|
Name |
Accession |
Description |
Interval |
E-value |
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
2-224 |
7.45e-109 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 313.56 E-value: 7.45e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPKLAMIFQDFALYPWLTALENVELALLHRKd 81
Cdd:COG1116 31 SLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDRGVVFQEPALLPWLTVLDNVALGLELRG- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 82 LSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEIYNMVfneE 161
Cdd:COG1116 110 VPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLW---Q 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1732728249 162 STVRAIIMVSHNLEEVVELSDKVIILGGRPASIIAEVEIKLPRPRN---TRDIEFQDYLDRLYSLL 224
Cdd:COG1116 187 ETGKTVLFVTHDVDEAVFLADRVVVLSARPGRIVEEIDVDLPRPRDrelRTSPEFAALRAEILDLL 252
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-202 |
4.51e-97 |
|
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: 282.05 E-value: 4.51e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPKLAMIFQDFALYPWLTALENVELALLHRKd 81
Cdd:cd03293 24 SLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRGYVFQQDALLPWLTVLDNVALGLELQG- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 82 LSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEIYNMVFNEE 161
Cdd:cd03293 103 VPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETG 182
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1732728249 162 STVraiIMVSHNLEEVVELSDKVIILGGRPASIIAEVEIKL 202
Cdd:cd03293 183 KTV---LLVTHDIDEAVFLADRVVVLSARPGRIVAEVEVDL 220
|
|
| ABC_ATP_SaoA |
NF040729 |
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC ... |
1-229 |
2.72e-69 |
|
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC transporter in which both the permease subunit SaoP, and the substrate-binding protein SaoB, are nearly always selenoproteins that were unrecognized as such until recently (2022). The SAO system is found in Clostridium difficile and various other anaerobic heterotrophs.
Pssm-ID: 468693 [Multi-domain] Cd Length: 248 Bit Score: 212.68 E-value: 2.72e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPKLAMIFQDFALYPWLTALENVELALLHRK 80
Cdd:NF040729 24 ISFDVEEGEFVSLLGPSGCGKTTLLTIIAGFQNATSGEILVNGNEVTKPGPDRGFVFQNYALFPWMTVKENIEYPMKQQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 81 dLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEIYNMVFNE 160
Cdd:NF040729 104 -MPKQEREKRLNELLEMAQLTGKENLYPHQISGGMKQRTAVIRALACKPEVLLMDEPLGAVDFQMRQILQEELESIWLKD 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1732728249 161 ESTVraiIMVSHNLEEVVELSDKVIILGGRPASIIAEVEIKLPRPRNTRDIEFQDYLDRLYSLLSISLK 229
Cdd:NF040729 183 KTTV---LMVTHDVDEAVYLSDRVIVMSRDKGKILEDLKIDLPRPRNRESEKYLEYKDHLTNILKKALN 248
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
9-187 |
1.15e-67 |
|
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: 207.37 E-value: 1.15e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 9 EFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTP---KLAMIFQDFALYPWLTALENVELALLHRKdLSKE 85
Cdd:cd03259 27 EFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPerrNIGMVFQDYALFPHLTVAENIAFGLKLRG-VPKA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 86 VRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEIYNMVFNEESTVr 165
Cdd:cd03259 106 EIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITT- 184
|
170 180
....*....|....*....|..
gi 1732728249 166 aiIMVSHNLEEVVELSDKVIIL 187
Cdd:cd03259 185 --IYVTHDQEEALALADRIAVM 204
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
2-190 |
2.84e-66 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 208.41 E-value: 2.84e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTP---KLAMIFQDFALYPWLTALENVELALLH 78
Cdd:COG3842 25 SLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPekrNVGMVFQDYALFPHLTVAENVAFGLRM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 79 RKdLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEIynmvf 158
Cdd:COG3842 105 RG-VPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREEL----- 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1732728249 159 neestvRAI--------IMVSHNLEEVVELSDKVIIL-GGR 190
Cdd:COG3842 179 ------RRLqrelgitfIYVTHDQEEALALADRIAVMnDGR 213
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1-211 |
5.35e-65 |
|
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: 201.16 E-value: 5.35e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPKLAMIFQDFALYPWLTALENVELALLH-R 79
Cdd:TIGR01184 4 VNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVFQNYSLLPWLTVRENIALAVDRvL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 80 KDLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEIYNMVFN 159
Cdd:TIGR01184 84 PDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQIWEE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1732728249 160 EESTVraiIMVSHNLEEVVELSDKVIILGGRPASIIAEV-EIKLPRPRNTRDI 211
Cdd:TIGR01184 164 HRVTV---LMVTHDVDEALLLSDRVVMLTNGPAANIGQIlEVPFPRPRDRLEV 213
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-187 |
7.60e-65 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 200.65 E-value: 7.60e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPK---------LAMIFQDFALYPWLTALENV 72
Cdd:COG1136 28 SLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERelarlrrrhIGFVFQFFNLLPELTALENV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 73 ELALLHRKdLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEglraE 152
Cdd:COG1136 108 ALPLLLAG-VSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGE----E 182
|
170 180 190
....*....|....*....|....*....|....*..
gi 1732728249 153 IYNMVF--NEESTvRAIIMVSHNlEEVVELSDKVIIL 187
Cdd:COG1136 183 VLELLRelNRELG-TTIVMVTHD-PELAARADRVIRL 217
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-187 |
1.50e-64 |
|
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: 199.64 E-value: 1.50e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPK---------LAMIFQDFALYPWLTALENV 72
Cdd:cd03255 24 SLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKelaafrrrhIGFVFQSFNLLPDLTALENV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 73 ELALLHRKDLSKEvRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAE 152
Cdd:cd03255 104 ELPLLLAGVPKKE-RRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMEL 182
|
170 180 190
....*....|....*....|....*....|....*
gi 1732728249 153 IYNMVFNEESTvraIIMVSHNlEEVVELSDKVIIL 187
Cdd:cd03255 183 LRELNKEAGTT---IVVVTHD-PELAEYADRIIEL 213
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
2-199 |
1.96e-63 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 198.16 E-value: 1.96e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPKLAMIFQDFALYPWLTALENVELALLHRKd 81
Cdd:COG4525 27 SLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRGVVFQKDALLPWLNVLDNVAFGLRLRG- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 82 LSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEIYNmVFNEe 161
Cdd:COG4525 106 VPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLD-VWQR- 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 1732728249 162 sTVRAIIMVSHNLEEVVELSDKVIILGGRPASIIAEVE 199
Cdd:COG4525 184 -TGKGVFLITHSVEEALFLATRLVVMSPGPGRIVERLE 220
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-197 |
1.16e-61 |
|
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: 192.89 E-value: 1.16e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTP--------KLAMIFQDFALYPWLTALENVE 73
Cdd:COG1127 25 SLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEkelyelrrRIGMLFQGGALFDSLTVFENVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 74 LALLHRKDLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAeglrAEI 153
Cdd:COG1127 105 FPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITS----AVI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1732728249 154 YNMV--FNEE--STVraiIMVSHNLEEVVELSDKVIILG-GRpasIIAE 197
Cdd:COG1127 181 DELIreLRDElgLTS---VVVTHDLDSAFAIADRVAVLAdGK---IIAE 223
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-190 |
5.22e-60 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 191.90 E-value: 5.22e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTP----KLAMIFQDFALYPWLTALENVELALL 77
Cdd:COG1118 22 SLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPprerRVGFVFQHYALFPHMTVAENIAFGLR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 78 HRKdLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEIYNMV 157
Cdd:COG1118 102 VRP-PSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLH 180
|
170 180 190
....*....|....*....|....*....|....
gi 1732728249 158 fneESTVRAIIMVSHNLEEVVELSDKVIIL-GGR 190
Cdd:COG1118 181 ---DELGGTTVFVTHDQEEALELADRVVVMnQGR 211
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-197 |
5.28e-58 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 183.47 E-value: 5.28e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTP--------KLAMIFQDFALYPWLTALENVE 73
Cdd:cd03261 20 DLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEaelyrlrrRMGMLFQSGALFDSLTVFENVA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 74 LALLHRKDLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEI 153
Cdd:cd03261 100 FPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLI 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1732728249 154 YNMvfNEE--STVraiIMVSHNLEEVVELSDKVIILG-GRpasIIAE 197
Cdd:cd03261 180 RSL--KKElgLTS---IMVTHDLDTAFAIADRIAVLYdGK---IVAE 218
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-190 |
4.40e-56 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 182.19 E-value: 4.40e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPK---LAMIFQDFALYPWLTALENVELALL 77
Cdd:COG3839 22 IDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKdrnIAMVFQSYALYPHMTVYENIAFPLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 78 HRKdLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEIYNMV 157
Cdd:COG3839 102 LRK-VPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLH 180
|
170 180 190
....*....|....*....|....*....|....
gi 1732728249 158 FNEESTvraIIMVSHNLEEVVELSDKVIIL-GGR 190
Cdd:COG3839 181 RRLGTT---TIYVTHDQVEAMTLADRIAVMnDGR 211
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
2-142 |
5.18e-55 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 175.95 E-value: 5.18e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPKLA-------MIFQDFALYPWLTALENVEL 74
Cdd:COG1126 21 SLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINklrrkvgMVFQQFNLFPHLTVLENVTL 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1732728249 75 ALLHRKDLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLD 142
Cdd:COG1126 101 APIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALD 168
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-187 |
1.85e-54 |
|
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: 174.35 E-value: 1.85e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKG-PTPK--LAMIFQDFALYPWLTALENVELALLH 78
Cdd:cd03300 20 SLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlPPHKrpVNTVFQNYALFPHLTVFENIAFGLRL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 79 RKDLSKEVRREIARkYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEIYNMVF 158
Cdd:cd03300 100 KKLPKAEIKERVAE-ALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQK 178
|
170 180
....*....|....*....|....*....
gi 1732728249 159 NEESTvraIIMVSHNLEEVVELSDKVIIL 187
Cdd:cd03300 179 ELGIT---FVFVTHDQEEALTMSDRIAVM 204
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-200 |
1.82e-53 |
|
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: 171.75 E-value: 1.82e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTP-----KLAMIFQD-----FALypwlTALEN 71
Cdd:COG1122 21 SLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLrelrrKVGLVFQNpddqlFAP----TVEED 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 72 VELALLHRKdLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITaeglRA 151
Cdd:COG1122 97 VAFGPENLG-LPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRG----RR 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1732728249 152 EIYNMVFNEESTVRAIIMVSHNLEEVVELSDKVIILG-------GRPASIIAEVEI 200
Cdd:COG1122 172 ELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDdgrivadGTPREVFSDYEL 227
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-197 |
2.19e-53 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 171.40 E-value: 2.19e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPK----LAMIFQDFALYPWLTALENVEL-AL 76
Cdd:COG1131 20 SLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEvrrrIGYVPQEPALYPDLTVRENLRFfAR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 77 LHrkDLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITaeglRAEIYNM 156
Cdd:COG1131 100 LY--GLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEA----RRELWEL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1732728249 157 VFNEESTVRAIIMVSHNLEEVVELSDKVIIL-GGRpasIIAE 197
Cdd:COG1131 174 LRELAAEGKTVLLSTHYLEEAERLCDRVAIIdKGR---IVAD 212
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
2-187 |
2.59e-51 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 167.44 E-value: 2.59e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPT---------PKLAMIFQDFALYPWLTALENV 72
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkelrelrrKKISMVFQSFALLPHRTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 73 ELALlHRKDLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAE 152
Cdd:cd03294 124 AFGL-EVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDE 202
|
170 180 190
....*....|....*....|....*....|....*
gi 1732728249 153 IYNMVFNEESTvraIIMVSHNLEEVVELSDKVIIL 187
Cdd:cd03294 203 LLRLQAELQKT---IVFITHDLDEALRLGDRIAIM 234
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1-187 |
4.11e-51 |
|
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: 165.12 E-value: 4.11e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPK---LAMIFQDFALYPWLTALENVELALl 77
Cdd:cd03301 19 LNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKdrdIAMVFQNYALYPHMTVYDNIAFGL- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 78 hrkDLSKEVRREIARKYL---ELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEIY 154
Cdd:cd03301 98 ---KLRKVPKDEIDERVRevaELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELK 174
|
170 180 190
....*....|....*....|....*....|...
gi 1732728249 155 NMVFNEESTvraIIMVSHNLEEVVELSDKVIIL 187
Cdd:cd03301 175 RLQQRLGTT---TIYVTHDQVEAMTMADRIAVM 204
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-190 |
5.02e-51 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 165.23 E-value: 5.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTP--------KLAMIFQDFALYPWLTALENV 72
Cdd:COG2884 21 VSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRreipylrrRIGVVFQDFRLLPDRTVYENV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 73 ELAL-LHRKDlSKEVRREIaRKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEglra 151
Cdd:COG2884 101 ALPLrVTGKS-RKEIRRRV-REVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSW---- 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1732728249 152 EIYNMV--FNEESTvrAIIMVSHNLEEVVELSDKVIIL-GGR 190
Cdd:COG2884 175 EIMELLeeINRRGT--TVLIATHDLELVDRMPKRVLELeDGR 214
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1-187 |
1.02e-50 |
|
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: 162.74 E-value: 1.02e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPT-------PKLAMIFQDFALYPWLTALENVE 73
Cdd:cd03229 19 VSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdelpplrRRIGMVFQDFALFPHLTVLENIA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 74 LALlhrkdlskevrreiarkylelvglggfedyyprelSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEI 153
Cdd:cd03229 99 LGL-----------------------------------SGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALL 143
|
170 180 190
....*....|....*....|....*....|....
gi 1732728249 154 YNMVFNEESTVraiIMVSHNLEEVVELSDKVIIL 187
Cdd:cd03229 144 KSLQAQLGITV---VLVTHDLDEAARLADRVVVL 174
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-187 |
1.03e-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: 1.03e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPK---LAMIFQDFALYPWLTALENVELALLH 78
Cdd:cd03296 22 SLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQernVGFVFQHYALFRHMTVFDNVAFGLRV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 79 RKDLSKEVRREIARK---YLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEIYN 155
Cdd:cd03296 102 KPRSERPPEAEIRAKvheLLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRR 181
|
170 180 190
....*....|....*....|....*....|..
gi 1732728249 156 mvFNEESTVrAIIMVSHNLEEVVELSDKVIIL 187
Cdd:cd03296 182 --LHDELHV-TTVFVTHDQEEALEVADRVVVM 210
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
2-187 |
1.22e-50 |
|
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: 163.79 E-value: 1.22e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTP-----KLAMIFQD-----FALypwlTALEN 71
Cdd:cd03225 21 SLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLkelrrKVGLVFQNpddqfFGP----TVEEE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 72 VELALLHRKdLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRA 151
Cdd:cd03225 97 VAFGLENLG-LPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLE 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 1732728249 152 EIYNMvfNEESTvrAIIMVSHNLEEVVELSDKVIIL 187
Cdd:cd03225 176 LLKKL--KAEGK--TIIIVTHDLDLLLELADRVIVL 207
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-142 |
2.07e-50 |
|
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: 163.08 E-value: 2.07e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTP-------KLAMIFQDFALYPWLTALENVEL 74
Cdd:cd03262 20 DLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKninelrqKVGMVFQQFNLFPHLTVLENITL 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1732728249 75 ALLHRKDLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLD 142
Cdd:cd03262 100 APIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALD 167
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
2-190 |
9.16e-50 |
|
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: 161.90 E-value: 9.16e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPKL--------AMIFQD--FALYPWLTALEN 71
Cdd:cd03257 25 SFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLrkirrkeiQMVFQDpmSSLNPRMTIGEQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 72 V-ELALLHRKDLSKEVRREIARKYLELVGLG-GFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITaegl 149
Cdd:cd03257 105 IaEPLRIHGKLSKKEARKEAVLLLLVGVGLPeEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSV---- 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1732728249 150 RAEIYNMvFNEESTVR--AIIMVSHNLEEVVELSDKVIIL-GGR 190
Cdd:cd03257 181 QAQILDL-LKKLQEELglTLLFITHDLGVVAKIADRVAVMyAGK 223
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
2-187 |
6.93e-49 |
|
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: 160.41 E-value: 6.93e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTP----KLAMIFQDFALYPWLTALENVE-LAL 76
Cdd:COG4555 21 SFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRearrQIGVLPDERGLYDRLTVRENIRyFAE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 77 LHrkDLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEIYNM 156
Cdd:COG4555 101 LY--GLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRAL 178
|
170 180 190
....*....|....*....|....*....|.
gi 1732728249 157 VfNEEstvRAIIMVSHNLEEVVELSDKVIIL 187
Cdd:COG4555 179 K-KEG---KTVLFSSHIMQEVEALCDRVVIL 205
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
18-142 |
7.05e-49 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 164.51 E-value: 7.05e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 18 GTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTP---------KLAMIFQDFALYPWLTALENVELAL-LhrKDLSKEVR 87
Cdd:COG4175 63 GSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKkelrelrrkKMSMVFQHFALLPHRTVLENVAFGLeI--QGVPKAER 140
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1732728249 88 REIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLD 142
Cdd:COG4175 141 RERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALD 195
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-195 |
1.13e-48 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 160.25 E-value: 1.13e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPKLAMIFQDFALYPWLTALENVELALlHRK 80
Cdd:PRK11248 20 INLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGVVFQNEGLLPWRNVQDNVAFGL-QLA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 81 DLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRaEIYNMVFNE 160
Cdd:PRK11248 99 GVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQ-TLLLKLWQE 177
|
170 180 190
....*....|....*....|....*....|....*
gi 1732728249 161 esTVRAIIMVSHNLEEVVELSDKVIILGGRPASII 195
Cdd:PRK11248 178 --TGKQVLLITHDIEEAVFMATELVLLSPGPGRVV 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-190 |
2.13e-48 |
|
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: 165.85 E-value: 2.13e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPK--------LAMIFQD-FA-LYPWLTALEN 71
Cdd:COG1123 285 SLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRslrelrrrVQMVFQDpYSsLNPRMTVGDI 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 72 VELALLHRKDLSKEVRREIARKYLELVGLG-GFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITaeglR 150
Cdd:COG1123 365 IAEPLRLHGLLSRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSV----Q 440
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1732728249 151 AEIYNMvFNE--ESTVRAIIMVSHNLEEVVELSDKVIIL-GGR 190
Cdd:COG1123 441 AQILNL-LRDlqRELGLTYLFISHDLAVVRYIADRVAVMyDGR 482
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
2-190 |
5.80e-48 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 157.61 E-value: 5.80e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTP---KLAMIFQDFALYPWLTALENVELALLH 78
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPaerPVSMLFQENNLFPHLTVAQNIGLGLRP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 79 RKDLSKEVRREIARKyLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAitaeGLRAEIYNMVf 158
Cdd:COG3840 99 GLKLTAEQRAQVEQA-LERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDP----ALRQEMLDLV- 172
|
170 180 190
....*....|....*....|....*....|....*
gi 1732728249 159 NE--ESTVRAIIMVSHNLEEVVELSDKVI-ILGGR 190
Cdd:COG3840 173 DElcRERGLTVLMVTHDPEDAARIADRVLlVADGR 207
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-190 |
2.22e-47 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 156.40 E-value: 2.22e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPKLAMIFQDFAL---YPwLTALENVELALLH 78
Cdd:COG1121 26 SLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIGYVPQRAEVdwdFP-ITVRDVVLMGRYG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 79 R----KDLSKEvRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITaeglRAEIY 154
Cdd:COG1121 105 RrglfRRPSRA-DREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAAT----EEALY 179
|
170 180 190
....*....|....*....|....*....|....*...
gi 1732728249 155 NMV--FNEEStvRAIIMVSHNLEEVVELSDKVIILGGR 190
Cdd:COG1121 180 ELLreLRREG--KTILVVTHDLGAVREYFDRVLLLNRG 215
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-190 |
3.01e-47 |
|
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: 155.96 E-value: 3.01e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPK---LAMIFQDFALYPWLTALENVELALLH 78
Cdd:cd03299 19 SLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEkrdISYVPQNYALFPHMTVYKNIAYGLKK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 79 RKDLSKEVRREIaRKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEIYNMVF 158
Cdd:cd03299 99 RKVDKKEIERKV-LEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRK 177
|
170 180 190
....*....|....*....|....*....|...
gi 1732728249 159 NEESTVraiIMVSHNLEEVVELSDKV-IILGGR 190
Cdd:cd03299 178 EFGVTV---LHVTHDFEEAWALADKVaIMLNGK 207
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1-189 |
8.63e-47 |
|
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: 154.77 E-value: 8.63e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTP-----KLAMIFQDFALYPWLTALENVEL- 74
Cdd:cd03295 20 LNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPvelrrKIGYVIQQIGLFPHMTVEENIALv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 75 -ALLHrkdLSKEVRREIARKYLELVGL--GGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRA 151
Cdd:cd03295 100 pKLLK---WPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQE 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 1732728249 152 EIYNMvfnEESTVRAIIMVSHNLEEVVELSDKVIILGG 189
Cdd:cd03295 177 EFKRL---QQELGKTIVFVTHDIDEAFRLADRIAIMKN 211
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-175 |
6.92e-46 |
|
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: 152.20 E-value: 6.92e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVkgpTP------------KLAMIFQDFALYPWLTAL 69
Cdd:COG4181 32 SLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDL---FAldedararlrarHVGFVFQSFQLLPTLTAL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 70 ENVELALlhrkdlskEVR-----REIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAI 144
Cdd:COG4181 109 ENVMLPL--------ELAgrrdaRARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAA 180
|
170 180 190
....*....|....*....|....*....|...
gi 1732728249 145 TAEglraEIYNMVF--NEESTVrAIIMVSHNLE 175
Cdd:COG4181 181 TGE----QIIDLLFelNRERGT-TLVLVTHDPA 208
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
2-173 |
3.42e-45 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 150.17 E-value: 3.42e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPK--------LAMIFQDFALYPWLTALENVE 73
Cdd:TIGR02982 25 NLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKqlvqlrrrIGYIFQAHNLLGFLTARQNVQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 74 LALLHRKDLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLrAEI 153
Cdd:TIGR02982 105 MALELQPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALDSKSGRDV-VEL 183
|
170 180
....*....|....*....|
gi 1732728249 154 YNMVFNEESTvrAIIMVSHN 173
Cdd:TIGR02982 184 MQKLAKEQGC--TILMVTHD 201
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
2-187 |
1.59e-44 |
|
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: 148.88 E-value: 1.59e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPK--------LAMIFQDFALYPWLTALENVE 73
Cdd:cd03258 25 SLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKelrkarrrIGMIFQHFNLLSSRTVFENVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 74 LALLHRKdLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEI 153
Cdd:cd03258 105 LPLEIAG-VPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALL 183
|
170 180 190
....*....|....*....|....*....|....
gi 1732728249 154 YNMvfNEESTVrAIIMVSHNLEEVVELSDKVIIL 187
Cdd:cd03258 184 RDI--NRELGL-TIVLITHEMEVVKRICDRVAVM 214
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-190 |
2.84e-44 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 148.67 E-value: 2.84e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPK--------LAMIFQDFALYPWLTALENVE 73
Cdd:COG3638 23 SLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRalrrlrrrIGMIFQQFNLVPRLSVLTNVL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 74 LALLHRKDL--------SKEVRrEIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAIT 145
Cdd:COG3638 103 AGRLGRTSTwrsllglfPPEDR-ERALEALERVGLADKAYQRADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKT 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1732728249 146 AE---GLRAEIynmvfNEESTVrAIIMVSHNLEEVVELSDKVIIL-GGR 190
Cdd:COG3638 182 ARqvmDLLRRI-----AREDGI-TVVVNLHQVDLARRYADRIIGLrDGR 224
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
2-204 |
3.72e-44 |
|
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: 148.41 E-value: 3.72e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPK-----LAMIFQDF--ALYPWLTALENVEL 74
Cdd:COG1124 25 SLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKafrrrVQMVFQDPyaSLHPRHTVDRILAE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 75 AL-LHRKDlskEVRREIARkYLELVGLG-GFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITaeglRAE 152
Cdd:COG1124 105 PLrIHGLP---DREERIAE-LLEQVGLPpSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSV----QAE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1732728249 153 IYNMV--FNEESTVrAIIMVSHNLEEVVELSDKVIIL-GGRpasIIAEVEIKLPR 204
Cdd:COG1124 177 ILNLLkdLREERGL-TYLFVSHDLAVVAHLCDRVAVMqNGR---IVEELTVADLL 227
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-187 |
4.64e-44 |
|
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: 145.62 E-value: 4.64e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPK----LAMIFQDFALYPWLTALENVELall 77
Cdd:cd03230 20 SLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEvkrrIGYLPEEPSLYENLTVRENLKL--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 78 hrkdlskevrreiarkylelvglggfedyyprelSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITaeglRAEIYNMV 157
Cdd:cd03230 97 ----------------------------------SGGMKQRLALAQALLHDPELLILDEPTSGLDPES----RREFWELL 138
|
170 180 190
....*....|....*....|....*....|
gi 1732728249 158 FNEESTVRAIIMVSHNLEEVVELSDKVIIL 187
Cdd:cd03230 139 RELKKEGKTILLSSHILEEAERLCDRVAIL 168
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
9-194 |
5.33e-44 |
|
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: 147.06 E-value: 5.33e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 9 EFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGE-----EVKGPTP----KLAMIFQDFALYPWLTALENVELALlhr 79
Cdd:cd03297 24 EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsRKKINLPpqqrKIGLVFQQYALFPHLNVRENLAFGL--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 80 KDLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEIYNMVFN 159
Cdd:cd03297 101 KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKN 180
|
170 180 190
....*....|....*....|....*....|....*.
