA 224
Cdd:cd03296 183 HDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASP 231
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
19-219 |
9.89e-50 |
|
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: 162.22 E-value: 9.89e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPP---AQRPVSMLFQENNLFNHLTVRQNIGLG 95
Cdd:cd03219 20 SFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPheiARLGIGRTFQIPRLFPELTVLENVMVA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 96 IHPGLKLN----------REQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALR 165
Cdd:cd03219 100 AQARTGSGlllararreeREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEET 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1994014911 166 QEMLTLVADVcQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:cd03219 180 EELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-209 |
2.10e-49 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 162.34 E-value: 2.10e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 1 MLKLNDVTWLY----QHLPM--RFTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKhNTTPPAQRPVs 74
Cdd:COG4525 3 MLTVRHVSVRYpgggQPQPAlqDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVP-VTGPGADRGV- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 75 mLFQENNLFNHLTVRQNIGLGihpgLKLNREQRAQVTAIAGQM----GMDTLLDRLPGELSGGQRQRAALARCLVRQQPV 150
Cdd:COG4525 81 -VFQKDALLPWLNVLDNVAFG----LRLRGVPKAERRARAEELlalvGLADFARRRIWQLSGGMRQRVGIARALAADPRF 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1994014911 151 LLLDEPFSALDPALRQEMLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVA--EGRIA 209
Cdd:COG4525 156 LLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSpgPGRIV 216
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-208 |
2.53e-49 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 161.74 E-value: 2.53e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 1 MLKLNDVTwlyqhlpMRF---------TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQR 71
Cdd:COG0411 4 LLEVRGLT-------KRFgglvavddvSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 72 P---VSMLFQENNLFNHLTVRQNIGLGIHPGLKLN---------------REQRAQVTAIAGQMGMDTLLDRLPGELSGG 133
Cdd:COG0411 77 ArlgIARTFQNPRLFPELTVLENVLVAAHARLGRGllaallrlprarreeREARERAEELLERVGLADRADEPAGNLSYG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1994014911 134 QRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRI 208
Cdd:COG0411 157 QQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
18-212 |
6.14e-49 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 164.35 E-value: 6.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 18 FTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQRPVSMLFQENNLFNHLTVRQNIGLgih 97
Cdd:PRK09452 33 LDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQSYALFPHMTVFENVAF--- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 98 pGLKL----NREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEM-LTLV 172
Cdd:PRK09452 110 -GLRMqktpAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMqNELK 188
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1994014911 173 AdvCQRQ-QLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDG 212
Cdd:PRK09452 189 A--LQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDG 227
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-218 |
8.59e-49 |
|
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: 160.16 E-value: 8.59e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 2 LKLNDVTWLYQHLPM---RFTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQ--RPVSML 76
Cdd:cd03295 1 IEFENVTKRYGGGKKavnNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 77 FQENNLFNHLTVRQNIGLGihpgLKLNREQRAQVTAIAGQ----MGMD--TLLDRLPGELSGGQRQRAALARCLVRQQPV 150
Cdd:cd03295 81 IQQIGLFPHMTVEENIALV----PKLLKWPKEKIRERADEllalVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1994014911 151 LLLDEPFSALDPALRQEMLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLL 218
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-158 |
1.32e-48 |
|
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: 156.65 E-value: 1.32e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGE--KHNTTPPAQRPVSMLFQENNLFNHLTVRQNIGLGI 96
Cdd:pfam00005 5 SLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQdlTDDERKSLRKEIGYVFQDPQLFPRLTVRENLRLGL 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1994014911 97 HPGLKLNREQRAQVTAIAGQMGM----DTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFS 158
Cdd:pfam00005 85 LLKGLSKREKDARAEEALEKLGLgdlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-219 |
1.34e-48 |
|
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: 159.28 E-value: 1.34e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 1 MLKLNDVTWLYQHLPMRFT------LSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPP-----A 69
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTalkdvsLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGkelrkA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 70 QRPVSMLFQENNLFNHLTVRQNIGLgihPgLKLNR----EQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLV 145
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVAL---P-LEIAGvpkaEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1994014911 146 RQQPVLLLDEPFSALDPALRQEMLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:cd03258 157 NNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFA 230
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
20-209 |
2.40e-48 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 162.51 E-value: 2.40e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 20 LSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQRPVSMLFQENNLFNHLTVRQNIGLGihpg 99
Cdd:PRK11000 24 LDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMVFQSYALYPHLSVAENMSFG---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 100 LKL---NREQRAQ-VTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVADV 175
Cdd:PRK11000 100 LKLagaKKEEINQrVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRL 179
|
170 180 190
....*....|....*....|....*....|....
gi 1994014911 176 CQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIA 209
Cdd:PRK11000 180 HKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVA 213
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-219 |
4.66e-48 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the 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: 159.15 E-value: 4.66e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 2 LKLNDVTWLYQ-HLPMRF------TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTP-----PA 69
Cdd:TIGR04521 1 IKLKNVSYIYQpGTPFEKkalddvSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKkkklkDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 70 QRPVSMLFQ--ENNLFnHLTVRQNIGLGihPG-LKLNRE---QRAQvTAIAgQMGMD-TLLDRLPGELSGGQRQRAALAR 142
Cdd:TIGR04521 81 RKKVGLVFQfpEHQLF-EETVYKDIAFG--PKnLGLSEEeaeERVK-EALE-LVGLDeEYLERSPFELSGGQMRRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1994014911 143 CLVRQQPVLLLDEPFSALDPALRQEMLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:TIGR04521 156 VLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFS 232
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
20-208 |
6.32e-48 |
|
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: 156.92 E-value: 6.32e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 20 LSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPA----QRPVSMLFQENNLFNHLTVRQNIGLG 95
Cdd:cd03262 21 LTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelRQKVGMVFQQFNLFPHLTVLENITLA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 96 IhpgLKLNREQRAQVTAIA----GQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTL 171
Cdd:cd03262 101 P---IKVKGMSKAEAEERAlellEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDV 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 1994014911 172 VADVCQRQQlTLLMVSHSVEDAARIAPRSIVVAEGRI 208
Cdd:cd03262 178 MKDLAEEGM-TMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
20-208 |
2.87e-47 |
|
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: 155.74 E-value: 2.87e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 20 LSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQRP-----VSMLFQE-NNLFN-HLTVRQNI 92
Cdd:cd03257 26 FSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKirrkeIQMVFQDpMSSLNpRMTIGEQI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 93 --GLGIHPGLKLNREQRAQVTAIAGQMGMD-TLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEML 169
Cdd:cd03257 106 aePLRIHGKLSKKEARKEAVLLLLVGVGLPeEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQIL 185
|
170 180 190
....*....|....*....|....*....|....*....
gi 1994014911 170 TLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRI 208
Cdd:cd03257 186 DLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
19-219 |
1.48e-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: 161.22 E-value: 1.48e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPA---SGSLLIDGEKHNTTPPAQRP--VSMLFQE-NNLFNHLTVRQNI 92
Cdd:COG1123 26 SLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGrrIGMVFQDpMTQLNPVTVGDQI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 93 GLGIHPGLKLNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:COG1123 106 AEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1994014911 173 ADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:COG1123 186 RELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
30-219 |
1.64e-46 |
|
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: 156.88 E-value: 1.64e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 30 VLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQRPVSMLFQENNLFNHLTVRQNIGLGIHPGLKLNREQRAQ 109
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 110 VTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVADVCQRQQLTLLMVSHS 189
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180 190
....*....|....*....|....*....|
gi 1994014911 190 VEDAARIAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYE 190
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
19-208 |
2.55e-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: 151.40 E-value: 2.55e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQRP-VSMLFQENNLFNHLTVRQNIglgih 97
Cdd:cd03230 20 SLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRrIGYLPEEPSLYENLTVRENL----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 98 pglklnreqraqvtaiagqmgmdtlldrlpgELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVADvCQ 177
Cdd:cd03230 95 -------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRE-LK 142
|
170 180 190
....*....|....*....|....*....|.
gi 1994014911 178 RQQLTLLMVSHSVEDAARIAPRSIVVAEGRI 208
Cdd:cd03230 143 KEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-219 |
4.62e-46 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 152.94 E-value: 4.62e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 1 MLKLNDVTWLYQHLPM--RFTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQRPV----S 74
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVlhNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 75 MLFQENNLFNHLTVRQNIGLG-IHPGLKLNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLL 153
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1994014911 154 DEPFSALDPALRQEMLTLVADVCQrQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAE-EGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
19-218 |
2.36e-45 |
|
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: 152.03 E-value: 2.36e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQ------RPVSMLFQENNLFNHLTVRQNI 92
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrKKISMVFQSFALLPHRTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 93 --GLGIHPGLKLNREQRAQvTAIAgQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLT 170
Cdd:cd03294 124 afGLEVQGVPRAEREERAA-EALE-LVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQD 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1994014911 171 LVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLL 218
Cdd:cd03294 202 ELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-211 |
3.10e-45 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 149.99 E-value: 3.10e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 3 KLNDVTWLY-QHLPMR-FTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEkhnttPPAQRP-----VSM 75
Cdd:cd03235 1 EVEDLTVSYgGHPVLEdVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK-----PLEKERkrigyVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 76 LFQENNLFNhLTVRQNIGLGI--HPGL--KLNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVL 151
Cdd:cd03235 76 RRSIDRDFP-ISVRDVVLMGLygHKGLfrRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 152 LLDEPFSALDPALRQEMLTLVADVCQRqQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWD 211
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRTVVASG 213
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
19-212 |
5.14e-45 |
|
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: 148.35 E-value: 5.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQRpvsmlfqennlfnhltvrqniglgihp 98
Cdd:cd03214 19 SLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL--------------------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 99 glklnREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVADVCQR 178
Cdd:cd03214 72 -----ARKIAYVPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARE 146
|
170 180 190
....*....|....*....|....*....|....
gi 1994014911 179 QQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDG 212
Cdd:cd03214 147 RGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
18-228 |
2.69e-44 |
|
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: 156.08 E-value: 2.69e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 18 FTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQ--RPVSMLFQENNLFNHlTVRQNiglg 95
Cdd:COG4987 354 LSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrRRIAVVPQRPHLFDT-TLREN---- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 96 ihpgLKLNREQ--RAQVTAIAGQMGMDTLLDRLP-------GE----LSGGQRQRAALARCLVRQQPVLLLDEPFSALDP 162
Cdd:COG4987 429 ----LRLARPDatDEELWAALERVGLGDWLAALPdgldtwlGEggrrLSGGERRRLALARALLRDAPILLLDEPTEGLDA 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1994014911 163 ALRQEMLTLVADVCQRQqlTLLMVSHSVEDAARiAPRSIVVAEGRIAWDGATDDLLSGNSSASALL 228
Cdd:COG4987 505 ATEQALLADLLEALAGR--TVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEELLAQNGRYRQLY 567
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
20-219 |
2.73e-44 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 151.80 E-value: 2.73e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 20 LSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGE------KHNTTPPAQRPVSMLFQENNLFNHLTVRQNIG 93
Cdd:TIGR02142 18 FTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfdsrKGIFLPPEKRRIGYVFQEARLFPHLSVRGNLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 94 LGihpgLKLNR--EQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTL 171
Cdd:TIGR02142 98 YG----MKRARpsERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPY 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1994014911 172 VADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:TIGR02142 174 LERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-221 |
3.06e-44 |
|
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: 155.69 E-value: 3.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 2 LKLNDVTWLY---QHLPMRFTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPA--QRPVSML 76
Cdd:COG4988 337 IELEDVSFSYpggRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAswRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 77 FQENNLFnHLTVRQNIGLGiHPGLklnreQRAQVTAIAGQMGMDTLLDRLP-------GE----LSGGQRQRAALARCLV 145
Cdd:COG4988 417 PQNPYLF-AGTIRENLRLG-RPDA-----SDEELEAALEAAGLDEFVAALPdgldtplGEggrgLSGGQAQRLALARALL 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1994014911 146 RQQPVLLLDEPFSALDPALRQEMLTLVADVCQRQqlTLLMVSHSVEDAARiAPRSIVVAEGRIAWDGATDDLLSGN 221
Cdd:COG4988 490 RDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
19-219 |
6.39e-44 |
|
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: 146.81 E-value: 6.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQRP---VSMLFQENNLFNHLTVRQNIGLG 95
Cdd:cd03224 20 SLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERAragIGYVPEGRRIFPELTVEENLLLG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 96 IHPGLKLNREQRaqvtaiagqmgMDTLLDRLP----------GELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALR 165
Cdd:cd03224 100 AYARRRAKRKAR-----------LERVYELFPrlkerrkqlaGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1994014911 166 QEMLTLVADVCqRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:cd03224 169 EEIFEAIRELR-DEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
18-219 |
2.35e-43 |
|
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: 154.99 E-value: 2.35e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 18 FTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQ--RPVSMLFQENNLFNHlTVRQNIGLG 95
Cdd:COG2274 494 ISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQIGVVLQDVFLFSG-TIRENITLG 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 96 iHPGLKLNR-EQRAQVTAIAG-----QMGMDTLLdrlpGE----LSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALR 165
Cdd:COG2274 573 -DPDATDEEiIEAARLAGLHDfiealPMGYDTVV----GEggsnLSGGQRQRLAIARALLRNPRILILDEATSALDAETE 647
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1994014911 166 QEMLTLVADVCQRQqlTLLMVSH---SVEDAARIaprsIVVAEGRIAWDGATDDLLS 219
Cdd:COG2274 648 AIILENLRRLLKGR--TVIIIAHrlsTIRLADRI----IVLDKGRIVEDGTHEELLA 698
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
18-207 |
3.72e-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: 143.29 E-value: 3.72e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 18 FTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQRP--VSMLFQENNLFNhLTVRQNIglg 95
Cdd:cd03228 21 VSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRknIAYVPQDPFLFS-GTIRENI--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 96 ihpglklnreqraqvtaiagqmgmdtlldrlpgeLSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVADV 175
Cdd:cd03228 97 ----------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRAL 142
|
170 180 190
....*....|....*....|....*....|....*
gi 1994014911 176 CQRQqlTLLMVSH---SVEDAARIaprsIVVAEGR 207
Cdd:cd03228 143 AKGK--TVIVIAHrlsTIRDADRI----IVLDDGR 171
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-224 |
7.63e-43 |
|
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: 145.23 E-value: 7.63e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 1 MLKLNDVTWLYQ--HLPMRFTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASG-SLLIDGEKHNTTPPAQ-RP---- 72
Cdd:COG1119 3 LLELRNVTVRRGgkTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWElRKrigl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 73 VSMLFQENnLFNHLTVRQ--------NIGLGIHPGlklnREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCL 144
Cdd:COG1119 83 VSPALQLR-FPRDETVLDvvlsgffdSIGLYREPT----DEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 145 VRQQPVLLLDEPFSALDPALRQEMLTLVADVCQRQQLTLLMVSHSVEDaarIAP---RSIVVAEGRIAWDGATDDLL-SG 220
Cdd:COG1119 158 VKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEE---IPPgitHVLLLKDGRVVAAGPKEEVLtSE 234
|
....
gi 1994014911 221 NSSA 224
Cdd:COG1119 235 NLSE 238
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-188 |
8.62e-43 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 143.77 E-value: 8.62e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 1 MLKLNDVT------WLYQHLpmrfTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGE-KHNTTPPAQRPV 73
Cdd:COG4133 2 MLEAENLScrrgerLLFSGL----SFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEpIRDAREDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 74 SMLFQENNLFNHLTVRQNigLGIHPGLKLNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLL 153
Cdd:COG4133 78 AYLGHADGLKPELTVREN--LRFWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190
....*....|....*....|....*....|....*
gi 1994014911 154 DEPFSALDPALRQEMLTLVADVCQRQQLtLLMVSH 188
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAAHLARGGA-VLLTTH 189
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-213 |
9.02e-43 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 144.04 E-value: 9.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 1 MLKLNDVTWLYQHLPMRF---TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQRP----- 72
Cdd:COG2884 1 MIRFENVSKRYPGGREALsdvSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPylrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 73 VSMLFQENNLFNHLTVRQNIGL-----GIHPglklnREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQ 147
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALplrvtGKSR-----KEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1994014911 148 QPVLLLDEPFSALDPALRQEMLTLVADVCQRqQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGA 213
Cdd:COG2884 156 PELLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRLVRDEA 220
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
19-217 |
7.54e-42 |
|
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: 141.93 E-value: 7.54e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLP-----PASGSLLIDGE---KHNTTPPA-QRPVSMLFQENNLFnHLTVR 89
Cdd:cd03260 20 SLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKdiyDLDVDVLElRRRVGMVFQKPNPF-PGSIY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 90 QNIGLG--IHpGLKLNREQRAQVTAIAGQMGM-DTLLDRL-PGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALR 165
Cdd:cd03260 99 DNVAYGlrLH-GIKLKEELDERVEEALRKAALwDEVKDRLhALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPIST 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1994014911 166 QEMLTLVADvcQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDL 217
Cdd:cd03260 178 AKIEELIAE--LKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
18-207 |
1.36e-41 |
|
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: 138.92 E-value: 1.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 18 FTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQ--RPVSMLFQennlfnhltvrqniglg 95
Cdd:cd00267 18 VSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElrRRIGYVPQ----------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 96 ihpglklnreqraqvtaiagqmgmdtlldrlpgeLSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVADV 175
Cdd:cd00267 81 ----------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLREL 126
|
170 180 190
....*....|....*....|....*....|..
gi 1994014911 176 CQRQQlTLLMVSHSVEDAARIAPRSIVVAEGR 207
Cdd:cd00267 127 AEEGR-TVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
18-218 |
1.51e-41 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 148.77 E-value: 1.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 18 FTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQ--RPVSMLFQENNLFnHLTVRQNIGLG 95
Cdd:COG1132 359 ISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIGVVPQDTFLF-SGTIRENIRYG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 96 ihpglklnREQ--RAQVTAIAGQMGMDTLLDRLP-------GE----LSGGQRQRAALARCLVRQQPVLLLDEPFSALDP 162
Cdd:COG1132 438 --------RPDatDEEVEEAAKAAQAHEFIEALPdgydtvvGErgvnLSGGQRQRIAIARALLKDPPILILDEATSALDT 509
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1994014911 163 ----ALRQEMLTLVADVcqrqqlTLLMVSH---SVEDAARIaprsIVVAEGRIAWDGATDDLL 218
Cdd:COG1132 510 eteaLIQEALERLMKGR------TTIVIAHrlsTIRNADRI----LVLDDGRIVEQGTHEELL 562
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
20-217 |
3.14e-41 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 143.71 E-value: 3.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 20 LSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQRPVSMLFQENNLFNHLTVRQNIGLGIHPg 99
Cdd:PRK11432 27 LTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQSYALFPHMSLGENVGYGLKM- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 100 LKLNREQRAQVTAIAGQM-GMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVADVCQR 178
Cdd:PRK11432 106 LGVPKEERKQRVKEALELvDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQ 185
|
170 180 190
....*....|....*....|....*....|....*....
gi 1994014911 179 QQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDL 217
Cdd:PRK11432 186 FNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
17-208 |
4.60e-41 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 139.56 E-value: 4.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 17 RFTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPP-AQRPVSMLFQENNLFNHLTVRQNigLG 95
Cdd:cd03263 20 DLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKaARQSLGYCPQFDALFDELTVREH--LR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 96 IHPGLK-LNREQ-RAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVA 173
Cdd:cd03263 98 FYARLKgLPKSEiKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLIL 177
|
170 180 190
....*....|....*....|....*....|....*
gi 1994014911 174 DVcqRQQLTLLMVSHSVEDAARIAPRSIVVAEGRI 208
Cdd:cd03263 178 EV--RKGRSIILTTHSMDEAEALCDRIAIMSDGKL 210
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-206 |
1.66e-40 |
|
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: 138.37 E-value: 1.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 20 LSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGeKHNTTPPAQRPVsmLFQENNLFNHLTVRQNIGLGIHPG 99
Cdd:TIGR01184 6 LTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEG-KQITEPGPDRMV--VFQNYSLLPWLTVRENIALAVDRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 100 LK-LNR-EQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVADVCQ 177
Cdd:TIGR01184 83 LPdLSKsERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQIWE 162
|
170 180
....*....|....*....|....*....