gi 1732728249 160 EESTVraiIMVSHNLEEVVELSDKVIIL-GGRPASI 194
Cdd:cd03297 181 LNIPV---IFVTHDLSEAEYLADRIVVMeDGRLQYI 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-187 |
5.66e-43 |
|
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: 145.02 E-value: 5.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEV-KGPTPKL-------AMIFQDFALYPWLTALENVE 73
Cdd:cd03256 21 SLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInKLKGKALrqlrrqiGMIFQQFNLIERLSVLENVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 74 LALLHRK-------DLSKEVRREIARKYLELVGLggFEDYYPR--ELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAI 144
Cdd:cd03256 101 SGRLGRRstwrslfGLFPKEEKQRALAALERVGL--LDKAYQRadQLSGGQQQRVAIARALMQQPKLILADEPVASLDPA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1732728249 145 TAE---GLRAEIyNMVFNeestvRAIIMVSHNLEEVVELSDKVIIL 187
Cdd:cd03256 179 SSRqvmDLLKRI-NREEG-----ITVIVSLHQVDLAREYADRIVGL 218
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
2-190 |
1.59e-42 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 146.76 E-value: 1.59e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTP--------KLAMIFQDFALYPWLTALENVE 73
Cdd:COG1135 25 SLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSErelraarrKIGMIFQHFNLLSSRTVAENVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 74 LALLHRKdLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAE---GLR 150
Cdd:COG1135 105 LPLEIAG-VPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRsilDLL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1732728249 151 AEIynmvfNEE--STvraIIMVSHNLEEVVELSDKVIIL-GGR 190
Cdd:COG1135 184 KDI-----NRElgLT---IVLITHEMDVVRRICDRVAVLeNGR 218
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
2-197 |
2.66e-42 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 145.23 E-value: 2.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKG-PTPKL------AMifQDFALYPWLTALENVEL 74
Cdd:COG1125 22 SLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDlDPVELrrrigyVI--QQIGLFPHMTVAENIAT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 75 --ALLHRkdlSKEVRREIARKYLELVGL--GGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLR 150
Cdd:COG1125 100 vpRLLGW---DKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILLMDEPFGALDPITREQLQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1732728249 151 AEIYNMvfnEESTVRAIIMVSHNLEEVVELSDKVIILG-------GRPASIIAE 197
Cdd:COG1125 177 DELLRL---QRELGKTIVFVTHDIDEALKLGDRIAVMRegrivqyDTPEEILAN 227
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1-191 |
2.86e-42 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 142.29 E-value: 2.86e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPKLAMIFQdFALYPW---LTALENVELALL 77
Cdd:cd03235 18 VSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGYVPQ-RRSIDRdfpISVRDVVLMGLY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 78 HRKDLSKEVR---REIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITaeglRAEIY 154
Cdd:cd03235 97 GHKGLFRRLSkadKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKT----QEDIY 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 1732728249 155 NMVFNEESTVRAIIMVSHNLEEVVELSDKVIILGGRP 191
Cdd:cd03235 173 ELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTV 209
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-197 |
3.03e-42 |
|
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: 142.96 E-value: 3.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTP------KLAMIFQDFALYPWLTALENVELA 75
Cdd:cd03219 20 SFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPheiarlGIGRTFQIPRLFPELTVLENVMVA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 76 LLHRKDLS---------KEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDaita 146
Cdd:cd03219 100 AQARTGSGlllararreEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLN---- 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1732728249 147 eglRAEIYNMV-----FNEEStvRAIIMVSHNLEEVVELSDKVIIL-GGRpasIIAE 197
Cdd:cd03219 176 ---PEETEELAelireLRERG--ITVLLVEHDMDVVMSLADRVTVLdQGR---VIAE 224
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
2-195 |
1.12e-41 |
|
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: 142.10 E-value: 1.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPK-----LAMIFQDFALYPWLTALENVELAL 76
Cdd:COG1120 21 SLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRelarrIAYVPQEPPAPFGLTVRELVALGR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 77 L-HRKDLSKEVR--REIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDaitaegLR--A 151
Cdd:COG1120 101 YpHLGLFGRPSAedREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLD------LAhqL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1732728249 152 EIYNMV--FNEESTvRAIIMVSHNLEEVVELSDKVIILG-------GRPASII 195
Cdd:COG1120 175 EVLELLrrLARERG-RTVVMVLHDLNLAARYADRLVLLKdgrivaqGPPEEVL 226
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-187 |
1.57e-41 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 144.48 E-value: 1.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPK---LAMIFQDFALYPWLTALENVELALL 77
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQqrdICMVFQSYALFPHMSLGENVGYGLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 78 HRKdLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEIYNMV 157
Cdd:PRK11432 105 MLG-VPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQ 183
|
170 180 190
....*....|....*....|....*....|..
gi 1732728249 158 --FNEEStvraiIMVSHNLEEVVELSDKVIIL 187
Cdd:PRK11432 184 qqFNITS-----LYVTHDQSEAFAVSDTVIVM 210
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-187 |
3.00e-41 |
|
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: 140.01 E-value: 3.00e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLR-----RPDSGKVLLMGEEVKGPTP-------KLAMIFQDFALYPwLTAL 69
Cdd:cd03260 20 SLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVdvlelrrRVGMVFQKPNPFP-GSIY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 70 ENVELALLHRKDLSKEVRREIARKYLELVGLGGFED--YYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITA- 146
Cdd:cd03260 99 DNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKdrLHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTa 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1732728249 147 --EGLRAEiynmvFNEESTvraIIMVSHNLEEVVELSDKVIIL 187
Cdd:cd03260 179 kiEELIAE-----LKKEYT---IVIVTHNMQQAARVADRTAFL 213
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2-190 |
3.21e-41 |
|
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: 139.54 E-value: 3.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTP----KLAMIFQDFALYPWLTALENVEL-AL 76
Cdd:COG4133 22 SFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREdyrrRLAYLGHADGLKPELTVRENLRFwAA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 77 LHRKDLSKEVRREIarkyLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDaitAEGlRAEIYNM 156
Cdd:COG4133 102 LYGLRADREAIDEA----LEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALD---AAG-VALLAEL 173
|
170 180 190
....*....|....*....|....*....|....
gi 1732728249 157 VFNEESTVRAIIMVSHNLEEVveLSDKVIILGGR 190
Cdd:COG4133 174 IAAHLARGGAVLLTTHQPLEL--AAARVLDLGDF 205
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1-139 |
5.74e-41 |
|
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: 137.01 E-value: 5.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPK-----LAMIFQDFALYPWLTALENVELA 75
Cdd:pfam00005 4 VSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKslrkeIGYVFQDPQLFPRLTVRENLRLG 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1732728249 76 LLHrKDLSKEVRREIARKYLELVGLGGFED----YYPRELSGGMKQRVAIARALAAQPVVLLMDEPFA 139
Cdd:pfam00005 84 LLL-KGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
2-190 |
9.38e-41 |
|
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: 142.55 E-value: 9.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGE----EVKG---PTPK--LAMIFQDFALYPWLTALENV 72
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdSARGiflPPHRrrIGYVFQEARLFPHLSVRGNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 73 ELAllhRKDLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDaitaEGLRAE 152
Cdd:COG4148 99 LYG---RKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALD----LARKAE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1732728249 153 IynMVFNEEstVRA-----IIMVSHNLEEVVELSDKVIIL-GGR 190
Cdd:COG4148 172 I--LPYLER--LRDeldipILYVSHSLDEVARLADHVVLLeQGR 211
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
2-187 |
1.16e-40 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 138.13 E-value: 1.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPKLAM---------IFQDFALYPWLTALENV 72
Cdd:TIGR03608 18 NLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASkfrreklgyLFQNFALIENETVEENL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 73 ELALLHRKdLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITaeglRAE 152
Cdd:TIGR03608 98 DLGLKYKK-LSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDPKN----RDE 172
|
170 180 190
....*....|....*....|....*....|....*
gi 1732728249 153 IYNMVFNEESTVRAIIMVSHNLeEVVELSDKVIIL 187
Cdd:TIGR03608 173 VLDLLLELNDEGKTIIIVTHDP-EVAKQADRVIEL 206
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-187 |
1.53e-40 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 137.64 E-value: 1.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTP-----KLAMIFQDFALYPwLTALENVELAL 76
Cdd:COG4619 20 SLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPpewrrQVAYVPQEPALWG-GTVRDNLPFPF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 77 LHRKdlsKEVRREIARKYLELVGLG-GFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEIYN 155
Cdd:COG4619 99 QLRE---RKFDRERALELLERLGLPpDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLRE 175
|
170 180 190
....*....|....*....|....*....|..
gi 1732728249 156 MVFNEEstvRAIIMVSHNLEEVVELSDKVIIL 187
Cdd:COG4619 176 YLAEEG---RAVLWVSHDPEQIERVADRVLTL 204
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-142 |
4.34e-40 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 137.53 E-value: 4.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPKL-------AMIFQDFALYPWLTALENVE 73
Cdd:PRK09493 20 IDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlirqeaGMVFQQFYLFPHLTALENVM 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1732728249 74 LALLHRKDLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLD 142
Cdd:PRK09493 100 FGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALD 168
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-187 |
4.44e-40 |
|
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: 143.51 E-value: 4.44e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPD---SGKVLLMGEEVKGPTPKL-----AMIFQDF--ALYPwLTALEN 71
Cdd:COG1123 26 SLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALrgrriGMVFQDPmtQLNP-VTVGDQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 72 VELALLhRKDLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRA 151
Cdd:COG1123 105 IAEALE-NLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILD 183
|
170 180 190
....*....|....*....|....*....|....*.
gi 1732728249 152 EIYNMVfneESTVRAIIMVSHNLEEVVELSDKVIIL 187
Cdd:COG1123 184 LLRELQ---RERGTTVLLITHDLGVVAEIADRVVVM 216
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
5-188 |
9.95e-40 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 139.83 E-value: 9.95e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 5 VHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPK---LAMIFQDFALYPWLTALENVELALL---H 78
Cdd:PRK10851 25 IPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARdrkVGFVFQHYALFRHMTVFDNIAFGLTvlpR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 79 RKDLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEIYNMvf 158
Cdd:PRK10851 105 RERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQL-- 182
|
170 180 190
....*....|....*....|....*....|
gi 1732728249 159 NEESTVRAiIMVSHNLEEVVELSDKVIILG 188
Cdd:PRK10851 183 HEELKFTS-VFVTHDQEEAMEVADRVVVMS 211
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
9-187 |
1.39e-39 |
|
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: 135.31 E-value: 1.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 9 EFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPK---LAMIFQDFALYPWLTALENVELALLHRKDLSKE 85
Cdd:cd03298 25 EITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAdrpVSMLFQENNLFAHLTVEQNVGLGLSPGLKLTAE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 86 VRREIArKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAitaeGLRAEIYNMVfneeSTVR 165
Cdd:cd03298 105 DRQAIE-VALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDP----ALRAEMLDLV----LDLH 175
|
170 180
....*....|....*....|....*..
gi 1732728249 166 A-----IIMVSHNLEEVVELSDKVIIL 187
Cdd:cd03298 176 AetkmtVLMVTHQPEDAKRLAQRVVFL 202
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
2-190 |
1.51e-39 |
|
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: 138.26 E-value: 1.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRP---DSGKVLLMGEEVKGPTPK---------LAMIFQDF--ALYPWLT 67
Cdd:COG0444 25 SFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKelrkirgreIQMIFQDPmtSLNPVMT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 68 ALENVELALLHRKDLSKEVRREIARKYLELVGLGGFEDY---YPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAI 144
Cdd:COG0444 105 VGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRldrYPHELSGGMRQRVMIARALALEPKLLIADEPTTALDVT 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1732728249 145 TaeglRAEIYNMvFNE--ESTVRAIIMVSHNLEEVVELSDKVIIL-GGR 190
Cdd:COG0444 185 I----QAQILNL-LKDlqRELGLAILFITHDLGVVAEIADRVAVMyAGR 228
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-197 |
2.68e-39 |
|
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: 135.94 E-value: 2.68e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTP------KLAMIFQDFALYPWLTALENVEL 74
Cdd:COG0411 23 VSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPhriarlGIARTFQNPRLFPELTVLENVLV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 75 ALLHRKDLS---------------KEVRREiARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFA 139
Cdd:COG0411 103 AAHARLGRGllaallrlprarreeREARER-AEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1732728249 140 NLDAitaeGLRAEIYNMVF--NEESTVrAIIMVSHNLEEVVELSDKVIIL-GGRpasIIAE 197
Cdd:COG0411 182 GLNP----EETEELAELIRrlRDERGI-TILLIEHDMDLVMGLADRIVVLdFGR---VIAE 234
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-190 |
2.06e-38 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 132.22 E-value: 2.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPD---SGKVLLMGEEV-KGPTPK--LAMIFQDFALYPWLTALENVEL 74
Cdd:COG4136 20 LSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLtALPAEQrrIGILFQDDLLFPHLSVGENLAF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 75 ALlhRKDLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAitaeGLRAEIY 154
Cdd:COG4136 100 AL--PPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDA----ALRAQFR 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 1732728249 155 NMVFnEESTVRAI--IMVSHNLEEvVELSDKVIILGGR 190
Cdd:COG4136 174 EFVF-EQIRQRGIpaLLVTHDEED-APAAGRVLDLGNW 209
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
2-187 |
2.73e-38 |
|
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: 133.19 E-value: 2.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPK--------LAMIFQDFALYPWLTALENVE 73
Cdd:TIGR02315 22 NLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKklrklrrrIGMIFQHYNLIERLTVLENVL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 74 LALLHRKD-------LSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITA 146
Cdd:TIGR02315 102 HGRLGYKPtwrsllgRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTS 181
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1732728249 147 EGLRAEIYNMvfNEESTVRAIIMVsHNLEEVVELSDKVIIL 187
Cdd:TIGR02315 182 KQVMDYLKRI--NKEDGITVIINL-HQVDLAKKYADRIVGL 219
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
2-188 |
6.36e-38 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 131.22 E-value: 6.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEV----KGPTPKL----AMIFQDFALYPWLTALENVE 73
Cdd:TIGR02673 22 SLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVnrlrGRQLPLLrrriGVVFQDFRLLPDRTVYENVA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 74 LALLHRKDLSKEVRREIARkYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEI 153
Cdd:TIGR02673 102 LPLEVRGKKEREIQRRVGA-ALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLDPDLSERILDLL 180
|
170 180 190
....*....|....*....|....*....|....*
gi 1732728249 154 ynMVFNEESTvrAIIMVSHNLEEVVELSDKVIILG 188
Cdd:TIGR02673 181 --KRLNKRGT--TVIVATHDLSLVDRVAHRVIILD 211
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1-188 |
9.85e-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: 130.61 E-value: 9.85e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKG----PTPKL----AMIFQDFALYPWLTALENV 72
Cdd:cd03292 20 INISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrgrAIPYLrrkiGVVFQDFRLLPDRNVYENV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 73 ELALlhrkDLSKEVRREIARKY---LELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAegl 149
Cdd:cd03292 100 AFAL----EVTGVPPREIRKRVpaaLELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTT--- 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1732728249 150 rAEIYNMV--FNEESTvrAIIMVSHNLEEVVELSDKVIILG 188
Cdd:cd03292 173 -WEIMNLLkkINKAGT--TVVVATHAKELVDTTRHRVIALE 210
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
2-200 |
2.68e-37 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 133.62 E-value: 2.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPK---LAMIFQDFALYPWLTALENVELALlh 78
Cdd:PRK11000 23 NLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAergVGMVFQSYALYPHLSVAENMSFGL-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 79 rkDLSKEVRREIARKY---LELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEIYN 155
Cdd:PRK11000 101 --KLAGAKKEEINQRVnqvAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISR 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1732728249 156 MvfnEESTVRAIIMVSHNLEEVVELSDKVIIL-GGRPASIIAEVEI 200
Cdd:PRK11000 179 L---HKRLGRTMIYVTHDQVEAMTLADKIVVLdAGRVAQVGKPLEL 221
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
9-206 |
6.32e-37 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 129.80 E-value: 6.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 9 EFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLlmgeevKGPTPkLA-------MIFQDFALYPWLTALENVELALlhrkd 81
Cdd:PRK11247 39 QFVAVVGRSGCGKSTLLRLLAGLETPSAGELL------AGTAP-LAearedtrLMFQDARLLPWKKVIDNVGLGL----- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 82 lsKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITaeglRAEIYNMVfneE 161
Cdd:PRK11247 107 --KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALT----RIEMQDLI---E 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1732728249 162 STVR----AIIMVSHNLEEVVELSDKVI-ILGGRpasIIAEVEIKLPRPR 206
Cdd:PRK11247 178 SLWQqhgfTVLLVTHDVSEAVAMADRVLlIEEGK---IGLDLTVDLPRPR 224
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-187 |
7.55e-37 |
|
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: 128.78 E-value: 7.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPK----LAMIFQDFALYPWLTALENVEL-AL 76
Cdd:cd03263 22 SLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAarqsLGYCPQFDALFDELTVREHLRFyAR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 77 LhrKDLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITaeglRAEIYNM 156
Cdd:cd03263 102 L--KGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPAS----RRAIWDL 175
|
170 180 190
....*....|....*....|....*....|.
gi 1732728249 157 VfNEESTVRAIIMVSHNLEEVVELSDKVIIL 187
Cdd:cd03263 176 I-LEVRKGRSIILTTHSMDEAEALCDRIAIM 205
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1-189 |
9.60e-37 |
|
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: 127.17 E-value: 9.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGeevkgptpklamifqdfalypwltalenvelallhrK 80
Cdd:cd03214 18 LSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDG------------------------------------K 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 81 DLSKEVRREIARK------YLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAitaeGLRAEIY 154
Cdd:cd03214 62 DLASLSPKELARKiayvpqALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDI----AHQIELL 137
|
170 180 190
....*....|....*....|....*....|....*.
gi 1732728249 155 NMVFNE-ESTVRAIIMVSHNLEEVVELSDKVIILGG 189
Cdd:cd03214 138 ELLRRLaRERGKTVVMVLHDLNLAARYADRVILLKD 173
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
9-187 |
3.81e-36 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 130.84 E-value: 3.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 9 EFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPK---LAMIFQDFALYPWLTALENVELALLHRKDLSKE 85
Cdd:PRK09452 41 EFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEnrhVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 86 VRREIaRKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEI------YNMVFn 159
Cdd:PRK09452 121 ITPRV-MEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELkalqrkLGITF- 198
|
170 180
....*....|....*....|....*...
gi 1732728249 160 eestvraiIMVSHNLEEVVELSDKVIIL 187
Cdd:PRK09452 199 --------VFVTHDQEEALTMSDRIVVM 218
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
2-187 |
6.16e-36 |
|
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: 124.28 E-value: 6.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKgptpklamifqdfalypwltalenvelallhrKD 81
Cdd:cd00267 19 SLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIA--------------------------------KL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 82 LSKEVRREIArkylelvglggfedYYPrELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEIYNMVfnee 161
Cdd:cd00267 67 PLEELRRRIG--------------YVP-QLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELA---- 127
|
170 180
....*....|....*....|....*.
gi 1732728249 162 STVRAIIMVSHNLEEVVELSDKVIIL 187
Cdd:cd00267 128 EEGRTVIIVTHDPELAELAADRVIVL 153
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
2-200 |
1.06e-35 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 129.19 E-value: 1.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPK---LAMIFQDFALYPWLTALENVELALLH 78
Cdd:PRK11650 24 DLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAdrdIAMVFQNYALYPHMSVRENMAYGLKI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 79 RKdLSKEvrrEIARKYLE---LVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEIYN 155
Cdd:PRK11650 104 RG-MPKA---EIEERVAEaarILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQR 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1732728249 156 MVFNEESTVraiIMVSHNLEEVVELSDKVIIL-GGRPASIIAEVEI 200
Cdd:PRK11650 180 LHRRLKTTS---LYVTHDQVEAMTLADRVVVMnGGVAEQIGTPVEV 222
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-187 |
1.53e-35 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 126.02 E-value: 1.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTP-------------KLAMIFQDFALYPWLT 67
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSlsqqkglirqlrqHVGFVFQNFNLFPHRT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 68 ALENVELALLHRKDLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAitae 147
Cdd:PRK11264 102 VLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDP---- 177
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1732728249 148 GLRAEIYNMVFNEESTVRAIIMVSHNLEEVVELSDKVIIL 187
Cdd:PRK11264 178 ELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFM 217
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
1-197 |
1.99e-35 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 127.12 E-value: 1.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEV-KGPTP---KLAMIFQDFALYPWLTALENVEL-A 75
Cdd:TIGR01188 12 VNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVvREPRKvrrSIGIVPQYASVDEDLTGRENLEMmG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 76 LLHrkDLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITaeglRAEIYN 155
Cdd:TIGR01188 92 RLY--GLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRT----RRAIWD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1732728249 156 MVFNEESTVRAIIMVSHNLEEVVELSDKVIILggRPASIIAE 197
Cdd:TIGR01188 166 YIRALKEEGVTILLTTHYMEEADKLCDRIAII--DHGRIIAE 205
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
2-198 |
1.86e-34 |
|
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: 125.99 E-value: 1.86e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGE-----EVKGPTP----KLAMIFQDFALYPWLTALENV 72
Cdd:TIGR02142 17 DFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfdsRKGIFLPpekrRIGYVFQEARLFPHLSVRGNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 73 ELAllhRKDLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAItaegLRAE 152
Cdd:TIGR02142 97 RYG---MKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDP----RKYE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1732728249 153 IynMVFNE---ESTVRAIIMVSHNLEEVVELSDKVIIL-GGRPASI--IAEV 198
Cdd:TIGR02142 170 I--LPYLErlhAEFGIPILYVSHSLQEVLRLADRVVVLeDGRVAAAgpIAEV 219
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
13-187 |
3.10e-34 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 121.53 E-value: 3.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 13 IVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPKLAMIF----QDFALYPWLTALENVE-LALLHRKDlSKEVR 87
Cdd:cd03264 30 LLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIgylpQEFGVYPNFTVREFLDyIAWLKGIP-SKEVK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 88 REIARkYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAeiynmVFNEESTVRAI 167
Cdd:cd03264 109 ARVDE-VLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRN-----LLSELGEDRIV 182
|
170 180
....*....|....*....|
gi 1732728249 168 IMVSHNLEEVVELSDKVIIL 187
Cdd:cd03264 183 ILSTHIVEDVESLCNQVAVL 202
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
2-190 |
4.38e-34 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 122.00 E-value: 4.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPK---LAMIFQDFALYPWLTALENVELAL-- 76
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSrrpVSMLFQENNLFSHLTVAQNIGLGLnp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 77 -LHRKDLSKEVRREIARKylelVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAitaeGLRAEIYN 155
Cdd:PRK10771 99 gLKLNAAQREKLHAIARQ----MGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDP----ALRQEMLT 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 1732728249 156 MVfNEESTVRAI--IMVSHNLEEVVELSDK-VIILGGR 190
Cdd:PRK10771 171 LV-SQVCQERQLtlLMVSHSLEDAARIAPRsLVVADGR 207
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1-189 |
6.10e-34 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 120.78 E-value: 6.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPKLAMI---FQDFALYPWLTALENVEL-AL 76
Cdd:cd03268 19 ISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIgalIEAPGFYPNLTARENLRLlAR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 77 LHRkdlskeVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDaitAEGLrAEIYNM 156
Cdd:cd03268 99 LLG------IRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLD---PDGI-KELREL 168
|
170 180 190
....*....|....*....|....*....|...
gi 1732728249 157 VFNEESTVRAIIMVSHNLEEVVELSDKVIILGG 189
Cdd:cd03268 169 ILSLRDQGITVLISSHLLSEIQKVADRIGIINK 201
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-201 |
1.79e-33 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 125.52 E-value: 1.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPKLA------MIFQDFALYPWLTALENVELA 75
Cdd:COG3845 25 SLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAialgigMVHQHFMLVPNLTVAENIVLG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 76 L-------LHRKDLSKEVrREIARKYlelvglgGFE---DYYPRELSGGMKQRVAIARALAAQPVVLLMDEP-------- 137
Cdd:COG3845 105 LeptkggrLDRKAARARI-RELSERY-------GLDvdpDAKVEDLSVGEQQRVEILKALYRGARILILDEPtavltpqe 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1732728249 138 ----FANLDAITAEGlraeiynmvfneestvRAIIMVSHNLEEVVELSDKVIIL-GGRpasIIAEVEIK 201
Cdd:COG3845 177 adelFEILRRLAAEG----------------KSIIFITHKLREVMAIADRVTVLrRGK---VVGTVDTA 226
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-200 |
2.24e-33 |
|
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: 121.00 E-value: 2.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPT------PKLAMIFQ-------------DFAL 62
Cdd:TIGR04520 22 SLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEEnlweirKKVGMVFQnpdnqfvgatvedDVAF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 63 ypwltALENVELAllhrkdlSKEVRREIArKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLD 142
Cdd:TIGR04520 102 -----GLENLGVP-------REEMRKRVD-EALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1732728249 143 AITaeglRAEIYNMV--FNEESTVrAIIMVSHNLEEVVeLSDKVIILG-------GRPASIIAEVEI 200
Cdd:TIGR04520 169 PKG----RKEVLETIrkLNKEEGI-TVISITHDMEEAV-LADRVIVMNkgkivaeGTPREIFSQVEL 229
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-197 |
2.63e-33 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 121.03 E-value: 2.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPT--------PKLAMIFQDFALYPWLTALENV 72
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsrlytvrKRMSMLFQSGALFTDMNVFDNV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 73 ELALLHRKDLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAE 152
Cdd:PRK11831 106 AYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1732728249 153 IYNMvfNEESTVRAIImVSHNLEEVVELSDKVIILGGRpaSIIAE 197
Cdd:PRK11831 186 ISEL--NSALGVTCVV-VSHDVPEVLSIADHAYIVADK--KIVAH 225
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-187 |
4.14e-33 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 124.36 E-value: 4.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPK------LAMIFQDFALYPWLTALENVELA 75
Cdd:COG1129 24 SLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRdaqaagIAIIHQELNLVPNLSVAENIFLG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 76 -------LLHRKDLskevrREIARKYLELVGLggfeDYYPR----ELSGGMKQRVAIARALAAQPVVLLMDEPFANLDai 144
Cdd:COG1129 104 reprrggLIDWRAM-----RRRARELLARLGL----DIDPDtpvgDLSVAQQQLVEIARALSRDARVLILDEPTASLT-- 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1732728249 145 taeglRAEIyNMVFNeesTVR-------AIIMVSHNLEEVVELSDKVIIL 187
Cdd:COG1129 173 -----EREV-ERLFR---IIRrlkaqgvAIIYISHRLDEVFEIADRVTVL 213
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1-197 |
2.84e-32 |
|
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: 116.70 E-value: 2.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEV-KGPTP---KLAMIFQDFALYPWLTALENVEL-A 75
Cdd:cd03265 19 VSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVvREPREvrrRIGIVFQDLSVDDELTGWENLYIhA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 76 LLHrkDLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEIYN 155
Cdd:cd03265 99 RLY--GVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEK 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1732728249 156 MVFNEESTvraIIMVSHNLEEVVELSDKV-IILGGRpasIIAE 197
Cdd:cd03265 177 LKEEFGMT---ILLTTHYMEEAEQLCDRVaIIDHGR---IIAE 213
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-190 |
3.60e-32 |
|
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: 115.17 E-value: 3.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTP-----KLAMIFQDFALYPwLTALENVelal 76
Cdd:cd03228 22 SLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLeslrkNIAYVPQDPFLFS-GTIRENI---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 77 lhrkdlskevrreiarkylelvglggfedyypreLSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEIYNM 156
Cdd:cd03228 97 ----------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRAL 142
|
170 180 190
....*....|....*....|....*....|....*
gi 1732728249 157 vfneeSTVRAIIMVSHNLeEVVELSDKVIIL-GGR 190
Cdd:cd03228 143 -----AKGKTVIVIAHRL-STIRDADRIIVLdDGR 171
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
2-190 |
9.99e-32 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 118.36 E-value: 9.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTP--------KLAMIFQDFALYPWLTALENVE 73
Cdd:PRK11153 25 SLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEkelrkarrQIGMIFQHFNLLSSRTVFDNVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 74 LALlhrkDLSKEVRREIARK---YLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAE--- 147
Cdd:PRK11153 105 LPL----ELAGTPKAEIKARvteLLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRsil 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1732728249 148 GLRAEIynmvfNEESTVrAIIMVSHNLEEVVELSDKV-IILGGR 190
Cdd:PRK11153 181 ELLKDI-----NRELGL-TIVLITHEMDVVKRICDRVaVIDAGR 218
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-147 |
1.23e-31 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 115.88 E-value: 1.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEV---KGPTPK--------LAMIFQDFALYPWLTALE 70
Cdd:PRK11124 22 TLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKairelrrnVGMVFQQYNLWPHLTVQQ 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1732728249 71 NVELALLHRKDLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDA-ITAE 147
Cdd:PRK11124 102 NLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPeITAQ 179
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-147 |
1.51e-31 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 115.50 E-value: 1.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTP-----------KLAMIFQDFALYPWLTALE 70
Cdd:COG4161 22 NLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKpsekairllrqKVGMVFQQYNLWPHLTVME 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1732728249 71 NVELALLHRKDLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLD-AITAE 147
Cdd:COG4161 102 NLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDpEITAQ 179
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-187 |
4.43e-31 |
|
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: 113.62 E-value: 4.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 3 FKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEV-KGPTP---KLAMIFQDFALYPWLTALENVE-LALL 77
Cdd:cd03266 26 FTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVvKEPAEarrRLGFVSDSTGLYDRLTARENLEyFAGL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 78 HRKDlskevRREIARKYLELVGLGGFEDYYPR---ELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEIY 154
Cdd:cd03266 106 YGLK-----GDELTARLEELADRLGMEELLDRrvgGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIR 180
|
170 180 190
....*....|....*....|....*....|...