gi 1994014911 178 RQQLTLLMVSHSVEDAARIAPRSIVVAEG 206
Cdd:TIGR01184 163 EHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
19-219 |
4.17e-40 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 138.37 E-value: 4.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQ--RPVSMLFQENNLFNHLTVRQNIGLGI 96
Cdd:PRK13548 22 SLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAVLPQHSSLSFPFTVEEVVAMGR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 97 HPGLKLNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVR------QQPVLLLDEPFSALDPALRQEMLT 170
Cdd:PRK13548 102 APHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepdgPPRWLLLDEPTSALDLAHQHHVLR 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1994014911 171 LVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGA-----TDDLLS 219
Cdd:PRK13548 182 LARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTpaevlTPETLR 235
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
19-230 |
5.14e-40 |
|
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: 137.42 E-value: 5.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQRP---VSMLFQENNLFNHLTVRQNIGLG 95
Cdd:COG0410 23 SLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIArlgIGYVPEGRRIFPSLTVEENLLLG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 96 IHPGLKLNREQRAqvtaiagqmgMDTLLDRLP----------GELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALR 165
Cdd:COG0410 103 AYARRDRAEVRAD----------LERVYELFPrlkerrrqraGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIV 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1994014911 166 QEMLTLVADVcQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLSGNSSASALLGI 230
Cdd:COG0410 173 EEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEVREAYLGV 236
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
20-217 |
6.10e-40 |
|
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: 137.43 E-value: 6.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 20 LSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGE-----KHNTTPPAQRPVSMLFQENNLFNHLTVRQNI-- 92
Cdd:TIGR02315 23 LNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTditklRGKKLRKLRRRIGMIFQHYNLIERLTVLENVlh 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 93 -GLGIHPGLK-----LNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVrQQPVLLL-DEPFSALDPALR 165
Cdd:TIGR02315 103 gRLGYKPTWRsllgrFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALA-QQPDLILaDEPIASLDPKTS 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1994014911 166 QEMLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDL 217
Cdd:TIGR02315 182 KQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
19-208 |
7.06e-40 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 140.36 E-value: 7.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQRPVSMLFQENNLFNHLTVRQNIGLGihp 98
Cdd:PRK11650 24 DLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAMVFQNYALYPHMSVRENMAYG--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 99 gLKlNR-----EQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVA 173
Cdd:PRK11650 101 -LK-IRgmpkaEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQ 178
|
170 180 190
....*....|....*....|....*....|....*
gi 1994014911 174 DVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRI 208
Cdd:PRK11650 179 RLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVA 213
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-218 |
9.45e-40 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 137.14 E-value: 9.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 1 MLKLNDVTWLYQHLPM--RFTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQ--RPVSML 76
Cdd:COG4604 1 MIEIKNVSKRYGGKVVldDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 77 FQENNLFNHLTVRQNIGLGIHP---GlKLNREQRAQV-TAIAgQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLL 152
Cdd:COG4604 81 RQENHINSRLTVRELVAFGRFPyskG-RLTAEDREIIdEAIA-YLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1994014911 153 LDEPFSALDPALRQEMLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLL 218
Cdd:COG4604 159 LDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEII 224
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
19-217 |
1.05e-39 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 139.83 E-value: 1.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQRPVSMLFQENNLFNHLTVRQNIGLGIHp 98
Cdd:PRK10851 22 SLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQHYALFRHMTVFDNIAFGLT- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 99 glKLNREQR-------AQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTL 171
Cdd:PRK10851 101 --VLPRRERpnaaaikAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRW 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1994014911 172 VADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDL 217
Cdd:PRK10851 179 LRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
20-219 |
3.28e-39 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 136.01 E-value: 3.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 20 LSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQ----RPVsmLFQENNLFNHLTVRQNIGLG 95
Cdd:COG4559 22 LTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElarrRAV--LPQHSSLAFPFTVEEVVALG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 96 IHPGLKLNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCL------VRQQP-VLLLDEPFSALDPALRQEM 168
Cdd:COG4559 100 RAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqlwepVDGGPrWLFLDEPTSALDLAHQHAV 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1994014911 169 LTLVADVCqRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:COG4559 180 LRLARQLA-RRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLT 229
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
19-212 |
7.18e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 135.95 E-value: 7.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDG----EKHNTTPPAQRPVSMLFQ--ENNLFNHlTVRQNI 92
Cdd:PRK13637 27 NIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditDKKVKLSDIRKKVGLVFQypEYQLFEE-TIEKDI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 93 GLG-IHPGLK----LNREQRAQvtAIAGqMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQE 167
Cdd:PRK13637 106 AFGpINLGLSeeeiENRVKRAM--NIVG-LDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDE 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1994014911 168 MLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDG 212
Cdd:PRK13637 183 ILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQG 227
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
19-218 |
5.54e-38 |
|
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: 131.90 E-value: 5.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPP---AQRPVSMLFQENNLFNHLTVRQNIgLG 95
Cdd:cd03218 20 SLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhkrARLGIGYLPQEASIFRKLTVEENI-LA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 96 IHPGLKLNREQRAQ-VTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVAD 174
Cdd:cd03218 99 VLEIRGLSKKEREEkLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKI 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1994014911 175 VCQRqQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLL 218
Cdd:cd03218 179 LKDR-GIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-206 |
6.87e-38 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 132.52 E-value: 6.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 1 MLKLNDVTWLYQHLPM--RFTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGeKHNTTPPAQRPVsmLFQ 78
Cdd:PRK11248 1 MLQISHLYADYGGKPAleDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG-KPVEGPGAERGV--VFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 79 ENNLFNHLTVRQNIGLGihpgLKLNREQRAQVTAIAGQM----GMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLD 154
Cdd:PRK11248 78 NEGLLPWRNVQDNVAFG----LQLAGVEKMQRLEIAHQMlkkvGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1994014911 155 EPFSALDPALRQEMLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEG 206
Cdd:PRK11248 154 EPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
19-208 |
7.89e-38 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 135.62 E-value: 7.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGErIAVL-GPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQ------RPVSMLFQENNLFNHLTVRQN 91
Cdd:COG4175 47 SFDVEEGE-IFVImGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKElrelrrKKMSMVFQHFALLPHRTVLEN 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 92 IGLGihpgLKL------NREQRAQvTAIAgQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALR 165
Cdd:COG4175 126 VAFG----LEIqgvpkaERRERAR-EALE-LVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIR 199
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1994014911 166 QEM----LTLVadvcQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRI 208
Cdd:COG4175 200 REMqdelLELQ----AKLKKTIVFITHDLDEALRLGDRIAIMKDGRI 242
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
19-208 |
8.34e-38 |
|
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: 130.99 E-value: 8.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGE-----KHNTTPPAQRPVSMLFQENNLFNHLTVRQNIG 93
Cdd:cd03292 21 NISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQdvsdlRGRAIPYLRRKIGVVFQDFRLLPDRNVYENVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 94 LGIHPGLKLNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVA 173
Cdd:cd03292 101 FALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLK 180
|
170 180 190
....*....|....*....|....*....|....*
gi 1994014911 174 DVCQRqQLTLLMVSHSVEDAARIAPRSIVVAEGRI 208
Cdd:cd03292 181 KINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-211 |
1.93e-37 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 131.36 E-value: 1.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 18 FTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQRP--VSMLFQennlfN-------HLTV 88
Cdd:COG1101 25 LNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAkyIGRVFQ-----DpmmgtapSMTI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 89 RQNIGL----GIHPGLK--LNREQRAQVTAIAGQMGMDtLLDRLP---GELSGGQRQRAALARCLVRQQPVLLLDEPFSA 159
Cdd:COG1101 100 EENLALayrrGKRRGLRrgLTKKRRELFRELLATLGLG-LENRLDtkvGLLSGGQRQALSLLMATLTKPKLLLLDEHTAA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1994014911 160 LDPALRQEMLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWD 211
Cdd:COG1101 179 LDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIILD 230
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-212 |
3.18e-37 |
|
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: 129.80 E-value: 3.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 1 MLKLNDVTWLYQHLPMRF------TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTP-PAQRPV 73
Cdd:cd03266 1 MITADALTKRFRDVKKTVqavdgvSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPaEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 74 SMLFQENNLFNHLTVRQNIGL--GIHpGLKlNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVL 151
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYfaGLY-GLK-GDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1994014911 152 LLDEPFSALDPALRQEMLTLVADVCqRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDG 212
Cdd:cd03266 159 LLDEPTTGLDVMATRALREFIRQLR-ALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
19-219 |
6.30e-37 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 132.12 E-value: 6.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQ-----RPVSMLFQENNLFNHLTVRQNIG 93
Cdd:COG1135 25 SLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraarRKIGMIFQHFNLLSSRTVAENVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 94 LgihPgLKLN----REQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEML 169
Cdd:COG1135 105 L---P-LEIAgvpkAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSIL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1994014911 170 TLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:COG1135 181 DLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFA 230
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
19-208 |
2.04e-36 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 128.21 E-value: 2.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTL---LNLIAGflpPASGSLLIDGEKHN-TTPPA-------QRPVSMLFQENNLFNHLT 87
Cdd:PRK11124 22 TLDCPQGETLVLLGPSGAGKSSLlrvLNLLEM---PRSGTLNIAGNHFDfSKTPSdkairelRRNVGMVFQQYNLWPHLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 88 VRQNIGLGIHPGLKLNREQ-RAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQ 166
Cdd:PRK11124 99 VQQNLIEAPCRVLGLSKDQaLARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1994014911 167 EMLTLVADVcQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRI 208
Cdd:PRK11124 179 QIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
20-219 |
4.35e-36 |
|
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: 127.93 E-value: 4.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 20 LSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGekHNTTPPAQ-----RPVSMLFQeN--NLFNHLTVRQNI 92
Cdd:TIGR04520 23 LSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENlweirKKVGMVFQ-NpdNQFVGATVEDDV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 93 GLGIHpGLKLNREQ-RAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTL 171
Cdd:TIGR04520 100 AFGLE-NLGVPREEmRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLET 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1994014911 172 VADVCQRQQLTLLMVSHSVEDAARiAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:TIGR04520 179 IRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFS 225
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
19-208 |
5.82e-36 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 127.05 E-value: 5.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHN--TTPPAQ------RPVSMLFQENNLFNHLTVRQ 90
Cdd:COG4161 22 NLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsQKPSEKairllrQKVGMVFQQYNLWPHLTVME 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 91 NIGLGIHPGLKLNREQ-RAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEML 169
Cdd:COG4161 102 NLIEAPCKVLGLSKEQaREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVV 181
|
170 180 190
....*....|....*....|....*....|....*....
gi 1994014911 170 TLVADVCQrQQLTLLMVSHSVEDAARIAPRSIVVAEGRI 208
Cdd:COG4161 182 EIIRELSQ-TGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
20-219 |
1.76e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 127.06 E-value: 1.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 20 LSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSL-----LIDGEKHNTT-PPAQRPVSMLFQ--ENNLFNHlTVRQN 91
Cdd:PRK13634 28 VSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVtigerVITAGKKNKKlKPLRKKVGIVFQfpEHQLFEE-TVEKD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 92 IGLG-IHPGLKlNREQRAQVTAIAGQMGMD-TLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEML 169
Cdd:PRK13634 107 ICFGpMNFGVS-EEDAKQKAREMIELVGLPeELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMM 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1994014911 170 TLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:PRK13634 186 EMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFA 235
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
19-199 |
2.64e-35 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 123.88 E-value: 2.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEkhnttppaqRPVSMLFQENNLFNHL--TVRQNIGLGI 96
Cdd:NF040873 12 DLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG---------ARVAYVPQRSEVPDSLplTVRDLVAMGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 97 --HPGL--KLNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:NF040873 83 waRRGLwrRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALL 162
|
170 180
....*....|....*....|....*..
gi 1994014911 173 ADVCqRQQLTLLMVSHSVEDAARIAPR 199
Cdd:NF040873 163 AEEH-ARGATVVVVTHDLELVRRADPC 188
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
19-224 |
5.52e-35 |
|
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: 131.14 E-value: 5.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPA--QRPVSMLFQENNLFnHLTVRQNIGLGi 96
Cdd:TIGR03375 485 SLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPAdlRRNIGYVPQDPRLF-YGTLRDNIALG- 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 97 hpglklnreqRAQVT-----AIAGQMGMDTLLDRLP-------GE----LSGGQRQRAALARCLVRQQPVLLLDEPFSAL 160
Cdd:TIGR03375 563 ----------APYADdeeilRAAELAGVTEFVRRHPdgldmqiGErgrsLSGGQRQAVALARALLRDPPILLLDEPTSAM 632
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1994014911 161 DPALRQEMLTLVADVCQRQqlTLLMVSH--SVEDaarIAPRSIVVAEGRIAWDGATDDLLSGNSSA 224
Cdd:TIGR03375 633 DNRSEERFKDRLKRWLAGK--TLVLVTHrtSLLD---LVDRIIVMDNGRIVADGPKDQVLEALRKG 693
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-217 |
6.05e-35 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 129.75 E-value: 6.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQ---RPVSMLFQENNLFNHLTVRQNIGLG 95
Cdd:COG1129 24 SLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaqaAGIAIIHQELNLVPNLSVAENIFLG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 96 IHP--GLKLN-REQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:COG1129 104 REPrrGGLIDwRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRII 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1994014911 173 ADVcQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDL 217
Cdd:COG1129 184 RRL-KAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-208 |
1.59e-34 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 124.36 E-value: 1.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHN--TTPPAQRPVSMLFQE-NNLFNHLTVRQNIGLG 95
Cdd:PRK13635 27 SFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSeeTVWDVRRQVGMVFQNpDNQFVGATVQDDVAFG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 96 IHpglklNR-----EQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLT 170
Cdd:PRK13635 107 LE-----NIgvpreEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLE 181
|
170 180 190
....*....|....*....|....*....|....*...
gi 1994014911 171 LVADVCQRQQLTLLMVSHSVEDAARiAPRSIVVAEGRI 208
Cdd:PRK13635 182 TVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEI 218
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
18-221 |
1.90e-34 |
|
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: 123.11 E-value: 1.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 18 FTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGekHN----TTPPAQRPVSMLFQENNLFNHlTVRQNIG 93
Cdd:cd03251 21 ISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDG--HDvrdyTLASLRRQIGLVSQDVFLFND-TVAENIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 94 LGIHpglklnREQRAQVTAIAGQMGMDTLLDRLP-------GE----LSGGQRQRAALARCLVRQQPVLLLDEPFSALDp 162
Cdd:cd03251 98 YGRP------GATREEVEEAARAANAHEFIMELPegydtviGErgvkLSGGQRQRIAIARALLKDPPILILDEATSALD- 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1994014911 163 aLRQEMltLVADVCQR--QQLTLLMVSH---SVEDAARIaprsIVVAEGRIAWDGATDDLLSGN 221
Cdd:cd03251 171 -TESER--LVQAALERlmKNRTTFVIAHrlsTIENADRI----VVLEDGKIVERGTHEELLAQG 227
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
20-215 |
2.42e-34 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 123.25 E-value: 2.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 20 LSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIdgekhNTTP--PAQRPVSMLFQENNLFNHLTVRQNIGLGih 97
Cdd:PRK11247 33 LHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLA-----GTAPlaEAREDTRLMFQDARLLPWKKVIDNVGLG-- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 98 pgLKLN-REQRAQVTAIAGqmgmdtLLDRL---PGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVA 173
Cdd:PRK11247 106 --LKGQwRDAALQALAAVG------LADRAnewPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1994014911 174 DVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATD 215
Cdd:PRK11247 178 SLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLTVD 219
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
19-222 |
4.73e-34 |
|
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: 122.21 E-value: 4.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPA--QRPVSMLFQENNLFNHlTVRQNIGLGi 96
Cdd:cd03252 22 SLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQVGVVLQENVLFNR-SIRDNIALA- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 97 HPGLKLNREQRAQVTAIAGQM------GMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLT 170
Cdd:cd03252 100 DPGMSMERVIEAAKLAGAHDFiselpeGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMR 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1994014911 171 LVADVCQRQqlTLLMVSHSVEdAARIAPRSIVVAEGRIAWDGATDDLLSGNS 222
Cdd:cd03252 180 NMHDICAGR--TVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELLAENG 228
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
19-215 |
8.51e-34 |
|
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: 121.00 E-value: 8.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQRP------VSMLFQENNLFNHLTVRQNI 92
Cdd:COG4181 32 SLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARArlrarhVGFVFQSFQLLPTLTALENV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 93 GLgihPgLKL--NREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLT 170
Cdd:COG4181 112 ML---P-LELagRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIID 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1994014911 171 LVADVCQRQQLTLLMVSHSVEDAARiAPRSIVVAEGRIAWDGATD 215
Cdd:COG4181 188 LLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTAAT 231
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
18-203 |
1.03e-33 |
|
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: 126.63 E-value: 1.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 18 FTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPA--QRPVSMLFQENNLFNHlTVRQNIGLG 95
Cdd:TIGR02857 341 VSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADswRDQIAWVPQHPFLFAG-TIAENIRLA 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 96 iHPGLKLNREQRAQVTAIAGQM------GMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEML 169
Cdd:TIGR02857 420 -RPDASDAEIREALERAGLDEFvaalpqGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVL 498
|
170 180 190
....*....|....*....|....*....|....
gi 1994014911 170 TLVADVCQRQqlTLLMVSHSVEDAARiAPRSIVV 203
Cdd:TIGR02857 499 EALRALAQGR--TVLLVTHRLALAAL-ADRIVVL 529
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
18-218 |
3.14e-33 |
|
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: 119.64 E-value: 3.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 18 FTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQ--RPVSMLFQENNLFNHlTVRQNIGLG 95
Cdd:cd03254 22 INFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrSMIGVVLQDTFLFSG-TIMENIRLG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 96 ihpglkLNREQRAQVTAIAGQMGMDTLLDRLP-----------GELSGGQRQRAALARCLVRQQPVLLLDEPFSALDP-- 162
Cdd:cd03254 101 ------RPNATDEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTet 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1994014911 163 --ALRQEMLTLvadvcqRQQLTLLMVSH---SVEDAARIaprsIVVAEGRIAWDGATDDLL 218
Cdd:cd03254 175 ekLIQEALEKL------MKGRTSIIIAHrlsTIKNADKI----LVLDDGKIIEEGTHDELL 225
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-212 |
3.34e-33 |
|
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: 118.18 E-value: 3.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 2 LKLNDVTWLY----QHLPMRFTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQRP-VSML 76
Cdd:cd03247 1 LSINNVSFSYpeqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSlISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 77 FQENNLFNHlTVRQNIGLgihpglklnreqraqvtaiagqmgmdtlldrlpgELSGGQRQRAALARCLVRQQPVLLLDEP 156
Cdd:cd03247 81 NQRPYLFDT-TLRNNLGR----------------------------------RFSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1994014911 157 FSALDPALRQEMLTLVADVCQRQqlTLLMVSH---SVEDAARIaprsIVVAEGRIAWDG 212
Cdd:cd03247 126 TVGLDPITERQLLSLIFEVLKDK--TLIWITHhltGIEHMDKI----LFLENGKIIMQG 178
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
29-208 |
3.67e-33 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 122.29 E-value: 3.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 29 AVLGPSGAGKSTLLNLIAGFLPPASGS------LLIDGEKHNTTPPAQRPVSMLFQENNLFNHLTVRQNIGLGIhpglkl 102
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRivlngrVLFDAEKGICLPPEKRRIGYVFQDARLFPHYKVRGNLRYGM------ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 103 NREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVADVCQRQQLT 182
Cdd:PRK11144 102 AKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIP 181
|
170 180
....*....|....*....|....*.
gi 1994014911 183 LLMVSHSVEDAARIAPRSIVVAEGRI 208
Cdd:PRK11144 182 ILYVSHSLDEILRLADRVVVLEQGKV 207
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
20-219 |
4.02e-33 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 119.75 E-value: 4.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 20 LSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEkhNTTP-P----AQRPVSMLFQENNLFNHLTVRQNIgL 94
Cdd:COG1137 24 LEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGE--DITHlPmhkrARLGIGYLPQEASIFRKLTVEDNI-L 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 95 GIHPGLKLNREQRAQ-VTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVA 173
Cdd:COG1137 101 AVLELRKLSKKEREErLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIR 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1994014911 174 DVCQRqQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:COG1137 181 HLKER-GIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILN 225
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
19-212 |
6.22e-33 |
|
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: 118.46 E-value: 6.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPA--QRPVSMLFQENNLFNHlTVRQNIGLGi 96
Cdd:cd03245 24 SLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAdlRRNIGYVPQDVTLFYG-TLRDNITLG- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 97 HPGLKLNREQRAQVTAiagqmGMDTLLDRLP-------GE----LSGGQRQRAALARCLVRQQPVLLLDEPFSALDPA-- 163
Cdd:cd03245 102 APLADDERILRAAELA-----GVTDFVNKHPngldlqiGErgrgLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNse 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1994014911 164 --LRQEMLTLVADVcqrqqlTLLMVSHSVEdAARIAPRSIVVAEGRIAWDG 212
Cdd:cd03245 177 erLKERLRQLLGDK------TLIIITHRPS-LLDLVDRIIVMDSGRIVADG 220
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
4-222 |
8.19e-33 |
|
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: 118.87 E-value: 8.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 4 LNDVTWLYQhlPMRFTL-----SVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGE--KHNTTPPAQRPVSML 76
Cdd:cd03253 3 FENVTFAYD--PGRPVLkdvsfTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQdiREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 77 FQENNLFNHlTVRQNIGLGihpGLKLNREqraQVTAIAGQMGMDTLLDRLP-------GE----LSGGQRQRAALARCLV 145
Cdd:cd03253 81 PQDTVLFND-TIGYNIRYG---RPDATDE---EVIEAAKAAQIHDKIMRFPdgydtivGErglkLSGGEKQRVAIARAIL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 146 RQQPVLLLDEPFSALDPALRQEMLTLVADVCQRQqlTLLMVSH---SVEDAARIaprsIVVAEGRIAWDGATDDLLSGNS 222
Cdd:cd03253 154 KNPPILLLDEATSALDTHTEREIQAALRDVSKGR--TTIVIAHrlsTIVNADKI----IVLKDGRIVERGTHEELLAKGG 227
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
28-212 |
8.32e-33 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 118.06 E-value: 8.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 28 IAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPA-QRPVSMLFQENNLFNHLTVRQ---NIGL--GIHPglk 101
Cdd:cd03264 28 YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKlRRRIGYLPQEFGVYPNFTVREfldYIAWlkGIPS--- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 102 lnREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVADVCQRQql 181
Cdd:cd03264 105 --KEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDR-- 180
|
170 180 190
....*....|....*....|....*....|.
gi 1994014911 182 TLLMVSHSVEDAARIAPRSIVVAEGRIAWDG 212
Cdd:cd03264 181 IVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-219 |
1.79e-32 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 120.29 E-value: 1.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 1 MLKLNDVTWLYQHLPMRFT------LSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPP-----A 69
Cdd:PRK11153 1 MIELKNISKVFPQGGRTIHalnnvsLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEkelrkA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 70 QRPVSMLFQENNLFNHLTVRQNIGLgihPgLKLNREQRAQVTAIAGQM----GMDTLLDRLPGELSGGQRQRAALARCLV 145
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVAL---P-LELAGTPKAEIKARVTELlelvGLSDKADRYPAQLSGGQKQRVAIARALA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1994014911 146 RQQPVLLLDEPFSALDPALRQEMLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:PRK11153 157 SNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFS 230
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-219 |
3.44e-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: 122.49 E-value: 3.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTL----LNLIagflpPASGSLLIDGEK-HNTTPPAQRP----VSMLFQE--NNLFNHLT 87
Cdd:COG4172 306 SLTLRRGETLGLVGESGSGKSTLglalLRLI-----PSEGEIRFDGQDlDGLSRRALRPlrrrMQVVFQDpfGSLSPRMT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 88 VRQNI--GLGIH-PGLKLnREQRAQVTAIAGQMGMD-TLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPA 163
Cdd:COG4172 381 VGQIIaeGLRVHgPGLSA-AERRARVAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVS 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1994014911 164 LRQEMLTLVADVCQRQQLTLLMVSH--SVEDAarIAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:COG4172 460 VQAQILDLLRDLQREHGLAYLFISHdlAVVRA--LAHRVMVMKDGKVVEQGPTEQVFD 515
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
20-226 |
5.46e-32 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 120.33 E-value: 5.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 20 LSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEK-HNTTP-PAQRPVSMLFQENNLFNHLTVRQNIGLGIH 97
Cdd:PRK09536 24 LSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDvEALSArAASRRVASVPQDTSLSFEFDVRQVVEMGRT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 98 PGL-KLNREQRAQVTAIAGQM---GMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVA 173
Cdd:PRK09536 104 PHRsRFDTWTETDRAAVERAMertGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVR 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1994014911 174 DVCQRQQlTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLSGNSSASA 226
Cdd:PRK09536 184 RLVDDGK-TAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAA 235
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
19-219 |
5.89e-32 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 120.14 E-value: 5.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQ------RPVSMLFQENNLFNHLTVRQNI 92
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevrrKKIAMVFQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 93 GLGIHPGLKLNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:PRK10070 128 AFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDEL 207
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1994014911 173 ADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:PRK10070 208 VKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
20-224 |
1.22e-31 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 116.44 E-value: 1.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 20 LSVERGERIAVLGPSGAGKSTLLNLIaGFLP-PASGSLLIDGE-------KHNTTPPAQRP--------VSMLFQENNLF 83
Cdd:COG4598 29 LTARKGDVISIIGSSGSGKSTFLRCI-NLLEtPDSGEIRVGGEeirlkpdRDGELVPADRRqlqrirtrLGMVFQSFNLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 84 NHLTVRQNIGLG-IHPgLKLNReqrAQVTAIAGQM----GMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFS 158
Cdd:COG4598 108 SHMTVLENVIEApVHV-LGRPK---AEAIERAEALlakvGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTS 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1994014911 159 ALDPALRQEMLTLVadvcqrQQL-----TLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLSGNSSA 224
Cdd:COG4598 184 ALDPELVGEVLKVM------RDLaeegrTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPKSE 248
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
20-219 |
2.11e-31 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 115.62 E-value: 2.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 20 LSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSL-----LIDGEKHNTTPPAQ-----RPVSMLFQENNLFNHLTVR 89
Cdd:PRK11264 24 LEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTARSLSQQKGLirqlrQHVGFVFQNFNLFPHRTVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 90 QNIglgIHPGLKLNREQRAQVTAIAGQM----GMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALR 165
Cdd:PRK11264 104 ENI---IEGPVIVKGEPKEEATARARELlakvGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELV 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1994014911 166 QEMLTLVADVCQRQQlTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:PRK11264 181 GEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFA 233
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
19-219 |
2.50e-31 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 115.50 E-value: 2.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQ--RPVSMLFQENNLFNHLTVRQNIGLGI 96
Cdd:PRK11231 22 SLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlaRRLALLPQHHLTPEGITVRELVAYGR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 97 HPGL----KLNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:PRK11231 102 SPWLslwgRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLM 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1994014911 173 ADVcQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:PRK11231 182 REL-NTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
19-219 |
2.90e-31 |
|
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: 116.69 E-value: 2.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPP---ASGSLLIDGEKHNTTPPAQ------RPVSMLFQE-----NNLFn 84
Cdd:COG0444 25 SFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKElrkirgREIQMIFQDpmtslNPVM- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 85 hlTVRQNIG--LGIHPGLKlNREQRAQVTAIAGQMGMDT---LLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSA 159
Cdd:COG0444 104 --TVGDQIAepLRIHGGLS-KAEARERAIELLERVGLPDperRLDRYPHELSGGMRQRVMIARALALEPKLLIADEPTTA 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1994014911 160 LDPALRQEMLTLVADVCQRQQLTLLMVSHSVEDAARIAPRsIVV--AeGRIAWDGATDDLLS 219
Cdd:COG0444 181 LDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADR-VAVmyA-GRIVEEGPVEELFE 240
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-218 |
3.29e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 115.47 E-value: 3.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 1 MLKLNDVTWLY--QHLPM--RFTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHN--TTPPAQRPVS 74
Cdd:PRK13632 7 MIKVENVSFSYpnSENNAlkNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISkeNLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 75 MLFQE-NNLFNHLTVRQNIGLGIHpGLKLNREQ-RAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLL 152
Cdd:PRK13632 87 IIFQNpDNQFIGATVEDDIAFGLE-NKKVPPKKmKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIII 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1994014911 153 LDEPFSALDPALRQEMLTLVADVCQRQQLTLLMVSHSVEDAArIAPRSIVVAEGRIAWDGATDDLL 218
Cdd:PRK13632 166 FDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEIL 230
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
19-203 |
5.88e-31 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 118.59 E-value: 5.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQ---RPVSMLFQENNLFNHLTVRQNIGLG 95
Cdd:COG3845 25 SLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaiaLGIGMVHQHFMLVPNLTVAENIVLG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 96 IHP--GLKLNREQ-RAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:COG3845 105 LEPtkGGRLDRKAaRARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEIL 184
|
170 180 190
....*....|....*....|....*....|.
gi 1994014911 173 ADVCqRQQLTLLMVSHSVEDAARIAPRsIVV 203
Cdd:COG3845 185 RRLA-AEGKSIIFITHKLREVMAIADR-VTV 213
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-208 |
6.02e-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: 113.72 E-value: 6.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 2 LKLNDVTWLYQHLPMR-----FTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGE-----KHNTTppaQR 71
Cdd:cd03248 12 VKFQNVTFAYPTRPDTlvlqdVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpisqyEHKYL---HS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 72 PVSMLFQENNLFNHlTVRQNIGLGIhPGLKLNREQRAQVTAIAG------QMGMDTLLDRLPGELSGGQRQRAALARCLV 145
Cdd:cd03248 89 KVSLVGQEPVLFAR-SLQDNIAYGL-QSCSFECVKEAAQKAHAHsfiselASGYDTEVGEKGSQLSGGQKQRVAIARALI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1994014911 146 RQQPVLLLDEPFSALDPALRQEMLTLVADVCQRQqlTLLMVSH---SVEDAARIaprsIVVAEGRI 208
Cdd:cd03248 167 RNPQVLILDEATSALDAESEQQVQQALYDWPERR--TVLVIAHrlsTVERADQI----LVLDGGRI 226
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
19-217 |
7.20e-31 |
|
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: 113.23 E-value: 7.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGekHNTTPPA---QRPVSMLFQENNLFNHLTVRQNigLG 95
Cdd:cd03265 20 SFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG--HDVVREPrevRRRIGIVFQDLSVDDELTGWEN--LY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 96 IHP---GLKlNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:cd03265 96 IHArlyGVP-GAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYI 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1994014911 173 ADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDL 217
Cdd:cd03265 175 EKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
19-208 |
1.49e-30 |
|
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: 111.97 E-value: 1.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKhntTPPAQRPVSMLFQENNLFNHL---TVRQNIGLG 95
Cdd:cd03226 20 SLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP---IKAKERRKSIGYVMQDVDYQLftdSVREELLLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 96 ihpgLKLNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVADv 175
Cdd:cd03226 97 ----LKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRE- 171
|
170 180 190
....*....|....*....|....*....|...
gi 1994014911 176 CQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRI 208
Cdd:cd03226 172 LAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-219 |
8.72e-30 |
|
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: 111.09 E-value: 8.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 18 FTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQ--RPVSMLFQENNLFNhLTVRQNIGLG 95
Cdd:cd03249 22 LSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlrSQIGLVSQEPVLFD-GTIAENIRYG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 96 IHPGLKLNREQRAQVTA----IAGQM-GMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALD---PALRQE 167
Cdd:cd03249 101 KPDATDEEVEEAAKKANihdfIMSLPdGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDaesEKLVQE 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1994014911 168 MLTLVadvcqRQQLTLLMVSH---SVEDAARIaprsIVVAEGRIAWDGATDDLLS 219
Cdd:cd03249 181 ALDRA-----MKGRTTIVIAHrlsTIRNADLI----AVLQNGQVVEQGTHDELMA 226
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
19-217 |
9.52e-30 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 111.78 E-value: 9.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTP-----PAQRPVSMLFQENNLFNHLTVRQNIG 93
Cdd:PRK11831 27 SLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsrlyTVRKRMSMLFQSGALFTDMNVFDNVA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 94 LGIHPGLKLNRE-QRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:PRK11831 107 YPLREHTQLPAPlLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLI 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1994014911 173 ADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDL 217
Cdd:PRK11831 187 SELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-211 |
1.10e-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: 108.28 E-value: 1.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPA---QRPVSMLFQennlfnhltvrqniglg 95
Cdd:cd03216 20 SLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRdarRAGIAMVYQ----------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 96 ihpglklnreqraqvtaiagqmgmdtlldrlpgeLSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVADV 175
Cdd:cd03216 83 ----------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRL 128
|
170 180 190
....*....|....*....|....*....|....*.
gi 1994014911 176 cQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWD 211
Cdd:cd03216 129 -RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
18-221 |
2.51e-29 |
|
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: 114.81 E-value: 2.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 18 FTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGE--KHNTTPPAQRPVSMLFQENNLFNHlTVRQNIGLG 95
Cdd:TIGR02203 351 ISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHdlADYTLASLRRQVALVSQDVVLFND-TIANNIAYG 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 96 ihpglKLNREQRAQVTAIAGQMGMDTLLDRLP-----------GELSGGQRQRAALARCLVRQQPVLLLDEPFSALDpal 164
Cdd:TIGR02203 430 -----RTEQADRAEIERALAAAYAQDFVDKLPlgldtpigengVLLSGGQRQRLAIARALLKDAPILILDEATSALD--- 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1994014911 165 rQEMLTLVADVCQR--QQLTLLMVSH---SVEDAARIaprsIVVAEGRIAWDGATDDLLSGN 221
Cdd:TIGR02203 502 -NESERLVQAALERlmQGRTTLVIAHrlsTIEKADRI----VVMDDGRIVERGTHNELLARN 558
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
18-219 |
3.18e-29 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 111.59 E-value: 3.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 18 FTLsvERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQ-----RPVSMLFQenNLFNHLTVRQNI 92
Cdd:PRK11308 36 FTL--ERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqkllrQKIQIVFQ--NPYGSLNPRKKV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 93 G------LGIHPglKLNR-EQRAQVTAIAGQMGMDT-LLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPAL 164
Cdd:PRK11308 112 GqileepLLINT--SLSAaERREKALAMMAKVGLRPeHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSV 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1994014911 165 RQEMLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:PRK11308 190 QAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFN 244
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
9-228 |
3.28e-29 |
|
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: 110.28 E-value: 3.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 9 WLYQHLPM--RFTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQ-----RPVSMLFQEN- 80
Cdd:TIGR02769 19 GAKQRAPVltNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrrafrRDVQLVFQDSp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 81 NLFN-HLTVRQNIGLGIHPGLKLNR-EQRAQVTAIAGQMGMDT-LLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPF 157
Cdd:TIGR02769 99 SAVNpRMTVRQIIGEPLRHLTSLDEsEQKARIAELLDMVGLRSeDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAV 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1994014911 158 SALDPALRQEMLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLSGNSSASALL 228
Cdd:TIGR02769 179 SNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLSFKHPAGRNL 249
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-212 |
5.10e-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: 108.07 E-value: 5.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 2 LKLNDVTWLYQHLPM--RFTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQRPVSMLFQE 79
Cdd:cd03268 1 LKTNDLTKTYGKKRVldDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 80 NNLFNHLTVRQNigLGIHPGLKLNREQRAQVtaIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSA 159
Cdd:cd03268 81 PGFYPNLTAREN--LRLLARLLGIRKKRIDE--VLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1994014911 160 LDPALRQEMLTLVADVcQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDG 212
Cdd:cd03268 157 LDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
19-217 |
8.95e-29 |
|
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: 109.79 E-value: 8.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGekHN-TTPPAQ--RPVSMLFQENNLFNHLTVRQNIGL- 94
Cdd:TIGR01188 13 NFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAG--YDvVREPRKvrRSIGIVPQYASVDEDLTGRENLEMm 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 95 GIHPGLKlNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVAD 174
Cdd:TIGR01188 91 GRLYGLP-KDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDYIRA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1994014911 175 VcQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDL 217
Cdd:TIGR01188 170 L-KEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
23-219 |
9.09e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 109.12 E-value: 9.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 23 ERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGE---KHNTTPpAQRPVSMLFQ--ENNLFNHlTVRQNIGLGih 97
Cdd:PRK13652 28 PRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitKENIRE-VRKFVGLVFQnpDDQIFSP-TVEQDIAFG-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 98 P-GLKLNREQRA-QVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVADV 175
Cdd:PRK13652 104 PiNLGLDEETVAhRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1994014911 176 CQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:PRK13652 184 PETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFL 227
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-208 |
1.11e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 109.05 E-value: 1.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 1 MLKLNDVTWLYQHLPMRFTLS-----VERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEK--HNTTPPAQRPV 73
Cdd:PRK13650 4 IIEVKNLTFKYKEDQEKYTLNdvsfhVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLltEENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 74 SMLFQE-NNLFNHLTVRQNIGLGI-HPGLKLnREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVL 151
Cdd:PRK13650 84 GMVFQNpDNQFVGATVEDDVAFGLeNKGIPH-EEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKII 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1994014911 152 LLDEPFSALDPALRQEMLTLVADVCQRQQLTLLMVSHSVEDAArIAPRSIVVAEGRI 208
Cdd:PRK13650 163 ILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQV 218
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
18-208 |
1.45e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 109.55 E-value: 1.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 18 FTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLID--------GEKHNTTPPAQRP----------VSMLFQ- 78
Cdd:PRK13631 45 ISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyigdkkNNHELITNPYSKKiknfkelrrrVSMVFQf 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 79 -ENNLFNHlTVRQNIGLGihP-GLKLNREQRAQVTAI-AGQMGMD-TLLDRLPGELSGGQRQRAALARCLVRQQPVLLLD 154
Cdd:PRK13631 125 pEYQLFKD-TIEKDIMFG--PvALGVKKSEAKKLAKFyLNKMGLDdSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFD 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1994014911 155 EPFSALDPALRQEMLTLVADvCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRI 208
Cdd:PRK13631 202 EPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKI 254
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
19-217 |
1.75e-28 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 109.44 E-value: 1.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQ-----RPVSMLFQenNLFNHL----TVR 89
Cdd:COG4608 38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRElrplrRRMQMVFQ--DPYASLnprmTVG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 90 QNIG--LGIHpGLKLNREQRAQVTAIAGQMGMDT-LLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQ 166
Cdd:COG4608 116 DIIAepLRIH-GLASKAERRERVAELLELVGLRPeHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQA 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1994014911 167 EMLTLVADVCQRQQLTLLMVSH--SVedaAR-IAPRSIVVAEGRIAWDGATDDL 217
Cdd:COG4608 195 QVLNLLEDLQDELGLTYLFISHdlSV---VRhISDRVAVMYLGKIVEIAPRDEL 245
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
19-228 |
2.63e-28 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 107.85 E-value: 2.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQ-----RPVSMLFQEN-NLFN-HLTVRQN 91
Cdd:PRK10419 32 SLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQrkafrRDIQMVFQDSiSAVNpRKTVREI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 92 IGLGIHPGLKLNR-EQRAQVTAIAGQMGMD-TLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEML 169
Cdd:PRK10419 112 IREPLRHLLSLDKaERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVI 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1994014911 170 TLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLSGNSSASALL 228
Cdd:PRK10419 192 RLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLTFSSPAGRVL 250
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-219 |
3.92e-28 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 111.46 E-value: 3.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 2 LKLNDVTWLYQHLPM----RFTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQ--RPVSM 75
Cdd:PRK11160 339 LTLNNVSFTYPDQPQpvlkGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAlrQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 76 LFQENNLFNHlTVRQNIGLGIHpglklnREQRAQVTAIAGQMGMDTLLDRLPG----------ELSGGQRQRAALARCLV 145
Cdd:PRK11160 419 VSQRVHLFSA-TLRDNLLLAAP------NASDEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGIARALL 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1994014911 146 RQQPVLLLDEPFSALDPALRQEMLTLVADVCQRQqlTLLMVSH---SVEDAARIaprsIVVAEGRIAWDGATDDLLS 219
Cdd:PRK11160 492 HDAPLLLLDEPTEGLDAETERQILELLAEHAQNK--TVLMITHrltGLEQFDRI----CVMDNGQIIEQGTHQELLA 562
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
20-214 |
4.35e-28 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 107.02 E-value: 4.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 20 LSVERGERIAVLGPSGAGKSTLLN----LIAGFLPPASGSLLI------DGEKHNTTPPAQRPVSMLFQENNLFNHLTVR 89
Cdd:PRK09984 25 LNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGSHIELLgrtvqrEGRLARDIRKSRANTGYIFQQFNLVNRLSVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 90 QNI---GLGIHPGLK-----LNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALD 161
Cdd:PRK09984 105 ENVligALGSTPFWRtcfswFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLD 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1994014911 162 PALRQEMLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGAT 214
Cdd:PRK09984 185 PESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSS 237
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
15-228 |
4.51e-28 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 111.09 E-value: 4.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 15 PMRFTLSveRGERIAVLGPSGAGKSTLLNLIAGFLpPASGSLLIDGEKHNTTPPAQ--RPVSMLFQENNLFnHLTVRQNI 92
Cdd:PRK11174 368 PLNFTLP--AGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESwrKHLSWVGQNPQLP-HGTLRDNV 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 93 GLGIHpglKLNREQ------RAQVTAIAGQM--GMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPAL 164
Cdd:PRK11174 444 LLGNP---DASDEQlqqaleNAWVSEFLPLLpqGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHS 520
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1994014911 165 RQEMLTLVADVCQRQqlTLLMVSHSVEDAARIaPRSIVVAEGRIAWDGATDDLLSGNSSASALL 228
Cdd:PRK11174 521 EQLVMQALNAASRRQ--TTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAGGLFATLL 581
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
19-189 |
4.61e-28 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 110.91 E-value: 4.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQ--RPVSMLFQENNLFnHLTVRQNIGLGi 96
Cdd:TIGR02868 355 SLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEvrRRVSVCAQDAHLF-DTTVRENLRLA- 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 97 hpglklnREQ--RAQVTAIAGQMGMDTLLDRLPG-----------ELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPA 163
Cdd:TIGR02868 433 -------RPDatDEELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPTEHLDAE 505
|
170 180
....*....|....*....|....*.
gi 1994014911 164 LRQEMLTLVADVCQRqqLTLLMVSHS 189
Cdd:TIGR02868 506 TADELLEDLLAALSG--RTVVLITHH 529
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
18-219 |
5.41e-28 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 106.99 E-value: 5.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 18 FTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGE--KHNTTPPAQRPVSMLFQENNLFNHLTVRQNIGLG 95
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEhiQHYASKEVARRIGLLAQNATTPGDITVQELVARG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 96 IHPGLKL-NREQRAQVTAIAGQM---GMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTL 171
Cdd:PRK10253 106 RYPHQPLfTRWRKEDEEAVTKAMqatGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLEL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1994014911 172 VADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:PRK10253 186 LSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVT 233
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
19-217 |
7.59e-28 |
|
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: 105.68 E-value: 7.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQRP---VSMLFQENNLFNHLTVRQNIGLG 95
Cdd:TIGR03410 20 SLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERAragIAYVPQGREIFPRLTVEENLLTG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 96 IHPGLKLNREQRAQVTA---IAGQMgmdtlLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:TIGR03410 100 LAALPRRSRKIPDEIYElfpVLKEM-----LGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVI 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1994014911 173 ADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDL 217
Cdd:TIGR03410 175 RRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
20-218 |
8.03e-28 |
|
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: 105.32 E-value: 8.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 20 LSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEkhnTTPPAQRPVSMLFQENNLF--NHLTVRQNI--GLG 95
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGA---SPGKGWRHIGYVPQRHEFAwdFPISVAHTVmsGRT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 96 IHPGLkLNREQRAQVTAIAG---QMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALD-PAlrQEMLTL 171
Cdd:TIGR03771 78 GHIGW-LRRPCVADFAAVRDalrRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDmPT--QELLTE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1994014911 172 VADVCQRQQLTLLMVSHSVEDAARIAPRsIVVAEGRIAWDGATDDLL 218
Cdd:TIGR03771 155 LFIELAGAGTAILMTTHDLAQAMATCDR-VVLLNGRVIADGTPQQLQ 200
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-217 |
9.91e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 106.75 E-value: 9.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDG------EKHNTTPPAQRPVSMLFQ--ENNLFNHLTVR- 89
Cdd:PRK13649 27 NLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtlitstSKNKDIKQIRKKVGLVFQfpESQLFEETVLKd 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 90 -----QNIGLGIHPGLKLNREQRAQVtAIAgqmgmDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPAL 164
Cdd:PRK13649 107 vafgpQNFGVSQEEAEALAREKLALV-GIS-----ESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1994014911 165 RQEMLTLVADVcQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDL 217
Cdd:PRK13649 181 RKELMTLFKKL-HQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
19-217 |
1.03e-27 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 105.89 E-value: 1.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLL---N----LIAGFLppASGSLLIDGEK--HNTTPPAQ--RPVSMLFQENNLFNHlT 87
Cdd:COG1117 31 NLDIPENKVTALIGPSGCGKSTLLrclNrmndLIPGAR--VEGEILLDGEDiyDPDVDVVElrRRVGMVFQKPNPFPK-S 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 88 VRQNI--GLGIHpGLKLNREQRAQV-TAIAGQMGMDTLLDRL--PG-ELSGGQRQRAALARCLVRQQPVLLLDEPFSALD 161
Cdd:COG1117 108 IYDNVayGLRLH-GIKSKSELDEIVeESLRKAALWDEVKDRLkkSAlGLSGGQQQRLCIARALAVEPEVLLMDEPTSALD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 162 P--ALRQE--MLTLvadvcqRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDL 217
Cdd:COG1117 187 PisTAKIEelILEL------KKDYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQI 240
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
20-209 |
2.32e-27 |
|
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: 103.97 E-value: 2.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 20 LSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQRP------VSMLFQENNLFNHLTVRQNIG 93
Cdd:TIGR02211 26 LSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAklrnkkLGFIYQFHHLLPDFTALENVA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 94 LGIHPGLKLNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVA 173
Cdd:TIGR02211 106 MPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNNAKIIFDLML 185
|
170 180 190
....*....|....*....|....*....|....*.
gi 1994014911 174 DVCQRQQLTLLMVSHSVEDAARIaPRSIVVAEGRIA 209
Cdd:TIGR02211 186 ELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQLF 220
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-212 |
3.03e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 105.31 E-value: 3.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 1 MLKLNDVTWLY---QHLPMRFTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPA----QRPV 73
Cdd:PRK13636 5 ILKVEELNYNYsdgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGlmklRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 74 SMLFQ--ENNLFNhLTVRQNIGLGIHpGLKL-NREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPV 150
Cdd:PRK13636 85 GMVFQdpDNQLFS-ASVYQDVSFGAV-NLKLpEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1994014911 151 LLLDEPFSALDPALRQEMLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDG 212
Cdd:PRK13636 163 LVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQG 224
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
19-208 |
4.09e-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: 102.29 E-value: 4.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQ--RPVSMLFQENNLFNHlTVRQNIglgi 96
Cdd:cd03246 22 SFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElgDHVGYLPQDDELFSG-SIAENI---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 97 hpglklnreqraqvtaiagqmgmdtlldrlpgeLSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVADVc 176
Cdd:cd03246 97 ---------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAAL- 142
|
170 180 190
....*....|....*....|....*....|..
gi 1994014911 177 QRQQLTLLMVSHSVEdAARIAPRSIVVAEGRI 208
Cdd:cd03246 143 KAAGATRIVIAHRPE-TLASADRILVLEDGRV 173
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-219 |
4.32e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 104.86 E-value: 4.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 2 LKLNDVTWLYQH-LPMRF------TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDG-EKHNTTP-----P 68
Cdd:PRK13646 3 IRFDNVSYTYQKgTPYEHqaihdvNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDiTITHKTKdkyirP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 69 AQRPVSMLFQ--ENNLFNHlTVRQNIGLGihP-GLKLNREQraqVTAIAGQMGMD-----TLLDRLPGELSGGQRQRAAL 140
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFED-TVEREIIFG--PkNFKMNLDE---VKNYAHRLLMDlgfsrDVMSQSPFQMSGGQMRKIAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1994014911 141 ARCLVRQQPVLLLDEPFSALDPALRQEMLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
12-208 |
5.60e-27 |
|
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: 102.74 E-value: 5.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 12 QHLPMRF---------TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKhnTTPPAQRPVSMLFQENNL 82
Cdd:cd03269 4 ENVTKRFgrvtalddiSFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKP--LDIAARNRIGYLPEERGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 83 FNHLTVR-QNIGLGIHPGLKLnREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALD 161
Cdd:cd03269 82 YPKMKVIdQLVYLAQLKGLKK-EEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1994014911 162 PALRQEMLTLVADVcQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRI 208
Cdd:cd03269 161 PVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
20-193 |
7.85e-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: 102.12 E-value: 7.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 20 LSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEK----HNTTPPAQRPVSMLFQ--ENNLFnHLTVRQNIG 93
Cdd:TIGR01166 13 FAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPldysRKGLLERRQRVGLVFQdpDDQLF-AADVDQDVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 94 LG-IHPGLKlNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:TIGR01166 92 FGpLNLGLS-EAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGREQMLAIL 170
|
170 180
....*....|....*....|.