gi 1732728249 155 NMvfneESTVRAIIMVSHNLEEVVELSDKVIIL 187
Cdd:cd03266 181 QL----RALGKCILFSTHIMQEVERLCDRVVVL 209
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
5-175 |
8.24e-31 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 113.34 E-value: 8.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 5 VHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMG-------EEVKGP--TPKLAMIFQDFALYPWLTALENVELA 75
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGqplhqmdEEARAKlrAKHVGFVFQSFMLIPTLNALENVELP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 76 LLHRKDLSKEvRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEIYN 155
Cdd:PRK10584 113 ALLRGESSRQ-SRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFS 191
|
170 180
....*....|....*....|
gi 1732728249 156 MVFNEESTvraIIMVSHNLE 175
Cdd:PRK10584 192 LNREHGTT---LILVTHDLQ 208
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
2-143 |
1.17e-30 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 112.20 E-value: 1.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKgptpKLAMIFQDFALY--------PWLTALENve 73
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR----RQRDEYHQDLLYlghqpgikTELTALEN-- 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 74 LALLHRkdLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDA 143
Cdd:PRK13538 95 LRFYQR--LHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDK 162
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
2-187 |
1.37e-30 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 113.78 E-value: 1.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVK-GPTPKLA----MIFQD--FALYPWLTALENVEL 74
Cdd:COG4167 33 SFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEyGDYKYRCkhirMIFQDpnTSLNPRLNIGQILEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 75 ALLHRKDLSKEVRREIARKYLELVGL-GGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAitaeGLRAEI 153
Cdd:COG4167 113 PLRLNTDLTAEEREERIFATLRLVGLlPEHANFYPHMLSSGQKQRVALARALILQPKIIIADEALAALDM----SVRSQI 188
|
170 180 190
....*....|....*....|....*....|....*
gi 1732728249 154 YNMVFNEESTVR-AIIMVSHNLEEVVELSDKVIIL 187
Cdd:COG4167 189 INLMLELQEKLGiSYIYVSQHLGIVKHISDKVLVM 223
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1-187 |
1.54e-30 |
|
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: 112.14 E-value: 1.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKG-PTPK-----LAMIFQDFALYPWLTALENVEL 74
Cdd:cd03224 19 VSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGlPPHEraragIGYVPEGRRIFPELTVEENLLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 75 ALLHRKDlsKEVRREIARKYlelvglggfeDYYPR----------ELSGGMKQRVAIARALAAQPVVLLMDEPFANLdai 144
Cdd:cd03224 99 GAYARRR--AKRKARLERVY----------ELFPRlkerrkqlagTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL--- 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1732728249 145 tAEGLRAEIYNMV--FNEESTvrAIIMVSHNLEEVVELSDKVIIL 187
Cdd:cd03224 164 -APKIVEEIFEAIreLRDEGV--TILLVEQNARFALEIADRAYVL 205
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-187 |
1.72e-30 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 113.14 E-value: 1.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPK------------------LAMIFQDFAL 62
Cdd:PRK10619 24 VSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvadknqlrllrtrLTMVFQHFNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 63 YPWLTALENVELALLHRKDLSKEVRREIARKYLELVGLGG-FEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANL 141
Cdd:PRK10619 104 WSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDErAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSAL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1732728249 142 DA-ITAEGLRaeIYNMVFNEESTvraIIMVSHNLEEVVELSDKVIIL 187
Cdd:PRK10619 184 DPeLVGEVLR--IMQQLAEEGKT---MVVVTHEMGFARHVSSHVIFL 225
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
3-187 |
2.39e-30 |
|
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: 111.60 E-value: 2.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 3 FKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVK-GPTPKLAMIFQDFALYPWLTALEN-VELALLhrK 80
Cdd:cd03269 21 FSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDiAARNRIGYLPEERGLYPKMKVIDQlVYLAQL--K 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 81 DLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEIYNMVFNE 160
Cdd:cd03269 99 GLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAG 178
|
170 180
....*....|....*....|....*..
gi 1732728249 161 estvRAIIMVSHNLEEVVELSDKVIIL 187
Cdd:cd03269 179 ----KTVILSTHQMELVEELCDRVLLL 201
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-187 |
2.99e-30 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 115.32 E-value: 2.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTP---KLAMIFQDFALYPWLTALENVELALL 77
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPyqrPINMMFQSYALFPHMTVEQNIAFGLK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 78 HRKDLSKEVRREIArKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEIYNMV 157
Cdd:PRK11607 118 QDKLPKAEIASRVN-EMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDIL 196
|
170 180 190
....*....|....*....|....*....|
gi 1732728249 158 fneESTVRAIIMVSHNLEEVVELSDKVIIL 187
Cdd:PRK11607 197 ---ERVGVTCVMVTHDQEEAMTMAGRIAIM 223
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-199 |
4.96e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 112.83 E-value: 4.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPKLAMIFQDFAL---YPWLTALENV---ELA 75
Cdd:PRK13637 27 NIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIRKKVGLvfqYPEYQLFEETiekDIA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 76 L-LHRKDLSKEVRREIARKYLELVGLG--GFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAE 152
Cdd:PRK13637 107 FgPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNK 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1732728249 153 IYNMVFNEESTvraIIMVSHNLEEVVELSDKVI-------ILGGRPASIIAEVE 199
Cdd:PRK13637 187 IKELHKEYNMT---IILVSHSMEDVAKLADRIIvmnkgkcELQGTPREVFKEVE 237
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
3-188 |
1.53e-29 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 112.13 E-value: 1.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 3 FKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTP--------KLAMIFQD-FA-LYPWLTALENV 72
Cdd:COG4608 39 FDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGrelrplrrRMQMVFQDpYAsLNPRMTVGDII 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 73 ELALLHRKDLSKEVRREIARKYLELVGLG-GFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAitaeGLRA 151
Cdd:COG4608 119 AEPLRIHGLASKAERRERVAELLELVGLRpEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDV----SIQA 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1732728249 152 EIYNM------------VFneestvraiimVSHNLeEVVE-LSDKVII--LG 188
Cdd:COG4608 195 QVLNLledlqdelgltyLF-----------ISHDL-SVVRhISDRVAVmyLG 234
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-196 |
5.81e-29 |
|
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: 108.40 E-value: 5.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVK------------GPTPKLAMIFQDfalypwLTAL 69
Cdd:cd03218 20 SLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITklpmhkrarlgiGYLPQEASIFRK------LTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 70 ENVELALLHRKDLSKEvRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAegl 149
Cdd:cd03218 94 ENILAVLEIRGLSKKE-REEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAV--- 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1732728249 150 rAEIYNMVFNEESTVRAIIMVSHNLEEVVELSDKVIILG-------GRPASIIA 196
Cdd:cd03218 170 -QDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYegkvlaeGTPEEIAA 222
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
2-187 |
5.85e-29 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 112.05 E-value: 5.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPT---------PKLAMIFQDFALYPWLTALENV 72
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaelrevrrKKIAMVFQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 73 ELALlHRKDLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAE 152
Cdd:PRK10070 128 AFGM-ELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDE 206
|
170 180 190
....*....|....*....|....*....|....*
gi 1732728249 153 IYNMVFNEEstvRAIIMVSHNLEEVVELSDKVIIL 187
Cdd:PRK10070 207 LVKLQAKHQ---RTIVFISHDLDEAMRIGDRIAIM 238
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-187 |
6.51e-29 |
|
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: 113.78 E-value: 6.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPK-----LAMIFQDFALYPwLTALENVelaL 76
Cdd:COG2274 495 SLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPAslrrqIGVVLQDVFLFS-GTIRENI---T 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 77 LHRKDLSKEVRREIARkyleLVGLGGFEDYYP-----------RELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAIT 145
Cdd:COG2274 571 LGDPDATDEEIIEAAR----LAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAET 646
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1732728249 146 AEGLRAEIYNMVFNeestvRAIIMVSHNLeEVVELSDKVIIL 187
Cdd:COG2274 647 EAIILENLRRLLKG-----RTVIIIAHRL-STIRLADRIIVL 682
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
2-142 |
9.05e-29 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 108.66 E-value: 9.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTP-----KLAMIFQDFAL-YPWlTALENVELA 75
Cdd:COG4559 21 SLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPwelarRRAVLPQHSSLaFPF-TVEEVVALG 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1732728249 76 LL-HRkdLSKEVRREIARKYLELVGLGGFED-YYPrELSGGMKQRVAIARALA-------AQPVVLLMDEPFANLD 142
Cdd:COG4559 100 RApHG--SSAAQDRQIVREALALVGLAHLAGrSYQ-TLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALD 172
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-187 |
9.07e-29 |
|
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: 112.93 E-value: 9.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPK-----LAMIFQDfalyPWL---TALENVE 73
Cdd:COG4988 357 SLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAswrrqIAWVPQN----PYLfagTIRENLR 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 74 LAllhRKDLSKEvrrEIARKyLELVGLGGFEDYYP-----------RELSGGMKQRVAIARALAAQPVVLLMDEPFANLD 142
Cdd:COG4988 433 LG---RPDASDE---ELEAA-LEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLD 505
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1732728249 143 AITAEGLRAEIYNMvfneeSTVRAIIMVSHNLeEVVELSDKVIIL 187
Cdd:COG4988 506 AETEAEILQALRRL-----AKGRTVILITHRL-ALLAQADRILVL 544
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
3-190 |
9.59e-29 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 107.98 E-value: 9.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 3 FKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTP---------KLAMIFQDFALYPWLTALENVE 73
Cdd:PRK11629 30 FSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakaelrnqKLGFIYQFHHLLPDFTALENVA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 74 LALLHRKDLSKEVRREiARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEglraEI 153
Cdd:PRK11629 110 MPLLIGKKKPAEINSR-ALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNAD----SI 184
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1732728249 154 YNMVfnEESTVR---AIIMVSHNLEEVVELSDKVIILGGR 190
Cdd:PRK11629 185 FQLL--GELNRLqgtAFLVVTHDLQLAKRMSRQLEMRDGR 222
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-190 |
1.17e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 109.43 E-value: 1.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVkgpTPKlamIFQDFA-------LYPWLTALENVE 73
Cdd:COG4152 20 VSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL---DPE---DRRRIGylpeergLYPKMKVGEQLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 74 -LALLHrkDLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAE 152
Cdd:COG4152 94 yLARLK--GLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDV 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 1732728249 153 IYNMvfNEESTvrAIIMVSHNLEEVVELSDKVIIL-GGR 190
Cdd:COG4152 172 IREL--AAKGT--TVIFSSHQMELVEELCDRIVIInKGR 206
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-187 |
1.42e-28 |
|
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: 107.23 E-value: 1.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGeevkGPTPKLAMI--FQdfalyPWLTALENVEL-ALLH 78
Cdd:cd03220 42 SFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG----RVSSLLGLGggFN-----PELTGRENIYLnGRLL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 79 --RKDLSKEVRREIarkyLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEIYNM 156
Cdd:cd03220 113 glSRKEIDEKIDEI----IEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLREL 188
|
170 180 190
....*....|....*....|....*....|.
gi 1732728249 157 VfneeSTVRAIIMVSHNLEEVVELSDKVIIL 187
Cdd:cd03220 189 L----KQGKTVILVSHDPSSIKRLCDRALVL 215
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-187 |
4.21e-28 |
|
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: 104.43 E-value: 4.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPK------LAMIFQdfalypwltalenvela 75
Cdd:cd03216 20 SLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRdarragIAMVYQ----------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 76 llhrkdlskevrreiarkylelvglggfedyypreLSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEIYN 155
Cdd:cd03216 83 -----------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRR 127
|
170 180 190
....*....|....*....|....*....|..
gi 1732728249 156 MVfneeSTVRAIIMVSHNLEEVVELSDKVIIL 187
Cdd:cd03216 128 LR----AQGVAVIFISHRLDEVFEIADRVTVL 155
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
2-189 |
4.22e-28 |
|
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: 105.42 E-value: 4.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPT--PKLAMIFQD--FALYpwltaLENVELALL 77
Cdd:cd03226 20 SLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKErrKSIGYVMQDvdYQLF-----TDSVREELL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 78 HRKDLSKEvRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLrAEIYNMV 157
Cdd:cd03226 95 LGLKELDA-GNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERV-GELIREL 172
|
170 180 190
....*....|....*....|....*....|..
gi 1732728249 158 FNEEstvRAIIMVSHNLEEVVELSDKVIILGG 189
Cdd:cd03226 173 AAQG---KAVIVITHDYEFLAKVCDRVLLLAN 201
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-188 |
8.30e-28 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 110.24 E-value: 8.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPK-----LAMIFQDfalyPWL---TALENVE 73
Cdd:COG4987 355 SLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDdlrrrIAVVPQR----PHLfdtTLRENLR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 74 LAllhRKDLSKEvrrEIaRKYLELVGLGGFEDYYP-----------RELSGGMKQRVAIARALAAQPVVLLMDEPFANLD 142
Cdd:COG4987 431 LA---RPDATDE---EL-WAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGLD 503
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1732728249 143 AITAEGLRAEIYnmvfnEESTVRAIIMVSHNLEEvVELSDKVIILG 188
Cdd:COG4987 504 AATEQALLADLL-----EALAGRTVLLITHRLAG-LERMDRILVLE 543
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-204 |
1.21e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 106.32 E-value: 1.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVK-------GPTPKLAMIFQD-----FAlyPwlTA 68
Cdd:PRK13639 21 INFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydkksllEVRKTVGIVFQNpddqlFA--P--TV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 69 LENVELALLHRKdLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEG 148
Cdd:PRK13639 97 EEDVAFGPLNLG-LSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQ 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1732728249 149 LRAEIYNMvfNEESTvrAIIMVSHNLEEVVELSDKV-------IILGGRPASIIAEVEI------KLPR 204
Cdd:PRK13639 176 IMKLLYDL--NKEGI--TIIISTHDVDLVPVYADKVyvmsdgkIIKEGTPKEVFSDIETirkanlRLPR 240
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
2-197 |
1.92e-27 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 104.73 E-value: 1.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVkgpTpKLAM----------------IFQDfalypw 65
Cdd:COG1137 23 SLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI---T-HLPMhkrarlgigylpqeasIFRK------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 66 LTALENVeLALLHRKDLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAIT 145
Cdd:COG1137 93 LTVEDNI-LAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1732728249 146 AeglrAEIYNMVFNEEStvRAI-IMVS-HNLEEVVELSDKV-IILGGRpasIIAE 197
Cdd:COG1137 172 V----ADIQKIIRHLKE--RGIgVLITdHNVRETLGICDRAyIISEGK---VLAE 217
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
3-143 |
6.17e-27 |
|
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: 102.44 E-value: 6.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 3 FKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEV----KGPTPKLAMIFQDFALYPWLTALENveLALLH 78
Cdd:TIGR01189 21 FTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLaeqrDEPHENILYLGHLPGLKPELSALEN--LHFWA 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1732728249 79 RkDLSKEVRReiARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDA 143
Cdd:TIGR01189 99 A-IHGGAQRT--IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
2-190 |
9.96e-27 |
|
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: 102.75 E-value: 9.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKG-PTPKLA-----------MIFQDfalypwLTAL 69
Cdd:COG0410 23 SLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGlPPHRIArlgigyvpegrRIFPS------LTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 70 ENVELALLHRKDlSKEVRREIARKYlelvglggfeDYYPR----------ELSGGMKQRVAIARALAAQPVVLLMDEPFa 139
Cdd:COG0410 97 ENLLLGAYARRD-RAEVRADLERVY----------ELFPRlkerrrqragTLSGGEQQMLAIGRALMSRPKLLLLDEPS- 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1732728249 140 nldaitaEGL----RAEIYNMV--FNEESTvrAIIMVSHNLEEVVELSDKVIIL-GGR 190
Cdd:COG0410 165 -------LGLapliVEEIFEIIrrLNREGV--TILLVEQNARFALEIADRAYVLeRGR 213
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-199 |
1.40e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 106.26 E-value: 1.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPKLAM---------------IFQDfalypwL 66
Cdd:COG1129 272 SFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIragiayvpedrkgegLVLD------L 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 67 TALENVELALLHRK------DLSKEvrREIARKYLELVGL--GGFEDYYpRELSGGMKQRVAIARALAAQPVVLLMDEPF 138
Cdd:COG1129 346 SIRENITLASLDRLsrggllDRRRE--RALAEEYIKRLRIktPSPEQPV-GNLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1732728249 139 ANLDAitaeGLRAEIYNMV--FNEESTvrAIIMVSHNLEEVVELSDKVIIL-GGRpasIIAEVE 199
Cdd:COG1129 423 RGIDV----GAKAEIYRLIreLAAEGK--AVIVISSELPELLGLSDRILVMrEGR---IVGELD 477
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2-142 |
1.49e-26 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 102.93 E-value: 1.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPK-----LAMIFQDFAL-YPWlTALENVELA 75
Cdd:PRK13548 22 SLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAelarrRAVLPQHSSLsFPF-TVEEVVAMG 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1732728249 76 LLHRKDLSKEVRReIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALA------AQPVVLLMDEPFANLD 142
Cdd:PRK13548 101 RAPHGLSRAEDDA-LVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALD 172
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
5-187 |
2.07e-26 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 100.77 E-value: 2.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 5 VHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVllmgeeVKGPTPKLAMIFQDFALyPW---LTALENVELALLHRKD 81
Cdd:NF040873 15 IPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV------RRAGGARVAYVPQRSEV-PDslpLTVRDLVAMGRWARRG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 82 LSKEVRRE---IARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITaeglRAEIYNMVF 158
Cdd:NF040873 88 LWRRLTRDdraAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES----RERIIALLA 163
|
170 180
....*....|....*....|....*....
gi 1732728249 159 NEESTVRAIIMVSHNLeEVVELSDKVIIL 187
Cdd:NF040873 164 EEHARGATVVVVTHDL-ELVRRADPCVLL 191
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
2-196 |
1.17e-25 |
|
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: 100.16 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVL-LMGEEVKGPT-----PKLAMIFQDFALY--PWLTALENVE 73
Cdd:COG1119 23 SWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrLFGERRGGEDvwelrKRIGLVSPALQLRfpRDETVLDVVL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 74 LAL-----LHRKdlSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEG 148
Cdd:COG1119 103 SGFfdsigLYRE--PTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGAREL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1732728249 149 LRAEIYNMVfneESTVRAIIMVSHNLEEVVELSDKVIILggRPASIIA 196
Cdd:COG1119 181 LLALLDKLA---AEGAPTLVLVTHHVEEIPPGITHVLLL--KDGRVVA 223
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-190 |
1.36e-25 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 104.09 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPK-----LAMIFQDFALYPwLTALENVELAl 76
Cdd:COG1132 360 SLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLEslrrqIGVVPQDTFLFS-GTIRENIRYG- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 77 lhRKDLSKEVRREIARK-------------YLELVGLGGfedyypRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDA 143
Cdd:COG1132 438 --RPDATDEEVEEAAKAaqahefiealpdgYDTVVGERG------VNLSGGQRQRIAIARALLKDPPILILDEATSALDT 509
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1732728249 144 ITAEGLRAEIYNMVFNeestvRAIIMVSHNLEEVVElSDKVIIL-GGR 190
Cdd:COG1132 510 ETEALIQEALERLMKG-----RTTIVIAHRLSTIRN-ADRILVLdDGR 551
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-198 |
2.52e-25 |
|
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: 102.96 E-value: 2.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKV-LLMGEE-----VKGP------TPKLAMIFQDFALYPWLTA 68
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnVRVGDEwvdmtKPGPdgrgraKRYIGILHQEYDLYPHRTV 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 69 LENVELALlhRKDLSKEVRREIARKYLELVGLGGFE-----DYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDA 143
Cdd:TIGR03269 383 LDNLTEAI--GLELPDELARMKAVITLKMVGFDEEKaeeilDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDP 460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1732728249 144 ITAEGLRAEIYNMVFNEESTvraIIMVSHNLEEVVELSDKV-------IILGGRPASIIAEV 198
Cdd:TIGR03269 461 ITKVDVTHSILKAREEMEQT---FIIVSHDMDFVLDVCDRAalmrdgkIVKIGDPEEIVEEL 519
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-188 |
7.38e-25 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 97.64 E-value: 7.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEV----KGPTP----KLAMIFQDFALYPWLTALENV 72
Cdd:PRK10908 21 VTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlkNREVPflrrQIGMIFQDHHLLMDRTVYDNV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 73 ELALLHRKDLSKEVRREIARKyLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEG-LRa 151
Cdd:PRK10908 101 AIPLIIAGASGDDIRRRVSAA-LDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGiLR- 178
|
170 180 190
....*....|....*....|....*....|....*...
gi 1732728249 152 eiynmVFNEESTVR-AIIMVSHNLEEVVELSDKVIILG 188
Cdd:PRK10908 179 -----LFEEFNRVGvTVLMATHDIGLISRRSYRMLTLS 211
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1-187 |
7.42e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 99.13 E-value: 7.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPT---------PKLAMIFQdfalYPWL----- 66
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETgnknlkklrKKVSLVFQ----FPEAqlfen 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 67 TALENVELALLHRkDLSKEVRREIARKYLELVGLG-GFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDait 145
Cdd:PRK13641 102 TVLKDVEFGPKNF-GFSEDEAKEKALKWLKKVGLSeDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD--- 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1732728249 146 AEGlRAEIYNMVFNEESTVRAIIMVSHNLEEVVELSDKVIIL 187
Cdd:PRK13641 178 PEG-RKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVL 218
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-200 |
7.59e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 98.52 E-value: 7.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPT-----PKLAMIFQ-------------DFALy 63
Cdd:PRK13632 29 SFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENlkeirKKIGIIFQnpdnqfigatvedDIAF- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 64 pwltALENvelallhrKDLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDa 143
Cdd:PRK13632 108 ----GLEN--------KKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLD- 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1732728249 144 itAEGlRAEIYN-MVFNEESTVRAIIMVSHNLEEVVeLSDKVIILG-------GRPASIIAEVEI 200
Cdd:PRK13632 175 --PKG-KREIKKiMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSegkliaqGKPKEILNNKEI 235
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
5-190 |
8.08e-25 |
|
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: 98.34 E-value: 8.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 5 VHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPK--------LAMIFQDF--ALYPWLTALENVEL 74
Cdd:TIGR02769 34 IEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKqrrafrrdVQLVFQDSpsAVNPRMTVRQIIGE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 75 ALLHRKDLSKEVRREIARKYLELVGL-GGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEI 153
Cdd:TIGR02769 114 PLRHLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELL 193
|
170 180 190
....*....|....*....|....*....|....*...
gi 1732728249 154 YNMvfnEESTVRAIIMVSHNLEEVVELSDKVIIL-GGR 190
Cdd:TIGR02769 194 RKL---QQAFGTAYLFITHDLRLVQSFCQRVAVMdKGQ 228
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-187 |
1.17e-24 |
|
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: 101.21 E-value: 1.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPK-----LAMIFQdfalYPWLTA---LENVE 73
Cdd:TIGR02857 342 SFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADswrdqIAWVPQ----HPFLFAgtiAENIR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 74 LAllhRKDLSKEvrrEIARKyLELVGLGGFEDYYP-----------RELSGGMKQRVAIARALAAQPVVLLMDEPFANLD 142
Cdd:TIGR02857 418 LA---RPDASDA---EIREA-LERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLD 490
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1732728249 143 AITAEGLRAEIynmvfNEESTVRAIIMVSHNLeEVVELSDKVIIL 187
Cdd:TIGR02857 491 AETEAEVLEAL-----RALAQGRTVLLVTHRL-ALAALADRIVVL 529
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-186 |
1.52e-24 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 101.34 E-value: 1.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTP-KLA--------MIFQDFALYPWLTALEN 71
Cdd:PRK10535 27 ISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDAdALAqlrrehfgFIFQRYHLLSHLTAAQN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 72 VELALLHrKDLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRA 151
Cdd:PRK10535 107 VEVPAVY-AGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMA 185
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1732728249 152 eIYNMVFNEESTVraiIMVSHN------LEEVVELSDKVII 186
Cdd:PRK10535 186 -ILHQLRDRGHTV---IIVTHDpqvaaqAERVIEIRDGEIV 222
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
18-187 |
1.63e-24 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 99.18 E-value: 1.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 18 GTGKTTLLRIIAGLRRPDSGKVLLMG-------EEVKGPTPK--LAMIFQDFALYPWLTAlenvelallhRKDLSKEVRR 88
Cdd:PRK11144 34 GAGKTSLINAISGLTRPQKGRIVLNGrvlfdaeKGICLPPEKrrIGYVFQDARLFPHYKV----------RGNLRYGMAK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 89 EIARKYLELVGLGGFE---DYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLraeiynMVFNEE--ST 163
Cdd:PRK11144 104 SMVAQFDKIVALLGIEpllDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKREL------LPYLERlaRE 177
|
170 180
....*....|....*....|....*
gi 1732728249 164 VR-AIIMVSHNLEEVVELSDKVIIL 187
Cdd:PRK11144 178 INiPILYVSHSLDEILRLADRVVVL 202
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-190 |
1.79e-24 |
|
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: 95.58 E-value: 1.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTP------KLAMIFQD---FALYPWLTALENV 72
Cdd:cd03215 20 SFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPrdairaGIAYVPEDrkrEGLVLDLSVAENI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 73 ELALLhrkdlskevrreiarkylelvglggfedyypreLSGGMKQRVAIARALAAQPVVLLMDEPFANLDAitaeGLRAE 152
Cdd:cd03215 100 ALSSL---------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDV----GAKAE 142
|
170 180 190
....*....|....*....|....*....|....*....