gi 1994014911 173 aDVCQRQQLTLLMVSHSVEDA 193
Cdd:TIGR01166 171 -RRLRAEGMTVVISTHDVDLA 190
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
19-219 |
8.39e-27 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 107.58 E-value: 8.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSL--LIDGEKHNTTPP-------AQRPVSMLFQENNLFNHLTVR 89
Cdd:TIGR03269 304 SLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvRVGDEWVDMTKPgpdgrgrAKRYIGILHQEYDLYPHRTVL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 90 QNIGLGIhpGLKLNRE---QRAQVTAIAgqMGMD-----TLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALD 161
Cdd:TIGR03269 384 DNLTEAI--GLELPDElarMKAVITLKM--VGFDeekaeEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMD 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1994014911 162 PALRQEMLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:TIGR03269 460 PITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
19-219 |
9.50e-27 |
|
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: 107.91 E-value: 9.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPA--QRPVSMLFQENNLFNHlTVRQNIGLGi 96
Cdd:TIGR01846 477 NLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAwlRRQMGVVLQENVLFSR-SIRDNIALC- 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 97 HPGLKLNREQRAQVTA-----IAGQ-MGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLT 170
Cdd:TIGR01846 555 NPGAPFEHVIHAAKLAgahdfISELpQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMR 634
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1994014911 171 LVADVCQRQqlTLLMVSHSVeDAARIAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:TIGR01846 635 NMREICRGR--TVIIIAHRL-STVRACDRIIVLEKGQIAESGRHEELLA 680
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
19-224 |
1.27e-26 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 103.12 E-value: 1.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGE----------------KHNTTPPAQRpVSMLFQENNL 82
Cdd:PRK10619 25 SLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQtinlvrdkdgqlkvadKNQLRLLRTR-LTMVFQHFNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 83 FNHLTVRQNIGLGIHPGLKLNR-EQRAQVTAIAGQMGMD-TLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSAL 160
Cdd:PRK10619 104 WSHMTVLENVMEAPIQVLGLSKqEARERAVKYLAKVGIDeRAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSAL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1994014911 161 DPALRQEMLTLVADVCQRQQlTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLSGNSSA 224
Cdd:PRK10619 184 DPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSP 246
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
20-219 |
1.68e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 103.23 E-value: 1.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 20 LSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGE--KHNTTP--PAQRPVSMLFQ--ENNLFNHlTVRQNIG 93
Cdd:PRK13639 23 FKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpiKYDKKSllEVRKTVGIVFQnpDDQLFAP-TVEEDVA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 94 LGihP-GLKLNREQ-RAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTL 171
Cdd:PRK13639 102 FG--PlNLGLSKEEvEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1994014911 172 VADVcQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:PRK13639 180 LYDL-NKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFS 226
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
19-228 |
2.10e-26 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 106.73 E-value: 2.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEkhnttPPAQ-------RPVSMLFQENNLFNHlTVRQN 91
Cdd:TIGR00958 501 TFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGV-----PLVQydhhylhRQVALVGQEPVLFSG-SVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 92 IGLGihpglkLNREQRAQVTAIAGQMGMDTLLDRLP-------GE----LSGGQRQRAALARCLVRQQPVLLLDEPFSAL 160
Cdd:TIGR00958 575 IAYG------LTDTPDEEIMAAAKAANAHDFIMEFPngydtevGEkgsqLSGGQKQRIAIARALVRKPRVLILDEATSAL 648
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1994014911 161 DPALRQemltLVADVCQRQQLTLLMVSH---SVEDAARIaprsIVVAEGRIAWDGATDDLLSGNSSASALL 228
Cdd:TIGR00958 649 DAECEQ----LLQESRSRASRTVLLIAHrlsTVERADQI----LVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-208 |
2.67e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 102.99 E-value: 2.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEK--HNTTPPA----QRPVSMLFQ--ENNLFNHlTVRQ 90
Cdd:PRK13641 27 SFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHitPETGNKNlkklRKKVSLVFQfpEAQLFEN-TVLK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 91 NIGLGihpglKLN---REQRAQVTAIA--GQMGMDT-LLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPAL 164
Cdd:PRK13641 106 DVEFG-----PKNfgfSEDEAKEKALKwlKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1994014911 165 RQEMLTLVADVcQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRI 208
Cdd:PRK13641 181 RKEMMQLFKDY-QKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
19-229 |
3.28e-26 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 101.51 E-value: 3.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTP---PAQRPVSMLFQENNLFNHLTVRQNIGLG 95
Cdd:PRK10895 23 SLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlhaRARRGIGYLPQEASIFRRLSVYDNLMAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 96 IHPGLKLNREQRA-QVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVAD 174
Cdd:PRK10895 103 LQIRDDLSAEQREdRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEH 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1994014911 175 VcQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLSGNSSASALLG 229
Cdd:PRK10895 183 L-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYLG 236
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-218 |
3.31e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 102.89 E-value: 3.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 1 MLKLNDVTWLYQ-HLPMR------FTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLI------DGEKHNTTP 67
Cdd:PRK13643 1 MIKFEKVNYTYQpNSPFAsralfdIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvsSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 68 PAQRPVSMLFQ--ENNLFNHlTVRQNIGLGIHpGLKLNREQRAQVTAIAGQM-GMDT-LLDRLPGELSGGQRQRAALARC 143
Cdd:PRK13643 81 PVRKKVGVVFQfpESQLFEE-TVLKDVAFGPQ-NFGIPKEKAEKIAAEKLEMvGLADeFWEKSPFELSGGQMRRVAIAGI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1994014911 144 LVRQQPVLLLDEPFSALDPALRQEMLTLVADVCQRQQlTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLL 218
Cdd:PRK13643 159 LAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQ-TVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
16-163 |
5.17e-26 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 100.33 E-value: 5.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 16 MRFT---LSVERGERI---------------AVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQRpVSMLF 77
Cdd:PRK13539 1 MMLEgedLACVRGGRVlfsglsftlaagealVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA-CHYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 78 QENNLFNHLTVRQNIG-----LGIHPGlklnreqraQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLL 152
Cdd:PRK13539 80 HRNAMKPALTVAENLEfwaafLGGEEL---------DIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWI 150
|
170
....*....|.
gi 1994014911 153 LDEPFSALDPA 163
Cdd:PRK13539 151 LDEPTAALDAA 161
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
2-228 |
5.46e-26 |
|
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: 105.41 E-value: 5.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 2 LKLNDVTWLY----QHLPMRFTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPA--QRPVSM 75
Cdd:TIGR03796 478 VELRNITFGYsplePPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREvlANSVAM 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 76 LFQENNLFNHlTVRQNIGLGIHPGLKLNREQRAQVTAIAGQM-----GMDTLLDRLPGELSGGQRQRAALARCLVRQQPV 150
Cdd:TIGR03796 558 VDQDIFLFEG-TVRDNLTLWDPTIPDADLVRACKDAAIHDVItsrpgGYDAELAEGGANLSGGQRQRLEIARALVRNPSI 636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 151 LLLDEPFSALDPALRQEmltlVADVCQRQQLTLLMVSH---SVEDAARIaprsIVVAEGRIAWDGATDDLLSGNSSASAL 227
Cdd:TIGR03796 637 LILDEATSALDPETEKI----IDDNLRRRGCTCIIVAHrlsTIRDCDEI----IVLERGKVVQRGTHEELWAVGGAYARL 708
|
.
gi 1994014911 228 L 228
Cdd:TIGR03796 709 I 709
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
20-218 |
6.78e-26 |
|
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: 104.90 E-value: 6.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 20 LSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPA--QRPVSMLFQENNLFNHlTVRQNIGLGih 97
Cdd:COG5265 379 FEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQAslRAAIGIVPQDTVLFND-TIAYNIAYG-- 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 98 pglklnREQ--RAQVTAIAGQMGMDTLLDRLP-------GE----LSGGQRQRAALARCLVRQQPVLLLDEPFSALDPAL 164
Cdd:COG5265 456 ------RPDasEEEVEAAARAAQIHDFIESLPdgydtrvGErglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRT 529
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1994014911 165 RQEMLTLVADVCQRQqlTLLMVSH---SVEDAARIaprsIVVAEGRIAWDGATDDLL 218
Cdd:COG5265 530 ERAIQAALREVARGR--TTLVIAHrlsTIVDADEI----LVLEAGRIVERGTHAELL 580
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-221 |
9.15e-26 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 104.72 E-value: 9.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 2 LKLNDVTWLYQ---HLPMR-FTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGekHN----TTPPAQRPV 73
Cdd:PRK11176 342 IEFRNVTFTYPgkeVPALRnINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDG--HDlrdyTLASLRNQV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 74 SMLFQENNLFNHlTVRQNIGLGIHPglKLNREQRAQVTAIAGQMG----MDTLLDRLPGE----LSGGQRQRAALARCLV 145
Cdd:PRK11176 420 ALVSQNVHLFND-TIANNIAYARTE--QYSREQIEEAARMAYAMDfinkMDNGLDTVIGEngvlLSGGQRQRIAIARALL 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 146 RQQPVLLLDEPFSALDPALR---QEMLtlvaDVCQRQQlTLLMVSH---SVEDAARIaprsIVVAEGRIAWDGATDDLLS 219
Cdd:PRK11176 497 RDSPILILDEATSALDTESEraiQAAL----DELQKNR-TSLVIAHrlsTIEKADEI----LVVEDGEIVERGTHAELLA 567
|
..
gi 1994014911 220 GN 221
Cdd:PRK11176 568 QN 569
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-218 |
1.25e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 101.70 E-value: 1.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEkhntTPPAQRP-----VSMLF-QENNLFNHLTVRQNi 92
Cdd:COG4586 42 SFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGY----VPFKRRKefarrIGVVFgQRSQLWWDLPAIDS- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 93 glgihpgLKLNR--------EQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPAL 164
Cdd:COG4586 117 -------FRLLKaiyripdaEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVS 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1994014911 165 RQEMLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLL 218
Cdd:COG4586 190 KEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELK 243
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
19-212 |
1.95e-25 |
|
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: 99.33 E-value: 1.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEkhntTPPAQRP-----VSMLF-QENNLFNHLTVRQNI 92
Cdd:cd03267 41 SFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL----VPWKRRKkflrrIGVVFgQKTQLWWDLPVIDSF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 93 GL-----GIHPglklnREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQE 167
Cdd:cd03267 117 YLlaaiyDLPP-----ARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQEN 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1994014911 168 MLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDG 212
Cdd:cd03267 192 IRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
25-184 |
2.12e-25 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 98.58 E-value: 2.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 25 GERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPA-QRPVSMLFQENNLFNHLTVRQNIGL--GIHPGlk 101
Cdd:TIGR01189 26 GEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEpHENILYLGHLPGLKPELSALENLHFwaAIHGG-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 102 lnrEQRAQVTAIAgQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVADVCQRQQL 181
Cdd:TIGR01189 104 ---AQRTIEDALA-AVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHLARGGI 179
|
...
gi 1994014911 182 TLL 184
Cdd:TIGR01189 180 VLL 182
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
14-229 |
2.56e-25 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 99.68 E-value: 2.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 14 LPMRF---------TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPP---AQRPVSMLFQENN 81
Cdd:PRK11300 11 LMMRFggllavnnvNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGhqiARMGVVRTFQHVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 82 LFNHLTVRQN--------IGLGIHPGL-KLNREQRAQVTAIA------GQMGMDTLLDRLPGELSGGQRQRAALARCLVR 146
Cdd:PRK11300 91 LFREMTVIENllvaqhqqLKTGLFSGLlKTPAFRRAESEALDraatwlERVGLLEHANRQAGNLAYGQQRRLEIARCMVT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 147 QQPVLLLDEPFSALDPALRQEMLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLSGNSSASA 226
Cdd:PRK11300 171 QPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNPDVIKA 250
|
...
gi 1994014911 227 LLG 229
Cdd:PRK11300 251 YLG 253
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
19-188 |
4.32e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 102.45 E-value: 4.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHnttppaqrpVSMLFQENNLFNHLTVRQNIGLGIHP 98
Cdd:COG0488 18 SLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLR---------IGYLPQEPPLDDDLTVLDTVLDGDAE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 99 GLKLNREQR--------------------------------AQVTAIAGQMGMDT-LLDRLPGELSGGQRQRAALARCLV 145
Cdd:COG0488 89 LRALEAELEeleaklaepdedlerlaelqeefealggweaeARAEEILSGLGFPEeDLDRPVSELSGGWRRRVALARALL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1994014911 146 rQQP-VLLLDEPFSALDpalrQEMLTLVADVCQRQQLTLLMVSH 188
Cdd:COG0488 169 -SEPdLLLLDEPTNHLD----LESIEWLEEFLKNYPGTVLVVSH 207
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
19-189 |
4.75e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 98.25 E-value: 4.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQ--RPVSMLFQENNLFNHlTVRQNIglgI 96
Cdd:PRK10247 27 SFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyrQQVSYCAQTPTLFGD-TVYDNL---I 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 97 HPGLKlnREQRAQVTAIAG---QMGM-DTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:PRK10247 103 FPWQI--RNQQPDPAIFLDdleRFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEII 180
|
170
....*....|....*..
gi 1994014911 173 ADVCQRQQLTLLMVSHS 189
Cdd:PRK10247 181 HRYVREQNIAVLWVTHD 197
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-219 |
5.11e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 98.83 E-value: 5.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLL---NLIAGFLPPA--SGSLLIDGEKHNTTPPAQ--RPVSMLFQENNLFNHLTVRQN 91
Cdd:PRK14247 23 NLEIPDNTITALMGPSGSGKSTLLrvfNRLIELYPEArvSGEVYLDGQDIFKMDVIElrRRVQMVFQIPNPIPNLSIFEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 92 IGLGihpgLKLNR--------EQRAQVTAIAGQMgMDTLLDRL---PGELSGGQRQRAALARCLVRQQPVLLLDEPFSAL 160
Cdd:PRK14247 103 VALG----LKLNRlvkskkelQERVRWALEKAQL-WDEVKDRLdapAGKLSGGQQQRLCIARALAFQPEVLLADEPTANL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1994014911 161 DPALRQEMLTLVADVcqRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:PRK14247 178 DPENTAKIESLFLEL--KKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFT 234
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
19-228 |
8.01e-25 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 101.96 E-value: 8.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPA--QRPVSMLFQENNLFNHlTVRQNIGLG- 95
Cdd:PRK13657 355 SFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAslRRNIAVVFQDAGLFNR-SIEDNIRVGr 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 96 -------IHPGLKlnreqRAQVTA-IAGQ-MGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDpALRQ 166
Cdd:PRK13657 434 pdatdeeMRAAAE-----RAQAHDfIERKpDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALD-VETE 507
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1994014911 167 EMLTLVADvCQRQQLTLLMVSH---SVEDAARIaprsIVVAEGRIAWDGATDDLLSGNSSASALL 228
Cdd:PRK13657 508 AKVKAALD-ELMKGRTTFIIAHrlsTVRNADRI----LVFDNGRVVESGSFDELVARGGRFAALL 567
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
25-208 |
1.14e-24 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 97.25 E-value: 1.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 25 GERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGE-----KHNTTPPAQRPVSMLFQENNLFNHLTVRQNIGLGIHPG 99
Cdd:PRK10908 28 GEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHditrlKNREVPFLRRQIGMIFQDHHLLMDRTVYDNVAIPLIIA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 100 LKLNREQRAQVTAIAGQMGmdtLLDR---LPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVADVc 176
Cdd:PRK10908 108 GASGDDIRRRVSAALDKVG---LLDKaknFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEF- 183
|
170 180 190
....*....|....*....|....*....|..
gi 1994014911 177 QRQQLTLLMVSHSVEDAARIAPRSIVVAEGRI 208
Cdd:PRK10908 184 NRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-221 |
1.15e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 99.00 E-value: 1.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 2 LKLNDVTWLY-QHLPMRF------TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSL--LIDGEKHNTTPPA--- 69
Cdd:PRK13651 3 IKVKNIVKIFnKKLPTELkaldnvSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewIFKDEKNKKKTKEkek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 70 ---------------------QRPVSMLFQ--ENNLFNHlTVRQNIGLG-IHPGL-KLNREQRAQvtAIAGQMGMD-TLL 123
Cdd:PRK13651 83 vleklviqktrfkkikkikeiRRRVGVVFQfaEYQLFEQ-TIEKDIIFGpVSMGVsKEEAKKRAA--KYIELVGLDeSYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 124 DRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVADVcQRQQLTLLMVSHSVEDAARIAPRSIVV 203
Cdd:PRK13651 160 QRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNL-NKQGKTIILVTHDLDNVLEWTKRTIFF 238
|
250
....*....|....*...
gi 1994014911 204 AEGRIAWDGATDDLLSGN 221
Cdd:PRK13651 239 KDGKIIKDGDTYDILSDN 256
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
18-210 |
1.25e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 101.29 E-value: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 18 FTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIdGekHNTTppaqrpVSMLFQENNLFN-HLTVRQNIGlGI 96
Cdd:COG0488 334 LSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-G--ETVK------IGYFDQHQEELDpDKTVLDELR-DG 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 97 HPGLKlnreqRAQVTAIAGQMGmdtlldrLPGE--------LSGGQRQRAALARcLVRQQP-VLLLDEPFSALDPalrqE 167
Cdd:COG0488 404 APGGT-----EQEVRGYLGRFL-------FSGDdafkpvgvLSGGEKARLALAK-LLLSPPnVLLLDEPTNHLDI----E 466
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1994014911 168 MLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAW 210
Cdd:COG0488 467 TLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
19-209 |
1.58e-24 |
|
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: 96.79 E-value: 1.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQ--RPVSMLFQENNLFNHlTVRQNIG-LG 95
Cdd:cd03244 24 SFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDlrSRISIIPQDPVLFSG-TIRSNLDpFG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 96 IHPGLKLNRE-QRAQVTAIAGQM--GMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:cd03244 103 EYSDEELWQAlERVGLKEFVESLpgGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTI 182
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1994014911 173 ADVCqrQQLTLLMVSHSVE---DAARIaprsIVVAEGRIA 209
Cdd:cd03244 183 REAF--KDCTVLTIAHRLDtiiDSDRI----LVLDKGRVV 216
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-212 |
1.78e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 97.85 E-value: 1.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 1 MLKLNDVTWLY-------QHLPMR-FTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDG---EKHNTTPPA 69
Cdd:PRK13633 4 MIKCKNVSYKYesneestEKLALDdVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtSDEENLWDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 70 QRPVSMLFQenNLFNHLT---VRQNIG-----LGIHPglklnREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALA 141
Cdd:PRK13633 84 RNKAGMVFQ--NPDNQIVatiVEEDVAfgpenLGIPP-----EEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1994014911 142 RCLVRQQPVLLLDEPFSALDPALRQEMLTLVADVCQRQQLTLLMVSHSVEDAARiAPRSIVVAEGRIAWDG 212
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEG 226
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
19-218 |
2.11e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 98.34 E-value: 2.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEK-HNTTPPAQRPVSMLFQENNLFNHLTVRQNIGL-GI 96
Cdd:PRK13537 27 SFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPvPSRARHARQRVGVVPQFDNLDPDFTVRENLLVfGR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 97 HPGLKlNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVADVC 176
Cdd:PRK13537 107 YFGLS-AAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1994014911 177 QRQQlTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLL 218
Cdd:PRK13537 186 ARGK-TILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALI 226
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
19-219 |
2.16e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 97.86 E-value: 2.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEK--HNTTPPAQRPVSMLFQE-NNLFNHLTVRQNIGLG 95
Cdd:PRK13642 27 SFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELltAENVWNLRRKIGMVFQNpDNQFVGATVEDDVAFG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 96 IHPGLKLNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVADV 175
Cdd:PRK13642 107 MENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEI 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1994014911 176 CQRQQLTLLMVSHSVEDAARiAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:PRK13642 187 KEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFA 229
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
19-211 |
2.90e-24 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 100.57 E-value: 2.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQ------RPVSMLFQENNLFNHLTVRQNI 92
Cdd:PRK10535 28 SLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAlaqlrrEHFGFIFQRYHLLSHLTAAQNV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 93 GL-GIHPGL-KLNREQRAQvtAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLT 170
Cdd:PRK10535 108 EVpAVYAGLeRKQRLLRAQ--ELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMA 185
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1994014911 171 LVADVCQRQQlTLLMVSHSVEDAARiAPRSIVVAEGRIAWD 211
Cdd:PRK10535 186 ILHQLRDRGH-TVIIVTHDPQVAAQ-AERVIEIRDGEIVRN 224
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
25-219 |
3.81e-24 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 100.12 E-value: 3.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 25 GERIAVLGPSGAGKSTLLNLIAGFLPPA---SGSLLIDGEKHNTtpPAQRPVSMLFQENNLF-NHLTVRQNigLGIHPGL 100
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDA--KEMRAISAYVQQDDLFiPTLTVREH--LMFQAHL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 101 KLNR-----EQRAQVTAIAGQMGM----DTLL---DRLPGeLSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEM 168
Cdd:TIGR00955 127 RMPRrvtkkEKRERVDEVLQALGLrkcaNTRIgvpGRVKG-LSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSV 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 169 LTLVADVCQRQQlTLLMVSHSvedaariaPRS---------IVVAEGRIAWDGATDDLLS 219
Cdd:TIGR00955 206 VQVLKGLAQKGK-TIICTIHQ--------PSSelfelfdkiILMAEGRVAYLGSPDQAVP 256
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
29-224 |
4.34e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 97.09 E-value: 4.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 29 AVLGPSGAGKSTLL-------NLIAGFlpPASGSLLIDGE---KHNTTPPAQRPVSMLFQENNLFNhLTVRQNIGLGIHP 98
Cdd:PRK14271 51 SLMGPTGSGKTTFLrtlnrmnDKVSGY--RYSGDVLLGGRsifNYRDVLEFRRRVGMLFQRPNPFP-MSIMDNVLAGVRA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 99 -GLKLNREQRAQVTAIAGQMGM-DTLLDRL---PGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVA 173
Cdd:PRK14271 128 hKLVPRKEFRGVAQARLTEVGLwDAVKDRLsdsPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIR 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1994014911 174 DVCQRqqLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLSGNSSA 224
Cdd:PRK14271 208 SLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHA 256
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
19-221 |
4.72e-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: 4.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDG------EKHNTtppaQRPVSMLFQENNLFNHlTVRQNI 92
Cdd:TIGR01193 494 SLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGfslkdiDRHTL----RQFINYLPQEPYIFSG-SILENL 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 93 GLGIHPGLklNREQRAQVTAIAG--------QMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPAL 164
Cdd:TIGR01193 569 LLGAKENV--SQDEIWAACEIAEikddienmPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTIT 646
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1994014911 165 RQEmltLVADVCQRQQLTLLMVSHSVEDAARiAPRSIVVAEGRIAWDGATDDLLSGN 221
Cdd:TIGR01193 647 EKK---IVNNLLNLQDKTIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDELLDRN 699
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
20-219 |
6.99e-24 |
|
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: 99.26 E-value: 6.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 20 LSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGE--KHNTTPPAQRPVSMLFQENNLFNHlTVRQNIGLGIH 97
Cdd:TIGR03797 474 LQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQdlAGLDVQAVRRQLGVVLQNGRLMSG-SIFENIAGGAP 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 98 PGLKLNREQrAQVTAIAGQ-----MGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDpalrQEMLTLV 172
Cdd:TIGR03797 553 LTLDEAWEA-ARMAGLAEDirampMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALD----NRTQAIV 627
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1994014911 173 ADVCQRQQLTLLMVSH---SVEDAARIaprsIVVAEGRIAWDGATDDLLS 219
Cdd:TIGR03797 628 SESLERLKVTRIVIAHrlsTIRNADRI----YVLDAGRVVQQGTYDELMA 673
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
20-195 |
7.21e-24 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 95.23 E-value: 7.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 20 LSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQRP------VSMLFQENNLFNHLTVRQNIG 93
Cdd:PRK10584 31 LVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAklrakhVGFVFQSFMLIPTLNALENVE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 94 LgihPGL---KLNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLT 170
Cdd:PRK10584 111 L---PALlrgESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIAD 187
|
170 180
....*....|....*....|....*
gi 1994014911 171 LVADVCQRQQLTLLMVSHSVEDAAR 195
Cdd:PRK10584 188 LLFSLNREHGTTLILVTHDLQLAAR 212
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
19-220 |
1.05e-23 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 95.62 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNT--TPPAQRPVSMLFQENNLFNHLTVRQNIGLGI 96
Cdd:PRK10575 31 SLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwsSKAFARKVAYLPQQLPAAEGMTVRELVAIGR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 97 HP---GL-KLNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:PRK10575 111 YPwhgALgRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALV 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1994014911 173 ADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLSG 220
Cdd:PRK10575 191 HRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRG 238
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
19-212 |
1.22e-23 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 94.65 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPA---SGSLLIDGEKHNttpPA--QRPVSMLFQENNLFNHLTVRQNIG 93
Cdd:cd03234 27 SLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRK---PDqfQKCVAYVRQDDILLPGLTVRETLT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 94 LGIHpgLKLNREQR-AQVTAIAGQMGMDTLLD------RLPGeLSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQ 166
Cdd:cd03234 104 YTAI--LRLPRKSSdAIRKKRVEDVLLRDLALtriggnLVKG-ISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTAL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1994014911 167 EMLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDG 212
Cdd:cd03234 181 NLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-212 |
1.58e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 98.24 E-value: 1.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 16 MRFTLsvERGERIAVLGPSGAGKST----LLNLIAgflppASGSLLIDGEK-HNTTP----PAQRPVSMLFQENN--LFN 84
Cdd:PRK15134 305 ISFTL--RPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPlHNLNRrqllPVRHRIQVVFQDPNssLNP 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 85 HLTVRQNI--GLGIHPGLKLNREQRAQVTAIAGQMGMD-TLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALD 161
Cdd:PRK15134 378 RLNVLQIIeeGLRVHQPTLSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1994014911 162 PALRQEMLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDG 212
Cdd:PRK15134 458 KTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQG 508
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
20-219 |
2.02e-23 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 97.83 E-value: 2.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 20 LSVERGERIAVLGPSGAGKS----TLLNLIAGFLPPASGSLLIDGEKHNTTPPAQ------RPVSMLFQE-----NNLFn 84
Cdd:COG4172 31 FDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERElrrirgNRIAMIFQEpmtslNPLH- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 85 hlTVRQNIG--LGIHPGLKlNREQRAQVTAIAGQMGMD---TLLDRLPGELSGGQRQRA----ALArclvrQQPVLLL-D 154
Cdd:COG4172 110 --TIGKQIAevLRLHRGLS-GAAARARALELLERVGIPdpeRRLDAYPHQLSGGQRQRVmiamALA-----NEPDLLIaD 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1994014911 155 EPFSALDPALRQEMLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:COG4172 182 EPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFA 246
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
18-219 |
2.04e-23 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 94.52 E-value: 2.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 18 FTLSVERGERIAVLGPSGAGKSTLLNLIAGFLpPASGSLLIDGEKHNTTPPAQ--RPVSMLFQENNLFNHLTVRQNIGLG 95
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAElaRHRAYLSQQQSPPFAMPVFQYLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 96 IHPGLKLNrEQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPV-------LLLDEPFSALDPALRQEM 168
Cdd:COG4138 94 QPAGASSE-AVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQVWPTinpegqlLLLDEPMNSLDVAQQAAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1994014911 169 LTLVADVCQrQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:COG4138 173 DRLLRELCQ-QGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMT 222
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
19-219 |
2.92e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 94.87 E-value: 2.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPP---ASGSLLIDGEKHN--TTPPAQRPVSMLFQE-NNLFNHLTVRQNI 92
Cdd:PRK13640 27 SFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTakTVWDIREKVGIVFQNpDNQFVGATVGDDV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 93 GLGIHpglklNR-----EQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQE 167
Cdd:PRK13640 107 AFGLE-----NRavprpEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQ 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1994014911 168 MLTLVADVCQRQQLTLLMVSHSVEDAArIAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:PRK13640 182 ILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPVEIFS 232
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
19-212 |
3.03e-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: 92.61 E-value: 3.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPA--SGSLLIDGekHNTTPPAQRPVS-MLFQENNLFNHLTVRQNIglg 95
Cdd:cd03213 29 SGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLING--RPLDKRSFRKIIgYVPQDDILHPTLTVRETL--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 96 ihpglklnreqraQVTAiagqmgmdtlldRLPGeLSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVADV 175
Cdd:cd03213 104 -------------MFAA------------KLRG-LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1994014911 176 CQrQQLTLLMVSHSvedaariaPRS---------IVVAEGRIAWDG 212
Cdd:cd03213 158 AD-TGRTIICSIHQ--------PSSeifelfdklLLLSQGRVIYFG 194
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-217 |
3.57e-23 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 97.04 E-value: 3.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 20 LSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPA---QRPVSMLFQENNLFNHLTVRQNIGLGi 96
Cdd:PRK15439 32 FTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAkahQLGIYLVPQEPLLFPNLSVKENILFG- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 97 hpglkLNREQRAQ--VTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPAlrqEMLTLVAD 174
Cdd:PRK15439 111 -----LPKRQASMqkMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPA---ETERLFSR 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1994014911 175 V--CQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDL 217
Cdd:PRK15439 183 IreLLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
17-212 |
3.78e-23 |
|
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: 97.39 E-value: 3.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 17 RFTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQR-PVSMLFQENNLFNHLTVRQNIGLG 95
Cdd:TIGR01257 948 RLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRqSLGMCPQHNILFHHLTVAEHILFY 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 96 IHPGLKLNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVADV 175
Cdd:TIGR01257 1028 AQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKY 1107
|
170 180 190
....*....|....*....|....*....|....*..
gi 1994014911 176 cqRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDG 212
Cdd:TIGR01257 1108 --RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
19-216 |
5.27e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 93.22 E-value: 5.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGekhnttppaqRPVSML-----FQennlfNHLTVRQNIG 93
Cdd:COG1134 46 SFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG----------RVSALLelgagFH-----PELTGRENIY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 94 LG--IHpGLKLN--REQRAQVTAIAGqMG--MDTlldrlP-GELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQ 166
Cdd:COG1134 111 LNgrLL-GLSRKeiDEKFDEIVEFAE-LGdfIDQ-----PvKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQK 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1994014911 167 ----EMLTLVADVCqrqqlTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDD 216
Cdd:COG1134 184 kclaRIRELRESGR-----TVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEE 232
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
19-219 |
5.28e-23 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 96.74 E-value: 5.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQ--RPVSMLFQENNLFNHlTVRQNIGlgi 96
Cdd:COG4618 352 SFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREElgRHIGYLPQDVELFDG-TIAENIA--- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 97 hpglKLNREQRAQVTAIAGQMGMDTLLDRLP-------GE----LSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALR 165
Cdd:COG4618 428 ----RFGDADPEKVVAAAKLAGVHEMILRLPdgydtriGEggarLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGE 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1994014911 166 QEMLTLVADVCQRQQlTLLMVSHSVEdAARIAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:COG4618 504 AALAAAIRALKARGA-TVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
19-213 |
6.68e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 93.65 E-value: 6.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHN--TTPPAQRPVSMLFQ--ENNLFNhLTVRQNIGL 94
Cdd:PRK13647 25 SLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNaeNEKWVRSKVGLVFQdpDDQVFS-STVWDDVAF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 95 G-IHPGL---KLNREQRAQVTAIagqmGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPAlRQEMLT 170
Cdd:PRK13647 104 GpVNMGLdkdEVERRVEEALKAV----RMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPR-GQETLM 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1994014911 171 LVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGA 213
Cdd:PRK13647 179 EILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGD 221
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
19-208 |
6.96e-23 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 92.57 E-value: 6.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPA------QRPVSMLFQENNLFNHLTVRQNI 92
Cdd:PRK11629 29 SFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaelrNQKLGFIYQFHHLLPDFTALENV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 93 GLGIHPGLKLNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:PRK11629 109 AMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLL 188
|
170 180 190
....*....|....*....|....*....|....*.
gi 1994014911 173 ADVCQRQQLTLLMVSHSVEDAARIApRSIVVAEGRI 208
Cdd:PRK11629 189 GELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRL 223
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-219 |
7.97e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 93.19 E-value: 7.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEK--------HNTTPPAQRPVSMLFQENNLFNHLTVRQ 90
Cdd:PRK14246 30 TIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVlyfgkdifQIDAIKLRKEVGMVFQQPNPFPHLSIYD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 91 NIGLGIHP-GLKLNREQRAQVTAIAGQMGM-DTLLDRL---PGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALR 165
Cdd:PRK14246 110 NIAYPLKShGIKEKREIKKIVEECLRKVGLwKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNS 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1994014911 166 QEMLTLVADVcqRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:PRK14246 190 QAIEKLITEL--KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFT 241
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
17-193 |
1.06e-22 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 91.40 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 17 RFTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEK-HNTTPPAQRPVSMLFQENNLFNHLTVRQNIGLg 95
Cdd:cd03231 18 GLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPlDFQRDSIARGLLYLGHAPGIKTTLSVLENLRF- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 96 IHPglklnREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVADV 175
Cdd:cd03231 97 WHA-----DHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGH 171
|
170
....*....|....*...
gi 1994014911 176 CQRQQLTLLMVSHSVEDA 193
Cdd:cd03231 172 CARGGMVVLTTHQDLGLS 189
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
29-197 |
1.27e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 92.60 E-value: 1.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 29 AVLGPSGAGKSTLL---NLIAGFLPPA--SGSLLIDGEkhNTTPP------AQRPVSMLFQENNLFNHLTVRQNIGLGih 97
Cdd:PRK14267 34 ALMGPSGCGKSTLLrtfNRLLELNEEArvEGEVRLFGR--NIYSPdvdpieVRREVGMVFQYPNPFPHLTIYDNVAIG-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 98 pgLKLNREQRAQVT-------AIAGQMGMDTLLDRL---PGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQE 167
Cdd:PRK14267 110 --VKLNGLVKSKKEldervewALKKAALWDEVKDRLndyPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAK 187
|
170 180 190
....*....|....*....|....*....|
gi 1994014911 168 MLTLVADVcqRQQLTLLMVSHSVEDAARIA 197
Cdd:PRK14267 188 IEELLFEL--KKEYTIVLVTHSPAQAARVS 215
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
19-200 |
1.87e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 92.15 E-value: 1.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLI--AGFLPP---ASGSLLIDGekHNTTPPA------QRPVSMLFQENNLFNhLT 87
Cdd:PRK14239 25 SLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNG--HNIYSPRtdtvdlRKEIGMVFQQPNPFP-MS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 88 VRQNIGLGihpgLKLNREQRAQV------TAIAGQMGMDTLLDRLPGE---LSGGQRQRAALARCLVRQQPVLLLDEPFS 158
Cdd:PRK14239 102 IYENVVYG----LRLKGIKDKQVldeaveKSLKGASIWDEVKDRLHDSalgLSGGQQQRVCIARVLATSPKIILLDEPTS 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1994014911 159 ALDP----ALRQEMLTLvadvcqRQQLTLLMVSHSVEDAARIAPRS 200
Cdd:PRK14239 178 ALDPisagKIEETLLGL------KDDYTMLLVTRSMQQASRISDRT 217
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
18-231 |
2.08e-22 |
|
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: 91.70 E-value: 2.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 18 FTLSVE-----RGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKhnttppaqrpVSMLFQENNLFNHLTVRQNI 92
Cdd:cd03237 13 FTLEVEggsisESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT----------VSYKPQYIKADYEGTVRDLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 93 -----GLGIHPGLKlnreqraqvTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDpalrQE 167
Cdd:cd03237 83 ssitkDFYTHPYFK---------TEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD----VE 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1994014911 168 MLTLVADVCQR----QQLTLLMVSHSVEDAARIAPRsIVVAEGRIAWDG---ATDDLLSGNSSASALLGIS 231
Cdd:cd03237 150 QRLMASKVIRRfaenNEKTAFVVEHDIIMIDYLADR-LIVFEGEPSVNGvanPPQSLRSGMNRFLKNLDIT 219
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
12-219 |
5.50e-22 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 91.00 E-value: 5.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 12 QHL----PMRFTLsvERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQRP--VSMLFQENNlfNH 85
Cdd:PRK15112 24 QTVeavkPLSFTL--REGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSqrIRMIFQDPS--TS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 86 LTVRQNIGLGIHPGLKLN-----REQRAQVTAIAGQMGMdtLLDRL---PGELSGGQRQRAALARCLVRQQPVLLLDEPF 157
Cdd:PRK15112 100 LNPRQRISQILDFPLRLNtdlepEQREKQIIETLRQVGL--LPDHAsyyPHMLAPGQKQRLGLARALILRPKVIIADEAL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1994014911 158 SALDPALRQEMLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:PRK15112 178 ASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLA 239
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-219 |
7.53e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 93.31 E-value: 7.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPP---AQRPVSMLFQENNLFNHLTVRQNIGLG 95
Cdd:PRK09700 25 NLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHklaAQLGIGIIYQELSVIDELTVLENLYIG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 96 IHPGLKLN-------REQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPAlRQEM 168
Cdd:PRK09700 105 RHLTKKVCgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNK-EVDY 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1994014911 169 LTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEG-----RIAWDGATDDLLS 219
Cdd:PRK09700 184 LFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGssvcsGMVSDVSNDDIVR 239
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-197 |
1.09e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 90.10 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 2 LKLNDVTWLY--QHLPMRFTLSVERGERIAVLGPSGAGKSTLLNLIaGFLPPASGSLLIDG----------EKHNTTPPA 69
Cdd:PRK14258 8 IKVNNLSFYYdtQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGrveffnqniyERRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 70 QRPVSMLFQENNLFNhLTVRQNIGLGI-----HPGLKLNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCL 144
Cdd:PRK14258 87 RRQVSMVHPKPNLFP-MSVYDNVAYGVkivgwRPKLEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARAL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1994014911 145 VRQQPVLLLDEPFSALDPALRQEMLTLVADVCQRQQLTLLMVSHSVEDAARIA 197
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLS 218
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
19-212 |
1.98e-21 |
|
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: 88.74 E-value: 1.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEkhnttppaqrpVSMLFQENNLFN-HLTVRQNIGL-GI 96
Cdd:cd03220 42 SFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR-----------VSSLLGLGGGFNpELTGRENIYLnGR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 97 HPGLKlNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRA--ALARCLvrQQPVLLLDEPFSALDPALRQEMLTLVAD 174
Cdd:cd03220 111 LLGLS-RKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLafAIATAL--EPDILLIDEVLAVGDAAFQEKCQRRLRE 187
|
170 180 190
....*....|....*....|....*....|....*...
gi 1994014911 175 VCQrQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDG 212
Cdd:cd03220 188 LLK-QGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-217 |
2.63e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 89.78 E-value: 2.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 1 MLKLNDVTwlyqhlpMRF---------TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGekhnttppaqR 71
Cdd:COG4152 1 MLELKGLT-------KRFgdktavddvSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG----------E 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 72 PVSmlfqennlfnhLTVRQNIGL-----GIHPGLKLnREQ------RAQVTAIAGQMGMDTLLDR--LPG-------ELS 131
Cdd:COG4152 64 PLD-----------PEDRRRIGYlpeerGLYPKMKV-GEQlvylarLKGLSKAEAKRRADEWLERlgLGDrankkveELS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 132 GGQRQRAALARCLVRQQPVLLLDEPFSALDP----ALRQEMLTLvadvcQRQQLTLLMVSHSVEDAARIAPRSIVVAEGR 207
Cdd:COG4152 132 KGNQQKVQLIAALLHDPELLILDEPFSGLDPvnveLLKDVIREL-----AAKGTTVIFSSHQMELVEELCDRIVIINKGR 206
|
250
....*....|
gi 1994014911 208 IAWDGATDDL 217
Cdd:COG4152 207 KVLSGSVDEI 216
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
12-215 |
2.63e-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: 88.22 E-value: 2.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 12 QHLPMRFTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGekHNTTPPAQRPVSMLFQENNLFNHLTVRQN 91
Cdd:TIGR03740 13 QTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDG--HPWTRKDLHKIGSLIESPPLYENLTAREN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 92 igLGIHPGLKLNREQRaqVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTL 171
Cdd:TIGR03740 91 --LKVHTTLLGLPDSR--IDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLDPIGIQELREL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1994014911 172 VADVCQrQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATD 215
Cdd:TIGR03740 167 IRSFPE-QGITVILSSHILSEVQQLADHIGIISEGVLGYQGKIN 209
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
19-219 |
6.06e-21 |
|
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: 90.87 E-value: 6.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQ--RPVSMLFQENNLFNHlTVRQNIGlgi 96
Cdd:TIGR01842 338 SFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfgKHIGYLPQDVELFPG-TVAENIA--- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 97 HPGLKLNREQRAQVTAIAG--------QMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDP----AL 164
Cdd:TIGR01842 414 RFGENADPEKIIEAAKLAGvhelilrlPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEegeqAL 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1994014911 165 RQEMLTLvadvcQRQQLTLLMVSHSVEdAARIAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:TIGR01842 494 ANAIKAL-----KARGITVVVITHRPS-LLGCVDKILVLQDGRIARFGERDEVLA 542
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-229 |
6.15e-21 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 87.63 E-value: 6.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 1 MLKLNDVTWLYQHLPM--RFTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQ---RPVSM 75
Cdd:PRK11614 5 MLSFDKVSAHYGKIQAlhEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKimrEAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 76 LFQENNLFNHLTVRQNIGLGihpGLKLNREQRAQVTAIAGQMgMDTLLDR---LPGELSGGQRQRAALARCLVRQQPVLL 152
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLAMG---GFFAERDQFQERIKWVYEL-FPRLHERriqRAGTMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1994014911 153 LDEPFSALDPALRQEMLTLVADVcQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLSGNSSASALLG 229
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAYLG 236
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-230 |
9.16e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 87.88 E-value: 9.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 1 MLKLNDVTWLYQHlPMRFTL-----SVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGE---KHNTTPpAQRP 72
Cdd:PRK13648 7 IIVFKNVSFQYQS-DASFTLkdvsfNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQaitDDNFEK-LRKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 73 VSMLFQE-NNLFNHLTVRQNIGLGIHPGLKLNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVL 151
Cdd:PRK13648 85 IGIVFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1994014911 152 LLDEPFSALDPALRQEMLTLVADVCQRQQLTLLMVSHSVEDAARiAPRSIVVAEGRIAWDGATDDLLsgnSSASALLGI 230
Cdd:PRK13648 165 ILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF---DHAEELTRI 239
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
4-219 |
9.22e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 88.14 E-value: 9.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 4 LNDVTWLY-QHLPMRF------TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDG-------EKHNTTPPA 69
Cdd:PRK13645 9 LDNVSYTYaKKTPFEFkalnntSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlKKIKEVKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 70 QRPVSMLFQ--ENNLFNHlTVRQNIGLG-IHPGLKlNREQRAQVTAIAGQMGM-DTLLDRLPGELSGGQRQRAALARCLV 145
Cdd:PRK13645 89 RKEIGLVFQfpEYQLFQE-TIEKDIAFGpVNLGEN-KQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1994014911 146 RQQPVLLLDEPFSALDPALRQEMLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:PRK13645 167 MDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-208 |
1.72e-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: 85.18 E-value: 1.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 1 MLKLNDVTWLYQHLPmrFTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQR---PVSML- 76
Cdd:cd03215 4 VLEVRGLSVKGAVRD--VSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAiraGIAYVp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 77 --FQENNLFNHLTVRQNIGLGIHpglklnreqraqvtaiagqmgmdtlldrlpgeLSGGQRQRAALARCLVRQQPVLLLD 154
Cdd:cd03215 82 edRKREGLVLDLSVAENIALSSL--------------------------------LSGGNQQKVVLARWLARDPRVLILD 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1994014911 155 EPFSALDPALRQEMLTLVADvCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRI 208
Cdd:cd03215 130 EPTRGVDVGAKAEIYRLIRE-LADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
20-207 |
2.00e-20 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 85.21 E-value: 2.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 20 LSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGekhnttppaqrPVSMLFQENNLFNhLTVRQNIgLGihpG 99
Cdd:cd03250 26 LEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-----------SIAYVSQEPWIQN-GTIRENI-LF---G 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 100 LKLNrEQRAQ--VTAIAgqmgMDTLLDRLP-------GE----LSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQ 166
Cdd:cd03250 90 KPFD-EERYEkvIKACA----LEPDLEILPdgdlteiGEkginLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1994014911 167 EmltlVADVCQRQQL----TLLMVSHSVE---DAARIaprsIVVAEGR 207
Cdd:cd03250 165 H----IFENCILGLLlnnkTRILVTHQLQllpHADQI----VVLDNGR 204
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
18-188 |
3.83e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 88.33 E-value: 3.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 18 FTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLlidgekhnTTPPAQRpvsMLF--QENNLfNHLTVRQNIglg 95
Cdd:COG4178 382 LSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI--------ARPAGAR---VLFlpQRPYL-PLGTLREAL--- 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 96 IHPGLKLNREqRAQVTAIAGQMGMDTLLDRL------PGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEML 169
Cdd:COG4178 447 LYPATAEAFS-DAELREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALY 525
|
170
....*....|....*....
gi 1994014911 170 TLVADvcQRQQLTLLMVSH 188
Cdd:COG4178 526 QLLRE--ELPGTTVISVGH 542
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
19-218 |
5.80e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 86.81 E-value: 5.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEK-HNTTPPAQRPVSMLFQENNLFNHLTVRQN-IGLGI 96
Cdd:PRK13536 61 SFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPvPARARLARARIGVVPQFDNLDLEFTVRENlLVFGR 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 97 HPGLKlNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALR----QEMLTLV 172
Cdd:PRK13536 141 YFGMS-TREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARhliwERLRSLL 219
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1994014911 173 AdvcqrQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLL 218
Cdd:PRK13536 220 A-----RGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALI 260
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
19-219 |
8.53e-20 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 85.26 E-value: 8.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPA--------SGSLLIDGEKHNTTPPAQ--RPVSMLFQENNLFNHLTV 88
Cdd:PRK13547 21 SLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRlaRLRAVLPQAAQPAFAFSA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 89 RQNIGLGIHP----GLKLNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQP---------VLLLDE 155
Cdd:PRK13547 101 REIVLLGRYPharrAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQLWPphdaaqpprYLLLDE 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1994014911 156 PFSALDPALRQEMLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:PRK13547 181 PTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLT 244
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-219 |
1.61e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 84.65 E-value: 1.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 1 MLKLNDVTWLY-QHLPM--RFTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLL---IDGEKHNTTPPAQRPVS 74
Cdd:PRK13644 1 MIRLENVSYSYpDGTPAleNINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLvsgIDTGDFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 75 MLFQE-NNLFNHLTVRQNIGLGIHPGLKLNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLL 153
Cdd:PRK13644 81 IVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1994014911 154 DEPFSALDPALRQEMLTLVADVcQRQQLTLLMVSHSVEDaARIAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:PRK13644 161 DEVTSMLDPDSGIAVLERIKKL-HEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-207 |
1.65e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 86.50 E-value: 1.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 20 LSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKH---NTTPPAQRPVSMLFQENNLFNHLTVRQNIGLGI 96
Cdd:PRK11288 25 FDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfaSTTAALAAGVAIIYQELHLVPEMTVAENLYLGQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 97 HP---GLKLNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDpALRQEMLTLVA 173
Cdd:PRK11288 105 LPhkgGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLS-AREIEQLFRVI 183
|
170 180 190
....*....|....*....|....*....|....
gi 1994014911 174 DVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGR 207
Cdd:PRK11288 184 RELRAEGRVILYVSHRMEEIFALCDAITVFKDGR 217
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
10-178 |
2.78e-19 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 82.54 E-value: 2.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 10 LYQHLpmrfTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNttppAQRPVsmlFQENNLFnhltvr 89
Cdd:PRK13538 16 LFSGL----SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR----RQRDE---YHQDLLY------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 90 qnigLGIHPGLK--------------LNREQRAQVTAIA-GQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLD 154
Cdd:PRK13538 79 ----LGHQPGIKteltalenlrfyqrLHGPGDDEALWEAlAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILD 154
|
170 180
....*....|....*....|....
gi 1994014911 155 EPFSALDPALRQEMLTLVADVCQR 178
Cdd:PRK13538 155 EPFTAIDKQGVARLEALLAQHAEQ 178
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
20-209 |
2.94e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 85.84 E-value: 2.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 20 LSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQ------------RpvsmlfQENNLFNHLT 87
Cdd:COG1129 273 FSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairagiayvpedR------KGEGLVLDLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 88 VRQNIGLGIHP-----GLKLNREQRAQVTAIAGQMGMDTL-LDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALD 161
Cdd:COG1129 347 IRENITLASLDrlsrgGLLDRRRERALAEEYIKRLRIKTPsPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGID 426
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1994014911 162 PALRQEMLTLVADVCqRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIA 209
Cdd:COG1129 427 VGAKAEIYRLIRELA-AEGKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
19-197 |
3.73e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 83.29 E-value: 3.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLL-------NLIAGFlpPASGSLLIDGekHNTTPP------AQRPVSMLFQENNLFNH 85
Cdd:PRK14243 30 WLDIPKNQITAFIGPSGCGKSTILrcfnrlnDLIPGF--RVEGKVTFHG--KNLYAPdvdpveVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 86 lTVRQNIGLGIH-PGLKLNREQRAQvTAIAGQMGMDTLLDRLPGE---LSGGQRQRAALARCLVRQQPVLLLDEPFSALD 161
Cdd:PRK14243 106 -SIYDNIAYGARiNGYKGDMDELVE-RSLRQAALWDEVKDKLKQSglsLSGGQQQRLCIARAIAVQPEVILMDEPCSALD 183
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1994014911 162 P--ALRQE--MLTLvadvcqRQQLTLLMVSHSVEDAARIA 197
Cdd:PRK14243 184 PisTLRIEelMHEL------KEQYTIIIVTHNMQQAARVS 217
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
2-219 |
1.08e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 81.90 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 2 LKLNDVTWLYQHLPmrFTLSVERGERIAVLGPSGAGKSTLLNLIAGFLpPASGSLLIDGEKHNTTPPAQ--RPVSMLFQE 79
Cdd:PRK03695 1 MQLNDVAVSTRLGP--LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAElaRHRAYLSQQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 80 NN-LFNhLTVRQNIGLGIHPGLKLnREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQP-------VL 151
Cdd:PRK03695 78 QTpPFA-MPVFQYLTLHQPDKTRT-EAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWPdinpagqLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1994014911 152 LLDEPFSALDPALRQEMLTLVADVCQrQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:PRK03695 156 LLDEPMNSLDVAQQAALDRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLT 222
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
18-207 |
1.65e-18 |
|
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: 80.94 E-value: 1.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 18 FTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLI--DGEKHNTTPPAQRPVsmlfqennlfnhLTVRQN-IG- 93
Cdd:COG4778 30 VSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLAQASPREI------------LALRRRtIGy 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 94 ---------------LGIHPGLKLNREqRAQVTAIAGQMgmdtlLDRL----------PGELSGGQRQRAALARCLVRQQ 148
Cdd:COG4778 98 vsqflrviprvsaldVVAEPLLERGVD-REEARARAREL-----LARLnlperlwdlpPATFSGGEQQRVNIARGFIADP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1994014911 149 PVLLLDEPFSALDPALRQEMLTLVADvCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGR 207
Cdd:COG4778 172 PLLLLDEPTASLDAANRAVVVELIEE-AKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
19-207 |
6.67e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 81.90 E-value: 6.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPAS--GSLLIDGEK---HNTTPPAQRPVSMLFQENNLFNHLTVRQNIG 93
Cdd:PRK13549 25 SLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEElqaSNIRDTERAGIAIIHQELALVKELSVLENIF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 94 LG--IHPGLKLNRE---QRAQvtAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEM 168
Cdd:PRK13549 105 LGneITPGGIMDYDamyLRAQ--KLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVL 182
|
170 180 190
....*....|....*....|....*....|....*....