gi 1732728249 153 IYNMVFNEESTVRAIIMVSHNLEEVVELSDKVIIL-GGR 190
Cdd:cd03215 143 IYRLIRELADAGKAVLLISSELDELLGLCDRILVMyEGR 181
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
3-187 |
3.91e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 97.11 E-value: 3.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 3 FKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPT-----PKLAMIFQ-------------DFALyp 64
Cdd:PRK13650 28 FHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENvwdirHKIGMVFQnpdnqfvgatvedDVAF-- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 65 wltALENvelallhrKDLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDE------PF 138
Cdd:PRK13650 106 ---GLEN--------KGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEatsmldPE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1732728249 139 ANLDAI-TAEGLRAEiYNMvfneestvrAIIMVSHNLEEVVeLSDKVIIL 187
Cdd:PRK13650 175 GRLELIkTIKGIRDD-YQM---------TVISITHDLDEVA-LSDRVLVM 213
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
2-187 |
4.37e-24 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 95.92 E-value: 4.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVllmgeEVKGPTP---KLAMIFQdfalyPWLTALENVEL-ALL 77
Cdd:COG1134 46 SFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV-----EVNGRVSallELGAGFH-----PELTGRENIYLnGRL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 78 HrkDLSkevRREIARKY---LELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEIY 154
Cdd:COG1134 116 L--GLS---RKEIDEKFdeiVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIR 190
|
170 180 190
....*....|....*....|....*....|...
gi 1732728249 155 NMVfneeSTVRAIIMVSHNLEEVVELSDKVIIL 187
Cdd:COG1134 191 ELR----ESGRTVIFVSHSMGAVRRLCDRAIWL 219
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-187 |
4.52e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 97.08 E-value: 4.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKV------------------LLMGEEVKGPTPK----------- 52
Cdd:PRK13651 27 SVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekekVLEKLVIQKTRFKkikkikeirrr 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 53 LAMIFQdFALYPWLTalENVElallhrKDL---------SKEVRREIARKYLELVGLGgfEDYYPR---ELSGGMKQRVA 120
Cdd:PRK13651 107 VGVVFQ-FAEYQLFE--QTIE------KDIifgpvsmgvSKEEAKKRAAKYIELVGLD--ESYLQRspfELSGGQKRRVA 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1732728249 121 IARALAAQPVVLLMDEPFANLDAITAEglraEIYNMVFNEESTVRAIIMVSHNLEEVVELSDKVIIL 187
Cdd:PRK13651 176 LAGILAMEPDFLVFDEPTAGLDPQGVK----EILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFF 238
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
2-153 |
6.94e-24 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 94.56 E-value: 6.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPKLAMIF---QDfALYPWLTALENVEL--AL 76
Cdd:PRK13539 22 SFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYlghRN-AMKPALTVAENLEFwaAF 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1732728249 77 LHRKDLSkevrreIARKyLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAiTAEGLRAEI 153
Cdd:PRK13539 101 LGGEELD------IAAA-LEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA-AAVALFAEL 169
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2-199 |
9.50e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 96.24 E-value: 9.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLmGEEVKGPT----------PKLAMIFQ--DFALYPwltal 69
Cdd:PRK13634 27 NVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGkknkklkplrKKVGIVFQfpEHQLFE----- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 70 ENVElallhrKDL---------SKEVRREIARKYLELVGLGgfEDYY---PRELSGGMKQRVAIARALAAQPVVLLMDEP 137
Cdd:PRK13634 101 ETVE------KDIcfgpmnfgvSEEDAKQKAREMIELVGLP--EELLarsPFELSGGQMRRVAIAGVLAMEPEVLVLDEP 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1732728249 138 FANLDaitAEGlRAEIYNMVFN--EESTVrAIIMVSHNLEEVVELSDKVIIL-------GGRPASIIAEVE 199
Cdd:PRK13634 173 TAGLD---PKG-RKEMMEMFYKlhKEKGL-TTVLVTHSMEDAARYADQIVVMhkgtvflQGTPREIFADPD 238
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
1-190 |
1.05e-23 |
|
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: 94.39 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEE-VKGPTPKLAMIFQDFALYPWLTALENVELALLHR 79
Cdd:TIGR03740 19 ISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPwTRKDLHKIGSLIESPPLYENLTARENLKVHTTLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 80 kDLSKEVRREIarkyLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEIYNmvFN 159
Cdd:TIGR03740 99 -GLPDSRIDEV----LNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLDPIGIQELRELIRS--FP 171
|
170 180 190
....*....|....*....|....*....|..
gi 1732728249 160 EESTvrAIIMVSHNLEEVVELSDKV-IILGGR 190
Cdd:TIGR03740 172 EQGI--TVILSSHILSEVQQLADHIgIISEGV 201
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-201 |
1.11e-23 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 94.96 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVK------------GPTPKLAMIFQDFALYpwlta 68
Cdd:PRK10895 22 VSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllplhararrgiGYLPQEASIFRRLSVY----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 69 lENVELALLHRKDLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAeg 148
Cdd:PRK10895 97 -DNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISV-- 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 149 lrAEIYNMVFNEESTVRAIIMVSHNLEEVVELSDKVIILG-------GRPASIIAEVEIK 201
Cdd:PRK10895 174 --IDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSqghliahGTPTEILQDEHVK 231
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1-143 |
1.45e-23 |
|
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: 93.71 E-value: 1.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPKLA----MIFQDFALYPWLTALENveLAL 76
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIArgllYLGHAPGIKTTLSVLEN--LRF 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1732728249 77 LHRKDLSKEVRREIARkylelVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDA 143
Cdd:cd03231 97 WHADHSDEQVEEALAR-----VGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
2-195 |
1.69e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 97.22 E-value: 1.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPK-----LAMIFQDFALYPWLTALENVELAL 76
Cdd:PRK09536 23 DLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARaasrrVASVPQDTSLSFEFDVRQVVEMGR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 77 ---LHRKDLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEI 153
Cdd:PRK09536 103 tphRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELV 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1732728249 154 YNMVFNEESTVRAIimvsHNLE-------EVVELSDKVIILGGRPASII 195
Cdd:PRK09536 183 RRLVDDGKTAVAAI----HDLDlaarycdELVLLADGRVRAAGPPADVL 227
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-187 |
2.38e-23 |
|
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: 92.28 E-value: 2.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPklaMIFQDFALYpwltALENVELallhrkd 81
Cdd:cd03246 22 SFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDP---NELGDHVGY----LPQDDEL------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 82 LSKEVRREIarkylelvglggfedyypreLSGGMKQRVAIARALAAQPVVLLMDEPFANLDaitAEGLRAeIYNMVFNEE 161
Cdd:cd03246 88 FSGSIAENI--------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLD---VEGERA-LNQAIAALK 143
|
170 180
....*....|....*....|....*.
gi 1732728249 162 STVRAIIMVSHNLeEVVELSDKVIIL 187
Cdd:cd03246 144 AAGATRIVIAHRP-ETLASADRILVL 168
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-187 |
3.17e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.06 E-value: 3.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVllmgeeVKGPTPKLAMIFQDFALYPWLTALENVELALLHRKD 81
Cdd:COG0488 18 SLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV------SIPKGLRIGYLPQEPPLDDDLTVLDTVLDGDAELRA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 82 LSKEVRR---------EIARKYLE--------------------LVGLG-GFEDYY--PRELSGGMKQRVAIARALAAQP 129
Cdd:COG0488 92 LEAELEEleaklaepdEDLERLAElqeefealggweaearaeeiLSGLGfPEEDLDrpVSELSGGWRRRVALARALLSEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1732728249 130 VVLLMDEPFANLDAITAEGLRaeiyNMVFNEESTVraiIMVSHN---LEEVV----ELSDKVIIL 187
Cdd:COG0488 172 DLLLLDEPTNHLDLESIEWLE----EFLKNYPGTV---LVVSHDryfLDRVAtrilELDRGKLTL 229
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-184 |
4.17e-23 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 93.56 E-value: 4.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLR-------IIAGLRRpdSGKVLLMGEEVKGPT--P-----KLAMIFQD---FAL-- 62
Cdd:COG1117 31 NLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGARV--EGEILLDGEDIYDPDvdVvelrrRVGMVFQKpnpFPKsi 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 63 YpwltalENVELALLHRKDLSKEVRREIARKYLELVGLggFEDYYPR------ELSGGMKQRVAIARALAAQPVVLLMDE 136
Cdd:COG1117 109 Y------DNVAYGLRLHGIKSKSELDEIVEESLRKAAL--WDEVKDRlkksalGLSGGQQQRLCIARALAVEPEVLLMDE 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1732728249 137 PFANLDAI-TA--EGLraeiynmvFNEESTVRAIIMVSHNLEEVVELSDKV 184
Cdd:COG1117 181 PTSALDPIsTAkiEEL--------ILELKKDYTIVIVTHNMQQAARVSDYT 223
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-190 |
4.25e-23 |
|
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: 93.06 E-value: 4.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPK-----LAMIFQDfalyPWL---TALENVE 73
Cdd:cd03254 23 NFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKslrsmIGVVLQD----TFLfsgTIMENIR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 74 LALLHRKDLSKEVRREIARKYLELVGLGGFEDYYPRE----LSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGL 149
Cdd:cd03254 99 LGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGEnggnLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLI 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1732728249 150 RAEIYNMVFNeestvRAIIMVSHNLEEVVElSDKVIIL-GGR 190
Cdd:cd03254 179 QEALEKLMKG-----RTSIIIAHRLSTIKN-ADKILVLdDGK 214
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-187 |
6.21e-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: 96.29 E-value: 6.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRrPDSGKVLLMGEEVKGPTPK--------LAMIFQD-FA-LYPWLTALEN 71
Cdd:COG4172 306 SLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRalrplrrrMQVVFQDpFGsLSPRMTVGQI 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 72 VELAL-LHRKDLSKEVRREIARKYLELVGL-GGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITaegl 149
Cdd:COG4172 385 IAEGLrVHGPGLSAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSV---- 460
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1732728249 150 RAEI----------YNMvfneestvrAIIMVSHNLEEVVELSDKVIIL 187
Cdd:COG4172 461 QAQIldllrdlqreHGL---------AYLFISHDLAVVRALAHRVMVM 499
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
2-187 |
7.05e-23 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 91.46 E-value: 7.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRP--DSGKVLLMGEEVKGPTPKLAMIF--QDFALYPWLTALENVELAll 77
Cdd:cd03213 29 SGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDKRSFRKIIGYvpQDDILHPTLTVRETLMFA-- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 78 hrkdlskevrreiarkyLELvglggfedyypRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAeglrAEIYNMV 157
Cdd:cd03213 107 -----------------AKL-----------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA----LQVMSLL 154
|
170 180 190
....*....|....*....|....*....|.
gi 1732728249 158 FNEESTVRAIIMVSHNL-EEVVELSDKVIIL 187
Cdd:cd03213 155 RRLADTGRTIICSIHQPsSEIFELFDKLLLL 185
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-197 |
8.22e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 93.54 E-value: 8.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 3 FKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPT-----PKLAMIFQ-------------DFALyp 64
Cdd:PRK13635 28 FSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETvwdvrRQVGMVFQnpdnqfvgatvqdDVAF-- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 65 wltALENVELAllhRKDLSKEVRREiarkyLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAI 144
Cdd:PRK13635 106 ---GLENIGVP---REEMVERVDQA-----LRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPR 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1732728249 145 TaeglRAEIYNMV--FNEESTVrAIIMVSHNLEEVVElSDKVIIL-GGRpasIIAE 197
Cdd:PRK13635 175 G----RREVLETVrqLKEQKGI-TVLSITHDLDEAAQ-ADRVIVMnKGE---ILEE 221
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
5-190 |
1.30e-22 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 92.44 E-value: 1.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 5 VHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEevkgPTPKLA------------MIFQDF--ALYPWLTALE 70
Cdd:PRK10419 35 LKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGE----PLAKLNraqrkafrrdiqMVFQDSisAVNPRKTVRE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 71 NVELALLHRKDLSKEVRREIARKYLELVGLG-GFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAItaegL 149
Cdd:PRK10419 111 IIREPLRHLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLV----L 186
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1732728249 150 RAEIYNMVFN-EESTVRAIIMVSHNLEEVVELSDKVIIL-GGR 190
Cdd:PRK10419 187 QAGVIRLLKKlQQQFGTACLFITHDLRLVERFCQRVMVMdNGQ 229
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
2-190 |
1.77e-22 |
|
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: 91.63 E-value: 1.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMG----EEVKGPTPKLAMIF-QDFALYPWLTALENveLAL 76
Cdd:cd03267 41 SFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGlvpwKRRKKFLRRIGVVFgQKTQLWWDLPVIDS--FYL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 77 LHR-KDLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEIYN 155
Cdd:cd03267 119 LAAiYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKE 198
|
170 180 190
....*....|....*....|....*....|....*.
gi 1732728249 156 MVFNEESTVraiIMVSHNLEEVVELSDKVIILG-GR 190
Cdd:cd03267 199 YNRERGTTV---LLTSHYMKDIEALARRVLVIDkGR 231
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-198 |
2.22e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 91.69 E-value: 2.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEV-KGPTPK----LAMIFQDFAL--YPWLTALENVE 73
Cdd:COG1101 25 LNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtKLPEYKrakyIGRVFQDPMMgtAPSMTIEENLA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 74 LALL--HRKDLSKEV---RREIARKYLELVGLgGFEDyypR------ELSGGMKQRVAIARALAAQPVVLLMDEPFANLD 142
Cdd:COG1101 105 LAYRrgKRRGLRRGLtkkRRELFRELLATLGL-GLEN---RldtkvgLLSGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1732728249 143 AITAEglraeiynMVFneESTVRAI-------IMVSHNLEEVVELSDKVIIL-GGRpasIIAEV 198
Cdd:COG1101 181 PKTAA--------LVL--ELTEKIVeennlttLMVTHNMEQALDYGNRLIMMhEGR---IILDV 231
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-196 |
3.30e-22 |
|
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: 90.34 E-value: 3.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTP-----KLAMIFQDfalyPWL---TALENVE 73
Cdd:cd03245 24 SLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPadlrrNIGYVPQD----VTLfygTLRDNIT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 74 LALLHRKDlskevrREIARKyLELVGLGGFEDYYP-----------RELSGGMKQRVAIARALAAQPVVLLMDEPFANLD 142
Cdd:cd03245 100 LGAPLADD------ERILRA-AELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARALLNDPPILLLDEPTSAMD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1732728249 143 AITAEGLRAEIYNMVFNeestvRAIIMVSHNLeEVVELSDKVIIL-GGRpasIIA 196
Cdd:cd03245 173 MNSEERLKERLRQLLGD-----KTLIIITHRP-SLLDLVDRIIVMdSGR---IVA 218
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
11-187 |
4.03e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 91.34 E-value: 4.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 11 VSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPT-----PKLAMIFQD-----FALypwlTALENVELALLHRK 80
Cdd:PRK13647 34 TALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENekwvrSKVGLVFQDpddqvFSS----TVWDDVAFGPVNMG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 81 DLSKEVRREiARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRaEIYNMVFNE 160
Cdd:PRK13647 110 LDKDEVERR-VEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLM-EILDRLHNQ 187
|
170 180
....*....|....*....|....*..
gi 1732728249 161 ESTVraiIMVSHNLEEVVELSDKVIIL 187
Cdd:PRK13647 188 GKTV---IVATHDVDLAAEWADQVIVL 211
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
3-192 |
4.64e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 92.33 E-value: 4.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 3 FKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTP--------KLAMIFQD-FA-LYPWLTALENV 72
Cdd:PRK11308 36 FTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPeaqkllrqKIQIVFQNpYGsLNPRKKVGQIL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 73 ELALLHRKDLSKEVRREIARKYLELVGLGG-FEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAitaeGLRA 151
Cdd:PRK11308 116 EEPLLINTSLSAAERREKALAMMAKVGLRPeHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDV----SVQA 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1732728249 152 EIYN--MVFNEESTVrAIIMVSHNLEEVVELSDKVIILG-GRPA 192
Cdd:PRK11308 192 QVLNlmMDLQQELGL-SYVFISHDLSVVEHIADEVMVMYlGRCV 234
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-219 |
1.50e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 90.18 E-value: 1.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLL---------MGEEVKGPTPKLAMIFQdfalYPWLTALEN 71
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvsstsKQKEIKPVRKKVGVVFQ----FPESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 72 VELALL----HRKDLSKEVRREIARKYLELVGLGG-FEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITa 146
Cdd:PRK13643 101 TVLKDVafgpQNFGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 147 eglRAEIYNMVFNEESTVRAIIMVSHNLEEVVELSDKV-------IILGGRPASIIAEVEI----KLPRPRNTrdiEFQD 215
Cdd:PRK13643 180 ---RIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVyllekghIISCGTPSDVFQEVDFlkahELGVPKAT---HFAD 253
|
....
gi 1732728249 216 YLDR 219
Cdd:PRK13643 254 QLQK 257
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
13-187 |
2.53e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 89.91 E-value: 2.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 13 IVAPTGTGKTTLLRIIAGLRRPDSGKV----------LLMGEEVKGPTPK-----------LAMIFQdFALYPWLTalEN 71
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdkKNNHELITNPYSKkiknfkelrrrVSMVFQ-FPEYQLFK--DT 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 72 VElallhrKDL---------SKEVRREIARKYLELVGLG-GFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANL 141
Cdd:PRK13631 134 IE------KDImfgpvalgvKKSEAKKLAKFYLNKMGLDdSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGL 207
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1732728249 142 DaitAEGLRaEIYNMVFNEESTVRAIIMVSHNLEEVVELSDKVIIL 187
Cdd:PRK13631 208 D---PKGEH-EMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVM 249
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-187 |
3.45e-21 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 88.92 E-value: 3.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGL----RRPDSGKVLL---------MGEEVKGPTPKLAMIFQDFALYPWLT 67
Cdd:PRK09984 23 VDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdKSAGSHIELLgrtvqregrLARDIRKSRANTGYIFQQFNLVNRLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 68 ALENVELALLHRKDLSK-------EVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFAN 140
Cdd:PRK09984 103 VLENVLIGALGSTPFWRtcfswftREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIAS 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1732728249 141 LDAITAEGLRAEIYNMVFNEESTVraiIMVSHNLEEVVELSDKVIIL 187
Cdd:PRK09984 183 LDPESARIVMDTLRDINQNDGITV---VVTLHQVDYALRYCERIVAL 226
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-190 |
3.52e-21 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 89.78 E-value: 3.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPD---SGKVLLMGEEVKG-PTPKL--------AMIFQD--FALYPWL 66
Cdd:PRK09473 35 LNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNlPEKELnklraeqiSMIFQDpmTSLNPYM 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 67 TALENV-ELALLHrKDLSKE------------VRREIARKYLELvglggfedyYPRELSGGMKQRVAIARALAAQPVVLL 133
Cdd:PRK09473 115 RVGEQLmEVLMLH-KGMSKAeafeesvrmldaVKMPEARKRMKM---------YPHEFSGGMRQRVMIAMALLCRPKLLI 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1732728249 134 MDEPFANLDaITAEGLRAEIYNMVFNEESTvrAIIMVSHNLEEVVELSDKVIIL-GGR 190
Cdd:PRK09473 185 ADEPTTALD-VTVQAQIMTLLNELKREFNT--AIIMITHDLGVVAGICDKVLVMyAGR 239
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
2-187 |
4.47e-21 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 87.49 E-value: 4.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEE-----VKGPTPKLAMIFQDFALY--------PWLTA 68
Cdd:COG4778 31 SFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdlAQASPREILALRRRTIGYvsqflrviPRVSA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 69 LENVELALLHRkDLSKEVRREIARKYLELVGLggfedyyPREL--------SGGMKQRVAIARALAAQPVVLLMDEPFAN 140
Cdd:COG4778 111 LDVVAEPLLER-GVDREEARARARELLARLNL-------PERLwdlppatfSGGEQQRVNIARGFIADPPLLLLDEPTAS 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1732728249 141 LDAITAEGLRAEIynmvfnEESTVR--AIIMVSHNLEEVVELSDKVIIL 187
Cdd:COG4778 183 LDAANRAVVVELI------EEAKARgtAIIGIFHDEEVREAVADRVVDV 225
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
2-199 |
5.28e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 88.61 E-value: 5.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMG------EEVKGPTPKLAMIFQ-------------DFAL 62
Cdd:PRK13633 30 NLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsdeENLWDIRNKAGMVFQnpdnqivativeeDVAF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 63 YPwltalENVELAllhrkdlSKEVRREIARKyLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLD 142
Cdd:PRK13633 110 GP-----ENLGIP-------PEEIRERVDES-LKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1732728249 143 AITaeglRAEIYNMV--FNEESTVrAIIMVSHNLEEVVElSDKVI-------ILGGRPASIIAEVE 199
Cdd:PRK13633 177 PSG----RREVVNTIkeLNKKYGI-TIILITHYMEEAVE-ADRIIvmdsgkvVMEGTPKEIFKEVE 236
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-187 |
6.66e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 87.66 E-value: 6.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRR--PD---SGKVLLMGEEV-KGPTPKL----AMIFQDFALYPWLTALE 70
Cdd:PRK14247 22 VNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIfKMDVIELrrrvQMVFQIPNPIPNLSIFE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 71 NVELAL-LHRKDLSKEVRREIARKYLELVGLggFEDYYPR------ELSGGMKQRVAIARALAAQPVVLLMDEPFANLDA 143
Cdd:PRK14247 102 NVALGLkLNRLVKSKKELQERVRWALEKAQL--WDEVKDRldapagKLSGGQQQRLCIARALAFQPEVLLADEPTANLDP 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1732728249 144 ITAEGLRAeiynmVFNEESTVRAIIMVSHNLEEVVELSDKVIIL 187
Cdd:PRK14247 180 ENTAKIES-----LFLELKKDMTIVLVTHFPQQAARISDYVAFL 218
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-187 |
9.43e-21 |
|
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: 86.90 E-value: 9.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPT-----PKLAMIFQDFALYPwLTALENVELAl 76
Cdd:cd03253 21 SFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTldslrRAIGVVPQDTVLFN-DTIGYNIRYG- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 77 lhRKDLSKEVRREIAR-------------KYLELVGLGGFEdyypreLSGGMKQRVAIARALAAQPVVLLMDEPFANLDA 143
Cdd:cd03253 99 --RPDATDEEVIEAAKaaqihdkimrfpdGYDTIVGERGLK------LSGGEKQRVAIARAILKNPPILLLDEATSALDT 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1732728249 144 ITaeglRAEIYNmVFNEESTVRAIIMVSHNLEEVVElSDKVIIL 187
Cdd:cd03253 171 HT----EREIQA-ALRDVSKGRTTIVIAHRLSTIVN-ADKIIVL 208
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-210 |
1.03e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 88.32 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTP----KLAMIFQDFALYPWLTALENveLAL 76
Cdd:PRK13537 26 LSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARharqRVGVVPQFDNLDPDFTVREN--LLV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 77 LHRK-DLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITaeglRAEIYN 155
Cdd:PRK13537 104 FGRYfGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQA----RHLMWE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1732728249 156 MVFNEESTVRAIIMVSHNLEEVVELSDKV-IILGGR------PASIIAE------VEIKLPRPRNTRD 210
Cdd:PRK13537 180 RLRSLLARGKTILLTTHFMEEAERLCDRLcVIEEGRkiaegaPHALIESeigcdvIEIYGPDPVALRD 247
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-187 |
1.08e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 89.97 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 3 FKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPK------LAMIFQDFALYPWLTALENVEL-- 74
Cdd:PRK11288 25 FDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaalaagVAIIYQELHLVPEMTVAENLYLgq 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 75 -----ALLHRKDLSKEVRREIARkylelvgLGgfEDYYP----RELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAIT 145
Cdd:PRK11288 105 lphkgGIVNRRLLNYEAREQLEH-------LG--VDIDPdtplKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSARE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1732728249 146 AE-------GLRAEiynmvfneestVRAIIMVSHNLEEVVELSDKVIIL 187
Cdd:PRK11288 176 IEqlfrvirELRAE-----------GRVILYVSHRMEEIFALCDAITVF 213
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-187 |
1.68e-20 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 89.36 E-value: 1.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKT----TLLRIIAGLRRPDSGKVLLMGEEVKGPTPK---------LAMIFQDfalyPwLTA 68
Cdd:COG4172 30 SFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERelrrirgnrIAMIFQE----P-MTS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 69 LeN---------VELALLHRKdLSKEVRREIARKYLELVGLGGFE---DYYPRELSGGMKQRVAIARALAAQPVVLLMDE 136
Cdd:COG4172 105 L-NplhtigkqiAEVLRLHRG-LSGAAARARALELLERVGIPDPErrlDAYPHQLSGGQRQRVMIAMALANEPDLLIADE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1732728249 137 PFANLDA-ITAE------GLRAEiYNMvfneestvrAIIMVSHNLEEVVELSDKVIIL 187
Cdd:COG4172 183 PTTALDVtVQAQildllkDLQRE-LGM---------ALLLITHDLGVVRRFADRVAVM 230
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
2-149 |
2.06e-20 |
|
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: 85.79 E-value: 2.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPD---SGKVLLMGEEVKGPTPK--LAMIFQDFALYPWLTALENVELAL 76
Cdd:cd03234 27 SLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKPDQFQkcVAYVRQDDILLPGLTVRETLTYTA 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1732728249 77 ---LHRKDLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGL 149
Cdd:cd03234 107 ilrLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNL 182
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
2-191 |
2.30e-20 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 86.20 E-value: 2.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKG-PTPKLAMI-----FQDFALYPWLTALENVELA 75
Cdd:PRK11300 25 NLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGlPGHQIARMgvvrtFQHVRLFREMTVIENLLVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 76 --------LLHRKDLSKEVRR------EIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANL 141
Cdd:PRK11300 105 qhqqlktgLFSGLLKTPAFRRaesealDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1732728249 142 DAITAEGLRAEIynMVFNEESTVrAIIMVSHNLEEVVELSDKVIILG-GRP 191
Cdd:PRK11300 185 NPKETKELDELI--AELRNEHNV-TVLLIEHDMKLVMGISDRIYVVNqGTP 232
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
2-187 |
3.01e-20 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 87.45 E-value: 3.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPK--------LAMIFQD--FALYPWLTALEN 71
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDewravrsdIQMIFQDplASLNPRMTIGEI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 72 V-ELALLHRKDLSKEVRREIARKYLELVGL-GGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAitaeGL 149
Cdd:PRK15079 121 IaEPLRTYHPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV----SI 196
|
170 180 190
....*....|....*....|....*....|....*....
gi 1732728249 150 RAEIYNMVFNEESTVR-AIIMVSHNLEEVVELSDKVIIL 187
Cdd:PRK15079 197 QAQVVNLLQQLQREMGlSLIFIAHDLAVVKHISDRVLVM 235
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-187 |
3.87e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 88.22 E-value: 3.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTT----LLRIIAGlrrpdSGKVLLMGEEVKGPTPK--------LAMIFQD--FALYPWL 66
Cdd:PRK15134 305 ISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQPLHNLNRRqllpvrhrIQVVFQDpnSSLNPRL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 67 TALENVELAL-LHRKDLSKEVRREIARKYLELVGLGGFEDY-YPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDai 144
Cdd:PRK15134 380 NVLQIIEEGLrVHQPTLSAAQREQQVIAVMEEVGLDPETRHrYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD-- 457
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1732728249 145 taEGLRAEIYNMVFNEESTVR-AIIMVSHNLEEVVELSDKVIIL 187
Cdd:PRK15134 458 --KTVQAQILALLKSLQQKHQlAYLFISHDLHVVRALCHQVIVL 499
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
9-174 |
4.91e-20 |
|
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: 87.80 E-value: 4.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 9 EFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKG-PTPKLAMIFQDFALYPWL---TALENVELAllhRKDLSK 84
Cdd:TIGR02868 362 ERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSlDQDEVRRRVSVCAQDAHLfdtTVRENLRLA---RPDATD 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 85 EvrrEIARKyLELVGLGGFEDYYP-----------RELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEI 153
Cdd:TIGR02868 439 E---ELWAA-LERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL 514
|
170 180
....*....|....*....|.
gi 1732728249 154 ynmvfNEESTVRAIIMVSHNL 174
Cdd:TIGR02868 515 -----LAALSGRTVVLITHHL 530
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1-142 |
5.78e-20 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 84.52 E-value: 5.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGP--TPKLAMIFQDFALYPWLTALENVE-LALL 77
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGdrSRFMAYLGHLPGLKADLSTLENLHfLCGL 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1732728249 78 HRKDlskevRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLD 142
Cdd:PRK13543 110 HGRR-----AKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-223 |
6.51e-20 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 87.55 E-value: 6.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLR--RPDSGKVL----------------------------LMGEEV----- 46
Cdd:TIGR03269 20 SFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIyhvalcekcgyverpskvgepcpvcggtLEPEEVdfwnl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 47 -----KGPTPKLAMIFQ-DFALYPWLTALENVeLALLHRKDLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVA 120
Cdd:TIGR03269 100 sdklrRRIRKRIAIMLQrTFALYGDDTVLDNV-LEALEEIGYEGKEAVGRAVDLIEMVQLSHRITHIARDLSGGEKQRVV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 121 IARALAAQPVVLLMDEPFANLDAITAEGLRAEIYNMVFNEESTvraIIMVSHNLEEVVELSDKVIILG-------GRPAS 193
Cdd:TIGR03269 179 LARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGIS---MVLTSHWPEVIEDLSDKAIWLEngeikeeGTPDE 255
|
250 260 270
....*....|....*....|....*....|
gi 1732728249 194 IIAEVEIKLPRPRNTRDIEFQDYLDRLYSL 223
Cdd:TIGR03269 256 VVAVFMEGVSEVEKECEVEVGEPIIKVRNV 285
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1-209 |
7.36e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 85.57 E-value: 7.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMG---------EEVKGPTPKLAMIFQdfalYPWLTALEN 71
Cdd:PRK13649 26 VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtlitstsknKDIKQIRKKVGLVFQ----FPESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 72 VELallhrKD---------LSKEVRREIARKYLELVGLGgfEDYY---PRELSGGMKQRVAIARALAAQPVVLLMDEPFA 139
Cdd:PRK13649 102 TVL-----KDvafgpqnfgVSQEEAEALAREKLALVGIS--ESLFeknPFELSGGQMRRVAIAGILAMEPKILVLDEPTA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 140 NLDAITaeglRAEIYNMVFNEESTVRAIIMVSHNLEEVVELSDKV-------IILGGRPASIIAEV----EIKLPRPRNT 208
Cdd:PRK13649 175 GLDPKG----RKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVyvlekgkLVLSGKPKDIFQDVdfleEKQLGVPKIT 250
|
.
gi 1732728249 209 R 209
Cdd:PRK13649 251 K 251
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-213 |
9.69e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 84.70 E-value: 9.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDS-----GKVLLMGEEVKGPTPKL-------AMIFQDFALYP---- 64
Cdd:PRK14258 26 VSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERRVNLnrlrrqvSMVHPKPNLFPmsvy 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 65 -----------WLTALE--NVELALLHRKDLSKEVRREIARKYLELvglggfedyyprelSGGMKQRVAIARALAAQPVV 131
Cdd:PRK14258 106 dnvaygvkivgWRPKLEidDIVESALKDADLWDEIKHKIHKSALDL--------------SGGQQQRLCIARALAVKPKV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 132 LLMDEPFANLDAITAEGLRAEIYNMVFNEESTvraIIMVSHNLEEVVELSDKVIILGGRPASIIAEVEIKL-------PR 204
Cdd:PRK14258 172 LLMDEPCFGLDPIASMKVESLIQSLRLRSELT---MVIVSHNLHQVSRLSDFTAFFKGNENRIGQLVEFGLtkkifnsPH 248
|
....*....
gi 1732728249 205 PRNTRDIEF 213
Cdd:PRK14258 249 DSRTREYVL 257
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-201 |
1.20e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 86.62 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSI--VAptGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPK------LAMIFQD---FALYPWLTALE 70
Cdd:COG3845 278 SLEVRAGEILGIagVA--GNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRerrrlgVAYIPEDrlgRGLVPDMSVAE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 71 NVELALLHRKDLSKEV---RREIARKYLELVglggfEDY---YP------RELSGGMKQRVAIARALAAQPVVLLMDEPF 138
Cdd:COG3845 356 NLILGRYRRPPFSRGGfldRKAIRAFAEELI-----EEFdvrTPgpdtpaRSLSGGNQQKVILARELSRDPKLLIAAQPT 430
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1732728249 139 ANLDAITAEGLRAEIYNMvfneestvR----AIIMVSHNLEEVVELSDKVIIL-GGRpasIIAEVEIK 201
Cdd:COG3845 431 RGLDVGAIEFIHQRLLEL--------RdagaAVLLISEDLDEILALSDRIAVMyEGR---IVGEVPAA 487
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-187 |
2.04e-19 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 84.07 E-value: 2.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEV-----KGPTPKLAMIFQD--FALYPWLTALENVE 73
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfgdySYRSQRIRMIFQDpsTSLNPRQRISQILD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 74 LALLHRKDLSKEVRREIARKYLELVGL-GGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAitaeGLRAE 152
Cdd:PRK15112 112 FPLRLNTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDM----SMRSQ 187
|
170 180 190
....*....|....*....|....*....|....*.
gi 1732728249 153 IYNMVFN-EESTVRAIIMVSHNLEEVVELSDKVIIL 187
Cdd:PRK15112 188 LINLMLElQEKQGISYIYVTQHLGMMKHISDQVLVM 223
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-187 |
2.65e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 83.56 E-value: 2.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGL------RRPDSGKVLLMGEEV-----KGPTPKLAMIFQDFALYPWLTAL 69
Cdd:PRK14246 29 ITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydsKIKVDGKVLYFGKDIfqidaIKLRKEVGMVFQQPNPFPHLSIY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 70 ENVELALLHRKDLSKEVRREIARKYLELVGLggFEDYYPR------ELSGGMKQRVAIARALAAQPVVLLMDEPFANLDA 143
Cdd:PRK14246 109 DNIAYPLKSHGIKEKREIKKIVEECLRKVGL--WKEVYDRlnspasQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDI 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1732728249 144 ITAEGLRAEIynmvfNEESTVRAIIMVSHNLEEVVELSDKVIIL 187
Cdd:PRK14246 187 VNSQAIEKLI-----TELKNEIAIVIVSHNPQQVARVADYVAFL 225
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-187 |
3.63e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 82.97 E-value: 3.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPD-----SGKVLLMGEEVKGPT-------PKLAMIFQDFALYPWLTA 68
Cdd:PRK14267 23 VDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDvdpievrREVGMVFQYPNPFPHLTI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 69 LENVELAL------LHRKDLSKEVRREIARKYLELVGLGGFEDYyPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLD 142
Cdd:PRK14267 103 YDNVAIGVklnglvKSKKELDERVEWALKKAALWDEVKDRLNDY-PSNLSGGQRQRLVIARALAMKPKILLMDEPTANID 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1732728249 143 AITAeglrAEIYNMVFnEESTVRAIIMVSHNLEEVVELSDKVIIL 187
Cdd:PRK14267 182 PVGT----AKIEELLF-ELKKEYTIVLVTHSPAQAARVSDYVAFL 221
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-201 |
5.61e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 83.11 E-value: 5.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMG------EEVKGPTPKLAMIFQ-------------DFA 61
Cdd:PRK13644 21 INLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtgdfSKLQGIRKLVGIVFQnpetqfvgrtveeDLA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 62 LYPwltalENVELALLhrkdlskEVRREIARKYLElVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANL 141
Cdd:PRK13644 101 FGP-----ENLCLPPI-------EIRKRVDRALAE-IGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSML 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1732728249 142 DAITAEGLRAEIYNMvfneESTVRAIIMVSHNLEEvVELSDKVII-------LGGRPASIIAEVEIK 201
Cdd:PRK13644 168 DPDSGIAVLERIKKL----HEKGKTIVYITHNLEE-LHDADRIIVmdrgkivLEGEPENVLSDVSLQ 229
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1-189 |
1.49e-18 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 81.05 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTP-----KLAMIFQDFALYPwLTALENVELA 75
Cdd:cd03249 22 LSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLrwlrsQIGLVSQEPVLFD-GTIAENIRYG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 76 llhRKDLSKEVRREIARK-------------YLELVGLGGFEdyypreLSGGMKQRVAIARALAAQPVVLLMDEPFANLD 142
Cdd:cd03249 101 ---KPDATDEEVEEAAKKanihdfimslpdgYDTLVGERGSQ------LSGGQKQRIAIARALLRNPKILLLDEATSALD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1732728249 143 AITaEGLRAEiynmVFNEESTVRAIIMVSHNLeEVVELSDKVIILGG 189
Cdd:cd03249 172 AES-EKLVQE----ALDRAMKGRTTIVIAHRL-STIRNADLIAVLQN 212
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
1-187 |
1.92e-18 |
|
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: 80.65 E-value: 1.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKG-PTPKLA-----------MIFqdfalyPWLTA 68
Cdd:TIGR03410 19 VSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKlPPHERAragiayvpqgrEIF------PRLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 69 LENVELALLHRKDLSKEVRREI-----------ARKylelvglGGfedyyprELSGGMKQRVAIARALAAQPVVLLMDEP 137
Cdd:TIGR03410 93 EENLLTGLAALPRRSRKIPDEIyelfpvlkemlGRR-------GG-------DLSGGQQQQLAIARALVTRPKLLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1732728249 138 fanldaitAEGLRAEIYNMVfneESTVR--------AIIMVSHNLEEVVELSDKVIIL 187
Cdd:TIGR03410 159 --------TEGIQPSIIKDI---GRVIRrlraeggmAILLVEQYLDFARELADRYYVM 205
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-199 |
3.69e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 82.55 E-value: 3.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGL--------RRPDSGKVLLMGEEVKGPTPKLAmifqDFALYPwltalenve 73
Cdd:COG4178 383 SLSLKPGERLLITGPSGSGKSTLLRAIAGLwpygsgriARPAGARVLFLPQRPYLPLGTLR----EALLYP--------- 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 74 lallhrkDLSKEVRREIARKYLELVGLGGF------EDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDaitaE 147
Cdd:COG4178 450 -------ATAEAFSDAELREALEAVGLGHLaerldeEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALD----E 518
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1732728249 148 GLRAEIYNMVFNEESTVrAIIMVSHNlEEVVELSDKVIILGGRPASIIAEVE 199
Cdd:COG4178 519 ENEAALYQLLREELPGT-TVISVGHR-STLAAFHDRVLELTGDGSWQLLPAE 568
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-187 |
4.68e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 82.14 E-value: 4.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPKLA------MIFQDFALYPWLTALENVEL 74
Cdd:PRK09700 24 VNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAaqlgigIIYQELSVIDELTVLENLYI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 75 A-LLHRKDLSKEV-----RREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEG 148
Cdd:PRK09700 104 GrHLTKKVCGVNIidwreMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDY 183
|
170 180 190
....*....|....*....|....*....|....*....
gi 1732728249 149 LRAeIYNMVFNEEstvRAIIMVSHNLEEVVELSDKVIIL 187
Cdd:PRK09700 184 LFL-IMNQLRKEG---TAIVYISHKLAEIRRICDRYTVM 218
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-187 |
7.42e-18 |
|
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: 78.67 E-value: 7.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGeevkgptpKLAMIFQdfalYPWL---TALENVELALLH 78
Cdd:cd03250 25 NLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--------SIAYVSQ----EPWIqngTIRENILFGKPF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 79 RKDLSKEVRREIA-RKYLEL--------VGLGGFEdyypreLSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAegl 149
Cdd:cd03250 93 DEERYEKVIKACAlEPDLEIlpdgdlteIGEKGIN------LSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVG--- 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 1732728249 150 rAEIYNMVFNEE-STVRAIIMVSHNLeEVVELSDKVIIL 187
Cdd:cd03250 164 -RHIFENCILGLlLNNKTRILVTHQL-QLLPHADQIVVL 200
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-187 |
8.03e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 81.64 E-value: 8.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPKLAM---------------IFQDFALYpW 65
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLarglvylpedrqssgLYLDAPLA-W 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 66 ltaleNVELALLHRKDLSKEVRREIAR--KYLELVGLG-GFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLD 142
Cdd:PRK15439 361 -----NVCALTHNRRGFWIKPARENAVleRYRRALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1732728249 143 AitaeGLRAEIYNMVFNEESTVRAIIMVSHNLEEVVELSDKVIIL 187
Cdd:PRK15439 436 V----SARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVM 476
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-200 |
8.18e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 79.67 E-value: 8.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVK-------GPTPKLAMIFQDFALYPWLTALENvE 73
Cdd:PRK13638 20 LNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDyskrgllALRQQVATVFQDPEQQIFYTDIDS-D 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 74 LALLHRKDLSKEvrREIARKY---LELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITaeglR 150
Cdd:PRK13638 99 IAFSLRNLGVPE--AEITRRVdeaLTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAG----R 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1732728249 151 AEIYNMVFNEESTVRAIIMVSHNLEEVVELSDKVIIL-------GGRPASIIAEVEI 200
Cdd:PRK13638 173 TQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLrqgqiltHGAPGEVFACTEA 229
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-187 |
8.31e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 78.99 E-value: 8.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTP-----KLAMIFQ----------DFALYPW 65
Cdd:PRK10247 26 ISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPeiyrqQVSYCAQtptlfgdtvyDNLIFPW 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 66 LTALENVELALLhRKDLSK-EVRREIARKYLElvglggfedyyprELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAI 144
Cdd:PRK10247 106 QIRNQQPDPAIF-LDDLERfALPDTILTKNIA-------------ELSGGEKQRISLIRNLQFMPKVLLLDEITSALDES 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1732728249 145 TAEGLRAEIYNMVfnEESTVrAIIMVSHNLEEVVElSDKVIIL 187
Cdd:PRK10247 172 NKHNVNEIIHRYV--REQNI-AVLWVTHDKDEINH-ADKVITL 210
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-187 |
9.71e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 79.46 E-value: 9.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPK-----LAMIFQ-------------DFAL 62
Cdd:PRK13652 23 INFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIRevrkfVGLVFQnpddqifsptveqDIAF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 63 YPWLTALEnvELALLHRKDlskevrreiarKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLD 142
Cdd:PRK13652 103 GPINLGLD--EETVAHRVS-----------SALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1732728249 143 AITAEGLRAEIYNMVFNEESTVraiIMVSHNLEEVVELSDKVIIL 187
Cdd:PRK13652 170 PQGVKELIDFLNDLPETYGMTV---IFSTHQLDLVPEMADYIYVM 211
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-222 |
1.01e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 79.84 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDS---GKVLLMGEEVKGPT-----PKLAMIFQD----FAlypWLTA 68
Cdd:PRK13640 26 ISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTvwdirEKVGIVFQNpdnqFV---GATV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 69 LENVELALLHRKdLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEG 148
Cdd:PRK13640 103 GDDVAFGLENRA-VPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 149 LRAEIYNMVFNEESTvraIIMVSHNLEEvVELSDKVIILG-------GRPASI-----------------------IAEV 198
Cdd:PRK13640 182 ILKLIRKLKKKNNLT---VISITHDIDE-ANMADQVLVLDdgkllaqGSPVEIfskvemlkeigldipfvyklknkLKEK 257
|
250 260
....*....|....*....|....
gi 1732728249 199 EIKLPRPRNTRDiEFQDYLDRLYS 222
Cdd:PRK13640 258 GISVPQEINTEE-KLVQYLCQLNS 280
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-200 |
1.36e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 79.28 E-value: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMG----------EEVKGPTPKLAMIFQdFALYPWL--TAL 69
Cdd:PRK13645 31 SLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlkkiKEVKRLRKEIGLVFQ-FPEYQLFqeTIE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 70 ENVELALLHRKDLSKEVRREIArKYLELVGLGgfEDYYPR---ELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITA 146
Cdd:PRK13645 110 KDIAFGPVNLGENKQEAYKKVP-ELLKLVQLP--EDYVKRspfELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGE 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1732728249 147 EglraEIYNMV--FNEESTVRaIIMVSHNLEEVVELSDKVIILG-------GRPASIIAEVEI 200
Cdd:PRK13645 187 E----DFINLFerLNKEYKKR-IIMVTHNMDQVLRIADEVIVMHegkvisiGSPFEIFSNQEL 244
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
1-187 |
1.36e-17 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 78.56 E-value: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPD----SGKVLLMGEEVKGPT---PKLAMIFQD--FALYPWLTALEN 71
Cdd:TIGR02770 5 LNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGltqtSGEILLDGRPLLPLSirgRHIATIMQNprTAFNPLFTMGNH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 72 VELALLHRKDLSKEVRREIARKyLELVGLGGFE---DYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEG 148
Cdd:TIGR02770 85 AIETLRSLGKLSKQARALILEA-LEAVGLPDPEevlKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQAR 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 1732728249 149 LRAEIYNMVfneESTVRAIIMVSHNLEEVVELSDKVIIL 187
Cdd:TIGR02770 164 VLKLLRELR---QLFGTGILLITHDLGVVARIADEVAVM 199
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
12-142 |
1.39e-17 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 78.59 E-value: 1.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 12 SIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGpTP------KLAMIFQDFALYPWLTALENVELALL--HRKDLS 83
Cdd:COG4604 31 ALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVAT-TPsrelakRLAILRQENHINSRLTVRELVAFGRFpySKGRLT 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1732728249 84 KEVRREIARkYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLD 142
Cdd:COG4604 110 AEDREIIDE-AIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLD 167
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
3-205 |
1.84e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 78.64 E-value: 1.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 3 FKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPK-----LAMIFQD--------FALYPWLTAL 69
Cdd:PRK13648 30 FNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEklrkhIGIVFQNpdnqfvgsIVKYDVAFGL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 70 ENvelallhrKDLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDaitAEGl 149
Cdd:PRK13648 110 EN--------HAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLD---PDA- 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1732728249 150 RAEIYNMV--FNEESTVrAIIMVSHNLEEVVElSDKVIILG-------GRPASI------IAEVEIKLPRP 205
Cdd:PRK13648 178 RQNLLDLVrkVKSEHNI-TIISITHDLSEAME-ADHVIVMNkgtvykeGTPTEIfdhaeeLTRIGLDLPFP 246
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-197 |
1.84e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 79.49 E-value: 1.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPT----PKLAMIFQDFALYPWLTALENVeLAL 76
Cdd:PRK13536 60 LSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARArlarARIGVVPQFDNLDLEFTVRENL-LVF 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 77 LHRKDLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDA----ITAEGLRAE 152
Cdd:PRK13536 139 GRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPharhLIWERLRSL 218
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1732728249 153 IynmvfneeSTVRAIIMVSHNLEEVVELSDKVIIL-------GGRPASIIAE 197
Cdd:PRK13536 219 L--------ARGKTILLTTHFMEEAERLCDRLCVLeagrkiaEGRPHALIDE 262
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-183 |
2.15e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 78.28 E-value: 2.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFkvHSHEFVSIVAPTGTGKTTLLRII--AGLRRPD---SGKVLLMGEEVKGPT-------PKLAMIFQDFALYPwLTA 68
Cdd:PRK14239 26 LDF--YPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIYSPRtdtvdlrKEIGMVFQQPNPFP-MSI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 69 LENVELALLHRKDLSKEVRREIARKylELVGLGGFEDYYPR------ELSGGMKQRVAIARALAAQPVVLLMDEPFANLD 142
Cdd:PRK14239 103 YENVVYGLRLKGIKDKQVLDEAVEK--SLKGASIWDEVKDRlhdsalGLSGGQQQRVCIARVLATSPKIILLDEPTSALD 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1732728249 143 AITAEGLRAEIYNMvfNEESTvraIIMVSHNLEEVVELSDK 183
Cdd:PRK14239 181 PISAGKIEETLLGL--KDDYT---MLLVTRSMQQASRISDR 216
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-187 |
3.75e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 78.21 E-value: 3.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 12 SIVAPTGTGKTTLLRI-------IAGLRRpdSGKVLLMGE------EVKGPTPKLAMIFQDFALYPwLTALENVELALLH 78
Cdd:PRK14271 51 SLMGPTGSGKTTFLRTlnrmndkVSGYRY--SGDVLLGGRsifnyrDVLEFRRRVGMLFQRPNPFP-MSIMDNVLAGVRA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 79 RKDLSKEVRREIARKYLELVGL-GGFEDYY---PRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEIY 154
Cdd:PRK14271 128 HKLVPRKEFRGVAQARLTEVGLwDAVKDRLsdsPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIR 207
|
170 180 190
....*....|....*....|....*....|...
gi 1732728249 155 NMvfneeSTVRAIIMVSHNLEEVVELSDKVIIL 187
Cdd:PRK14271 208 SL-----ADRLTVIIVTHNLAQAARISDRAALF 235
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-187 |
4.24e-17 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 78.63 E-value: 4.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGL----RRPDSGKVLLMGEEVKGPTPK---------LAMIFQD--FALYPW 65
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypGRVMAEKLEFNGQDLQRISEKerrnlvgaeVAMIFQDpmTSLNPC 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 66 LTALENVELALLHRKDLSKEVRREIARKYLELVGLGGFE---DYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLD 142
Cdd:PRK11022 106 YTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPAsrlDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALD 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1732728249 143 AItaegLRAEIYNMVFN-EESTVRAIIMVSHNLEEVVELSDKVIIL 187
Cdd:PRK11022 186 VT----IQAQIIELLLElQQKENMALVLITHDLALVAEAAHKIIVM 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-187 |
8.88e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.57 E-value: 8.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLmgeevkGPTPKLAMIFQDFA-LYPWLTALENVelallhrK 80
Cdd:COG0488 335 SLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL------GETVKIGYFDQHQEeLDPDKTVLDEL-------R 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 81 DLSKEVRREIARKYLELVGLGGFEDYYP-RELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLraeiynmvfn 159
Cdd:COG0488 402 DGAPGGTEQEVRGYLGRFLFSGDDAFKPvGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEAL---------- 471
|
170 180 190
....*....|....*....|....*....|....
gi 1732728249 160 EESTVR---AIIMVSHN---LEEVVelsDKVIIL 187
Cdd:COG0488 472 EEALDDfpgTVLLVSHDryfLDRVA---TRILEF 502
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-190 |
1.39e-16 |
|
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: 78.52 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVK----GPTPKLAMIFQDFALYPWLTALENVeLAL 76
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIEtnldAVRQSLGMCPQHNILFHHLTVAEHI-LFY 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 77 LHRKDLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITaeglRAEIYNM 156
Cdd:TIGR01257 1028 AQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYS----RRSIWDL 1103
|
170 180 190
....*....|....*....|....*....|....*
gi 1732728249 157 VFNEESTvRAIIMVSHNLEEVVELSDKV-IILGGR 190
Cdd:TIGR01257 1104 LLKYRSG-RTIIMSTHHMDEADLLGDRIaIISQGR 1137
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
4-210 |
1.69e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 75.97 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 4 KVHSHEFVSIVAPTGTGKTTLLR-------IIAGLRRpdSGKVLLMGEEVKGPT-------PKLAMIFQDFALYPwLTAL 69
Cdd:PRK14243 32 DIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRV--EGKVTFHGKNLYAPDvdpvevrRRIGMVFQKPNPFP-KSIY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 70 ENVELA---LLHRKDLSKEVRR---------EIARKyLELVGLGgfedyypreLSGGMKQRVAIARALAAQPVVLLMDEP 137
Cdd:PRK14243 109 DNIAYGariNGYKGDMDELVERslrqaalwdEVKDK-LKQSGLS---------LSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 138 FANLDAITAegLRAEIYNMVFNEESTvraIIMVSHNLEEVVELSDKVIIL-------GGRPASII----AEVEIKLPRPR 206
Cdd:PRK14243 179 CSALDPIST--LRIEELMHELKEQYT---IIIVTHNMQQAARVSDMTAFFnveltegGGRYGYLVefdrTEKIFNSPQQQ 253
|
....