gi 1994014911 169 LTLVADVcQRQQLTLLMVSHSVEDAARIAPRSIVVAEGR 207
Cdd:PRK13549 183 LDIIRDL-KAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-207 |
7.75e-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: 81.79 E-value: 7.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 20 LSVERGERIAVLGPSGAGKSTLLNLIAGFLPPAS--GSLLIDGEK---HNTTPPAQRPVSMLFQENNLFNHLTVRQNIGL 94
Cdd:TIGR02633 22 LEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPlkaSNIRDTERAGIVIIHQELTLVPELSVAENIFL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 95 G---IHPGLKLNREQ---RAQvtAIAGQMGMDTLLDRLP-GELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQE 167
Cdd:TIGR02633 102 GneiTLPGGRMAYNAmylRAK--NLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEI 179
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1994014911 168 MLTLVADVcQRQQLTLLMVSHSVEDAARIAPRSIVVAEGR 207
Cdd:TIGR02633 180 LLDIIRDL-KAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-221 |
8.21e-18 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 80.52 E-value: 8.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQR-----PVSMLFQENnlFNHLTVRQNIG 93
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravrsDIQMIFQDP--LASLNPRMTIG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 94 LGI-------HPglKLNREQ-RAQVTAIAGQMGM-DTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPAL 164
Cdd:PRK15079 119 EIIaeplrtyHP--KLSRQEvKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSI 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1994014911 165 RQEMLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRiAWDGATDDLLSGN 221
Cdd:PRK15079 197 QAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGH-AVELGTYDEVYHN 252
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
25-208 |
8.50e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 78.74 E-value: 8.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 25 GERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQ-----RPVSMLFQENnlFNHLTVRQNIGLGIHPG 99
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKlqalrRDIQFIFQDP--YASLDPRQTVGDSIMEP 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 100 LKLNR-----EQRAQVTAIAGQMGMDTLLD-RLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVA 173
Cdd:PRK10261 428 LRVHGllpgkAAAARVAWLLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLL 507
|
170 180 190
....*....|....*....|....*....|....*
gi 1994014911 174 DVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRI 208
Cdd:PRK10261 508 DLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
20-217 |
1.15e-16 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 76.28 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 20 LSVERGERIAVLGPSGAGKSTLLNLIAGFLPPA----SGSLLIDGEKHNTTPPAQRPVSMLFQE-NNLFNHL-TVRQNig 93
Cdd:PRK10418 24 LTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGKPVAPCALRGRKIATIMQNpRSAFNPLhTMHTH-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 94 lGIHPGLKLNRE-QRAQVTAIAGQMGMD---TLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEML 169
Cdd:PRK10418 102 -ARETCLALGKPaDDATLTAALEAVGLEnaaRVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARIL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1994014911 170 TLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDL 217
Cdd:PRK10418 181 DLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
25-218 |
1.85e-16 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 75.73 E-value: 1.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 25 GERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLI---DGEKHNTTPPAQRPVSMLFQENNLFNHLTVRQ----------N 91
Cdd:PRK11701 32 GEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDLYALSEAERRRLLRTEWGFVHQHPRDglrmqvsaggN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 92 IG---LGIhpGLKLNREQRAQVTAIAGQMGMDTL-LDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQE 167
Cdd:PRK11701 112 IGerlMAV--GARHYGDIRATAGDWLERVEIDAArIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQAR 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1994014911 168 MLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLL 218
Cdd:PRK11701 190 LLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVL 240
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-227 |
2.13e-16 |
|
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: 77.56 E-value: 2.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPA-SGSLLIDGEKHNTTPPAQ---RPVSMLFQE---NNLFNHLTVRQN 91
Cdd:TIGR02633 280 SFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQairAGIAMVPEDrkrHGIVPILGVGKN 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 92 IGLGIhpglkLNR-EQRAQVTAIAGQMGMDTLLDRLP----------GELSGGQRQRAALARCLVRQQPVLLLDEPFSAL 160
Cdd:TIGR02633 360 ITLSV-----LKSfCFKMRIDAAAELQIIGSAIQRLKvktaspflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGV 434
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1994014911 161 DPALRQEMLTLVADVCQrQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLSGNSSASAL 227
Cdd:TIGR02633 435 DVGAKYEIYKLINQLAQ-EGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDFVNHALTQEQVLAAAL 500
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
19-161 |
2.47e-16 |
|
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: 77.28 E-value: 2.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPasgsllIDGEkhnTTPPAQRPVSMLFQENNLFNHLTVRQNIGLGIHP 98
Cdd:TIGR03719 25 SLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKD------FNGE---ARPQPGIKVGYLPQEPQLDPTKTVRENVEEGVAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 99 GLK-LNR---------EQRAQVTAIAGQMG---------------------MDTLldRLP------GELSGGQRQRAALA 141
Cdd:TIGR03719 96 IKDaLDRfneisakyaEPDADFDKLAAEQAelqeiidaadawdldsqleiaMDAL--RCPpwdadvTKLSGGERRRVALC 173
|
170 180
....*....|....*....|
gi 1994014911 142 RCLVRQQPVLLLDEPFSALD 161
Cdd:TIGR03719 174 RLLLSKPDMLLLDEPTNHLD 193
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
18-188 |
2.72e-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: 2.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 18 FTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLlidgekhnTTPPAQRPVSMlfqennlfnhltvrqniglgih 97
Cdd:cd03221 19 ISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV--------TWGSTVKIGYF---------------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 98 pglklnrEQraqvtaiagqmgmdtlldrlpgeLSGGQRQRAALARCLVRQQPVLLLDEPFSALDPalrqEMLTLVADVCQ 177
Cdd:cd03221 69 -------EQ-----------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDL----ESIEALEEALK 114
|
170
....*....|.
gi 1994014911 178 RQQLTLLMVSH 188
Cdd:cd03221 115 EYPGTVILVSH 125
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
15-172 |
3.09e-16 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 74.50 E-value: 3.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 15 PMRFtlSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGeKHNTTPPAQRPVSMLFQENNLFNHLTVRQNigL 94
Cdd:PRK13543 29 PLDF--HVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDG-KTATRGDRSRFMAYLGHLPGLKADLSTLEN--L 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1994014911 95 GIHPGLKLNREQRAQVTAIAgQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPalrqEMLTLV 172
Cdd:PRK13543 104 HFLCGLHGRRAKQMPGSALA-IVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL----EGITLV 176
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
18-161 |
6.73e-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: 75.98 E-value: 6.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 18 FTLSVE-----RGERIAVLGPSGAGKSTLLNLIAGFLPPASGSllIDGEKHnttppaqrpVSMLFQENNLFNHLTVRQNI 92
Cdd:COG1245 354 FSLEVEggeirEGEVLGIVGPNGIGKTTFAKILAGVLKPDEGE--VDEDLK---------ISYKPQYISPDYDGTVEEFL 422
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1994014911 93 GLGIHPGLKLNREQraqvTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALD 161
Cdd:COG1245 423 RSANTDDFGSSYYK----TEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
7-230 |
9.37e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 74.15 E-value: 9.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 7 VTWLYQHLPMR-FTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPpAQRPVSMLFQENNL--- 82
Cdd:PRK15056 14 VTWRNGHTALRdASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQAL-QKNLVAYVPQSEEVdws 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 83 FNHLtVRQNIGLGIHPGLKLNR----EQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFS 158
Cdd:PRK15056 93 FPVL-VEDVVMMGRYGHMGWLRrakkRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFT 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1994014911 159 ALDPALRQEMLTLVADVcQRQQLTLLMVSHSVEDAARIAPRSIVVaEGRIAWDGATDDLLSGNSSASALLGI 230
Cdd:PRK15056 172 GVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYTVMV-KGTVLASGPTETTFTAENLELAFSGV 241
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
12-195 |
9.71e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 75.93 E-value: 9.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 12 QHLPMRF---------TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGS--LL---IDGEKHNTtppaQRPVSMLF 77
Cdd:NF033858 270 RGLTMRFgdftavdhvSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEawLFgqpVDAGDIAT----RRRVGYMS 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 78 QENNLFNHLTVRQNIGLgiHPGL-KLNREQRAQ-VTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDE 155
Cdd:NF033858 346 QAFSLYGELTVRQNLEL--HARLfHLPAAEIAArVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDE 423
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1994014911 156 PFSALDPALRQEMLTLVADVCQRQQLTLLMVSHSVEDAAR 195
Cdd:NF033858 424 PTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAER 463
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
19-161 |
1.87e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 74.77 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPasgsllIDGEkhnTTPPAQRPVSMLFQENNLFNHLTVRQNIGLGIHP 98
Cdd:PRK11819 27 SLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKE------FEGE---ARPAPGIKVGYLPQEPQLDPEKTVRENVEEGVAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 99 GL-KLNR---------EQRAQVTAIAGQMG---------------------MDTLldRLP------GELSGGQRQRAALA 141
Cdd:PRK11819 98 VKaALDRfneiyaayaEPDADFDALAAEQGelqeiidaadawdldsqleiaMDAL--RCPpwdakvTKLSGGERRRVALC 175
|
170 180
....*....|....*....|
gi 1994014911 142 RCLVRQQPVLLLDEPFSALD 161
Cdd:PRK11819 176 RLLLEKPDMLLLDEPTNHLD 195
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
25-219 |
3.10e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 74.15 E-value: 3.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 25 GERIAVLGPSGAGKSTLLNLIAGFLPPAS--GSLLIDGEKhnTTPPAQRPVSMLFQENNLFNHLTVRQNI---GLGIHPG 99
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRK--PTKQILKRTGFVTQDDILYPHLTVRETLvfcSLLRLPK 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 100 LKLNREQRAQVTAIAGQMGMDTLLDRLPGE-----LSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVAD 174
Cdd:PLN03211 172 SLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGS 251
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1994014911 175 VCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:PLN03211 252 LAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMA 296
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
19-209 |
3.45e-15 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 71.67 E-value: 3.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTP--PAQRPVSMLFQENNLFNHlTVRQNIGlgi 96
Cdd:cd03369 28 SFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPleDLRSSLTIIPQDPTLFSG-TIRSNLD--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 97 hpglKLNREQRAQV-TAIAGQMGMDTlldrlpgeLSGGQRQRAALARCLVRQQPVLLLDEPFSALD---PALRQEML-TL 171
Cdd:cd03369 104 ----PFDEYSDEEIyGALRVSEGGLN--------LSQGQRQLLCLARALLKRPRVLVLDEATASIDyatDALIQKTIrEE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1994014911 172 VADVcqrqqlTLLMVSH---SVEDAARIaprsIVVAEGRIA 209
Cdd:cd03369 172 FTNS------TILTIAHrlrTIIDYDKI----LVMDAGEVK 202
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
2-188 |
4.99e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 71.14 E-value: 4.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 2 LKLNDVTW-LYQHLPmrftLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDgekhnttppaqrpvsmlFQEN 80
Cdd:COG2401 36 VELRVVERyVLRDLN----LEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-----------------VPDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 81 NLFNHLTVRQNIGLGIHPglklnreqrAQVTAIAGQMGMDT--LLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFS 158
Cdd:COG2401 95 QFGREASLIDAIGRKGDF---------KDAVELLNAVGLSDavLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCS 165
|
170 180 190
....*....|....*....|....*....|
gi 1994014911 159 ALDPALRQEMLTLVADVCQRQQLTLLMVSH 188
Cdd:COG2401 166 HLDRQTAKRVARNLQKLARRAGITLVVATH 195
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
10-219 |
9.27e-15 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 72.74 E-value: 9.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 10 LYQHLPMRFT-LSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLlidgEKHNTTP------PAQRPVSMLFQENNl 82
Cdd:PRK10938 13 LSDTKTLQLPsLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGER----QSQFSHItrlsfeQLQKLVSDEWQRNN- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 83 fNHL----------TVRQNIGLGIHpglklnREQRAQvtAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLL 152
Cdd:PRK10938 88 -TDMlspgeddtgrTTAEIIQDEVK------DPARCE--QLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1994014911 153 LDEPFSALDPALRQEMLTLVADVcQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:PRK10938 159 LDEPFDGLDVASRQQLAELLASL-HQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQ 224
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
4-208 |
1.32e-14 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 72.35 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 4 LNDVTWLYQHLPMRFTLS--VERGERIAVLGPSGAGKSTLLNLIAGFLPPA-------------SGSLLIDGEKHnttpp 68
Cdd:PRK10938 263 LNNGVVSYNDRPILHNLSwqVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGysndltlfgrrrgSGETIWDIKKH----- 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 69 aqrpvsMLFQENNLfnHL------TVRQNIGLGIHPGLKLNREQRAQVTAIAGQ----MGMDTLLDRLP-GELSGGQrQR 137
Cdd:PRK10938 338 ------IGYVSSSL--HLdyrvstSVRNVILSGFFDSIGIYQAVSDRQQKLAQQwldiLGIDKRTADAPfHSLSWGQ-QR 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1994014911 138 AAL-ARCLVRQQPVLLLDEPFSALDPALRQEMLTLVaDVCQRQQLT-LLMVSHSVEDAAR-IAPRSIVVAEGRI 208
Cdd:PRK10938 409 LALiVRALVKHPTLLILDEPLQGLDPLNRQLVRRFV-DVLISEGETqLLFVSHHAEDAPAcITHRLEFVPDGDI 481
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-206 |
1.75e-14 |
|
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: 72.35 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 1 MLKLNDVTWLYQHLPM----RFTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTT-PPAQRPVSM 75
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSSpavdRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNiSDVHQNMGY 2016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 76 LFQENNLFNHLTVRQNIGLgiHPGLK-LNREQRAQVTAIAGQ-MGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLL 153
Cdd:TIGR01257 2017 CPQFDAIDDLLTGREHLYL--YARLRgVPAEEIEKVANWSIQsLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLL 2094
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1994014911 154 DEPFSALDPALRQEMLTLVADVCqRQQLTLLMVSHSVEDAARIAPRSIVVAEG 206
Cdd:TIGR01257 2095 DEPTTGMDPQARRMLWNTIVSII-REGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
19-189 |
2.19e-14 |
|
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: 68.33 E-value: 2.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDgEKHNTTPPAQRPvsmlfqennLFNHLTVRQNIglgIHP 98
Cdd:cd03223 21 SFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMP-EGEDLLFLPQRP---------YLPLGTLREQL---IYP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 99 glklnreqraqvtaiagqmgmdtlLDRlpgELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPalrqEMLTLVADVCQR 178
Cdd:cd03223 88 ------------------------WDD---VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDE----ESEDRLYQLLKE 136
|
170
....*....|.
gi 1994014911 179 QQLTLLMVSHS 189
Cdd:cd03223 137 LGITVISVGHR 147
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-219 |
2.20e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 71.66 E-value: 2.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLP--PA---SGSLLIDGEKH-NTTPPAQRPV-----SMLFQE-----NNL 82
Cdd:PRK15134 29 SLQIEAGETLALVGESGSGKSVTALSILRLLPspPVvypSGDIRFHGESLlHASEQTLRGVrgnkiAMIFQEpmvslNPL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 83 fnHLTVRQNIG-LGIHPGLKlnRE-QRAQVTAIAGQMGMDTLLDRL---PGELSGGQRQRAALARCLVRQQPVLLLDEPF 157
Cdd:PRK15134 109 --HTLEKQLYEvLSLHRGMR--REaARGEILNCLDRVGIRQAAKRLtdyPHQLSGGERQRVMIAMALLTRPELLIADEPT 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1994014911 158 SALDPALRQEMLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:PRK15134 185 TALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFS 246
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-206 |
3.30e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 70.04 E-value: 3.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 1 MLKLNDVTWLYQHLPMR--FTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPA----QRPVS 74
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLkgLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGllalRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 75 MLFQ--ENNLFnHLTVRQNIGLGIH----PGLKLNREQRAQVTAIAGQMgmdtlLDRLPGE-LSGGQRQRAALARCLVRQ 147
Cdd:PRK13638 81 TVFQdpEQQIF-YTDIDSDIAFSLRnlgvPEAEITRRVDEALTLVDAQH-----FRHQPIQcLSHGQKKRVAIAGALVLQ 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1994014911 148 QPVLLLDEPFSALDPALRQEMLTLVADVCQrQQLTLLMVSHSVE------DAARIAPRSIVVAEG 206
Cdd:PRK13638 155 ARYLLLDEPTAGLDPAGRTQMIAIIRRIVA-QGNHVIISSHDIDliyeisDAVYVLRQGQILTHG 218
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
19-191 |
3.36e-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: 68.90 E-value: 3.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASG-----SLLIDGEKHNTTPPAQR-PVSMLFQENNLFNhLTVRQNI 92
Cdd:cd03290 21 NIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGkvhwsNKNESEPSFEATRSRNRySVAYAAQKPWLLN-ATVEENI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 93 GLGiHPglkLNReQRAQVTAIAGQMGMDtlLDRLP-------GE----LSGGQRQRAALARCLVRQQPVLLLDEPFSALD 161
Cdd:cd03290 100 TFG-SP---FNK-QRYKAVTDACSLQPD--IDLLPfgdqteiGErginLSGGQRQRICVARALYQNTNIVFLDDPFSALD 172
|
170 180 190
....*....|....*....|....*....|.
gi 1994014911 162 PALRQEMLTL-VADVCQRQQLTLLMVSHSVE 191
Cdd:cd03290 173 IHLSDHLMQEgILKFLQDDKRTLVLVTHKLQ 203
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
17-219 |
4.56e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 70.16 E-value: 4.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 17 RFTLSVERGERIAVLGPSGAGKSTLLNLIAGFLP-PA---SGSLLIDGEKHNTTPPAQR------PVSMLFQE--NNLFN 84
Cdd:PRK11022 25 RISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPGrvmAEKLEFNGQDLQRISEKERrnlvgaEVAMIFQDpmTSLNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 85 HLTVRQNI--GLGIHPG-LKLNREQRA-QVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSAL 160
Cdd:PRK11022 105 CYTVGFQImeAIKVHQGgNKKTRRQRAiDLLNQVGIPDPASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTAL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1994014911 161 DPALRQEMLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:PRK11022 185 DVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFR 243
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
18-161 |
6.16e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 70.22 E-value: 6.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 18 FTLSVE-----RGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDgEKHNTTP----PAQrpvsmlfqennlfnHLTV 88
Cdd:PRK13409 353 FSLEVEggeiyEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKISYKPqyikPDY--------------DGTV 417
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1994014911 89 RQNIGlGIHPGLKLNREQraqvTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALD 161
Cdd:PRK13409 418 EDLLR-SITDDLGSSYYK----SEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
20-209 |
8.86e-14 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 68.17 E-value: 8.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 20 LSVERGERIAVLGPSGAGKSTLLNLIAGFlpPA----SGSLLIDGEKHNTTPP---AQRPVSMLFQ---EnnlFNHLTVR 89
Cdd:COG0396 21 LTIKPGEVHAIMGPNGSGKSTLAKVLMGH--PKyevtSGSILLDGEDILELSPderARAGIFLAFQypvE---IPGVSVS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 90 Q--NIGLGIHPGLKLNREQ-RAQVTAIAGQMGMDT-LLDR-LPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALD-PA 163
Cdd:COG0396 96 NflRTALNARRGEELSAREfLKLLKEKMKELGLDEdFLDRyVNEGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDiDA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1994014911 164 LRqemltLVADVCQR---QQLTLLMVSHSvedaAR----IAP-RSIVVAEGRIA 209
Cdd:COG0396 176 LR-----IVAEGVNKlrsPDRGILIITHY----QRildyIKPdFVHVLVDGRIV 220
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-188 |
9.49e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 67.28 E-value: 9.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 1 MLKLNDVTWLYQHLPM--RFTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPA-QRPVSMLF 77
Cdd:PRK13540 1 MLDVIELDFDYHDQPLlqQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTyQKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 78 QENNLFNHLTVRQNIGLGIHpglklNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPF 157
Cdd:PRK13540 81 HRSGINPYLTLRENCLYDIH-----FSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170 180 190
....*....|....*....|....*....|...
gi 1994014911 158 SALDpalRQEMLTLVADV--CQRQQLTLLMVSH 188
Cdd:PRK13540 156 VALD---ELSLLTIITKIqeHRAKGGAVLLTSH 185
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
20-219 |
1.01e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 70.15 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 20 LSVERGERIAVLGPSGAGKSTLLNLIAGFLPPAS-GSLLIDGEkhnttppaqrpVSMLFQENNLFNhLTVRQNIGLGIHp 98
Cdd:PLN03130 638 LDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRGT-----------VAYVPQVSWIFN-ATVRDNILFGSP- 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 99 gLKLNREQRA-QVTAIAGQmgmdtlLDRLPG-----------ELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQ 166
Cdd:PLN03130 705 -FDPERYERAiDVTALQHD------LDLLPGgdlteigergvNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGR 777
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1994014911 167 EmltlVADVCQRQQL---TLLMVS---HSVEDAARIaprsIVVAEGRIAWDGATDDLLS 219
Cdd:PLN03130 778 Q----VFDKCIKDELrgkTRVLVTnqlHFLSQVDRI----ILVHEGMIKEEGTYEELSN 828
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
20-228 |
1.94e-13 |
|
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: 67.96 E-value: 1.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 20 LSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLlidgeKHNTTPPAQRPVSMLFQEnnlfnhlTVRQNIGLGIHpg 99
Cdd:cd03291 58 LKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-----KHSGRISFSSQFSWIMPG-------TIKENIIFGVS-- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 100 lklNREQRAQVTAIAGQMGMDtlLDRLP-------GE----LSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEM 168
Cdd:cd03291 124 ---YDEYRYKSVVKACQLEED--ITKFPekdntvlGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEI 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1994014911 169 LTlvADVCQ-RQQLTLLMVSHSVEDaARIAPRSIVVAEGRIAWDGATDDLLSGNSSASALL 228
Cdd:cd03291 199 FE--SCVCKlMANKTRILVTSKMEH-LKKADKILILHEGSSYFYGTFSELQSLRPDFSSKL 256
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-188 |
2.95e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 68.46 E-value: 2.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 2 LKLNDVTWLYQHL-----PMRFTLsvERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEK-HNTTPPAQRP-VS 74
Cdd:PRK10522 323 LELRNVTFAYQDNgfsvgPINLTI--KRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPvTAEQPEDYRKlFS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 75 MLFQENNLFNHLTVRQniGLGIHPGLK---LNREQRAQVTAIAGQMGMDTlldrlpgELSGGQRQRAALARCLVRQQPVL 151
Cdd:PRK10522 401 AVFTDFHLFDQLLGPE--GKPANPALVekwLERLKMAHKLELEDGRISNL-------KLSKGQKKRLALLLALAEERDIL 471
|
170 180 190
....*....|....*....|....*....|....*..