gi 1732728249 207 NTRD 210
Cdd:PRK14243 254 ATRD 257
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
2-200 |
2.39e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 77.28 E-value: 2.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRrPD---SGKVLLMGEEVKGPTPK------LAMIFQDFALYPWLTALENV 72
Cdd:PRK13549 25 SLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIRdteragIAIIHQELALVKELSVLENI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 73 ----ELALLHRKDLSKEVRReiARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEG 148
Cdd:PRK13549 104 flgnEITPGGIMDYDAMYLR--AQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAV 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1732728249 149 LraeiYNMVFNEESTVRAIIMVSHNLEEVVELSDKVIIL------GGRPASIIAEVEI 200
Cdd:PRK13549 182 L----LDIIRDLKAHGIACIYISHKLNEVKAISDTICVIrdgrhiGTRPAAGMTEDDI 235
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
9-192 |
2.77e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 77.01 E-value: 2.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 9 EFVSIVAPTGTGKTTLLRIIAGLRRPD---SGKVLLMGEEVKGPTPKL--AMIFQDFALYPWLTALE--NVELALLHRKD 81
Cdd:TIGR00955 52 ELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRAisAYVQQDDLFIPTLTVREhlMFQAHLRMPRR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 82 LSKEVRREIARKYLELVGLG-------GFEDYYpRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEIY 154
Cdd:TIGR00955 132 VTKKEKRERVDEVLQALGLRkcantriGVPGRV-KGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLK 210
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1732728249 155 NMVFNEestvRAIIMVSHN-LEEVVELSDKVIIL-GGRPA 192
Cdd:TIGR00955 211 GLAQKG----KTIICTIHQpSSELFELFDKIILMaEGRVA 246
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1-189 |
3.05e-16 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 77.07 E-value: 3.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEV-----KGPTPKLAMIFQDFALYPWlTALENVELA 75
Cdd:TIGR00958 500 LTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLvqydhHYLHRQVALVGQEPVLFSG-SVRENIAYG 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 76 LlhrKDLSKEVRREIARKYLELVGLGGFEDYYPRE-------LSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEG 148
Cdd:TIGR00958 579 L---TDTPDEEIMAAAKAANAHDFIMEFPNGYDTEvgekgsqLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQL 655
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1732728249 149 LRAeiynmvfNEESTVRAIIMVSHNLeEVVELSDKVIILGG 189
Cdd:TIGR00958 656 LQE-------SRSRASRTVLLIAHRL-STVERADQILVLKK 688
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
9-146 |
4.86e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 76.46 E-value: 4.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 9 EFVSIVAPTGTGKTTLLRIIAGLRRPDS--GKVLLMGEEVKGPTPK-LAMIFQDFALYPWLTALENVELALLHR--KDLS 83
Cdd:PLN03211 95 EILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQILKrTGFVTQDDILYPHLTVRETLVFCSLLRlpKSLT 174
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1732728249 84 KEVRREIARKYLELVGLGGFEDY-----YPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITA 146
Cdd:PLN03211 175 KQEKILVAESVISELGLTKCENTiignsFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAA 242
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-204 |
1.06e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 74.11 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEV----KGPT---PKLAMIFQ--DFALYPwLTALEN 71
Cdd:PRK13636 25 ININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysrKGLMklrESVGMVFQdpDNQLFS-ASVYQD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 72 VELALLHRKDLSKEVRREIaRKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAeglrA 151
Cdd:PRK13636 104 VSFGAVNLKLPEDEVRKRV-DNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGV----S 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1732728249 152 EIYNMVFN-EESTVRAIIMVSHNLEEVVELSDKVI-------ILGGRPASIIAE------VEIKLPR 204
Cdd:PRK13636 179 EIMKLLVEmQKELGLTIIIATHDIDIVPLYCDNVFvmkegrvILQGNPKEVFAEkemlrkVNLRLPR 245
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
1-187 |
1.11e-15 |
|
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: 75.46 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVK-------GPTpkLAMIFQDFALYPWlTALENVE 73
Cdd:TIGR01842 337 ISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKqwdretfGKH--IGYLPQDVELFPG-TVAENIA 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 74 lallhRKDLSKEVRREIARKYL----ELVGlgGFEDYYPRE-------LSGGMKQRVAIARALAAQPVVLLMDEPFANLD 142
Cdd:TIGR01842 414 -----RFGENADPEKIIEAAKLagvhELIL--RLPDGYDTVigpggatLSGGQRQRIALARALYGDPKLVVLDEPNSNLD 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1732728249 143 aitAEGLRAeIYNMVFNEESTVRAIIMVSHNLeEVVELSDKVIIL 187
Cdd:TIGR01842 487 ---EEGEQA-LANAIKALKARGITVVVITHRP-SLLGCVDKILVL 526
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1-190 |
1.13e-15 |
|
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: 73.27 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGE-----EVKGPTPKLAMIFQDFALYPwLTALENVELA 75
Cdd:cd03248 33 VSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpisqyEHKYLHSKVSLVGQEPVLFA-RSLQDNIAYG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 76 LlhrKDLSKEVRREIARKYLELVGLGGFEDYYPRE-------LSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEG 148
Cdd:cd03248 112 L---QSCSFECVKEAAQKAHAHSFISELASGYDTEvgekgsqLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQ 188
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1732728249 149 LRAEIYnmvfnEESTVRAIIMVSHNLeEVVELSDKVIIL-GGR 190
Cdd:cd03248 189 VQQALY-----DWPERRTVLVIAHRL-STVERADQILVLdGGR 225
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-187 |
2.29e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 74.51 E-value: 2.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKT----TLLRII--AG--------LRRPDSGKVLLMGEE-------VKGPtpKLAMIFQD 59
Cdd:PRK10261 35 LSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGglvqcdkmLLRRRSRQVIELSEQsaaqmrhVRGA--DMAMIFQE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 60 --FALYPWLTALENVELALLHRKDLSKEVRREIARKYLELVGLGGFEDY---YPRELSGGMKQRVAIARALAAQPVVLLM 134
Cdd:PRK10261 113 pmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTIlsrYPHQLSGGMRQRVMIAMALSCRPAVLIA 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1732728249 135 DEPFANLDAItaegLRAEIYNM--VFNEESTVrAIIMVSHNLEEVVELSDKVIIL 187
Cdd:PRK10261 193 DEPTTALDVT----IQAQILQLikVLQKEMSM-GVIFITHDMGVVAEIADRVLVM 242
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
2-190 |
2.74e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 72.41 E-value: 2.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGlrRPD----SGKVLLMGEEVKGPTPK------LAMIFQdfalYP------- 64
Cdd:COG0396 20 NLTIKPGEVHAIMGPNGSGKSTLAKVLMG--HPKyevtSGSILLDGEDILELSPDeraragIFLAFQ----YPveipgvs 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 65 ---WL-TALENVELALLHRKDLSKEVRreiarKYLELVGLGgfEDYYPREL----SGGMKQRVAIARALAAQPVVLLMDE 136
Cdd:COG0396 94 vsnFLrTALNARRGEELSAREFLKLLK-----EKMKELGLD--EDFLDRYVnegfSGGEKKRNEILQMLLLEPKLAILDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 137 PFANLDaitAEGLR--AEIYNMVFNEEstvRAIIMVSHN---LEEVVelSDKVIIL-GGR 190
Cdd:COG0396 167 TDSGLD---IDALRivAEGVNKLRSPD---RGILIITHYqriLDYIK--PDFVHVLvDGR 218
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
9-192 |
2.79e-15 |
|
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: 72.44 E-value: 2.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 9 EFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVK-GP---TPKLAMIFQDFalypwltalenvelalLHRKDLSK 84
Cdd:cd03237 26 EVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSyKPqyiKADYEGTVRDL----------------LSSITKDF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 85 ----EVRREIArKYLELVGLggfEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDaiTAEGLRAE--IYNMVF 158
Cdd:cd03237 90 ythpYFKTEIA-KPLQIEQI---LDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD--VEQRLMASkvIRRFAE 163
|
170 180 190
....*....|....*....|....*....|....
gi 1732728249 159 NEESTVraiIMVSHNLEEVVELSDKVIILGGRPA 192
Cdd:cd03237 164 NNEKTA---FVVEHDIIMIDYLADRLIVFEGEPS 194
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1-187 |
3.07e-15 |
|
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: 70.80 E-value: 3.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKgptpklamifqdfalypwltalenvelallhrk 80
Cdd:cd03247 21 LSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVS--------------------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 81 DLSKEVRREIA----RKYLELVGLGgfeDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEglraEIYNM 156
Cdd:cd03247 68 DLEKALSSLISvlnqRPYLFDTTLR---NNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITER----QLLSL 140
|
170 180 190
....*....|....*....|....*....|.
gi 1732728249 157 VFnEESTVRAIIMVSHNLEEvVELSDKVIIL 187
Cdd:cd03247 141 IF-EVLKDKTLIWITHHLTG-IEHMDKILFL 169
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1-190 |
3.35e-15 |
|
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: 72.13 E-value: 3.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTP-----KLAMIFQDFALYPwLTALENVELA 75
Cdd:cd03252 21 ISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPawlrrQVGVVLQENVLFN-RSIRDNIALA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 76 llhRKDLSKEVRREIAR-------------KYLELVGLGGFEdyypreLSGGMKQRVAIARALAAQPVVLLMDEPFANLD 142
Cdd:cd03252 100 ---DPGMSMERVIEAAKlagahdfiselpeGYDTIVGEQGAG------LSGGQRQRIAIARALIHNPRILIFDEATSALD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1732728249 143 aitAEGLRAEIYNMvfNEESTVRAIIMVSHNLeEVVELSDKVIIL-GGR 190
Cdd:cd03252 171 ---YESEHAIMRNM--HDICAGRTVIIIAHRL-STVKNADRIIVMeKGR 213
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1-187 |
3.59e-15 |
|
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: 74.01 E-value: 3.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVK-----------GPTPKLAMIFQDFALYPWLT-A 68
Cdd:TIGR01193 493 ISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKdidrhtlrqfiNYLPQEPYIFSGSILENLLLgA 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 69 LENVELALLHRKDLSKEVRREIARKYLelvGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEG 148
Cdd:TIGR01193 573 KENVSQDEIWAACEIAEIKDDIENMPL---GYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKK 649
|
170 180 190
....*....|....*....|....*....|....*....
gi 1732728249 149 LraeIYNMVFNEESTvraIIMVSHNLeEVVELSDKVIIL 187
Cdd:TIGR01193 650 I---VNNLLNLQDKT---IIFVAHRL-SVAKQSDKIIVL 681
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-187 |
5.31e-15 |
|
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: 69.40 E-value: 5.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLmgeevkGPTPKLAmifqdfalypwltalenvelallhrkd 81
Cdd:cd03221 20 SLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW------GSTVKIG--------------------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 82 lskevrreiarkylelvglggfedYYPReLSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEIYNmvFNee 161
Cdd:cd03221 67 ------------------------YFEQ-LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKE--YP-- 117
|
170 180
....*....|....*....|....*....
gi 1732728249 162 stvRAIIMVSHN---LEEVVelsDKVIIL 187
Cdd:cd03221 118 ---GTVILVSHDryfLDQVA---TKIIEL 140
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-200 |
6.36e-15 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 72.94 E-value: 6.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRrPD---SGKVLLMGEEVKGPTPK------LAMIFQDFALYPWLTALEN 71
Cdd:TIGR02633 20 IDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPLKASNIRdteragIVIIHQELTLVPELSVAEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 72 VELA--LLH---RKDLSKEVRReiARKYLELVGLGGFEDYYP-RELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAIT 145
Cdd:TIGR02633 99 IFLGneITLpggRMAYNAMYLR--AKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKE 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1732728249 146 AEGLraeiYNMVFNEESTVRAIIMVSHNLEEVVELSDKVIIL------GGRPASIIAEVEI 200
Cdd:TIGR02633 177 TEIL----LDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIrdgqhvATKDMSTMSEDDI 233
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-187 |
6.47e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 72.43 E-value: 6.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVllmgeEVKGPTP---------KLAMIF-QDFALYPWLTALEN 71
Cdd:COG4586 42 SFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEV-----RVLGYVPfkrrkefarRIGVVFgQRSQLWWDLPAIDS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 72 VElalLHRK--DLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGL 149
Cdd:COG4586 117 FR---LLKAiyRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAI 193
|
170 180 190
....*....|....*....|....*....|....*...
gi 1732728249 150 RAEIYNMvfNEESTVrAIIMVSHNLEEVVELSDKVIIL 187
Cdd:COG4586 194 REFLKEY--NRERGT-TILLTSHDMDDIEALCDRVIVI 228
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-190 |
1.27e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 72.34 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPK------LAMIFQDF---ALYPWLTALENV 72
Cdd:PRK10762 272 SFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdglangIVYISEDRkrdGLVLGMSVKENM 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 73 ELALLhrKDLSKEVRReiARKYLELVGLGGFEDYY----P------RELSGGMKQRVAIARALAAQPVVLLMDEPFANLD 142
Cdd:PRK10762 352 SLTAL--RYFSRAGGS--LKHADEQQAVSDFIRLFniktPsmeqaiGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1732728249 143 AitaeGLRAEIYNMV--FNEESTvrAIIMVSHNLEEVVELSDKVIIL-GGR 190
Cdd:PRK10762 428 V----GAKKEIYQLInqFKAEGL--SIILVSSEMPEVLGMSDRILVMhEGR 472
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-187 |
1.48e-14 |
|
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: 70.34 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPT-----PKLAMIFQDFALYPWlTALENVELAl 76
Cdd:cd03251 22 SLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTlaslrRQIGLVSQDVFLFND-TVAENIAYG- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 77 lhRKDLSKEVRREIARKYLELVGLGGFEDYYPRE-------LSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGL 149
Cdd:cd03251 100 --RPGATREEVEEAARAANAHEFIMELPEGYDTVigergvkLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLV 177
|
170 180 190
....*....|....*....|....*....|....*...
gi 1732728249 150 RAEIYNMVFNeestvRAIIMVSHNLeEVVELSDKVIIL 187
Cdd:cd03251 178 QAALERLMKN-----RTTFVIAHRL-STIENADRIVVL 209
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-198 |
1.94e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 71.48 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPKLAmIFQDFALYP----------WLTALEN 71
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDA-IRAGIMLCPedrkaegiipVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 72 VELA----------LLHRKDLSKEVRREIARkyLELVGLGGFEDYypRELSGGMKQRVAIARALAAQPVVLLMDEPFANL 141
Cdd:PRK11288 352 INISarrhhlragcLINNRWEAENADRFIRS--LNIKTPSREQLI--MNLSGGNQQKAILGRWLSEDMKVILLDEPTRGI 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1732728249 142 DAitaeGLRAEIYNMVFNEESTVRAIIMVSHNLEEVVELSDKVIILggRPASIIAEV 198
Cdd:PRK11288 428 DV----GAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVM--REGRIAGEL 478
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
10-187 |
2.67e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 70.19 E-value: 2.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 10 FVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTP---------KLAMIFQdfalYPWLTALE-NVELALLH- 78
Cdd:PRK13646 35 YYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyirpvrkRIGMVFQ----FPESQLFEdTVEREIIFg 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 79 RKDLSKEVRREIARKYLELVGLGGFEDYY---PRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITaeglRAEIYN 155
Cdd:PRK13646 111 PKNFKMNLDEVKNYAHRLLMDLGFSRDVMsqsPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQS----KRQVMR 186
|
170 180 190
....*....|....*....|....*....|....
gi 1732728249 156 MV--FNEESTvRAIIMVSHNLEEVVELSDKVIIL 187
Cdd:PRK13646 187 LLksLQTDEN-KTIILVSHDMNEVARYADEVIVM 219
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
3-189 |
2.74e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 69.91 E-value: 2.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 3 FKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPK--LAMIFQ----DFAlYPWLtaLENV---- 72
Cdd:PRK15056 28 FTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKnlVAYVPQseevDWS-FPVL--VEDVvmmg 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 73 ---ELALLHRkdlSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITaegl 149
Cdd:PRK15056 105 rygHMGWLRR---AKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKT---- 177
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1732728249 150 RAEIYNMVFNEESTVRAIIMVSHNLEEVVELSDKVIILGG 189
Cdd:PRK15056 178 EARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKG 217
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-194 |
2.98e-14 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 71.15 E-value: 2.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLlriIAGLRR---PDSGKVLLMGEEVKGPTPK-----LAMIFQDFALYPwLTALENVE 73
Cdd:PRK13657 355 SFEAKPGQTVAIVGPTGAGKSTL---INLLQRvfdPQSGRILIDGTDIRTVTRAslrrnIAVVFQDAGLFN-RSIEDNIR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 74 LAllhRKDLSKEVRRE----------IARK---YLELVGLGGfedyypRELSGGMKQRVAIARALAAQPVVLLMDEPFAN 140
Cdd:PRK13657 431 VG---RPDATDEEMRAaaeraqahdfIERKpdgYDTVVGERG------RQLSGGERQRLAIARALLKDPPILILDEATSA 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1732728249 141 LDAITAEGLRAEIYNMVFNEE--------STVR--AIIMVSHNlEEVVELS--DKVIILGGRPASI 194
Cdd:PRK13657 502 LDVETEAKVKAALDELMKGRTtfiiahrlSTVRnaDRILVFDN-GRVVESGsfDELVARGGRFAAL 566
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
13-143 |
4.89e-14 |
|
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: 70.35 E-value: 4.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 13 IVAPTGTGKTTLLRIIAGLRRPDSGKVLLMgeevkgPTPKLAMIFQDFALYPWLTALENVELALLHRKDLSKEVrREIAR 92
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVDKDFNGEARPQ------PGIKVGYLPQEPQLDPTKTVRENVEEGVAEIKDALDRF-NEISA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 93 KYLE------------------LVGLGGFE-----------------DYYPRELSGGMKQRVAIARALAAQPVVLLMDEP 137
Cdd:TIGR03719 109 KYAEpdadfdklaaeqaelqeiIDAADAWDldsqleiamdalrcppwDADVTKLSGGERRRVALCRLLLSKPDMLLLDEP 188
|
....*.
gi 1732728249 138 FANLDA 143
Cdd:TIGR03719 189 TNHLDA 194
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
18-201 |
7.89e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 70.03 E-value: 7.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 18 GTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPK------LAMIFQDFALYPWLTALENVEL----------------- 74
Cdd:PRK10762 40 GAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKssqeagIGIIHQELNLIPQLTIAENIFLgrefvnrfgridwkkmy 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 75 ----ALLHRKDLSKEVRReiarkyleLVGlggfedyyprELSGGMKQRVAIARALAAQPVVLLMDEPfanLDAITaEGLR 150
Cdd:PRK10762 120 aeadKLLARLNLRFSSDK--------LVG----------ELSIGEQQMVEIAKVLSFESKVIIMDEP---TDALT-DTET 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1732728249 151 AEIYNmVFNE-ESTVRAIIMVSHNLEEVVELSDKVIILggRPASIIAEVEIK 201
Cdd:PRK10762 178 ESLFR-VIRElKSQGRGIVYISHRLKEIFEICDDVTVF--RDGQFIAEREVA 226
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
2-188 |
8.66e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.57 E-value: 8.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDS-GKVLLMGEEVKGPTPK------LAMIFQD---FALYPWLTALEN 71
Cdd:PRK13549 282 SFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGKPVKIRNPQqaiaqgIAMVPEDrkrDGIVPVMGVGKN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 72 VELALLHRK------DLSKE---VRREIAR-----KYLEL-VGlggfedyyprELSGGMKQRVAIARALAAQPVVLLMDE 136
Cdd:PRK13549 362 ITLAALDRFtggsriDDAAElktILESIQRlkvktASPELaIA----------RLSGGNQQKAVLAKCLLLNPKILILDE 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1732728249 137 PFANLDAitaeGLRAEIYNMVFNEESTVRAIIMVSHNLEEVVELSDKVIILG 188
Cdd:PRK13549 432 PTRGIDV----GAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMH 479
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-188 |
9.50e-14 |
|
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: 69.47 E-value: 9.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPD-SGKVLLMGEEVKGPTP------KLAMIFQD---FALYPWLTALE 70
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPaqairaGIAMVPEDrkrHGIVPILGVGK 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 71 NVELALLH------RKDLSKE---VRREIARkylelVGLGGFEDYYP-RELSGGMKQRVAIARALAAQPVVLLMDEPFAN 140
Cdd:TIGR02633 359 NITLSVLKsfcfkmRIDAAAElqiIGSAIQR-----LKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1732728249 141 LDAitaeGLRAEIYNMVFNEESTVRAIIMVSHNLEEVVELSDKVIILG 188
Cdd:TIGR02633 434 VDV----GAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIG 477
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-190 |
1.03e-13 |
|
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: 69.39 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPklamifQDFALY----PwltalENVELall 77
Cdd:COG4618 352 SFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDR------EELGRHigylP-----QDVEL--- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 78 hrkdLSKEVRREIAR-------KYLE---LVGL----GGFEDYY-------PRELSGGMKQRVAIARALAAQPVVLLMDE 136
Cdd:COG4618 418 ----FDGTIAENIARfgdadpeKVVAaakLAGVhemiLRLPDGYdtrigegGARLSGGQRQRIGLARALYGDPRLVVLDE 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1732728249 137 PFANLDAITAEGLRAEIYNMvfneestvRA----IIMVSHNLeEVVELSDKVIIL-GGR 190
Cdd:COG4618 494 PNSNLDDEGEAALAAAIRAL--------KArgatVVVITHRP-SLLAAVDKLLVLrDGR 543
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-176 |
1.11e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 69.49 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRrPDSGKVLLMGEEVKGPTPK-----LAMIFQDFALyPWLTALENVelaL 76
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPEswrkhLSWVGQNPQL-PHGTLRDNV---L 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 77 LHRKDLSKE-VRREIARKYL-ELV-----GLggfeDYYPRE----LSGGMKQRVAIARALAAQPVVLLMDEPFANLDAIT 145
Cdd:PRK11174 445 LGNPDASDEqLQQALENAWVsEFLpllpqGL----DTPIGDqaagLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHS 520
|
170 180 190
....*....|....*....|....*....|.
gi 1732728249 146 AEGLraeiyNMVFNEESTVRAIIMVSHNLEE 176
Cdd:PRK11174 521 EQLV-----MQALNAASRRQTTLMVTHQLED 546
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-197 |
1.82e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 67.81 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPT-----PKLAMIFQD-FALYPWLTALENVEL 74
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENvwnlrRKIGMVFQNpDNQFVGATVEDDVAF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 75 ALLHRKDLSKEVRREIARKYLElVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITaeglRAEIY 154
Cdd:PRK13642 106 GMENQGIPREEMIKRVDEALLA-VNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTG----RQEIM 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1732728249 155 NMVFN-EESTVRAIIMVSHNLEEVVElSDKVIILggRPASIIAE 197
Cdd:PRK13642 181 RVIHEiKEKYQLTVLSITHDLDEAAS-SDRILVM--KAGEIIKE 221
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-187 |
2.43e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 68.58 E-value: 2.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKT-TLLRIIAGLRRPD----SGKVLLMGEE-----------VKGPtpKLAMIFQD--FAL 62
Cdd:PRK15134 28 VSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESllhaseqtlrgVRGN--KIAMIFQEpmVSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 63 YPwltaLENVELALLHRKDLSKEVRREIAR----KYLELVGL----GGFEDYyPRELSGGMKQRVAIARALAAQPVVLLM 134
Cdd:PRK15134 106 NP----LHTLEKQLYEVLSLHRGMRREAARgeilNCLDRVGIrqaaKRLTDY-PHQLSGGERQRVMIAMALLTRPELLIA 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1732728249 135 DEPFANLDaITAEG--------LRAEIyNMvfneestvrAIIMVSHNLEEVVELSDKVIIL 187
Cdd:PRK15134 181 DEPTTALD-VSVQAqilqllreLQQEL-NM---------GLLFITHNLSIVRKLADRVAVM 230
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2-187 |
3.38e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 68.15 E-value: 3.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPKLA------MIFQDFALYPWLTALENVELA 75
Cdd:PRK15439 31 DFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAhqlgiyLVPQEPLLFPNLSVKENILFG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 76 LLHRKDLSKEVRREIAR--KYLELVGLGGFEDYYPRELsggmkqrVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEI 153
Cdd:PRK15439 111 LPKRQASMQKMKQLLAAlgCQLDLDSSAGSLEVADRQI-------VEILRGLMRDSRILILDEPTASLTPAETERLFSRI 183
|
170 180 190
....*....|....*....|....*....|....
gi 1732728249 154 YNMvfneESTVRAIIMVSHNLEEVVELSDKVIIL 187
Cdd:PRK15439 184 REL----LAQGVGIVFISHKLPEIRQLADRISVM 213
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1-187 |
4.39e-13 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 67.61 E-value: 4.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVllmgeEVKGPTpklAMIFQDFALYPWLTALENVELALLhRK 80
Cdd:PRK13545 43 ISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DIKGSA---ALIAISSGLNGQLTGIENIELKGL-MM 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 81 DLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLD-AITAEGLraEIYNMvFN 159
Cdd:PRK13545 114 GLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDqTFTKKCL--DKMNE-FK 190
|
170 180
....*....|....*....|....*...
gi 1732728249 160 EEStvRAIIMVSHNLEEVVELSDKVIIL 187
Cdd:PRK13545 191 EQG--KTIFFISHSLSQVKSFCTKALWL 216
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
2-190 |
5.58e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 66.10 E-value: 5.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEvKGPTPKLAM---------------IFQDFA--LYP 64
Cdd:PRK11701 26 SFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRD-GQLRDLYALseaerrrllrtewgfVHQHPRdgLRM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 65 WLTALENVELALL-----HRKDLskevrREIARKYLELVGLGGFE-DYYPRELSGGMKQRVAIARALAAQPVVLLMDEPF 138
Cdd:PRK11701 105 QVSAGGNIGERLMavgarHYGDI-----RATAGDWLERVEIDAARiDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPT 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1732728249 139 ANLDAitaeGLRAEIYNMVfneESTVR----AIIMVSHNLEEVVELSDKVIIL-GGR 190
Cdd:PRK11701 180 GGLDV----SVQARLLDLL---RGLVRelglAVVIVTHDLAVARLLAHRLLVMkQGR 229
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
1-187 |
9.18e-13 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 65.62 E-value: 9.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVllmGEEVKGPTPKLamifqdfalypwLTALENVELALLHRK 80
Cdd:TIGR02323 22 VSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTA---TYIMRSGAELE------------LYQLSEAERRRLMRT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 81 D-----------LSKEVR--------------------REIARKYLELVGLG-GFEDYYPRELSGGMKQRVAIARALAAQ 128
Cdd:TIGR02323 87 EwgfvhqnprdgLRMRVSaganigerlmaigarhygniRATAQDWLEEVEIDpTRIDDLPRAFSGGMQQRLQIARNLVTR 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1732728249 129 PVVLLMDEPFANLDAitaeGLRAEIYNMVfneESTVR----AIIMVSHNLEEVVELSDKVIIL 187
Cdd:TIGR02323 167 PRLVFMDEPTGGLDV----SVQARLLDLL---RGLVRdlglAVIIVTHDLGVARLLAQRLLVM 222
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1-151 |
1.17e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 66.50 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLmgeevkGPTPKLAMIFQDfalypwltalenvelallhRK 80
Cdd:TIGR03719 341 LSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI------GETVKLAYVDQS-------------------RD 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 81 DL--SKEVRREIARKyLELVGLGGFE----DYYPR-------------ELSGGMKQRVAIARALAAQPVVLLMDEPFANL 141
Cdd:TIGR03719 396 ALdpNKTVWEEISGG-LDIIKLGKREipsrAYVGRfnfkgsdqqkkvgQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDL 474
|
170
....*....|
gi 1732728249 142 DaitAEGLRA 151
Cdd:TIGR03719 475 D---VETLRA 481
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1-189 |
1.33e-12 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 63.33 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGL--------RRPDSGKVLLMGEEVKGPTPKLAmifqDFALYPWLtalenv 72
Cdd:cd03223 20 LSFEIKPGDRLLITGPSGTGKSSLFRALAGLwpwgsgriGMPEGEDLLFLPQRPYLPLGTLR----EQLIYPWD------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 73 elallhrkdlskevrreiarkylelvglggfedyypRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDaitaEGLRAE 152
Cdd:cd03223 90 ------------------------------------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALD----EESEDR 129
|
170 180 190
....*....|....*....|....*....|....*..