gi 1994014911 152 LLDEPFSALDPALRQEMLTLVADVCQRQQLTLLMVSH 188
Cdd:PRK10522 472 LLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISH 508
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-188 |
3.44e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 68.21 E-value: 3.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 4 LNDVTWLYQHLPM---RFTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGekhnttppaqRPVSMLfqen 80
Cdd:PRK10790 343 IDNVSFAYRDDNLvlqNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDG----------RPLSSL---- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 81 nlfNHLTVRQNIGL--------------GIHPGLKLNREQ------RAQVTAIAGQM--GMDTLLDRLPGELSGGQRQRA 138
Cdd:PRK10790 409 ---SHSVLRQGVAMvqqdpvvladtflaNVTLGRDISEEQvwqaleTVQLAELARSLpdGLYTPLGEQGNNLSVGQKQLL 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1994014911 139 ALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVADVcqRQQLTLLMVSH 188
Cdd:PRK10790 486 ALARVLVQTPQILILDEATANIDSGTEQAIQQALAAV--REHTTLVVIAH 533
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
18-209 |
4.00e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.01 E-value: 4.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 18 FTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGE--KHNTTPPAQRPVSMLFQENN----LFNHLTVRQN 91
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKpiDIRSPRDAIRAGIMLCPEDRkaegIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 92 IGLG-----IHPGLKLNREQRAQVTA--IAgQMGMDTL-LDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPA 163
Cdd:PRK11288 352 INISarrhhLRAGCLINNRWEAENADrfIR-SLNIKTPsREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVG 430
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1994014911 164 LRQEMLTLVADVCQrQQLTLLMVSHSVEDAARIAPRSIVVAEGRIA 209
Cdd:PRK11288 431 AKHEIYNVIYELAA-QGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
14-161 |
4.25e-13 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 67.89 E-value: 4.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 14 LPMrftlsVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLlidgekhnTTPPAQRPVSMLFQENNLFNHLT-VRQNi 92
Cdd:COG1245 93 LPV-----PKKGKVTGILGPNGIGKSTALKILSGELKPNLGDY--------DEEPSWDEVLKRFRGTELQDYFKkLANG- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 93 glGIHPGLK------------------LNR-EQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLL 153
Cdd:COG1245 159 --EIKVAHKpqyvdlipkvfkgtvrelLEKvDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFF 236
|
....*...
gi 1994014911 154 DEPFSALD 161
Cdd:COG1245 237 DEPSSYLD 244
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-217 |
4.52e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 68.08 E-value: 4.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 20 LSVERGERIAVLGPSGAGKSTLLNLIAGFLPPA-SGSLLIDGEkhnttppaqrpVSMLFQENNLFNhLTVRQNIGLGihP 98
Cdd:PLN03232 638 LEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAeTSSVVIRGS-----------VAYVPQVSWIFN-ATVRENILFG--S 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 99 GLKLNREQRA-QVTAIAGQmgmdtlLDRLPGE-----------LSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQ 166
Cdd:PLN03232 704 DFESERYWRAiDVTALQHD------LDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAH 777
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1994014911 167 EmltlVADVCQRQQL---TLLMVSHSVEDAARIaPRSIVVAEGRIAWDGATDDL 217
Cdd:PLN03232 778 Q----VFDSCMKDELkgkTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAEL 826
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-209 |
5.01e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.50 E-value: 5.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQR-PVSMLF-----QENNLFNHLTVRQNI 92
Cdd:PRK09700 283 SFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAvKKGMAYitesrRDNGFFPNFSIAQNM 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 93 glGIHPGLKLNR---------EQRAQVTAIAGQMGMD---TLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSAL 160
Cdd:PRK09700 363 --AISRSLKDGGykgamglfhEVDEQRTAENQRELLAlkcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGI 440
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1994014911 161 DPALRQEMLTLVADVCQrQQLTLLMVSHSVEDAARIAPRSIVVAEGRIA 209
Cdd:PRK09700 441 DVGAKAEIYKVMRQLAD-DGKVILMVSSELPEIITVCDRIAVFCEGRLT 488
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-160 |
6.01e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 67.34 E-value: 6.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPP---AQRPVSMLFQENNLFNHLTVRQNIGLG 95
Cdd:PRK10762 24 ALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPkssQEAGIGIIHQELNLIPQLTIAENIFLG 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1994014911 96 IHP----GLKLNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSAL 160
Cdd:PRK10762 104 REFvnrfGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDAL 172
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
20-217 |
6.49e-13 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 67.07 E-value: 6.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 20 LSVERGERIAVLGPSGAGK------STLLNLIAGFLPPASGSLLIDGEKHNTTPPAQRPVSMLFQENnlfnhLTVRQNIG 93
Cdd:NF000106 34 LDVREGTVLGVLGP*GAA**rgalpAHV*GPDAGRRPWRF*TWCANRRALRRTIG*HRPVR*GRRES-----FSGRENLY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 94 LgIHPGLKLNR-EQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:NF000106 109 M-IGR*LDLSRkDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1994014911 173 ADVCqRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDL 217
Cdd:NF000106 188 RSMV-RDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-217 |
1.11e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 66.80 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKS----TLLNLI--AGFLPPASGSLLIDGEKH----NTTPPAQ------RPVSMLFQE--N 80
Cdd:PRK10261 36 SFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGLVQCDKMLLRRRSRQvielSEQSAAQmrhvrgADMAMIFQEpmT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 81 NLFNHLTVRQNIGLGIHPGLKLNREQR-AQVTAIAGQMGM---DTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEP 156
Cdd:PRK10261 116 SLNPVFTVGEQIAESIRLHQGASREEAmVEAKRMLDQVRIpeaQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEP 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1994014911 157 FSALDPALRQEMLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDL 217
Cdd:PRK10261 196 TTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-228 |
1.51e-12 |
|
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: 66.51 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKhnttppAQRPVSMLFQENNLfnhltvRQNIGLGiHP 98
Cdd:TIGR00957 658 TFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSV------AYVPQQAWIQNDSL------RENILFG-KA 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 99 glkLNrEQRAQVTAIAGQMGMDtlLDRLPG-----------ELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQE 167
Cdd:TIGR00957 725 ---LN-EKYYQQVLEACALLPD--LEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKH 798
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1994014911 168 ML-TLVADVCQRQQLTLLMVSHSVEdaarIAPRS---IVVAEGRIAWDGATDDLLSGNSSASALL 228
Cdd:TIGR00957 799 IFeHVIGPEGVLKNKTRILVTHGIS----YLPQVdviIVMSGGKISEMGSYQELLQRDGAFAEFL 859
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
24-202 |
1.98e-12 |
|
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: 62.78 E-value: 1.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 24 RGERIAVLGPSGAGKSTLLNLIAGFLPPASGS-LLIDGEKHNTTPPAQRpvsmlfqennlfnhltvrqniglgihpglkl 102
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQL------------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 103 nreqraqvtaiagqmgMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPA-----LRQEMLTLVADVCQ 177
Cdd:smart00382 50 ----------------LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEqeallLLLEELRLLLLLKS 113
|
170 180
....*....|....*....|....*
gi 1994014911 178 RQQLTLLMVSHSVEDAARIAPRSIV 202
Cdd:smart00382 114 EKNLTVILTTNDEKDLGPALLRRRF 138
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
19-219 |
2.22e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 65.59 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGF--LPPASGSLL-----------IDGEKHNTTPPAQRPVSMLFQENNLFN- 84
Cdd:TIGR03269 20 SFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyVERPSKVGEPCPVCGGTLEPEEVDFWNl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 85 ----HLTVRQNIGLGIHPGLKLNREQRAQVTAI--------AGQMGMDTLLD------------RLPGELSGGQRQRAAL 140
Cdd:TIGR03269 100 sdklRRRIRKRIAIMLQRTFALYGDDTVLDNVLealeeigyEGKEAVGRAVDliemvqlshritHIARDLSGGEKQRVVL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1994014911 141 ARCLVRQQPVLLLDEPFSALDPALRQEMLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:TIGR03269 180 ARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-169 |
4.58e-12 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 64.93 E-value: 4.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLlidgeKHNTTPPAQRPVSMLFQEnnlfnhlTVRQNIGLGIHp 98
Cdd:TIGR01271 446 SFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-----KHSGRISFSPQTSWIMPG-------TIKDNIIFGLS- 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 99 glklNREQRAQVTAIAGQMGMDTLL----DRLP-GE----LSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEML 169
Cdd:TIGR01271 513 ----YDEYRYTSVIKACQLEEDIALfpekDKTVlGEggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIF 588
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
18-188 |
5.08e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 64.59 E-value: 5.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 18 FTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSL----------------LIDGEKhnttppaqrpvsmlfqenn 81
Cdd:PRK11147 338 FSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhcgtklevayfdqhraELDPEK------------------- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 82 lfnhlTVRQNIGLGihpglklnreqrAQVTAIAGQ----MG--MDTLLD----RLPGE-LSGGQRQRAALARCLVRQQPV 150
Cdd:PRK11147 399 -----TVMDNLAEG------------KQEVMVNGRprhvLGylQDFLFHpkraMTPVKaLSGGERNRLLLARLFLKPSNL 461
|
170 180 190
....*....|....*....|....*....|....*...
gi 1994014911 151 LLLDEPFSALDpalrQEMLTLVADVCQRQQLTLLMVSH 188
Cdd:PRK11147 462 LILDEPTNDLD----VETLELLEELLDSYQGTVLLVSH 495
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
18-209 |
5.24e-12 |
|
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: 62.54 E-value: 5.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 18 FTLSVERGERIAVLGPSGAGKSTLLNLIAGFlP---PASGSLLIDGEKHNTTPP---AQRPVSMLFQENNLFnhltvrqn 91
Cdd:cd03217 19 VNLTIKKGEVHALMGPNGSGKSTLAKTIMGH-PkyeVTEGEILFKGEDITDLPPeerARLGIFLAFQYPPEI-------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 92 iglgihPGLKLNreqraqvtaiagqmgmdTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALD-PALRqemlt 170
Cdd:cd03217 90 ------PGVKNA-----------------DFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDiDALR----- 141
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1994014911 171 LVADVCQR---QQLTLLMVSHSVEDAARIAP-RSIVVAEGRIA 209
Cdd:cd03217 142 LVAEVINKlreEGKSVLIITHYQRLLDYIKPdRVHVLYDGRIV 184
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
21-217 |
5.68e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.57 E-value: 5.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 21 SVERGERIAVLGPSGAGKSTLLNLIAGFLPPAS-GSLLIDGEKHNTTPPAQ---RPVSMLFQE---NNLFNHLTVRQNIG 93
Cdd:PRK13549 284 SLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGKPVKIRNPQQaiaQGIAMVPEDrkrDGIVPVMGVGKNIT 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 94 LGI-----HPG-LKLNREQRAQVTAIAgQMGMDTLLDRLP-GELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQ 166
Cdd:PRK13549 364 LAAldrftGGSrIDDAAELKTILESIQ-RLKVKTASPELAiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKY 442
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1994014911 167 EMLTLVADVCQrQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDL 217
Cdd:PRK13549 443 EIYKLINQLVQ-QGVAIIVISSELPEVLGLSDRVLVMHEGKLKGDLINHNL 492
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-224 |
5.80e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 64.61 E-value: 5.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 1 MLKLNDVTWLYQ-HLP---MRFTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDG---EKHNTTPpAQRPV 73
Cdd:PLN03232 1234 SIKFEDVHLRYRpGLPpvlHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDcdvAKFGLTD-LRRVL 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 74 SMLFQENNLFNHlTVRQNIG-LGIHPGLKLNRE-QRAQVTAIAGQ--MGMDTLLDRLPGELSGGQRQRAALARCLVRQQP 149
Cdd:PLN03232 1313 SIIPQSPVLFSG-TVRFNIDpFSEHNDADLWEAlERAHIKDVIDRnpFGLDAEVSEGGENFSVGQRQLLSLARALLRRSK 1391
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1994014911 150 VLLLDEPFSALDpaLRQEMLTLVADVCQRQQLTLLMVSH---SVEDAARIaprsIVVAEGRIAWDGATDDLLSGNSSA 224
Cdd:PLN03232 1392 ILVLDEATASVD--VRTDSLIQRTIREEFKSCTMLVIAHrlnTIIDCDKI----LVLSSGQVLEYDSPQELLSRDTSA 1463
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
18-208 |
7.74e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 64.25 E-value: 7.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 18 FTLsvERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQ------RPVSMLFQENNLFNHLTVRQN 91
Cdd:PRK10762 273 FTL--RKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglangiVYISEDRKRDGLVLGMSVKEN 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 92 IGLG-----IHPGLKLNR-EQRAQVTAIAGQMGMDT-LLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPAL 164
Cdd:PRK10762 351 MSLTalryfSRAGGSLKHaDEQQAVSDFIRLFNIKTpSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGA 430
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1994014911 165 RQEMLTLVADVCQrQQLTLLMVSHSVEDAARIAPRSIVVAEGRI 208
Cdd:PRK10762 431 KKEIYQLINQFKA-EGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
19-223 |
8.65e-12 |
|
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: 62.95 E-value: 8.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPpASGSLLIDGEKHNTTPPAQ--RPVSMLFQENNLFNHlTVRQNIglgi 96
Cdd:cd03289 24 SFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKwrKAFGVIPQKVFIFSG-TFRKNL---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 97 HPGLKLNREQRAQVtaiAGQMGMDTLLDRLPGEL-----------SGGQRQRAALARCLVRQQPVLLLDEPFSALDP--- 162
Cdd:cd03289 98 DPYGKWSDEEIWKV---AEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPity 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1994014911 163 -ALRQEMLTLVADVcqrqqlTLLMVSHSVEdAARIAPRSIVVAEGRIAWDGATDDLLSGNSS 223
Cdd:cd03289 175 qVIRKTLKQAFADC------TVILSEHRIE-AMLECQRFLVIEENKVRQYDSIQKLLNEKSH 229
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
19-209 |
8.77e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 63.92 E-value: 8.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQRPVSMLF------QENNLFNHLTVRQNI 92
Cdd:PRK15439 283 SLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVylpedrQSSGLYLDAPLAWNV 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 93 -GLGIH-PGLKLNREQ-RAQVTAIAGQMGMD-TLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEM 168
Cdd:PRK15439 363 cALTHNrRGFWIKPAReNAVLERYRRALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDI 442
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1994014911 169 LTLVADVCQrQQLTLLMVSHSVEDAARIAPRSIVVAEGRIA 209
Cdd:PRK15439 443 YQLIRSIAA-QNVAVLFISSDLEEIEQMADRVLVMHQGEIS 482
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-155 |
1.19e-11 |
|
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: 63.66 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 2 LKLNDVTWLYQHL--PMRFT-----LSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEkhnTTPPAQRPV- 73
Cdd:COG4615 328 LELRGVTYRYPGEdgDEGFTlgpidLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQ---PVTADNREAy 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 74 ----SMLFQENNLFNHLtvrqnigLGIHPGlklnrEQRAQVTAIAGQMGMDT--------LLDRlpgELSGGQRQRAALA 141
Cdd:COG4615 405 rqlfSAVFSDFHLFDRL-------LGLDGE-----ADPARARELLERLELDHkvsvedgrFSTT---DLSQGQRKRLALL 469
|
170
....*....|....
gi 1994014911 142 RCLVRQQPVLLLDE 155
Cdd:COG4615 470 VALLEDRPILVFDE 483
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-218 |
1.58e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 63.64 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLidgekhnttppAQRPVSMLFQENNLFNhLTVRQNIglgihp 98
Cdd:PTZ00243 680 SVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-----------AERSIAYVPQQAWIMN-ATVRGNI------ 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 99 gLKLNREQRA---------QVTAIAGQM--GMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQe 167
Cdd:PTZ00243 742 -LFFDEEDAArladavrvsQLEADLAQLggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGE- 819
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1994014911 168 mltLVADVCQRQQL---TLLMVSHSVEDAARiAPRSIVVAEGRIAWDGATDDLL 218
Cdd:PTZ00243 820 ---RVVEECFLGALagkTRVLATHQVHVVPR-ADYVVALGDGRVEFSGSSADFM 869
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
18-168 |
1.58e-11 |
|
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: 62.00 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 18 FTLSVER-GERIAVLGPSGAGKSTLLNLIAGFLPPASGsllidgeKHnTTPPAQRPVSMLFQENNLFNHLTVRQNIGLG- 95
Cdd:cd03236 18 HRLPVPReGQVLGLVGPNGIGKSTALKILAGKLKPNLG-------KF-DDPPDWDEILDEFRGSELQNYFTKLLEGDVKv 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 96 -IHP--------------GLKLNR-EQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSA 159
Cdd:cd03236 90 iVKPqyvdlipkavkgkvGELLKKkDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSY 169
|
....*....
gi 1994014911 160 LDpaLRQEM 168
Cdd:cd03236 170 LD--IKQRL 176
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
27-209 |
1.98e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 62.96 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 27 RIAVLGPSGAGKSTLLNLIAGFLPPASGSLLidgekhnTTPPAQRPVsmlfqennlFNHLTVrQNIGLGIHPGLKLNR-- 104
Cdd:PLN03073 537 RIAMVGPNGIGKSTILKLISGELQPSSGTVF-------RSAKVRMAV---------FSQHHV-DGLDLSSNPLLYMMRcf 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 105 ----EQRaqVTAIAGQMGMDTLLDRLPG-ELSGGQRQRAALARCLVRQQPVLLLDEPFSALD----PALRQEMLTLvadv 175
Cdd:PLN03073 600 pgvpEQK--LRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDldavEALIQGLVLF---- 673
|
170 180 190
....*....|....*....|....*....|....
gi 1994014911 176 cqrqQLTLLMVSHSVEDAARIAPRSIVVAEGRIA 209
Cdd:PLN03073 674 ----QGGVLMVSHDEHLISGSVDELWVVSEGKVT 703
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-206 |
6.23e-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: 6.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPpASGSLLIDGEKHNTTPPAQ--RPVSMLFQENNLFNHlTVRQNIglgi 96
Cdd:TIGR01271 1239 SFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTwrKAFGVIPQKVFIFSG-TFRKNL---- 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 97 HPGLKLNREQraqVTAIAGQMGMDTLLDRLPGEL-----------SGGQRQRAALARCLVRQQPVLLLDEPFSALDPA-- 163
Cdd:TIGR01271 1313 DPYEQWSDEE---IWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVtl 1389
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1994014911 164 --LRQEMLTLVADvCqrqqlTLLMVSHSVEdaARIAPRSIVVAEG 206
Cdd:TIGR01271 1390 qiIRKTLKQSFSN-C-----TVILSEHRVE--ALLECQQFLVIEG 1426
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
74-195 |
7.17e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.58 E-value: 7.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 74 SMLFQENNLFNhLTVRQNIGLGIHPGLKLNREQRAQVTAIagqmgmDTLLDRLPGE-----------LSGGQRQRAALAR 142
Cdd:PTZ00265 1299 SIVSQEPMLFN-MSIYENIKFGKEDATREDVKRACKFAAI------DEFIESLPNKydtnvgpygksLSGGQKQRIAIAR 1371
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1994014911 143 CLVRQQPVLLLDEPFSALDPALRQEMLTLVADVCQRQQLTLLMVSHSVEDAAR 195
Cdd:PTZ00265 1372 ALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR 1424
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
20-161 |
7.91e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.12 E-value: 7.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 20 LSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEkhnttppaqRPVSMLFQ------ENNLFN--------- 84
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQD---------LIVARLQQdpprnvEGTVYDfvaegieeq 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 85 --HLTVRQNIG--LGIHPGLK-LNREQRAQ--------------VTAIAGQMGMDTllDRLPGELSGGQRQRAALARCLV 145
Cdd:PRK11147 95 aeYLKRYHDIShlVETDPSEKnLNELAKLQeqldhhnlwqlenrINEVLAQLGLDP--DAALSSLSGGWLRKAALGRALV 172
|
170
....*....|....*.
gi 1994014911 146 RQQPVLLLDEPFSALD 161
Cdd:PRK11147 173 SNPDVLLLDEPTNHLD 188
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
19-160 |
8.28e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.90 E-value: 8.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEK---HNTTPPAQRPVSMLFQENNLFNHLTVRQNIGLG 95
Cdd:PRK10982 18 NLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEidfKSSKEALENGISMVHQELNLVLQRSVMDNMWLG 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1994014911 96 IHP--GLKLNREQRAQVT-AIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSAL 160
Cdd:PRK10982 98 RYPtkGMFVDQDKMYRDTkAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
19-218 |
9.26e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 60.91 E-value: 9.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDG----EKHNTTPPAQRPVSM---LfqENNLFNHLTVRQN 91
Cdd:NF033858 21 SLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGgdmaDARHRRAVCPRIAYMpqgL--GKNLYPTLSVFEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 92 I-------GLGihpglklNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPAL 164
Cdd:NF033858 99 LdffgrlfGQD-------AAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLS 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1994014911 165 RQEMLTLVADVC-QRQQLTLLMVSHSVEDAARIaprSIVVA--EGRIAWDGATDDLL 218
Cdd:NF033858 172 RRQFWELIDRIRaERPGMSVLVATAYMEEAERF---DWLVAmdAGRVLATGTPAELL 225
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
17-161 |
1.11e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 60.72 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 17 RFTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIdGEKhnttppaqrpVSMLF---QENNLFNHLTVRQNI- 92
Cdd:TIGR03719 340 DLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GET----------VKLAYvdqSRDALDPNKTVWEEIs 408
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1994014911 93 -GLGIhpgLKL-NRE--QRAQVTAIaGQMGMDTllDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALD 161
Cdd:TIGR03719 409 gGLDI---IKLgKREipSRAYVGRF-NFKGSDQ--QKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
17-188 |
1.49e-10 |
|
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: 60.53 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 17 RFTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPaQRPvsmlfqennLFNHLTVRQNIglgI 96
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVP-QRP---------YMTLGTLRDQI---I 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 97 HPGLKLNREQR----AQVTAIAGQMGMDTLLDRLPG---------ELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPA 163
Cdd:TIGR00954 537 YPDSSEDMKRRglsdKDLEQILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVD 616
|
170 180
....*....|....*....|....*
gi 1994014911 164 LRQEMLTLvadvCQRQQLTLLMVSH 188
Cdd:TIGR00954 617 VEGYMYRL----CREFGITLFSVSH 637
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
19-188 |
1.53e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 59.36 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLidgekhnttPPAQRPVSMLFQENNLFNHLTVRQNIGLGIHP 98
Cdd:PRK09544 24 SLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---------RNGKLRIGYVPQKLYLDTTLPLTVNRFLRLRP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 99 GLKlnreqRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVADVCQR 178
Cdd:PRK09544 95 GTK-----KEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRE 169
|
170
....*....|
gi 1994014911 179 QQLTLLMVSH 188
Cdd:PRK09544 170 LDCAVLMVSH 179
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
14-168 |
1.69e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.21 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 14 LPMrftlsVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNttppaqrpVSMLFQENNLFNHLT-VRQNi 92
Cdd:PRK13409 93 LPI-----PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPSWDE--------VLKRFRGTELQNYFKkLYNG- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 93 glGIHPGLK------------------LNR-EQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLL 153
Cdd:PRK13409 159 --EIKVVHKpqyvdlipkvfkgkvrelLKKvDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFF 236
|
170
....*....|....*
gi 1994014911 154 DEPFSALDpaLRQEM 168
Cdd:PRK13409 237 DEPTSYLD--IRQRL 249
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
16-218 |
2.90e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 59.34 E-value: 2.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 16 MRFTLsvERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIdgekHNTTPPAQR------PVSMLFQENNLFNHlTVR 89
Cdd:PRK10789 334 VNFTL--KPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRF----HDIPLTKLQldswrsRLAVVSQTPFLFSD-TVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 90 QNIGLGIHPGLKLNREQRAQVTAIagqmgMDTLLdRLP-------GE----LSGGQRQRAALARCLVRQQPVLLLDEPFS 158
Cdd:PRK10789 407 NNIALGRPDATQQEIEHVARLASV-----HDDIL-RLPqgydtevGErgvmLSGGQKQRISIARALLLNAEILILDDALS 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1994014911 159 ALDPALRQEMLTLVADvcQRQQLTLLMVSH---SVEDAARIaprsIVVAEGRIAWDGATDDLL 218
Cdd:PRK10789 481 AVDGRTEHQILHNLRQ--WGEGRTVIISAHrlsALTEASEI----LVMQHGHIAQRGNHDQLA 537
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-219 |
2.92e-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: 59.57 E-value: 2.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEK------HNTtppaQRPVSMLFQENNLFNHlTVRQNI 92
Cdd:TIGR00957 1306 NVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNiakiglHDL----RFKITIIPQDPVLFSG-SLRMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 93 glgiHPGLKLNREQRAQVTAIAGQMG-MDTLLDRLPGE-------LSGGQRQRAALARCLVRQQPVLLLDEPFSALDpaL 164
Cdd:TIGR00957 1381 ----DPFSQYSDEEVWWALELAHLKTfVSALPDKLDHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVD--L 1454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1994014911 165 RQEMLTLVADVCQRQQLTLLMVSH---SVEDAARIaprsIVVAEGRIAWDGATDDLLS 219
Cdd:TIGR00957 1455 ETDNLIQSTIRTQFEDCTVLTIAHrlnTIMDYTRV----IVLDKGEVAEFGAPSNLLQ 1508
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
18-163 |
4.43e-10 |
|
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: 57.27 E-value: 4.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 18 FTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPA---SGSLLIDG-EKHNTTPPAQRPVSMLFQENNLFNHLTVRQNIG 93
Cdd:cd03233 26 FSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGiPYKEFAEKYPGEIIYVSEEDVHFPTLTVRETLD 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 94 LGIHpgLKLNREQRAqvtaiagqmgmdtlldrlpgeLSGGQRQRAALARCLVRQQPVLLLDEPFSALDPA 163
Cdd:cd03233 106 FALR--CKGNEFVRG---------------------ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSS 152
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
18-217 |
7.24e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 57.81 E-value: 7.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 18 FTLSVerGERIAVLGPSGAGKSTLLNLIAGFLPP---ASGSLLIDGEKHNTTPPAQ------RPVSMLFQE--NNLFNHL 86
Cdd:PRK09473 37 FSLRA--GETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPEKElnklraEQISMIFQDpmTSLNPYM 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 87 TVRQNIG--LGIHPGLKLNREQRAQVTAIAG--------QMGMdtlldrLPGELSGGQRQRAALARCLVRQQPVLLLDEP 156
Cdd:PRK09473 115 RVGEQLMevLMLHKGMSKAEAFEESVRMLDAvkmpearkRMKM------YPHEFSGGMRQRVMIAMALLCRPKLLIADEP 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1994014911 157 FSALDPALRQEMLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDL 217
Cdd:PRK09473 189 TTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-207 |
8.54e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 57.88 E-value: 8.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPAS--GSLLIDGEK---HNTTPPAQRPVSMLFQENNLFNHLTVRQNIG 93
Cdd:NF040905 21 NLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVcrfKDIRDSEALGIVIIHQELALIPYLSIAENIF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 94 LGIHP---GLKLNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLT 170
Cdd:NF040905 101 LGNERakrGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLD 180
|
170 180 190
....*....|....*....|....*....|....*..
gi 1994014911 171 LVADVcQRQQLTLLMVSHSVEDAARIAPRSIVVAEGR 207
Cdd:NF040905 181 LLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
18-161 |
2.24e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.67 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 18 FTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIdGEKhnttppaqrpVSMLFQE---NNLFNHLTVRQNI-- 92
Cdd:PRK11819 343 LSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GET----------VKLAYVDqsrDALDPNKTVWEEIsg 411
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1994014911 93 GLGIhpgLKL-NRE--QRAQVTAIaGQMGMDTllDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALD 161
Cdd:PRK11819 412 GLDI---IKVgNREipSRAYVGRF-NFKGGDQ--QKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
18-218 |
3.00e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.44 E-value: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 18 FTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIdGEKHNTTPPAQRPVSMLFQENNLFNHLTV-RQniglgi 96
Cdd:PRK15064 338 LNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW-SENANIGYYAQDHAYDFENDLTLFDWMSQwRQ------ 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 97 hPGlklNREQraQVTAIAGQM--GMDTlLDRLPGELSGGQRQRAALARcLVRQQP-VLLLDEPFSALD-PALrqEMLTLV 172
Cdd:PRK15064 411 -EG---DDEQ--AVRGTLGRLlfSQDD-IKKSVKVLSGGEKGRMLFGK-LMMQKPnVLVMDEPTNHMDmESI--ESLNMA 480
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1994014911 173 ADVCQRqqlTLLMVSHSVEDAARIAPRSI-VVAEGRIAWDGATDDLL 218
Cdd:PRK15064 481 LEKYEG---TLIFVSHDREFVSSLATRIIeITPDGVVDFSGTYEEYL 524
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
22-203 |
1.31e-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: 52.96 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 22 VERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKhnttpPAQRPvsmlfqennlfnhltvrQNIglgihpglk 101
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGIT-----PVYKP-----------------QYI--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 102 lnreqraqvtaiagqmgmdtlldrlpgELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVADVCQRQQL 181
Cdd:cd03222 71 ---------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKK 123
|
170 180
....*....|....*....|..
gi 1994014911 182 TLLMVSHSVEDAARIAPRSIVV 203
Cdd:cd03222 124 TALVVEHDLAVLDYLSDRIHVF 145
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
25-188 |
1.41e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.41 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 25 GERIAVLGPSGAGKSTLLNLIAGFLPPASGSL-LIDGEKHNTTppAQRPVSMLFQENNLFNHLTvrqniglGIHPglkln 103
Cdd:PRK10636 338 GSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYF--AQHQLEFLRADESPLQHLA-------RLAP----- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 104 REQRAQVTAIAGQMGM--DTLLDrLPGELSGGQRQRAALArCLVRQQP-VLLLDEPFSALDPALRQEMLTLVADVcqrqQ 180
Cdd:PRK10636 404 QELEQKLRDYLGGFGFqgDKVTE-ETRRFSGGEKARLVLA-LIVWQRPnLLLLDEPTNHLDLDMRQALTEALIDF----E 477
|
....*...
gi 1994014911 181 LTLLMVSH 188
Cdd:PRK10636 478 GALVVVSH 485
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
17-219 |
3.98e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 52.88 E-value: 3.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 17 RFTLSVERGERIAVLGPSGAGKSTLLNLIAGFLP-----PASGSLLIDGEKHNTTPPAQRP-----VSMLFQENNlfNHL 86
Cdd:PRK15093 25 RVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrvTADRMRFDDIDLLRLSPRERRKlvghnVSMIFQEPQ--SCL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 87 TVRQNIGLGIH---PGLKLN---------REQRA-QVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLL 153
Cdd:PRK15093 103 DPSERVGRQLMqniPGWTYKgrwwqrfgwRKRRAiELLHRVGIKDHKDAMRSFPYELTEGECQKVMIAIALANQPRLLIA 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1994014911 154 DEPFSALDPALRQEMLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:PRK15093 183 DEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVT 248
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
17-219 |
1.54e-07 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 51.06 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 17 RFTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPP----ASGSLLIDGEKHNTTPPAQR------PVSMLFQE------- 79
Cdd:COG4170 25 RVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPRERrkiigrEIAMIFQEpsscldp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 80 -NNLFNHLTvrQNIGLGIHPGLKLNREQRAQVTAIA-----GQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLL 153
Cdd:COG4170 105 sAKIGDQLI--EAIPSWTFKGKWWQRFKWRKKRAIEllhrvGIKDHKDIMNSYPHELTEGECQKVMIAMAIANQPRLLIA 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1994014911 154 DEPFSALDPALRQEMLTLVADVCQRQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLLS 219
Cdd:COG4170 183 DEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILK 248
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
18-208 |
1.63e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 51.18 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 18 FTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPAQRPVSMLF------QENNLFNHLTVRQN 91
Cdd:COG3845 277 VSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVAyipedrLGRGLVPDMSVAEN 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 92 IGLGIHPGLKLNR---EQRAQVTAIAGQMgMDTLLDRLPGE------LSGGQRQRAALARCLVRQQPVLLLDEPFSALDP 162
Cdd:COG3845 357 LILGRYRRPPFSRggfLDRKAIRAFAEEL-IEEFDVRTPGPdtparsLSGGNQQKVILARELSRDPKLLIAAQPTRGLDV 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1994014911 163 ----ALRQEMLTLvadvcqRQQ-LTLLMVSHSVEDAARIAPRSIVVAEGRI 208
Cdd:COG3845 436 gaieFIHQRLLEL------RDAgAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
19-224 |
3.30e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.51 E-value: 3.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTPPA--QRPVSMLFQENNLFNHlTVRQNIG-LG 95
Cdd:PLN03130 1259 SFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMdlRKVLGIIPQAPVLFSG-TVRFNLDpFN 1337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 96 IHPGLKL-NREQRAQVTAIA--GQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALD---PALRQEML 169
Cdd:PLN03130 1338 EHNDADLwESLERAHLKDVIrrNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDvrtDALIQKTI 1417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1994014911 170 TLVADVCqrqqlTLLMVSH---SVEDAARIaprsIVVAEGRIAWDGATDDLLSGNSSA 224
Cdd:PLN03130 1418 REEFKSC-----TMLIIAHrlnTIIDCDRI----LVLDAGRVVEFDTPENLLSNEGSA 1466
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
25-228 |
4.26e-07 |
|
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: 49.52 E-value: 4.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 25 GERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNTTP--PAQRPVSMLFQENNLFNhltvrQNIGLGIHPGLKL 102
Cdd:cd03288 47 GQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPlhTLRSRLSIILQDPILFS-----GSIRFNLDPECKC 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 103 NREQRAQVTAIAGqmgMDTLLDRLPGEL-----------SGGQRQRAALARCLVRQQPVLLLDEPFSALDPA----LRQE 167
Cdd:cd03288 122 TDDRLWEALEIAQ---LKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASIDMAteniLQKV 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1994014911 168 MLTLVADvcqRQQLTLLMVSHSVEDAARIaprsIVVAEGRIAWDGATDDLLSGNSSASALL 228
Cdd:cd03288 199 VMTAFAD---RTVVTIAHRVSTILDADLV----LVLSRGILVECDTPENLLAQEDGVFASL 252
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
32-194 |
5.11e-07 |
|
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: 48.76 E-value: 5.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 32 GPSGAGKSTLLNLIagflppasgSLLIDGEKHNTTPPAQRPVSMLF-QENNLFNHLTVRQNIGLGIhpglKLNREQRAQV 110
Cdd:cd03240 29 GQNGAGKTTIIEAL---------KYALTGELPPNSKGGAHDPKLIReGEVRAQVKLAFENANGKKY----TITRSLAILE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 111 TAI-AGQMGMDTLLDRLPGELSGGQRQ------RAALARCLVRQQPVLLLDEPFSALDPA-LRQEMLTLVADVCQRQQLT 182
Cdd:cd03240 96 NVIfCHQGESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEnIEESLAEIIEERKSQKNFQ 175
|
170
....*....|....
gi 1994014911 183 LLMVSH--SVEDAA 194
Cdd:cd03240 176 LIVITHdeELVDAA 189
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
2-202 |
1.02e-06 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 48.03 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 2 LKLNDVTWLYQHLPMRFTlSVERGERIAVLGPSGAGKSTLLNLIAGFL---PPASGSlliDGEKHNTTPPAQRPVSMLFQ 78
Cdd:cd03279 6 LELKNFGPFREEQVIDFT-GLDNNGLFLICGPTGAGKSTILDAITYALygkTPRYGR---QENLRSVFAPGEDTAEVSFT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 79 -ENNLFNHLTVRQniglgihpgLKLNREQRAQvTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCL----VRQQP---- 149
Cdd:cd03279 82 fQLGGKKYRVERS---------RGLDYDQFTR-IVLLPQGEFDRFLARPVSTLSGGETFLASLSLALalseVLQNRggar 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1994014911 150 --VLLLDEPFSALDPALRQEMLTLVADVcQRQQLTLLMVSHSVEDAARIAPRSIV 202
Cdd:cd03279 152 leALFIDEGFGTLDPEALEAVATALELI-RTENRMVGVISHVEELKERIPQRLEV 205
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
22-161 |
1.98e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.18 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 22 VERGERIAVLGPSGAGKSTLLNLIAGFLPPA---SGSLLIDGEKHNTTppAQRPVSMLFQENNLFNHLTVRQNIGLGIH- 97
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLNVLAERVTTGvitGGDRLVNGRPLDSS--FQRSIGYVQQQDLHLPTSTVRESLRFSAYl 863
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1994014911 98 --PGLKLNREQRAQVTAIAGQMGMDTLLDRL---PGE-LSGGQRQRAALARCLVrQQPVLL--LDEPFSALD 161
Cdd:TIGR00956 864 rqPKSVSKSEKMEYVEEVIKLLEMESYADAVvgvPGEgLNVEQRKRLTIGVELV-AKPKLLlfLDEPTSGLD 934
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
3-190 |
2.14e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.96 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 3 KLNDVTW-----LYQHLPMRFTLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEkhnttppaqrpVSMLF 77
Cdd:PRK13545 23 KLKDLFFrskdgEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS-----------AALIA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 78 QENNLFNHLTVRQNIGL-GIHPGLKlnREQRAQVT-AIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDE 155
Cdd:PRK13545 92 ISSGLNGQLTGIENIELkGLMMGLT--KEKIKEIIpEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE 169
|
170 180 190
....*....|....*....|....*....|....*
gi 1994014911 156 PFSALDPALRQEMLTLVADVcQRQQLTLLMVSHSV 190
Cdd:PRK13545 170 ALSVGDQTFTKKCLDKMNEF-KEQGKTIFFISHSL 203
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
16-161 |
2.16e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.10 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 16 MRFTLSveRGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDgEKHNTTPPA----QRPVSMLFQENNLFNHlTVRQN 91
Cdd:PTZ00265 404 LNFTLT--EGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN-DSHNLKDINlkwwRSKIGVVSQDPLLFSN-SIKNN 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 92 I--------------------GLGIHPGLKLNREQRAQVTAIAGQM---------------------------------- 117
Cdd:PTZ00265 480 IkyslyslkdlealsnyynedGNDSQENKNKRNSCRAKCAGDLNDMsnttdsneliemrknyqtikdsevvdvskkvlih 559
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1994014911 118 --------GMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALD 161
Cdd:PTZ00265 560 dfvsalpdKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
128-209 |
3.20e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.42 E-value: 3.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 128 GELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVADVCQRQQlTLLMVSHSVEDAARIAPRSIVVAEGR 207
Cdd:PRK10982 390 GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDK-GIIIISSEMPELLGITDRILVMSNGL 468
|
..
gi 1994014911 208 IA 209
Cdd:PRK10982 469 VA 470
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
32-173 |
5.10e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 45.63 E-value: 5.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 32 GPSGAGKSTLLNLIAGFLPPASGSLLIdgeKHNTTPPAQRPVSMLFQEN-NLFNHLTVRQNiglgihpgLKLNREQRAQV 110
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYY---KNCNINNIAKPYCTYIGHNlGLKLEMTVFEN--------LKFWSEIYNSA 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1994014911 111 TAIAGQM---GMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVA 173
Cdd:PRK13541 102 ETLYAAIhyfKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIV 167
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
25-163 |
5.72e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 46.64 E-value: 5.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 25 GERIAVLGPSGAGKSTLLNLIA----GFLPPASGSLLIDGEKHNTTPPAQRPVSMLFQENNL-FNHLTVRQNIGLGIH-- 97
Cdd:TIGR00956 87 GELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVhFPHLTVGETLDFAARck 166
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1994014911 98 -PGLK---LNREQRAQVTA--IAGQMGMDTLLDRLPGE-----LSGGQRQRAALARCLVRQQPVLLLDEPFSALDPA 163
Cdd:TIGR00956 167 tPQNRpdgVSREEYAKHIAdvYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSA 243
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-218 |
8.29e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.58 E-value: 8.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 19 TLSVERGERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEkhnttppaqrpVSMLFQENNLFNHLTVRQNIGLG-IH 97
Cdd:PRK13546 44 SLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-----------VSVIAISAGLSGQLTGIENIEFKmLC 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 98 PGLKlNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQRAALARCLVRQQPVLLLDEPFSALDPALRQEMLTLVADVcQ 177
Cdd:PRK13546 113 MGFK-RKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEF-K 190
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1994014911 178 RQQLTLLMVSHSVEDAARIAPRSIVVAEGRIAWDGATDDLL 218
Cdd:PRK13546 191 EQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL 231
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
22-161 |
1.02e-05 |
|
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: 44.54 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 22 VERGERIAVLGPSGAGKSTLLNLIAG--FLPPASGSLLIDGEKHNTTppAQRPVSMLFQENNLFNHLTVRQniGLGIHPG 99
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLDKN--FQRSTGYVEQQDVHSPNLTVRE--ALRFSAL 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1994014911 100 LKlnreqraqvtaiagqmgmdtlldrlpgELSGGQRQRAALARCLVRQQPVLLLDEPFSALD 161
Cdd:cd03232 106 LR---------------------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
20-166 |
1.75e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 44.63 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 20 LSVERGERIAVLGPSGAGKSTLLNLIAGFlpPA----SGSLLIDGEKHNTTPP---AQRPVSMLFQ--------ENNLFN 84
Cdd:CHL00131 28 LSINKGEIHAIMGPNGSGKSTLSKVIAGH--PAykilEGDILFKGESILDLEPeerAHLGIFLAFQypieipgvSNADFL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 85 HL---TVRQNIGLG----------IHPGLKLnreqraqvtaiagqMGMD-TLLDRLPGE-LSGGQRQRAALARCLVRQQP 149
Cdd:CHL00131 106 RLaynSKRKFQGLPeldplefleiINEKLKL--------------VGMDpSFLSRNVNEgFSGGEKKRNEILQMALLDSE 171
|
170
....*....|....*...
gi 1994014911 150 VLLLDEPFSALD-PALRQ 166
Cdd:CHL00131 172 LAILDETDSGLDiDALKI 189
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
91-191 |
8.54e-05 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 42.76 E-value: 8.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 91 NIGLGIHPGLKLNREQRAQVTAIAGQMGMDTLLDRLPGELSGGQRQ-RAALARCLVRQQP--VLLLDEPFSALDPALRQE 167
Cdd:pfam13304 198 NLSDLGEGIEKSLLVDDRLRERGLILLENGGGGELPAFELSDGTKRlLALLAALLSALPKggLLLIDEPESGLHPKLLRR 277
|
90 100
....*....|....*....|....
gi 1994014911 168 MLTLVADvCQRQQLTLLMVSHSVE 191
Cdd:pfam13304 278 LLELLKE-LSRNGAQLILTTHSPL 300
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
24-47 |
8.65e-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: 42.00 E-value: 8.65e-05
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
25-223 |
1.09e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 42.84 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 25 GERIAVLGPSGAGKSTLLNLIAGFLPPASGSLLIDGEKHNT--TPPAQRPVSMLFQENNLFNHlTVRQNIglgiHPGLKL 102
Cdd:PTZ00243 1336 REKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAygLRELRRQFSMIPQDPVLFDG-TVRQNV----DPFLEA 1410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 103 NREQ----------RAQVTAIAGqmGMDTLLDRLPGELSGGQRQRAALARCLV-RQQPVLLLDEPFSALDPAL-RQEMLT 170
Cdd:PTZ00243 1411 SSAEvwaalelvglRERVASESE--GIDSRVLEGGSNYSVGQRQLMCMARALLkKGSGFILMDEATANIDPALdRQIQAT 1488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1994014911 171 LVADVCQRQQLTLLMVSHSVEDAARIaprsIVVAEGRIAWDGATDDLLSGNSS 223
Cdd:PTZ00243 1489 VMSAFSAYTVITIAHRLHTVAQYDKI----IVMDHGAVAEMGSPRELVMNRQS 1537
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
20-191 |
3.62e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 40.00 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 20 LSVERGERIAVLGPSGAGKSTLLNliAGFlpPASGSLLIdgEKHNTTPPAQrPVSMLFQENNLFnhltvrqNIGLGIhpg 99
Cdd:cd03238 16 VSIPLNVLVVVTGVSGSGKSTLVN--EGL--YASGKARL--ISFLPKFSRN-KLIFIDQLQFLI-------DVGLGY--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 100 LKLNREqraqvtaiagqmgMDTlldrlpgeLSGGQRQRAALARCL-VRQQPVL-LLDEPFSALDPALRQEMLTLVADVCQ 177
Cdd:cd03238 79 LTLGQK-------------LST--------LSGGELQRVKLASELfSEPPGTLfILDEPSTGLHQQDINQLLEVIKGLID 137
|
170
....*....|....
gi 1994014911 178 rQQLTLLMVSHSVE 191
Cdd:cd03238 138 -LGNTVILIEHNLD 150
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
29-188 |
9.43e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 38.49 E-value: 9.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 29 AVLGPSGAGKSTLLNLIAgflppasgslLIDGEKHNttppaqrpvsmlfqennlfnhltvRQNIGLGIHPGlklnrEQRA 108
Cdd:cd03227 25 IITGPNGSGKSTILDAIG----------LALGGAQS------------------------ATRRRSGVKAG-----CIVA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014911 109 QVTAiagqmgmdTLLDRLPGeLSGGQRQRAALA----RCLVRQQPVLLLDEPFSALDPALRQEMLTLVADVCQrQQLTLL 184
Cdd:cd03227 66 AVSA--------ELIFTRLQ-LSGGEKELSALAlilaLASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLV-KGAQVI 135
|
....
gi 1994014911 185 MVSH 188
Cdd:cd03227 136 VITH 139
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
24-47 |
1.28e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 38.29 E-value: 1.28e-03
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
113-174 |
1.77e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 36.44 E-value: 1.77e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1994014911 113 IAGQMGMDTLLDRLPGELSGGQRQR-------AALAR--CLVRQQPV----LLLDEPFSALDPALRQEMLTLVAD 174
Cdd:pfam13558 16 VRDEDGSEVETYRRSGGLSGGEKQLlaylplaAALAAqyGSAEGRPPaprlVFLDEAFAKLDEENIRTALELLRA 90
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
29-66 |
2.24e-03 |
|
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 37.44 E-value: 2.24e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1994014911 29 AVLGPSGAGKSTLLNLIAGflppasGSLLIDGEKHNTT 66
Cdd:cd00882 1 VVVGRGGVGKSSLLNALLG------GEVGEVSDVPGTT 32
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
27-47 |
2.40e-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: 36.44 E-value: 2.40e-03
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
131-161 |
2.91e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 38.30 E-value: 2.91e-03
10 20 30
....*....|....*....|....*....|.
gi 1994014911 131 SGGQRQRAALARCLVRQQPVLLLDEPFSALD 161
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
26-47 |
3.98e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 37.49 E-value: 3.98e-03
|
| VirB4 |
COG3451 |
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ... |
15-46 |
4.50e-03 |
|
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442674 [Multi-domain] Cd Length: 546 Bit Score: 37.62 E-value: 4.50e-03
10 20 30
....*....|....*....|....*....|...
gi 1994014911 15 PMRFTLSVERGER-IAVLGPSGAGKSTLLNLIA 46
Cdd:COG3451 193 PVFFDFHDGLDNGnTLILGPSGSGKSFLLKLLL 225
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
20-46 |
9.30e-03 |
|
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.
Pssm-ID: 410880 [Multi-domain] Cd Length: 265 Bit Score: 36.38 E-value: 9.30e-03
10 20
....*....|....*....|....*..
gi 1994014911 20 LSVERGERIAVLGPSGAGKSTLLNLIA 46
Cdd:cd01136 62 LTCGEGQRIGIFAGSGVGKSTLLGMIA 88
|
|
| PRK13830 |
PRK13830 |
conjugal transfer protein TrbE; Provisional |
15-46 |
9.34e-03 |
|
conjugal transfer protein TrbE; Provisional
Pssm-ID: 237525 [Multi-domain] Cd Length: 818 Bit Score: 36.75 E-value: 9.34e-03
10 20 30
....*....|....*....|....*....|..
gi 1994014911 15 PMRFTLSVERGERIAVLGPSGAGKSTLLNLIA 46
Cdd:PRK13830 446 PFRLNLHVDDVGHTLIFGPTGSGKSTLLALIA 477
|
|
| Dynamin_N |
pfam00350 |
Dynamin family; |
28-50 |
9.91e-03 |
|
Dynamin family;
Pssm-ID: 459775 [Multi-domain] Cd Length: 168 Bit Score: 35.67 E-value: 9.91e-03
|
| VirB11 |
COG0630 |
Type IV secretory pathway ATPase VirB11/Archaellum biosynthesis ATPase ArlI/FlaI [Cell ... |
20-53 |
9.91e-03 |
|
Type IV secretory pathway ATPase VirB11/Archaellum biosynthesis ATPase ArlI/FlaI [Cell motility, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440395 [Multi-domain] Cd Length: 462 Bit Score: 36.60 E-value: 9.91e-03
10 20 30
....*....|....*....|....*....|....
gi 1994014911 20 LSVERGERIAVLGPSGAGKSTLLNLIAGFLPPAS 53
Cdd:COG0630 285 LLLENGKSVLVAGGTASGKTTLLNALLSFIPPDA 318
|
|
| |