gi 1732728249 153 IYNMVfNEESTvrAIIMVSHNlEEVVELSDKVIILGG 189
Cdd:cd03223 130 LYQLL-KELGI--TVISVGHR-PSLWKFHDRVLDLDG 162
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
4-192 |
1.35e-12 |
|
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: 66.35 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 4 KVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVllmGEEVK---GP---TPKLAMIFQDFalypwltaLENVelall 77
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV---DEDLKisyKPqyiSPDYDGTVEEF--------LRSA----- 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 78 HRKDL-SKEVRREIARKylelVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDA----ITAEGLRAE 152
Cdd:COG1245 426 NTDDFgSSYYKTEIIKP----LGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrlAVAKAIRRF 501
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1732728249 153 IynmvfneESTVRAIIMVSHNLEEVVELSDKVIILGGRPA 192
Cdd:COG1245 502 A-------ENRGKTAMVVDHDIYLIDYISDRLMVFEGEPG 534
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-187 |
1.59e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 65.70 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPD----------SGKVLL----------MGEEVkgptpklAMIFQD- 59
Cdd:COG4170 26 VSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtadrfrwNGIDLLklsprerrkiIGREI-------AMIFQEp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 60 -FALYPWLTALENVELALLHRKDLSK-----EVRREIARKYLELVGLGGFEDY---YPRELSGGMKQRVAIARALAAQPV 130
Cdd:COG4170 99 sSCLDPSAKIGDQLIEAIPSWTFKGKwwqrfKWRKKRAIELLHRVGIKDHKDImnsYPHELTEGECQKVMIAMAIANQPR 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1732728249 131 VLLMDEPFANLDAITaeglRAEIYNMV--FNEESTVrAIIMVSHNLEEVVELSDKVIIL 187
Cdd:COG4170 179 LLIADEPTNAMESTT----QAQIFRLLarLNQLQGT-SILLISHDLESISQWADTITVL 232
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-187 |
2.51e-12 |
|
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: 65.51 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPT-----PKLAMIFQDFALYPwLTALENVELAL 76
Cdd:TIGR02203 352 SLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTlaslrRQVALVSQDVVLFN-DTIANNIAYGR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 77 LHRKDlSKEVRREIARKYLElvglgGFEDYYPR-----------ELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAIT 145
Cdd:TIGR02203 431 TEQAD-RAEIERALAAAYAQ-----DFVDKLPLgldtpigengvLLSGGQRQRLAIARALLKDAPILILDEATSALDNES 504
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1732728249 146 AEGLRAEIYNMVFNeestvRAIIMVSHNLeEVVELSDKVIIL 187
Cdd:TIGR02203 505 ERLVQAALERLMQG-----RTTLVIAHRL-STIEKADRIVVM 540
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1-187 |
3.04e-12 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 65.12 E-value: 3.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPK-----LAMIFQDfalyPWLTA---LENV 72
Cdd:PRK10790 360 INLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSvlrqgVAMVQQD----PVVLAdtfLANV 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 73 ELAllhrKDLSKEVRREIarkyLELVGLGGFEDYYP-----------RELSGGMKQRVAIARALAAQPVVLLMDEPFANL 141
Cdd:PRK10790 436 TLG----RDISEEQVWQA----LETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALARVLVQTPQILILDEATANI 507
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1732728249 142 DAITAEGLRAEIynMVFNEESTvraIIMVSHNLEEVVElSDKVIIL 187
Cdd:PRK10790 508 DSGTEQAIQQAL--AAVREHTT---LVVIAHRLSTIVE-ADTILVL 547
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-195 |
3.99e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 64.81 E-value: 3.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTP----KLAMIF-----QDFALYPWLTALEN 71
Cdd:PRK09700 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPldavKKGMAYitesrRDNGFFPNFSIAQN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 72 VELA-------------LLHRKDlskevRREIARKYLELVGLGGFE-DYYPRELSGGMKQRVAIARALAAQPVVLLMDEP 137
Cdd:PRK09700 362 MAISrslkdggykgamgLFHEVD-----EQRTAENQRELLALKCHSvNQNITELSGGNQQKVLISKWLCCCPEVIIFDEP 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1732728249 138 FANLDAitaeGLRAEIYNMVFNEESTVRAIIMVSHNLEEVVELSDKVIIL-GGRPASII 195
Cdd:PRK09700 437 TRGIDV----GAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFcEGRLTQIL 491
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-187 |
4.20e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 64.88 E-value: 4.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPK--------LAMIFQD--FALYPWLTALE 70
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGklqalrrdIQFIFQDpyASLDPRQTVGD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 71 NV-ELALLHRKDLSKEVRREIArKYLELVGLGGFEDY-YPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAitaeG 148
Cdd:PRK10261 423 SImEPLRVHGLLPGKAAAARVA-WLLERVGLLPEHAWrYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV----S 497
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1732728249 149 LRAEIYNMVFNEESTVR-AIIMVSHNLEEVVELSDKVIIL 187
Cdd:PRK10261 498 IRGQIINLLLDLQRDFGiAYLFISHDMAVVERISHRVAVM 537
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
11-187 |
4.33e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 63.59 E-value: 4.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 11 VSIVAPTGTGKTTLLRIIAGLRRPDSGKVllmgeeVKGPTPKLAMIFQDFALYPWLTalenveLALLHRKDLSKEVRREI 90
Cdd:PRK09544 33 LTLLGPNGAGKSTLVRVVLGLVAPDEGVI------KRNGKLRIGYVPQKLYLDTTLP------LTVNRFLRLRPGTKKED 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 91 ARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDaitAEGLRAeIYNMVFNEESTVR-AIIM 169
Cdd:PRK09544 101 ILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD---VNGQVA-LYDLIDQLRRELDcAVLM 176
|
170
....*....|....*...
gi 1732728249 170 VSHNLEEVVELSDKVIIL 187
Cdd:PRK09544 177 VSHDLHLVMAKTDEVLCL 194
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1-223 |
4.67e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 63.85 E-value: 4.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEV-----KGPTPKLAMIFQDFALYPWLTALENVELA 75
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIqhyasKEVARRIGLLAQNATTPGDITVQELVARG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 76 LLHRKDLSKEVRRE---IARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDaITAEGLRAE 152
Cdd:PRK10253 106 RYPHQPLFTRWRKEdeeAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD-ISHQIDLLE 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1732728249 153 IYNMVFNEESTVRAIIMvsHNLEEVVELSDKVIILggRPASIIAEVEIKlprprntrDIEFQDYLDRLYSL 223
Cdd:PRK10253 185 LLSELNREKGYTLAAVL--HDLNQACRYASHLIAL--REGKIVAQGAPK--------EIVTAELIERIYGL 243
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
18-172 |
5.32e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 62.66 E-value: 5.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 18 GTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGP----TPKLAMIFQDFALYPWLTALENVeLALLHRKDLSKEVrREIARk 93
Cdd:PRK13540 37 GAGKTTLLKLIAGLLNPEKGEILFERQSIKKDlctyQKQLCFVGHRSGINPYLTLRENC-LYDIHFSPGAVGI-TELCR- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 94 yleLVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEIynmvfnEESTVR--AIIMVS 171
Cdd:PRK13540 114 ---LFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKI------QEHRAKggAVLLTS 184
|
.
gi 1732728249 172 H 172
Cdd:PRK13540 185 H 185
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1-190 |
5.41e-12 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 63.68 E-value: 5.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEevkgptpkLAMIFQDFALYPWLTALENVELALLHRK 80
Cdd:PRK13546 43 ISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE--------VSVIAISAGLSGQLTGIENIEFKMLCMG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 81 DLSKEVrREIARKYLELVGLGGFeDYYP-RELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEIYNmvFN 159
Cdd:PRK13546 115 FKRKEI-KAMTPKIIEFSELGEF-IYQPvKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYE--FK 190
|
170 180 190
....*....|....*....|....*....|..
gi 1732728249 160 EEStvRAIIMVSHNLEEVVELSDKVI-ILGGR 190
Cdd:PRK13546 191 EQN--KTIFFVSHNLGQVRQFCTKIAwIEGGK 220
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1-189 |
5.84e-12 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 62.28 E-value: 5.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPD---SGKVLLMGEEVKgptpKLAMIFQDFALY--------PWLTAL 69
Cdd:cd03233 26 FSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYK----EFAEKYPGEIIYvseedvhfPTLTVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 70 ENVELALLHRKDlskevrreiarkylELVglggfedyypRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITA--- 146
Cdd:cd03233 102 ETLDFALRCKGN--------------EFV----------RGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTAlei 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1732728249 147 -EGLR--AEIYNMVfneestvrAIIMVSHNLEEVVELSDKVIILGG 189
Cdd:cd03233 158 lKCIRtmADVLKTT--------TFVSLYQASDEIYDLFDKVLVLYE 195
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-187 |
7.36e-12 |
|
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: 62.51 E-value: 7.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTP-----KLAMIFQDfalyPWL---TALENve 73
Cdd:cd03244 24 SFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLhdlrsRISIIPQD----PVLfsgTIRSN-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 74 LALLHRKDlSKEVRReiarkYLELVGLGGFEDYYP-----------RELSGGMKQRVAIARALAAQPVVLLMDEPFANLD 142
Cdd:cd03244 98 LDPFGEYS-DEELWQ-----ALERVGLKEFVESLPggldtvveeggENLSVGQRQLLCLARALLRKSKILVLDEATASVD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1732728249 143 AITAEGLRAEIYNMVFNeestvRAIIMVSHNLEEVVElSDKVIIL 187
Cdd:cd03244 172 PETDALIQKTIREAFKD-----CTVLTIAHRLDTIID-SDRILVL 210
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
2-201 |
8.74e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.98 E-value: 8.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPKLA------MIFQDFALYPWLTALENVELA 75
Cdd:PRK10982 18 NLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEAlengisMVHQELNLVLQRSVMDNMWLG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 76 LLHRKDL---SKEVRREIARKYLELVglggfEDYYPRE----LSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEG 148
Cdd:PRK10982 98 RYPTKGMfvdQDKMYRDTKAIFDELD-----IDIDPRAkvatLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNH 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1732728249 149 LRAEIYNMvfnEESTVrAIIMVSHNLEEVVELSDKVIILggRPASIIAEVEIK 201
Cdd:PRK10982 173 LFTIIRKL---KERGC-GIVYISHKMEEIFQLCDEITIL--RDGQWIATQPLA 219
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
5-192 |
1.31e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 63.29 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 5 VHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLmgeEVK---GP---TPKLAMIFQDFalypwltaLENVELALLh 78
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP---ELKisyKPqyiKPDYDGTVEDL--------LRSITDDLG- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 79 rkdlSKEVRREIARKylelVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDA----ITAeglRAeIY 154
Cdd:PRK13409 430 ----SSYYKSEIIKP----LQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrlAVA---KA-IR 497
|
170 180 190
....*....|....*....|....*....|....*...
gi 1732728249 155 NMVFNEESTVraiIMVSHNLEEVVELSDKVIILGGRPA 192
Cdd:PRK13409 498 RIAEEREATA---LVVDHDIYMIDYISDRLMVFEGEPG 532
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1-187 |
2.52e-11 |
|
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: 61.80 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGP--------TPKLAMIFQ-DFALYPWLTALEN 71
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSqfswimpgTIKENIIFGvSYDEYRYKSVVKA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 72 VELallhRKDLSKevrreIARKYLELVGLGGFEdyypreLSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEglra 151
Cdd:cd03291 136 CQL----EEDITK-----FPEKDNTVLGEGGIT------LSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEK---- 196
|
170 180 190
....*....|....*....|....*....|....*.
gi 1732728249 152 EIYNMVFNEESTVRAIIMVSHNLEEvVELSDKVIIL 187
Cdd:cd03291 197 EIFESCVCKLMANKTRILVTSKMEH-LKKADKILIL 231
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
9-197 |
3.26e-11 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 61.01 E-value: 3.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 9 EFVSIVAPTGTGKTTLLRIIAGLRrPDSGKVLLMGEEVKG-PTPKLA---------------M-IFQDFALY-PWLTALE 70
Cdd:COG4138 23 ELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDwSAAELArhraylsqqqsppfaMpVFQYLALHqPAGASSE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 71 NVELALLhrkdlskevrrEIARKyLELvglggfEDYYPR---ELSGGMKQRVAIARALA-------AQPVVLLMDEPFAN 140
Cdd:COG4138 102 AVEQLLA-----------QLAEA-LGL------EDKLSRpltQLSGGEWQRVRLAAVLLqvwptinPEGQLLLLDEPMNS 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1732728249 141 LD------------AITAEGlraeiynmvfneestvRAIIMVSHNL-------EEVVELSDKVIILGGRPASIIAE 197
Cdd:COG4138 164 LDvaqqaaldrllrELCQQG----------------ITVVMSSHDLnhtlrhaDRVWLLKQGKLVASGETAEVMTP 223
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-187 |
4.07e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 60.66 E-value: 4.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKG-PTPKL-----AMIFQDFALYPWLTALENVEL 74
Cdd:PRK11614 24 VSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwQTAKImreavAIVPEGRRVFSRMTVEENLAM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 75 ALLHRKdlSKEVRREIARKYlelvglggfeDYYPR----------ELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAI 144
Cdd:PRK11614 104 GGFFAE--RDQFQERIKWVY----------ELFPRlherriqragTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPI 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1732728249 145 TAEglraEIYNMVFNEESTVRAIIMVSHNLEEVVELSDKVIIL 187
Cdd:PRK11614 172 IIQ----QIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVL 210
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
2-187 |
4.61e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 60.72 E-value: 4.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLrRPDSGKVLLMGEEVKG-PTPKLAM----------------IFQDFALY- 63
Cdd:PRK03695 16 SAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAwSAAELARhraylsqqqtppfampVFQYLTLHq 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 64 PWLTALENVELALlhrkdlskevrREIArkylELVGLGgfeDYYPR---ELSGGMKQRVAIARAL-----AAQPV--VLL 133
Cdd:PRK03695 95 PDKTRTEAVASAL-----------NEVA----EALGLD---DKLGRsvnQLSGGEWQRVRLAAVVlqvwpDINPAgqLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1732728249 134 MDEPFANLDaITAEGLraeIYNMVFNEESTVRAIIMVSHNLEEVVELSDKVIIL 187
Cdd:PRK03695 157 LDEPMNSLD-VAQQAA---LDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLL 206
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
13-143 |
6.17e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 61.29 E-value: 6.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 13 IVAPTGTGKTTLLRIIAGLRRPDSGKVLLMgeevkgPTPKLAMIFQDFALYPWLTALENVELALLHRKDLSKEVrREIAR 92
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEARPA------PGIKVGYLPQEPQLDPEKTVRENVEEGVAEVKAALDRF-NEIYA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 93 KYLE------------------LVGLGGFE-----------------DYYPRELSGGMKQRVAIARALAAQPVVLLMDEP 137
Cdd:PRK11819 111 AYAEpdadfdalaaeqgelqeiIDAADAWDldsqleiamdalrcppwDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEP 190
|
....*.
gi 1732728249 138 FANLDA 143
Cdd:PRK11819 191 TNHLDA 196
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
2-146 |
7.09e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.59 E-value: 7.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAG--LRRPDSGKVLLMgeevkgptpklamifqDFALYPWLTALENVelALLHR 79
Cdd:COG2401 50 NLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVP----------------DNQFGREASLIDAI--GRKGD 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1732728249 80 KDLSKEVrreiarkyLELVGLGgfeDYY-----PRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITA 146
Cdd:COG2401 112 FKDAVEL--------LNAVGLS---DAVlwlrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTA 172
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1-195 |
1.79e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.13 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPKLAmIFQDFAL----------YPWL---- 66
Cdd:PRK10982 267 VSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEA-INHGFALvteerrstgiYAYLdigf 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 67 -TALENVE-----LALLHRKDLSKEVRREI------ARKYLELVGlggfedyyprELSGGMKQRVAIARALAAQPVVLLM 134
Cdd:PRK10982 346 nSLISNIRnyknkVGLLDNSRMKSDTQWVIdsmrvkTPGHRTQIG----------SLSGGNQQKVIIGRWLLTQPEILML 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1732728249 135 DEPFANLDAitaeGLRAEIYNMVFNEESTVRAIIMVSHNLEEVVELSDKVIILG-GRPASII 195
Cdd:PRK10982 416 DEPTRGIDV----GAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSnGLVAGIV 473
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-197 |
2.06e-10 |
|
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: 59.83 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPK-----LAMIFQDFALYPwLTALENVELAl 76
Cdd:COG5265 378 SFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQAslraaIGIVPQDTVLFN-DTIAYNIAYG- 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 77 lhRKDLSKEVRREIAR-------------KYLELVGLGGFEdyypreLSGGMKQRVAIARALAAQPVVLLMDEPFANLDA 143
Cdd:COG5265 456 --RPDASEEEVEAAARaaqihdfieslpdGYDTRVGERGLK------LSGGEKQRVAIARTLLKNPPILIFDEATSALDS 527
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1732728249 144 ITAEGLRAEIynmvfNEESTVRAIIMVSHNLEEVVElSDKVIIL-GGRpasiIAE 197
Cdd:COG5265 528 RTERAIQAAL-----REVARGRTTLVIAHRLSTIVD-ADEILVLeAGR----IVE 572
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
11-192 |
2.38e-10 |
|
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: 58.53 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 11 VSIVAPTGTGKTTLLRIIAGLRRPDSGKVllmgeevkGPTPKLAMIFQDF---ALYPWLTALENVELALLHRKD------ 81
Cdd:cd03236 29 LGLVGPNGIGKSTALKILAGKLKPNLGKF--------DDPPDWDEILDEFrgsELQNYFTKLLEGDVKVIVKPQyvdlip 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 82 ----------LSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDA---ITAEG 148
Cdd:cd03236 101 kavkgkvgelLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIkqrLNAAR 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1732728249 149 LRAEIynmvfNEEStvRAIIMVSHNLEEVVELSDKVIILGGRPA 192
Cdd:cd03236 181 LIREL-----AEDD--NYVLVVEHDLAVLDYLSDYIHCLYGEPG 217
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
3-187 |
3.45e-10 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 57.81 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 3 FKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGP-----TPKLAMIFQDFALYPWlTALENVelall 77
Cdd:cd03369 29 FKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIpledlRSSLTIIPQDPTLFSG-TIRSNL----- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 78 hrkDLSKEVRREIARKYLELVGLGgfedyypRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITaeglRAEIyNMV 157
Cdd:cd03369 103 ---DPFDEYSDEEIYGALRVSEGG-------LNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT----DALI-QKT 167
|
170 180 190
....*....|....*....|....*....|
gi 1732728249 158 FNEESTVRAIIMVSHNLEEVVELsDKVIIL 187
Cdd:cd03369 168 IREEFTNSTILTIAHRLRTIIDY-DKILVM 196
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-151 |
3.48e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.98 E-value: 3.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLmgeevkGPTPKLAMIFQdfalypwltalenvelallHRK 80
Cdd:PRK11819 343 LSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI------GETVKLAYVDQ-------------------SRD 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 81 DL--SKEVRREIARKyLELVGLGGFE----DYYPR-------------ELSGGMKQRVAIARALAAQPVVLLMDEPFANL 141
Cdd:PRK11819 398 ALdpNKTVWEEISGG-LDIIKVGNREipsrAYVGRfnfkggdqqkkvgVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDL 476
|
170
....*....|
gi 1732728249 142 DaitAEGLRA 151
Cdd:PRK11819 477 D---VETLRA 483
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
13-142 |
4.15e-10 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 58.10 E-value: 4.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 13 IVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPK-----LAMIFQDFALYPWLTALENVE------LALLHRkd 81
Cdd:PRK11231 33 LIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRqlarrLALLPQHHLTPEGITVRELVAygrspwLSLWGR-- 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1732728249 82 LSKEVRREIARKyLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLD 142
Cdd:PRK11231 111 LSAEDNARVNQA-MEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD 170
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
107-187 |
4.22e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 59.27 E-value: 4.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 107 YPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEIYNMvfnEESTVRAIIMVSHNLEEvVELSDKVII 186
Cdd:PTZ00265 1355 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDI---KDKADKTIITIAHRIAS-IKRSDKIVV 1430
|
.
gi 1732728249 187 L 187
Cdd:PTZ00265 1431 F 1431
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-187 |
4.34e-10 |
|
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: 59.26 E-value: 4.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 5 VHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVkgpTPKLAMIFQDFALYP-------WLTALENVELALL 77
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI---LTNISDVHQNMGYCPqfdaiddLLTGREHLYLYAR 2038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 78 HRKDLSKEVRReIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITaeglRAEIYNMV 157
Cdd:TIGR01257 2039 LRGVPAEEIEK-VANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQA----RRMLWNTI 2113
|
170 180 190
....*....|....*....|....*....|
gi 1732728249 158 FNEESTVRAIIMVSHNLEEVVELSDKVIIL 187
Cdd:TIGR01257 2114 VSIIREGRAVVLTSHSMEECEALCTRLAIM 2143
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1-173 |
7.71e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 58.33 E-value: 7.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLlmgeevKGPTPKLAMIFQDFalypwLTALENVELALLHRK 80
Cdd:PLN03073 528 LNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF------RSAKVRMAVFSQHH-----VDGLDLSSNPLLYMM 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 81 DLSKEVRREIARKYLELVGLGGFEDYYPR-ELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLraeIYNMVFN 159
Cdd:PLN03073 597 RCFPGVPEQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEAL---IQGLVLF 673
|
170
....*....|....
gi 1732728249 160 EEstvrAIIMVSHN 173
Cdd:PLN03073 674 QG----GVLMVSHD 683
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
9-174 |
1.15e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 57.53 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 9 EFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKG---PTPKLAM--------IFQDfalypwlTALENVELALl 77
Cdd:PRK11160 367 EKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADyseAALRQAIsvvsqrvhLFSA-------TLRDNLLLAA- 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 78 hrKDLSKEVRREIarkyLELVGLGGF-EDYYP---------RELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAE 147
Cdd:PRK11160 439 --PNASDEALIEV----LQQVGLEKLlEDDKGlnawlgeggRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETER 512
|
170 180
....*....|....*....|....*..
gi 1732728249 148 glraEIYNMVFnEESTVRAIIMVSHNL 174
Cdd:PRK11160 513 ----QILELLA-EHAQNKTVLMITHRL 534
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
9-187 |
1.24e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 56.63 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 9 EFVSIVAPTGTGKT----TLLRII-AGLRRPdSGKVLLMGEEVKG---PTPKLAMIFQD--FALYPWLTALENVELALLH 78
Cdd:PRK10418 30 RVLALVGGSGSGKSltcaAALGILpAGVRQT-AGRVLLDGKPVAPcalRGRKIATIMQNprSAFNPLHTMHTHARETCLA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 79 RkdlSKEVRREIARKYLELVGLGGFE---DYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITaeglRAEIYN 155
Cdd:PRK10418 109 L---GKPADDATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVA----QARILD 181
|
170 180 190
....*....|....*....|....*....|....*.
gi 1732728249 156 MVfneESTVR----AIIMVSHNLEEVVELSDKVIIL 187
Cdd:PRK10418 182 LL---ESIVQkralGMLLVTHDMGVVARLADDVAVM 214
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1-187 |
1.54e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 57.61 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGP--------TPKLAMIFQ-DFALYPWLTALEN 71
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPqtswimpgTIKDNIIFGlSYDEYRYTSVIKA 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 72 VELallhRKDLSKevrreIARKYLELVGLGGFEdyypreLSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEglra 151
Cdd:TIGR01271 525 CQL----EEDIAL-----FPEKDKTVLGEGGIT------LSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEK---- 585
|
170 180 190
....*....|....*....|....*....|....*.
gi 1732728249 152 EIYNMVFNEESTVRAIIMVSHNLEEvVELSDKVIIL 187
Cdd:TIGR01271 586 EIFESCLCKLMSNKTRILVTSKLEH-LKKADKILLL 620
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
69-205 |
1.72e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 57.35 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 69 LENVELALLHRKDLSKEVRREIARKYLELVGLGGfedyypRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEG 148
Cdd:PTZ00265 544 IKDSEVVDVSKKVLIHDFVSALPDKYETLVGSNA------SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYL 617
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1732728249 149 LRAEIYNMVFNEEstvRAIIMVSHNLeEVVELSDKVIILGGRPASIIAEVEIKLPRP 205
Cdd:PTZ00265 618 VQKTINNLKGNEN---RITIIIAHRL-STIRYANTIFVLSNRERGSTVDVDIIGEDP 670
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-142 |
2.86e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 56.52 E-value: 2.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPK-----LAMIFQDFALYPWLTALENvelal 76
Cdd:PRK10522 343 NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEdyrklFSAVFTDFHLFDQLLGPEG----- 417
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1732728249 77 lhrkdlsKEVRREIARKYLELVGLGG---FEDYYPR--ELSGGMKQRVAIARALAAQPVVLLMDEPFANLD 142
Cdd:PRK10522 418 -------KPANPALVEKWLERLKMAHkleLEDGRISnlKLSKGQKKRLALLLALAEERDILLLDEWAADQD 481
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1-175 |
3.65e-09 |
|
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: 55.03 E-value: 3.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPTPKLAMIFQDFALY-----PWL---TALENV 72
Cdd:cd03290 20 INIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAyaaqkPWLlnaTVEENI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 73 ELALLHRKDLSKEVRREIA-RKYLELVGLGGFEDYYPR--ELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGL 149
Cdd:cd03290 100 TFGSPFNKQRYKAVTDACSlQPDIDLLPFGDQTEIGERgiNLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHL 179
|
170 180
....*....|....*....|....*.
gi 1732728249 150 RAEIYNMVFNEEStvRAIIMVSHNLE 175
Cdd:cd03290 180 MQEGILKFLQDDK--RTLVLVTHKLQ 203
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
9-187 |
5.35e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.89 E-value: 5.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 9 EFVSIVAPTGTGKTTLLRIIA----GLRRPDSGKVLLMG----EEVKGPTPKLAMIFQDFALYPWLTALENVELALLHR- 79
Cdd:TIGR00956 88 ELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGitpeEIKKHYRGDVVYNAETDVHFPHLTVGETLDFAARCKt 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 80 -----KDLSKEVRRE-IARKYLELVGLGGFEDY-----YPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITA-E 147
Cdd:TIGR00956 168 pqnrpDGVSREEYAKhIADVYMATYGLSHTRNTkvgndFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATAlE 247
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1732728249 148 GLRAEIYNMVFNEESTVRAIIMVShnlEEVVELSDKVIIL 187
Cdd:TIGR00956 248 FIRALKTSANILDTTPLVAIYQCS---QDAYELFDKVIVL 284
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
7-206 |
7.72e-09 |
|
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: 52.76 E-value: 7.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 7 SHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLmgeevkgptpklamifqdfalypwltalenvelallhrkdLSKEV 86
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY----------------------------------------IDGED 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 87 RREIARKYLELVGLGGfedyYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEIYNMVF--NEESTV 164
Cdd:smart00382 41 ILEEVLDQLLLIIVGG----KKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLllLKSEKN 116
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1732728249 165 RAIIMVSHNLEevvelsdkviILGGRPASIIAEVEIKLPRPR 206
Cdd:smart00382 117 LTVILTTNDEK----------DLGPALLRRRFDRRIVLLLIL 148
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
11-137 |
8.19e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.13 E-value: 8.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 11 VSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMG---------EEVkgpTPKLAMIFQDFA--LYPWLTALENVEL-ALL- 77
Cdd:NF033858 30 VGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGgdmadarhrRAV---CPRIAYMPQGLGknLYPTLSVFENLDFfGRLf 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1732728249 78 -HRKdlsKEVRREIARkYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEP 137
Cdd:NF033858 107 gQDA---AERRRRIDE-LLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEP 163
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
11-192 |
9.48e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 54.79 E-value: 9.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 11 VSIVAPTGTGKTTLLRIIAGLRRPDSGKVllmGEEvkgptPKLAMIFQDFA---LYPWLTALENVELALLHR-------- 79
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGELKPNLGDY---DEE-----PSWDEVLKRFRgteLQDYFKKLANGEIKVAHKpqyvdlip 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 80 -------KDLSKEV-RREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDA---ITAEG 148
Cdd:COG1245 174 kvfkgtvRELLEKVdERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIyqrLNVAR 253
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1732728249 149 LRAEIYNMvfneestVRAIIMVSHNLEEVVELSDKVIILGGRPA 192
Cdd:COG1245 254 LIRELAEE-------GKYVLVVEHDLAILDYLADYVHILYGEPG 290
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
11-192 |
2.15e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.66 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 11 VSIVAPTGTGKTTLLRIIAGLRRPDSGKVllmgeevKGPTPKLAMI--FQDFALYPWLTALENVELALLHR--------- 79
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSGELIPNLGDY-------EEEPSWDEVLkrFRGTELQNYFKKLYNGEIKVVHKpqyvdlipk 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 80 ------KDLSKEV-RREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDaiTAEGLRAE 152
Cdd:PRK13409 175 vfkgkvRELLKKVdERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD--IRQRLNVA 252
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1732728249 153 IynmVFNEESTVRAIIMVSHNLEEVVELSDKVIILGGRPA 192
Cdd:PRK13409 253 R---LIRELAEGKYVLVVEHDLAVLDYLADNVHIAYGEPG 289
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
92-187 |
3.78e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 52.88 E-value: 3.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 92 RKYLELVGLGGFEDY------YPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITaeglRAEIYNMV--FNEEST 163
Cdd:PRK15093 134 RRAIELLHRVGIKDHkdamrsFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTT----QAQIFRLLtrLNQNNN 209
|
90 100
....*....|....*....|....
gi 1732728249 164 VrAIIMVSHNLEEVVELSDKVIIL 187
Cdd:PRK15093 210 T-TILLISHDLQMLSQWADKINVL 232
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-187 |
6.76e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 52.67 E-value: 6.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAG-LRRPDSGKVLLMGEEVKgpTPKLAMIFQ-----------DFALYPWLTA 68
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRGSVAY--VPQVSWIFNatvrenilfgsDFESERYWRA 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 69 LENVelALLHRKDLskevrreIARKYLELVGLGGFedyyprELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEg 148
Cdd:PLN03232 714 IDVT--ALQHDLDL-------LPGRDLTEIGERGV------NISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAH- 777
|
170 180 190
....*....|....*....|....*....|....*....
gi 1732728249 149 lraEIYNMVFNEESTVRAIIMVSHNLeEVVELSDKVIIL 187
Cdd:PLN03232 778 ---QVFDSCMKDELKGKTRVLVTNQL-HFLPLMDRIILV 812
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
13-172 |
7.93e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 50.64 E-value: 7.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 13 IVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEV-KGPTPKLAMIFQDFALYPWLTALENVELallHRKDLSKEVRREIA 91
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNInNIAKPYCTYIGHNLGLKLEMTVFENLKF---WSEIYNSAETLYAA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 92 RKYLELVGLGGFEDYyprELSGGMKQRVAIARALAAQPVVLLMDEPFANLDaitaEGLRAEIYNMVFNEESTVRAIIMVS 171
Cdd:PRK13541 108 IHYFKLHDLLDEKCY---SLSSGMQKIVAIARLIACQSDLWLLDEVETNLS----KENRDLLNNLIVMKANSGGIVLLSS 180
|
.
gi 1732728249 172 H 172
Cdd:PRK13541 181 H 181
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-172 |
9.43e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.87 E-value: 9.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 3 FKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVkgptpkLAMIFQDfalyPWLTALENV---------E 73
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLI------VARLQQD----PPRNVEGTVydfvaegieE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 74 LA--------LLHR--KDLSKEVRREIAR------------------KYLELVGLGGfeDYYPRELSGGMKQRVAIARAL 125
Cdd:PRK11147 94 QAeylkryhdISHLveTDPSEKNLNELAKlqeqldhhnlwqlenrinEVLAQLGLDP--DAALSSLSGGWLRKAALGRAL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1732728249 126 AAQPVVLLMDEPFANLDAITAEGLraEIYNMVFNEestvrAIIMVSH 172
Cdd:PRK11147 172 VSNPDVLLLDEPTNHLDIETIEWL--EGFLKTFQG-----SIIFISH 211
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
18-137 |
2.04e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.89 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 18 GTGKTTLLRIIAGLRRPDSGKVLLMGEEVkgpTPK-LAM------IFQDFALYPWLTALENVELallHRK--DLSKEvrr 88
Cdd:NF033858 302 GCGKSTTMKMLTGLLPASEGEAWLFGQPV---DAGdIATrrrvgyMSQAFSLYGELTVRQNLEL---HARlfHLPAA--- 372
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1732728249 89 EIARKYLELV---GLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEP 137
Cdd:NF033858 373 EIAARVAEMLerfDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEP 424
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
2-187 |
2.46e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.56 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDS--GKVLLMGEEVKGPTPK------LAMIFQDFALYPWLTALENVE 73
Cdd:NF040905 21 NLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCRFKDIRdsealgIVIIHQELALIPYLSIAENIF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 74 LALLHRK----DLSKEVRReiARKYLELVGLGgfEDyyPRELSG----GMKQRVAIARALAAQPVVLLMDEPFANLDAIT 145
Cdd:NF040905 101 LGNERAKrgviDWNETNRR--ARELLAKVGLD--ES--PDTLVTdigvGKQQLVEIAKALSKDVKLLILDEPTAALNEED 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1732728249 146 AE-------GLRAEiynmvfneestvrAI--IMVSHNLEEVVELSDKVIIL 187
Cdd:NF040905 175 SAalldlllELKAQ-------------GItsIIISHKLNEIRRVADSITVL 212
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
18-195 |
3.13e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 49.79 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 18 GTGKTTLLRIIAGLRRPDSGKVLLMGEEV-----KGPTPKLAMIFQDF--------------ALYPWLTALenvelALLH 78
Cdd:PRK10575 47 GSGKSTLLKMLGRHQPPSEGEILLDAQPLeswssKAFARKVAYLPQQLpaaegmtvrelvaiGRYPWHGAL-----GRFG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 79 RKDlskevrREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEIYNMVF 158
Cdd:PRK10575 122 AAD------REKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQ 195
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1732728249 159 NEESTVRAII----MVSHNLEEVVELSDKVIILGGRPASII 195
Cdd:PRK10575 196 ERGLTVIAVLhdinMAARYCDYLVALRGGEMIAQGTPAELM 236
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-201 |
3.84e-07 |
|
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: 48.68 E-value: 3.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLR--RPDSGKVLLMGEEVKGPTPK------LAMIFQdfalYPwlTALENVE 73
Cdd:cd03217 20 NLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEerarlgIFLAFQ----YP--PEIPGVK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 74 LAllhrkdlskevrreiarKYLELVGLGgfedyypreLSGGMKQRVAIARALAAQPVVLLMDEPFANLDaITAEGLRAEI 153
Cdd:cd03217 94 NA-----------------DFLRYVNEG---------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLD-IDALRLVAEV 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1732728249 154 YNMVFNEEstvRAIIMVSHNlEEVVEL--SDKV-IILGGR-----PASIIAEVEIK 201
Cdd:cd03217 147 INKLREEG---KSVLIITHY-QRLLDYikPDRVhVLYDGRivksgDKELALEIEKK 198
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1-143 |
6.22e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 49.74 E-value: 6.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVkGPTPKLAMIF----QDFALY--PW--------- 65
Cdd:PLN03130 636 INLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVIRGTV-AYVPQVSWIFnatvRDNILFgsPFdperyerai 714
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1732728249 66 -LTALENvELALLHRKDLSkevrrEIARKYLELvglggfedyyprelSGGMKQRVAIARALAAQPVVLLMDEPFANLDA 143
Cdd:PLN03130 715 dVTALQH-DLDLLPGGDLT-----EIGERGVNI--------------SGGQKQRVSMARAVYSNSDVYIFDDPLSALDA 773
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
9-192 |
6.64e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 47.95 E-value: 6.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 9 EFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVllmgeEVKGPTPKlamifqdfalypwltalenvelallhrkdlskevrr 88
Cdd:cd03222 26 EVIGIVGPNGTGKTTAVKILAGQLIPNGDND-----EWDGITPV------------------------------------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 89 eiarkylelvglggfedYYPR--ELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEIYNMVFNEESTVra 166
Cdd:cd03222 65 -----------------YKPQyiDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTA-- 125
|
170 180
....*....|....*....|....*.
gi 1732728249 167 iIMVSHNLEEVVELSDKVIILGGRPA 192
Cdd:cd03222 126 -LVVEHDLAVLDYLSDRIHVFEGEPG 150
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1-192 |
1.40e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 48.56 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMG--------EEVKGptpKLAMIFQDfalyPWL---TAL 69
Cdd:PRK10789 334 VNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDipltklqlDSWRS---RLAVVSQT----PFLfsdTVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 70 ENVELAllhRKDLSKEVRREIAR-------------KYLELVGLGGFEdyypreLSGGMKQRVAIARALAAQPVVLLMDe 136
Cdd:PRK10789 407 NNIALG---RPDATQQEIEHVARlasvhddilrlpqGYDTEVGERGVM------LSGGQKQRISIARALLLNAEILILD- 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1732728249 137 pfanlDAITAEGLRAEiYNMVFN--EESTVRAIIMVSHNLEEVVELSDKVIILGGRPA 192
Cdd:PRK10789 477 -----DALSAVDGRTE-HQILHNlrQWGEGRTVIISAHRLSALTEASEILVMQHGHIA 528
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
81-187 |
1.47e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 48.19 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 81 DLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEIYNMVFNE 160
Cdd:NF000106 115 DLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDG 194
|
90 100
....*....|....*....|....*..
gi 1732728249 161 EStvraIIMVSHNLEEVVELSDKVIIL 187
Cdd:NF000106 195 AT----VLLTTQYMEEAEQLAHELTVI 217
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
13-185 |
1.75e-06 |
|
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: 46.83 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 13 IVAPTGTGKTTLLriiaglrrpDSGKVLLMGEevKGPTPKLAMIFQDFAlypwlTALEN---VELALLHRKDLSKEVRRE 89
Cdd:cd03240 27 IVGQNGAGKTTII---------EALKYALTGE--LPPNSKGGAHDPKLI-----REGEVraqVKLAFENANGKKYTITRS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 90 IAR-KYLELVGLGGFEDYYPRE---LSGGMKQ------RVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEIYNMVfn 159
Cdd:cd03240 91 LAIlENVIFCHQGESNWPLLDMrgrCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESLAEIIEER-- 168
|
170 180
....*....|....*....|....*.
gi 1732728249 160 EESTVRAIIMVSHNlEEVVELSDKVI 185
Cdd:cd03240 169 KSQKNFQLIVITHD-EELVDAADHIY 193
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
111-191 |
2.04e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 46.55 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 111 LSGGMKQRVAIARALAAQP--VVLLMDEPFANLDAITAEGLRAEIYNMVfNEESTVraiIMVSHNlEEVVELSDKVIILG 188
Cdd:cd03238 88 LSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVIKGLI-DLGNTV---ILIEHN-LDVLSSADWIIDFG 162
|
...
gi 1732728249 189 GRP 191
Cdd:cd03238 163 PGS 165
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1-189 |
2.92e-06 |
|
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: 47.63 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKgpTPKLAMIFQDfalypwlTALENVelalLHRK 80
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAY--VPQQAWIQND-------SLRENI----LFGK 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 81 DLSKEVRREIARKY-----LELVGLGGFEDYYPR--ELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEglraEI 153
Cdd:TIGR00957 724 ALNEKYYQQVLEACallpdLEILPSGDRTEIGEKgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGK----HI 799
|
170 180 190
....*....|....*....|....*....|....*...
gi 1732728249 154 YNMVFNEESTV--RAIIMVSHNLEEVVELsDKVIILGG 189
Cdd:TIGR00957 800 FEHVIGPEGVLknKTRILVTHGISYLPQV-DVIIVMSG 836
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-176 |
3.21e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.32 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGlRRPD--SGKVLLMGEEvKGPTPKLAMIFQDFAL--------YPWLTALE 70
Cdd:PRK10938 279 LSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQgySNDLTLFGRR-RGSGETIWDIKKHIGYvssslhldYRVSTSVR 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 71 NVELALLHrkD---LSKEV---RREIARKYLELVGLGGFEDYYP-RELSGGMKQRVAIARALAAQPVVLLMDEPFANLDA 143
Cdd:PRK10938 357 NVILSGFF--DsigIYQAVsdrQQKLAQQWLDILGIDKRTADAPfHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDP 434
|
170 180 190
....*....|....*....|....*....|...
gi 1732728249 144 ITAEGLRAEIYNMVFNEESTvraIIMVSHNLEE 176
Cdd:PRK10938 435 LNRQLVRRFVDVLISEGETQ---LLFVSHHAED 464
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-185 |
6.64e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.42 E-value: 6.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKG--PTPKLAMIFQDFALYPWLTA------LENV 72
Cdd:PRK15064 338 LNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGyyAQDHAYDFENDLTLFDWMSQwrqegdDEQA 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 73 ELALLHRKDLSKEvrrEIARKylelvglggfedyyPRELSGGMKQRVAIARALAAQPVVLLMDEPFANLD--AITAEGLR 150
Cdd:PRK15064 418 VRGTLGRLLFSQD---DIKKS--------------VKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDmeSIESLNMA 480
|
170 180 190
....*....|....*....|....*....|....*
gi 1732728249 151 AEIYnmvfneESTVraiIMVSHNLEEVVELSDKVI 185
Cdd:PRK15064 481 LEKY------EGTL---IFVSHDREFVSSLATRII 506
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
11-146 |
9.08e-06 |
|
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: 44.93 E-value: 9.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 11 VSIVAPTGTGKTTLLRIIAGlRRPD---SGKVLLMGEEVKGP-TPKLAMIFQDFALYPWLTALENVEL-ALLhrkdlske 85
Cdd:cd03232 36 TALMGESGAGKTTLLDVLAG-RKTAgviTGEILINGRPLDKNfQRSTGYVEQQDVHSPNLTVREALRFsALL-------- 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1732728249 86 vrreiarkylelvglggfedyypRELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITA 146
Cdd:cd03232 107 -----------------------RGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAA 144
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-172 |
1.49e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 44.63 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGlrRPD----SGKVLLMGEEVKGPTPKL---AMIFQDFAlYP--------- 64
Cdd:CHL00131 26 LNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLEPEErahLGIFLAFQ-YPieipgvsna 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 65 -WLTALENVELALLHRKDLSKEVRREIARKYLELVGLGG-FEDYYPRE-LSGGMKQRVAIARALAAQPVVLLMDEPFANL 141
Cdd:CHL00131 103 dFLRLAYNSKRKFQGLPELDPLEFLEIINEKLKLVGMDPsFLSRNVNEgFSGGEKKRNEILQMALLDSELAILDETDSGL 182
|
170 180 190
....*....|....*....|....*....|.
gi 1732728249 142 DaITAEGLRAEIYNMVFNEEstvRAIIMVSH 172
Cdd:CHL00131 183 D-IDALKIIAEGINKLMTSE---NSIILITH 209
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
17-172 |
2.01e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 45.22 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 17 TGTGKTTLLRIIAGlrRPDSGKVllMGEEVKGPTPKLAMIFQDFALY--------PWLTALENVELALLHR--KDLSKEV 86
Cdd:PLN03140 915 SGAGKTTLMDVLAG--RKTGGYI--EGDIRISGFPKKQETFARISGYceqndihsPQVTVRESLIYSAFLRlpKEVSKEE 990
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 87 RREIARKYLELVGLGGFEDY---YP--RELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAeglrAEIYNMVFNEE 161
Cdd:PLN03140 991 KMMFVDEVMELVELDNLKDAivgLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAA----AIVMRTVRNTV 1066
|
170
....*....|.
gi 1732728249 162 STVRAIIMVSH 172
Cdd:PLN03140 1067 DTGRTVVCTIH 1077
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1-136 |
2.05e-05 |
|
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: 45.12 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGL--------RRPDSGKVLL------MG-----EEVKGPTPKLAMIFQDFA 61
Cdd:TIGR00954 471 LSFEVPSGNNLLICGPNGCGKSSLFRILGELwpvyggrlTKPAKGKLFYvpqrpyMTlgtlrDQIIYPDSSEDMKRRGLS 550
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1732728249 62 LYPWLTALENVELALLhrkdLSKEVRREIARKYLElvglggfedyyprELSGGMKQRVAIARALAAQPVVLLMDE 136
Cdd:TIGR00954 551 DKDLEQILDNVQLTHI----LEREGGWSAVQDWMD-------------VLSGGEKQRIAMARLFYHKPQFAILDE 608
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1-188 |
2.83e-05 |
|
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: 44.52 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 1 MNFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDsGKVLLMGeevkgptpklaMIFQDFALYPWLTALENVE-----LA 75
Cdd:TIGR01271 1238 LSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDG-----------VSWNSVTLQTWRKAFGVIPqkvfiFS 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 76 LLHRKDLSKEVR---REIArKYLELVGLGGFEDYYPREL-----------SGGMKQRVAIARALAAQPVVLLMDEPFANL 141
Cdd:TIGR01271 1306 GTFRKNLDPYEQwsdEEIW-KVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKILLLDEPSAHL 1384
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1732728249 142 DAITAEGLRAEIYNMVFNeeSTVraiIMVSHNLEEVVELSDKVIILG 188
Cdd:TIGR01271 1385 DPVTLQIIRKTLKQSFSN--CTV---ILSEHRVEALLECQQFLVIEG 1426
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
18-142 |
1.12e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.85 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 18 GTGKTTLLRIIAGLRRPDSGKVLLmgeeVKGPtpKLAMIFQDfalypWLTALENVELALLHRKDLSKEVRREIARKYLEL 97
Cdd:PRK10636 348 GAGKSTLIKLLAGELAPVSGEIGL----AKGI--KLGYFAQH-----QLEFLRADESPLQHLARLAPQELEQKLRDYLGG 416
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1732728249 98 VGLGGFEDYYPRE-LSGGMKQRVAIARALAAQPVVLLMDEPFANLD 142
Cdd:PRK10636 417 FGFQGDKVTEETRrFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
111-198 |
1.43e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.08 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 111 LSGGMKQRVAIARALAAQPVVLLMDEPFANLDAitaeGLRAEIYNMVFNEESTVRAIIMVSHNLEEVVELSDKVIILG-G 189
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDV----GAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNeG 480
|
....*....
gi 1732728249 190 RpasIIAEV 198
Cdd:NF040905 481 R---ITGEL 486
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
3-187 |
1.50e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 42.46 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 3 FKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEV-----KGPTPKLAMIFQDFALYPWlTALENVELALl 77
Cdd:PTZ00243 1331 FRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIgayglRELRRQFSMIPQDPVLFDG-TVRQNVDPFL- 1408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 78 hrKDLSKEVRREiarkyLELVGL--------GGFEDyypRELSG------GMKQRVAIARALAAQ-PVVLLMDEPFANLD 142
Cdd:PTZ00243 1409 --EASSAEVWAA-----LELVGLrervasesEGIDS---RVLEGgsnysvGQRQLMCMARALLKKgSGFILMDEATANID 1478
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1732728249 143 aitaEGLRAEIYNMVFNEESTvRAIIMVSHNLEEVVELsDKVIIL 187
Cdd:PTZ00243 1479 ----PALDRQIQATVMSAFSA-YTVITIAHRLHTVAQY-DKIIVM 1517
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
109-142 |
1.66e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.15 E-value: 1.66e-04
10 20 30
....*....|....*....|....*....|....
gi 1732728249 109 RELSGGMKQRVAIARALAAQPVVLLMDEPFANLD 142
Cdd:PLN03073 343 KTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-142 |
2.43e-04 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 41.54 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVLLMGEEVKGPT-----PKLAMIFQDFALYPwLTALENVELA- 75
Cdd:PRK11176 363 NFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTlaslrNQVALVSQNVHLFN-DTIANNIAYAr 441
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1732728249 76 --LLHRKDLSKEVRREIARKYLE--------LVGLGGFEdyypreLSGGMKQRVAIARALAAQPVVLLMDEPFANLD 142
Cdd:PRK11176 442 teQYSREQIEEAARMAYAMDFINkmdngldtVIGENGVL------LSGGQRQRIAIARALLRDSPILILDEATSALD 512
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
9-195 |
3.28e-04 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 40.97 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 9 EFVSIVAPTGTGKTTLLRIIAG-LRRPD-------SGKVLLMGEEVKG-PTPKLAMIFqdfALYPWLT----ALENVELA 75
Cdd:PRK13547 28 RVTALLGRNGAGKSTLLKALAGdLTGGGaprgarvTGDVTLNGEPLAAiDAPRLARLR---AVLPQAAqpafAFSAREIV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 76 LL------HRKDLSKEVRREIARKYLELVGLGGFEDYYPRELSGGMKQRVAIARALA---------AQPVVLLMDEPFAN 140
Cdd:PRK13547 105 LLgryphaRRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAqlwpphdaaQPPRYLLLDEPTAA 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1732728249 141 LDAITAEGLRAEIYNMVFNEESTVRAII----MVSHNLEEVVELSDKVIILGGRPASII 195
Cdd:PRK13547 185 LDLAHQHRLLDTVRRLARDWNLGVLAIVhdpnLAARHADRIAMLADGAIVAHGAPADVL 243
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
111-189 |
3.95e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 41.30 E-value: 3.95e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1732728249 111 LSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAEIYNMVFNEESTVRAiimvSHNLeEVVELSDKVIILGG 189
Cdd:PTZ00243 783 LSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLA----THQV-HVVPRADYVVALGD 856
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
111-179 |
4.12e-04 |
|
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: 40.61 E-value: 4.12e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1732728249 111 LSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLRAeiynmVFNEESTVRAIIMVSHNLEEVVE 179
Cdd:cd03289 139 LSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRK-----TLKQAFADCTVILSEHRIEAMLE 202
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
111-188 |
4.64e-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: 39.65 E-value: 4.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 111 LSGGMKQRVAIARALA---AQPVVL-LMDEPFANLDAITAEGLRAEIYNMvFNEESTVraiIMVSHNlEEVVELSDKVII 186
Cdd:cd03227 78 LSGGEKELSALALILAlasLKPRPLyILDEIDRGLDPRDGQALAEAILEH-LVKGAQV---IVITHL-PELAELADKLIH 152
|
..
gi 1732728249 187 LG 188
Cdd:cd03227 153 IK 154
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
2-74 |
6.75e-04 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 39.66 E-value: 6.75e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1732728249 2 NFKVHSHEFVSIVAPTGTGKTTLLRIIAGLRRPDSGKVL-LMGEEVkgptPKLAMIFqdfaLYPWLTALENVEL 74
Cdd:PRK15177 7 DFVMGYHEHIGILAAPGSGKTTLTRLLCGLDAPDEGDFIgLRGDAL----PLGANSF----ILPGLTGEENARM 72
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
110-172 |
7.99e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.88 E-value: 7.99e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1732728249 110 ELSGGMKQRVAIARALAAQPVVLLMDEPFANLDAITAEGLrAEIYNmvfNEESTvraIIMVSH 172
Cdd:PRK15064 155 EVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWL-EDVLN---ERNST---MIIISH 210
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
17-146 |
1.28e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 39.71 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732728249 17 TGTGKTTLLRIIAGlrRPDSGkVLLMGEE-VKGptPKLAMIFQDFALY--------PWLTALENVELALLHR--KDLSKE 85
Cdd:TIGR00956 798 SGAGKTTLLNVLAE--RVTTG-VITGGDRlVNG--RPLDSSFQRSIGYvqqqdlhlPTSTVRESLRFSAYLRqpKSVSKS 872
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1732728249 86 VRREIARKYLELVGLggfEDY------YPRE-LSGGMKQRVAIARALAAQPVVLL-MDEPFANLDAITA 146
Cdd:TIGR00956 873 EKMEYVEEVIKLLEM---ESYadavvgVPGEgLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTA 938
|
|
| |
